AI-based structure prediction empowers integrative structural analysis of human nuclear pores
Open accessPublished version of a preprint
Abstract
INTRODUCTION: The eukaryotic nucleus protects the genome and is enclosed by the two membranes of the nuclear envelope. Nuclear pore complexes (NPCs) perforate the nuclear envelope to facilitate nucleocytoplasmic transport. With a molecular weight of ∼120 MDa, the human NPC is one of the largest protein complexes. Its ~1000 proteins are taken in multiple copies from a set of about 30 distinct nucleoporins (NUPs). They can be roughly categorized into two classes. Scaffold NUPs contain folded domains and form a cylindrical scaffold architecture around a central channel. Intrinsically disordered NUPs line the scaffold and extend into the central channel, where they interact with cargo complexes. The NPC architecture is highly dynamic. It responds to changes in nuclear envelope tension with conformational breathing that manifests in dilation and constriction movements. Elucidating the scaffold architecture, ultimately at atomic resolution, will be important for gaining a more precise understanding of NPC function and dynamics but imposes a substantial challenge for structural biologists. RATIONALE: Considerable progress has been made toward this goal by a joint effort in the field. A synergistic combination of complementary approaches has turned out to be critical. In situ structural biology techniques were used to reveal the overall layout of the NPC scaffold that defines the spatial reference for molecular modeling. High-resolution structures of many NUPs were determined in vitro. Proteomic analysis and extensive biochemical work unraveled the interaction network of NUPs. Integrative modeling has been used to combine the different types of data, resulting in a rough outline of the NPC scaffold. Previous structural models of the human NPC, however, were patchy and limited in accuracy owing to several challenges: (i) Many of the high-resolution structures of individual NUPs have been solved from distantly related species and, consequently, do not comprehensively cover their human counterparts. (ii) The scaffold is interconnected by a set of intrinsically disordered linker NUPs that are not straightforwardly accessible to common structural biology techniques. (iii) The NPC scaffold intimately embraces the fused inner and outer nuclear membranes in a distinctive topology and cannot be studied in isolation. (iv) The conformational dynamics of scaffold NUPs limits the resolution achievable in structure determination. RESULTS: In this study, we used artificial intelligence (AI)–based prediction to generate an extensive repertoire of structural models of human NUPs and their subcomplexes. The resulting models cover various domains and interfaces that so far remained structurally uncharacterized. Benchmarking against previous and unpublished x-ray and cryo–electron microscopy structures revealed unprecedented accuracy. We obtained well-resolved cryo–electron tomographic maps of both the constricted and dilated conformational states of the human NPC. Using integrative modeling, we fitted the structural models of individual NUPs into the cryo–electron microscopy maps. We explicitly included several linker NUPs and traced their trajectory through the NPC scaffold. We elucidated in great detail how membrane-associated and transmembrane NUPs are distributed across the fusion topology of both nuclear membranes. The resulting architectural model increases the structural coverage of the human NPC scaffold by about twofold. We extensively validated our model against both earlier and new experimental data. The completeness of our model has enabled microsecond-long coarse-grained molecular dynamics simulations of the NPC scaffold within an explicit membrane environment and solvent. These simulations reveal that the NPC scaffold prevents the constriction of the otherwise stable double-membrane fusion pore to small diameters in the absence of membrane tension. CONCLUSION: Our 70-MDa atomically resolved model covers >90% of the human NPC scaffold. It captures conformational changes that occur during dilation and constriction. It also reveals the precise anchoring sites for intrinsically disordered NUPs, the identification of which is a prerequisite for a complete and dynamic model of the NPC. Our study exemplifies how AI-based structure prediction may accelerate the elucidation of subcellular architecture at atomic resolution. A 70-MDa model of the human nuclear pore complex scaffold architecture.: The structural model of the human NPC scaffold is shown for the constricted state as a cut-away view. High-resolution models are color coded according to nucleoporin subcomplex membership. The nuclear envelope is shown as a gray surface.
AI snapshot
Written from the paper’s full text.
TL;DR
The paper combines AI-based structure prediction with cryo-ET and integrative modeling to build a near-complete model of the human nuclear pore complex scaffold in constricted and dilated states. It shows linker Nups organize the scaffold, maps membrane-anchoring hubs, and uses molecular dynamics to argue the scaffold widens the nuclear envelope pore rather than stabilizing membrane fusion.
Key findings
- The near-complete human NPC scaffold model includes 25 of ~30 Nups, accounts for 70 MDa and >90% of scaffold molecular weight, compared with 16 Nups and 35 MDa (46% of scaffold) in the previous model; cryo-ET maps reached 12 Å for the cytoplasmic ring, 12.6 Å for the inner ring, and 23.2 Å for the nuclear ring, and the dilated in cellulo inner-ring diameter was 54 Å versus 42 Å in the constricted state.
- Linker Nups perform dedicated spatial organization: the Nup35 dimer bridges adjacent inner-ring spokes via SLiMs to Nup155 and Nup93, while the Nup93 N-terminus connects Nup205, Nup188, Nup62, Nup58, and Nup54 within the same subcomplex/spoke rather than across spokes.
- A transmembrane interaction hub is proposed at the inner-ring/outer-ring interface, formed by Aladin–NDC1 with Nup155 and Nup35; Gp210 was modeled as a luminal ring, and gp210 deletion in HEK293 cells removed luminal ring density without changing overall scaffold diameter.
- In 1 µs Martini MD simulations, a double-membrane pore without proteins constricted toward a catenoid-like shape, whereas the NPC scaffold kept the pore wider; the scaffold constricted by about 9%, and lateral tension could maintain or widen the pore, with the membrane wrapping tightly around the inner ring in an octagonal shape.
Methods
- Cryo-ET of purified HeLa nuclear envelopes and in cellulo HeLa/HEK293 cells after cryo-FIB thinning, with a geometrically restrained classification procedure and subtomogram averaging.
- AI-based structure prediction using AlphaFold, RoseTTAfold, and ColabFold for individual Nups and subcomplexes, validated against unreleased X-ray structures and cryo-EM densities, followed by integrative fitting and refinement with Assembline.
- Coarse-grained Martini molecular dynamics simulations of double-membrane pores and the NPC scaffold with explicit membrane and water over 1 µs; proximity labeling mass spectrometry with BirA-tagged Aladin; CRISPR/Cas9 gp210 deletion in HEK293 cells.
Limitations
- Stated: not all subunit or domain combinations modeled with AI-based structure prediction were consistent with complementary data, so experimental structure determination will still be required where a priori knowledge remains sparse; the precise location of Pom121 remains unknown, and neither AlphaFold nor RoseTTAfold built high-confidence models for it.
- Stated: peripheral Nups such as parts of the Nup214 and Nup358 complexes are flexible, and their entire EM density is unlikely to be resolved in the near future.
- Evident from the text: the nuclear-ring map is lower resolution (23.2 Å) than the cytoplasmic and inner-ring maps, and several assignments rely on AI predictions, unpublished X-ray structures, and validation against EM density rather than fully independent atomic structures.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
0 of 21 cited sources checked · 0 supported · 0 flagged
- Findingown data
The copy of Nup93 in the cytoplasmic ring is located underneath the Nup358 complex.
“The copy of Nup93 in the CR is located underneath the Nup358 complex, further corroborating a role of Nup358 in stabilizing the higher order structure (21).”
Quote in the paperSubstantial claim - Findingown data
Yet another copy of Nup93 unique to the cytoplasmic ring bridges the inner Y-complexes from two consecutive spokes.
“Yet another copy of Nup93 that is unique to the CR bridges the inner Y-complexes from two consecutive spokes.”
Quote in the paperSubstantial claim - Findingown data
The AI-based models excellently fit the EM densities.
“The AI-based models also excellently fit our EM densities (Fig. S7A-E).”
Quote in the paperSubstantial claim - Findingown data
Two previously undetected copies of Nup93 bridge the inner and outer Y-complexes both in the cytoplasmic and nuclear rings, with an inherent C2 symmetry.
“Two previously undetected copies of Nup93 bridge the inner and outer Y-complexes both in the CR and NR, with an inherent C2 symmetry.”
Quote in the paperSubstantial claim - Findingown data
AI-based models of Nups and their subcomplexes built using AlphaFold and RoseTTAfold are consistent with unreleased X-ray crystallography structures, cryo-EM maps, and complementary data.
“We demonstrate that AI-based models of Nups and their subcomplexes built using AlphaFold (27) and RoseTTAfold (28) are consistent with unreleased X-ray crystallography structures, cryo-EM maps, and complementary data.”
- Also stated in: § A near-complete model of the human NPC scaffold · plain
“In addition, we validated the accuracy of the models by comparison to yet unreleased structures solved by X-ray crystallography for human Nup358, Nup93, Nup88, Nup98, and of Nup205 and Nup188 from Chaetomium thermophilum (Fig. S6).”
Quote in the paperSubstantial claim - Also stated in: § A near-complete model of the human NPC scaffold · plain
- Findingown data
They form an overall Z-shaped outline within an individual spoke.
“They form an overall Z-shaped outline within an individual spoke (Fig. 3).”
Quote in the paperNot a substantial claim - Findingown data
Proximity labeling mass spectrometry with BirA-tagged Aladin identified NDC1 and Nup35 as the most prominently enriched interactors.
“We confirmed this interaction using proximity labeling mass spectrometry with BirA-tagged Aladin and identified NDC1 and Nup35 as the most prominently enriched interactors (Fig. S12).”
Quote in the paperSubstantial claim- Rests on an assumption: Proximity labeling mass spectrometry with BirA-tagged Aladin reliably identifies the most prominently enriched interactors of Aladin.
- Findingown data
The Nup35 linker regions bridge between neighboring spokes of the inner ring.
“The resulting connectivity map (Fig. 2) reveals that the Nup35 linker regions bridge between neighboring spokes of the IR.”
Quote in the paperSubstantial claim - Findingnone given
Not all subunit or domain combinations that the authors attempted to model with AI-based structure prediction led to structural models consistent with complementary data.
“Not all subunit or domain combinations that we attempted to model with AI-based structure prediction led to structural models that were consistent with complementary data”
Quote in the paperSubstantial claim - Findingnone given
The coarse-grained dynamic model is of sufficient quality for molecular simulations.
“Our analysis demonstrates that coarse-grained dynamic model is of sufficient quality for molecular simulations, which in future could quantitively and predictively describe how the NPC interplays with the nuclear membrane and how it responds to mechanical challenges.”
Quote in the paperSubstantial claim - Findingown data
The membrane-anchoring motifs of the human NPC are distributed over the entire scaffold.
“The membrane-anchoring motifs of the human NPC are distributed over the entire scaffold.”
Quote in the paperSubstantial claim - Findingown data
The Gp210 model fitted the density sufficiently well to allow tracing Gp210 monomers in the cryo-EM map of the Xenopus laevis NPC.
“Already as a rigid body, this model fitted the density sufficiently well to allow tracing Gp210 monomers in the cryo-EM map of the Xenopus laevis NPC, which is superbly resolved in the luminal region (50).”
Quote in the paperSubstantial claim - Findingown data
The membrane-binding motifs arrange in similar clusters in both the constricted and dilated state.
“The membrane-binding motifs arrange in similar clusters in both the constricted and dilated state.”
Quote in the paperSubstantial claim - Findingown data
The opening of the relaxed double-membrane pore is considerably smaller than even the most constricted NPC conformations.
“Interestingly, the opening of the relaxed double-membrane pore is considerably smaller than even the most constricted NPC conformations.”
Quote in the paperSubstantial claim - Findingreasoning
A Nup35 bridge between adjacent spokes is the only arrangement geometrically possible for both the constricted and the dilated NPC state.
“A Nup35 bridge between adjacent spokes is the only arrangement geometrically possible for both the constricted and the dilated NPC state.”
Quote in the paperSubstantial claim - Findingown data
In the cytoplasmic and nuclear rings, the linkage between Nup93 and Nup205 is geometrically possible.
“In the CR and NR, the linkage between Nup93 and Nup205 is geometrically possible, emphasizing the similar architectural design of the respective complexes.”
Quote in the paperSubstantial claim - Findingown data
The model includes 25 out of ~30 Nups.
“Figure: include 25 out of ~30 Nups, and account for 70 MDa of the molecular weight of the NPC (>90% of the scaffold molecular weight) in comparison to 16 Nups and 35 MDa (46% of the scaffold) of the previous model, and largely account for the EM density observed in the constricted and dilated states.”
Quote in the paperSubstantial claim - Findingown data
The connectivity map captures the 3D trajectory of linker Nups through the assembled scaffold.
“Our connectivity map captures the 3D trajectory of linker Nups through the assembled scaffold.”
Quote in the paperSubstantial claim - Findingown data
An Aladin-binding SLiM in Nup35 is located between the amphipathic helix and Nup155-binding SLiM.
“We also predicted an Aladin-binding SLiM in Nup35, located between the amphipathic helix and Nup155-binding SLiM (Fig. 3, Fig. S9).”
Quote in the paperSubstantial claim - Findingown data
Aladin and NDC1 form a transmembrane interaction hub with the inner and connector copies of Nup155.
“Aladin and NDC1 form a transmembrane interaction hub with the inner and connector copies of Nup155”
Quote in the paperSubstantial claim - Findingown data
The model includes all known membrane-binding domains except for Pom121.
“Taken together, our model includes all known membrane-binding domains except for the celltype specifically expressed Pom121, the precise location of which within the NPC remains unknown, and neither AlphaFold or RoseTTAfold could build structural models with high confidence.”
Quote in the paperSubstantial claim - Findingown data
In MD simulations with explicit membrane and water, the membrane pore wrapped tightly around the IR plane, adopting an octagonal shape.
“In these simulations, we found that the membrane pore wrapped tightly around the IR plane, adopting an octagonal shape (Fig. 4C).”
Quote in the paperSubstantial claim - Findingown data
Eight copies of Gp210 per spoke were assigned.
“Thus, we could assign eight copies of Gp210 per spoke (Fig. S13).”
Quote in the paperSubstantial claim - Findingown data
The AI-based model of the Nup214 sub-complex interacts with Nup85 pointing towards the central channel.
“The AI-based model of the Nup214 sub-complex interacts with Nup85 pointing towards the central channel, likely to optimally position the associated helicase crucial for mRNA export.”
Quote in the paperNot a substantial claim - Findingown data
The diameter of the NPC scaffold constricted by about 9% in these simulations.
“We also observed that the diameter of the NPC scaffold constricted by about 9% (Fig. 4B).”
Quote in the paperSubstantial claim - Findingown data
Modeling of individual Gp210 fragments and inter-Gp210 interactions led to an overall model that explained the entire density of the luminal ring of the Xenopus cryo-EM map, including the C-terminal transmembrane helix.
“Modeling of individual Gp210 fragments and inter-Gp210 interactions with AlphaFold/ColabFold (Fig. S13) led to an overall model that explained the entire density of the luminal ring of the Xenopus cryo-EM map, including the C-terminal transmembrane helix.”
Quote in the paperSubstantial claim - Findingown data
An isolated half-toroidal double-membrane pore shaped initially as in the tomographic structure of the constricted NPC tightens over the course of 1 μs of MD toward the catenoid-like shape predicted by membrane elastic theory.
“An isolated half-toroidal double-membrane pore shaped initially as in the tomographic structure of the constricted NPC (left) tightens over the course of 1 µs of MD (right) toward the catenoid-like shape (green) predicted by membrane elastic theory.”
Quote in the paperSubstantial claim - Findingown data
The model largely accounts for the EM density observed in the constricted and dilated states.
“Figure: include 25 out of ~30 Nups, and account for 70 MDa of the molecular weight of the NPC (>90% of the scaffold molecular weight) in comparison to 16 Nups and 35 MDa (46% of the scaffold) of the previous model, and largely account for the EM density observed in the constricted and dilated states.”
Quote in the paperSubstantial claim - Findingown data
The Nup35 dimer interconnects adjacent spokes across different sub-complex species, thus facilitating cylindrical assembly of the IR in both constricted and dilated states.
“The Nup35 dimer interconnects adjacent spokes across different sub-complex species, thus facilitating cylindrical assembly of the IR in both constricted (top) and dilated (bottom) states.”
Quote in the paperSubstantial claim - Findingown data
The N-terminus of Nup93 isostoichiometrically connects the subunits Nup205, Nup188, Nup62, Nup58 and Nup54 within the same sub-complex species.
“The N-terminus of Nup93 isostoichiometrically connects the subunits Nup205, Nup188, Nup62, Nup58 and Nup54 within the same sub-complex species.”
Quote in the paperSubstantial claim - Findingown data
Systematic fitting of the NDC1-Aladin hetero-dimeric models to the EM map unambiguously identified two locations within the inner ring.
“Systematic fitting of the hetero-dimeric models to the EM map unambiguously identified two locations within the IR (Fig. S11).”
Quote in the paperSubstantial claim - Findingown data
AlphaFold predicted an interaction between the C-terminus of Nup155 and the N-terminal SLiM in Gle1 with high confidence scores.
“Using AlphaFold we predicted an interaction between the C-terminus of Nup155 and the N-terminal SLiM in Gle1 with high confidence scores (Fig. S12B).”
Quote in the paperSubstantial claim - Findingown data
At even higher tension, the membrane spontaneously detached from the NPC scaffold.
“At even higher tension, the membrane spontaneously detached from the NPC scaffold (Fig. S20).”
Quote in the paperNot a substantial claim - Findingown data
RoseTTAfold model of full-length Gp210 is elongated with clearly defined interfaces between consecutive domains.
“We used RoseTTAfold to model full-length Gp210 and obtained an elongated model with clearly defined interfaces between consecutive domains.”
Quote in the paperSubstantial claim - Findingown data
The membrane-binding bpropellers of the Y-complex (Nup160 and Nup133) and the inner ring (Nup155) are distributed as multiple pairs over the entire scaffold, following a well-defined pattern.
“The resulting membrane association map reveals that the membrane-binding bpropellers of the Y-complex (Nup160 and Nup133) and the IR (Nup155) are distributed as multiple pairs over the entire scaffold, whereby they follow a well-defined pattern.”
Quote in the paperSubstantial claim - Findingnone given
The model also contains several peripheral Nups, e.g. parts of the Nup214 and Nup358 complexes.
“The model also contains several peripheral Nups, e.g.parts of the Nup214 and Nup358 complexes.”
Quote in the paperNot a substantial claim - Findingown data
The NPC widens by ~10% in response to lateral membrane tension (ΔP=2 bar) compared to a zero-tension simulation (ΔP=0).
“The NPC (cyan) widens by ~10% in response to lateral membrane tension (right; ΔP=2 bar) compared to a zero-tension simulation (left; ΔP=0).”
Quote in the paperNot a substantial claim - Interpretationown data
Linker Nups spatially organize the scaffold within and across subcomplexes to establish the higher-order structure.
“We show that linker Nups spatially organize the scaffold within and across subcomplexes to establish the higher-order structure.”
- Also stated in: § Linker Nups fulfill dedicated roles of spatial organization within the higher-order assembly · plain
“In conclusion, the individual linker Nups specialize in dedicated spatial organization functions responsible for distinct aspects of assembly and maintenance of the NPC scaffold architecture.”
- Also stated in: § Discussion and conclusions · hedged
“Taken together with previous analysis of NPC assembly (9-13, 19), it suggests that the linker Nups facilitate dedicated spatial organization functions.”
Quote in the paperSubstantial claim - Also stated in: § Linker Nups fulfill dedicated roles of spatial organization within the higher-order assembly · plain
- Premisecitation
NDC1 is the only human transmembrane Nup conserved across eukaryotes.
“Among the three human transmembrane proteins, NDC1 is the only one that is conserved across eukaryotes (40).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [40] source
Not checked in the free run.
- Interpretationown data
The model provides a more accurate starting point for simulations of nucleocytoplasmic transport by providing native constraints on the diameter and a more precise mapping of the positions where the FG tails emanate from the scaffold.
“The model also provides a more accurate starting point for simulations of nucleocytoplasmic transport by providing the native constraints on the diameter and a more precise mapping of the positions where the FG tails emanate from the scaffold (Fig. S14).”
Quote in the paperSubstantial claim - Interpretationreasoning
The membrane shape defines the outline of the NPC scaffold and not vice versa.
“These data argue that the membrane shape defines the outline of the NPC scaffold and not vice versa.”
Quote in the paperSubstantial claim - Premisecitation
AlphaFold and RoseTTAfold have demonstrated unprecedented accuracy in predicting structures of complexes.
“However, AlphaFold and RoseTTAfold have recently demonstrated unprecedented accuracy in predicting structures of monomeric proteins (27,28,(61)(62)(63)(64)(65)(66) and complexes (35,62,67,68).”
Quote in the paperSubstantial claim0 of 3 sources checked - Interpretationreasoning
Nup93 acts as an architectural organizer within, but not across spokes.
“Thus, Nup93 acts as an architectural organizer within, but not across spokes.”
Quote in the paperSubstantial claim - Interpretationcitation
Intricate structures such as the NPC can now be modeled thanks to in situ and in cellulo cryo-ET and powerful AI-based prediction.
“Thanks to in situ and in cellulo cryo-ET and powerful AI-based prediction (27,28), intricate structures such as the NPC can be now modeled.”
Quote in the paperSubstantial claim0 of 2 sources checked - Interpretationown data
The NPC scaffold keeps the pore wider than it would be without the scaffold.
“The NPC scaffold thus keeps the pore wider than it would be without the scaffold.”
Quote in the paperSubstantial claim - Premisecitation
AlphaFold and RoseTTAfold have demonstrated unprecedented accuracy in predicting structures of monomeric proteins.
“However, AlphaFold and RoseTTAfold have recently demonstrated unprecedented accuracy in predicting structures of monomeric proteins (27,28,(61)(62)(63)(64)(65)(66) and complexes (35,62,67,68).”
Quote in the paperSubstantial claim0 of 3 sources checked - Interpretationreasoning
The Nup35 dimer functions as an architectural organizer for the inner ring membrane coat in a horizontal direction along the membrane plane.
“It strongly suggests that the Nup35 dimer, which is critical during early NPC biogenesis (39), functions as an architectural organizer for the IR membrane coat in a horizontal direction along the membrane plane.”
Quote in the paperSubstantial claim - Interpretationreasoning
The core of the transmembrane interaction hub is formed by Aladin-NDC1 heterodimer at the interface between the outer and inner rings.
“We propose that its core is formed by Aladin-NDC1 heterodimer at the interface between the outer and inner rings.”
Quote in the paperSubstantial claim - Interpretationreasoning
The stoichiometric assembly of the Nup62 subcomplex together with Nup205/188-Nup93 heterodimer is likely pre-assembled away from sites of NPC biogenesis.
“Thus, the stoichiometric assembly of the Nup62 subcomplex together with Nup205/188-Nup93 heterodimer is likely pre-assembled away from sites of NPC biogenesis, explaining the importance of the linker for intra-subcomplex interactions.”
Quote in the paperSubstantial claim - Interpretationown data
Experimental structure determination will still be required in the future for cases in which a priori knowledge remains sparse.
“emphasizing that experimental structure determination will still be required in the future for cases in which a priori knowledge remains sparse.”
Quote in the paperNot a substantial claim - Interpretationreasoning
The connections of Nup93 within individual IR complexes and to the Nup214-complex suggest a role in ensuring isostoichiometric assembly.
“The connections of Nup93 within individual IR complexes and to the Nup214-complex suggest a role in ensuring isostoichiometric assembly.”
Quote in the paperSubstantial claim - Premisecitation
Some species maintain the fusion topology in the absence of NPCs, e.g. during semi-closed mitosis in Drosophila melanogaster.
“Indeed, some species maintain the fusion topology in the absence of NPCs, e.g. during semi-closed mitosis in Drosophila melanogaster (59).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [59] source
Not checked in the free run.
- Study design and conductown data
The authors successfully validated their models by comparing them to unpublished crystal structures, their cryo-EM maps, and biochemical data.
“Indeed, we could successfully validate our models by comparing them to unpublished crystal structures, our cryo-EM maps, and biochemical data.”
Quote in the paperSubstantial claim - Premisecitation
Ultrastructural analysis of post-mitotic NPC assembly has revealed that NE holes are formed at small diameters and dilate once NPC subcomplexes are recruited.
“This notion agrees with the ultrastructural analysis of post-mitotic NPC assembly, which has revealed that NE holes are formed at small diameters and dilate once NPC subcomplexes are recruited (60).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [60] source
Not checked in the free run.
- Interpretationown data
The tightening of the NPC scaffold is primarily due to mechanical tension in the pore widened beyond the catenoid shape.
“We attribute this tightening primarily to mechanical tension in the pore widened beyond the catenoid shape.”
Quote in the paperSubstantial claim - Premisecitation
AlphaFold and RoseTTAfold accurately assess their confidence at the level of individual residues and interdomain contacts.
“The programs were also shown to accurately assess their confidence at the level of individual residues and interdomain contacts (27,28,62).”
Quote in the paperSubstantial claim0 of 3 sources checked - Interpretationreasoning
In the IR membrane coat, multiple interactions converge into a transmembrane interaction hub.
“In the IR membrane coat, multiple interactions converge into an intriguing transmembrane interaction hub.”
Quote in the paperSubstantial claim - Interpretationreasoning
The transmembrane interaction hub is likely a spatial organizer for two proximate copies of Nup155 within the same spoke that point towards the outer rings and IR, respectively.
“This transmembrane interaction hub is likely a spatial organizer for two proximate copies of Nup155 within the same spoke that point towards the outer rings and IR, respectively.”
Quote in the paperSubstantial claim - Premisecitation
Nup35 associates with Nup155 early during NPC assembly.
“Since Nup35 associates with Nup155 early during NPC assembly (39), its dimerizing domain appears critical to scaffold its flexible linkers towards neighboring spokes within IR membrane coat.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [39] source
Not checked in the free run.
- Interpretationreasoning
The central position of Aladin within the NPC might explain functional consequences of mutations in the Aladin/AAAS that are implicated in the AAA syndrome.
“The central position of Aladin within the NPC might explain functional consequences of mutations in the Aladin/AAAS that are implicated in the AAA syndrome (46-48) and is consistent with the absence of Aladin in fungi, which lack the Nup155 connectors (25).”
Quote in the paperNot a substantial claim - Interpretationreasoning
The entire EM density for those peripheral Nups is unlikely to be resolved in the near future due to their flexibility.
“Although the entire EM density for those peripheral Nups is unlikely to be resolved in the near future due to their flexibility”
Quote in the paperSubstantial claim
- May combine two claims. 25
- Classified as probably not a substantial claim. 4
May combine two claims.
Findingown dataWithin the inner ring, Nup188 localizes to the outer sub-complexes, while Nup205 localizes to the inner sub-complexes.
“Within the IR, Nup188 localizes to the outer, while Nup205 localizes to the inner sub-complexes, consistent with previous analysis in other species (12,22,23).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe paper reports a near-complete structural model of the human NPC scaffold (>90% of scaffold) with explicit membrane and in multiple conformational states (constricted and dilated).
“Here, we report a near-complete structural model of the human NPC scaffold with explicit membrane and in multiple conformational states.”
- Also stated in: § ! Introduction · plain
“we have combined cryo-electron tomography (cryo-ET) analysis of the human NPC from isolated NEs and within intact cells with artificial intelligence (AI)-based structural prediction to infer a model of >90% of the human NPC scaffold at unprecedented precision and in multiple conformations.”
- Also stated in: § Discussion and conclusions · plain
“We have built a near-complete model of the human NPC scaffold in the constricted state (smaller diameter) as adopted in purified nuclear envelopes and in the dilated state as adopted in cells”
Quote in the paperSubstantial claim- Also stated in: § ! Introduction · plain
May combine two claims.
FindingcitationTwo copies of Nup205 localize in the cytoplasmic ring and one in the nuclear ring.
“We furthermore localized two copies of Nup205 in the CR and one in the NR (29), thus resolving previous ambiguities (11,19,21).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe model of the Gp210 ring matches the luminal density visible in the in cellulo EM map, allowing modeling of the ring in both constricted and dilated NPC.
“The model of the Gp210 ring also matches the luminal density visible in our in cellulo EM map, allowing us to model the ring in the context of both constricted and dilated NPC (Fig. 1, Fig. S13).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataApplying lateral tension on the double membrane could maintain the pore width or widen it.
“Second, by applying lateral tension on the double membrane, we could maintain the pore width or widen it (Fig. 4B, Fig. S15B).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataIn the model, the Nup35 dimer is positioned into previously unassigned EM density between spokes, and each of the two copies reaches out with its SLiMs to Nup155 and Nup93 of the adjacent spokes.
“In our model, the Nup35 dimer is positioned into previously unassigned EM density between spokes, and each of the two copies reaches out with its SLiMs to Nup155 and Nup93 of the adjacent spokes (Fig. 2A).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe C-terminal transmembrane helix of Gp210 is long enough to span the NE and reaches the IR in the vicinity of the NDC1/Aladin/Nup155/Nup35 transmembrane interaction hub.
“This helix is long enough to span the NE and reaches the IR in the vicinity of the NDC1/Aladin/Nup155/Nup35 transmembrane interaction hub.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe model accounts for 70 MDa of the molecular weight of the NPC (>90% of the scaffold molecular weight), compared to 16 Nups and 35 MDa (46% of the scaffold) of the previous model.
“Figure: include 25 out of ~30 Nups, and account for 70 MDa of the molecular weight of the NPC (>90% of the scaffold molecular weight) in comparison to 16 Nups and 35 MDa (46% of the scaffold) of the previous model, and largely account for the EM density observed in the constricted and dilated states.”
Quote in the paperSubstantial claim- Rests on an assumption: The previous model of the human NPC scaffold included 16 Nups and accounted for 35 MDa (46% of the scaffold molecular weight).
May combine two claims.
Findingown dataAlphaFold/Colabfold models of NDC1 and Aladin as monomers and as a heterodimeric complex have high-confidence scores.
“Using AlphaFold/Colabfold, we could model the structures both as monomers and a heterodimeric complex with high-confidence scores (Fig. S5, Fig. S9).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe two locations are C2-symmetrically equivalent across the nuclear envelope plane, assigning two copies of Aladin and NDC1 per spoke.
“The two locations are C2-symmetrically equivalent across the nuclear envelope plane, thus assigning two copies of Aladin and NDC1 per spoke, corroborating experimentally determined stoichiometry (43).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataTheir relative arrangement is not changing uniformly during dilation; rather, the relative distances within the spokes remain constant while the spacing of the spokes increases.
“Their relative arrangement is not changing uniformly during dilation, rather the relative distances within the spokes remain constant while the spacing of the spokes increases (Fig. 3).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe model includes multiple previously unassigned domains and proteins, resolves long-standing ambiguities in alternative Nup assignments, lays out a connectivity map of the protein linkers across the NPC scaffold, maps out the membrane-anchoring motifs, and provides a high-quality basis for further investigations of NPC dynamics and function.
“Our model includes multiple previously unassigned domains and proteins, resolves long-standing ambiguities in alternative Nup assignments, lays out a connectivity map of the protein linkers across the NPC scaffold, maps out the membrane-anchoring motifs, and provides a high-quality basis for further investigations of NPC dynamics and function.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe AI-based models correctly recapitulated SLiM interactions known from X-ray structures but also revealed previously unknown additional human Nup-SLiM interactions.
“The AI-based models correctly recapitulated SLiM interactions known from X-ray structures but also revealed previously unknown additional human Nup-SLiM interactions.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe membrane fusion topology per se is stable under certain conditions, relaxing toward a catenoid shape with zero membrane bending energy.
“Our simulations suggest that the membrane fusion topology per se is stable under certain conditions, relaxing toward a catenoid shape with zero membrane bending energy.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe NDC1/Aladin/Nup155/Nup35 membrane-binding hub is situated at the interface of the inner ring with the outer rings and is distinct from the additional Nup155 pair at the NE symmetry plane.
“The NDC1/Aladin/Nup155/Nup35 membrane-binding hub is situated at the interface of the IR with the outer rings and is distinct from the additional Nup155 pair at the NE symmetry plane.”
Quote in the paperSubstantial claimMay combine two claims.
FindingreasoningIn comparison to the X-ray structures, the AI-based models more extensively covered the structured domains, thus reducing the length of the linkers connecting between the anchor points and restricting their possible conformational freedom within our model.
“In comparison to the X-ray structures, the AI-based models more extensively covered the structured domains, thus reducing the length of the linkers connecting between the anchor points and restricting their possible conformational freedom within our model.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe linkers at the N-terminus of Nup93 copies that connect anchor points at Nup205 or Nup188, and Nup62 complex in the inner ring, cannot reach across spokes in either the constricted or the dilated state, and thus connect subunits within a single inner ring sub-complex inside the same spoke.
“In contrast, the connectivity map demonstrates that the linkers at the N-terminus of Nup93 copies that connect anchor points at Nup205 or Nup188, and Nup62 complex in the IR, cannot reach across spokes in either the constricted or the dilated state, and thus connect subunits within a single IR sub-complex inside the same spoke.”
Quote in the paperSubstantial claimMay combine two claims.
Findingnone givenThe resulting model of the NPC scaffold is almost complete and exhibits near-atomic level precision at several interfaces.
“resulting model of the NPC scaffold is almost complete and exhibits near-atomic level precision at several interfaces.”
Quote in the paperSubstantial claimMay combine two claims.
Interpretationown dataMicrosecond-long MD simulations suggest that the scaffold is not required to stabilize the inner and outer nuclear membrane fusion, but rather widens the central pore.
“Microsecond-long molecular dynamics simulations suggest that the scaffold is not required to stabilize the inner and outer nuclear membrane fusion, but rather widens the central pore.”
- Also stated in: § The NPC scaffold prevents membrane constriction in the absence of membrane tension · plain
“Taken together, our data support a model in which the role of the NPC scaffold is not to stabilize the membrane fusion per se, but rather to widen the diameter of the membrane hole without necessitating a wider envelope.”
- Also stated in: § Discussion and conclusions · hedged
“Our analysis instead suggests that NPCs stabilize a pore that is wider than in the relaxed, tensionless double membrane hole.”
Quote in the paperSubstantial claim- Also stated in: § The NPC scaffold prevents membrane constriction in the absence of membrane tension · plain
May combine two claims.
Interpretationown dataThe NPC scaffold in the gp210-deleted map appears overall unchanged, including its diameter, suggesting Gp210 is not required for faithful NPC assembly.
“The NPC scaffold in the resulting map appears overall unchanged, including its diameter, suggesting the Gp210 is not required for faithful NPC assembly.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S2 (checkable).
InterpretationreasoningEven if AI-based modeling does not yield high confidence results, the models can still serve as tools for hypothesis generation and subsequent experimental validation.
“However, even if AI-based modeling does not yield high confidence results, the models can still serve as tools for hypothesis generation and subsequent experimental validation.”
Quote in the paperNot a substantial claimMay combine two claims.
PremisecitationAladin is absent in fungi, which lack the Nup155 connectors.
“and is consistent with the absence of Aladin in fungi, which lack the Nup155 connectors (25).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [25]
Not checked in the free run.
May combine two claims.
InterpretationreasoningThe hub also binds Nup35, which connects to Nup155 copies of neighboring spokes, facilitating horizontal, cylindrical oligomerization.
“The hub also binds Nup35, which connects to Nup155 copies of neighboring spokes, thus facilitating the horizontal, cylindrical oligomerization.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationRecent work in fungi has identified constricted NPCs inside of cells under specific physiological conditions.
“whereby recent work in fungi has identified constricted NPCs inside of cells under specific physiological conditions (23).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [23]
Not checked in the free run.
May combine two claims.
InterpretationreasoningTogether with Nup155, Nup35, Aladin and NDC1 form a transmembrane interaction hub that anchors the inner membrane coat of the inner ring and orients the Nup155 connectors towards the outer rings.
“We therefore propose that together with Nup155, Nup35, Aladin and NDC1 form a transmembrane interaction hub that anchors the inner membrane coat of the IR and orients the Nup155 connectors towards the outer rings.”
Quote in the paperSubstantial claimMay combine two claims.
Interpretationown dataThe often-emphasized notion that 'NPCs fuse the INM and ONM' or that they 'stabilize the fusion of the INM and ONM' is not necessarily supported by our analysis.
“The often-emphasized notion that 'NPCs fuse the INM and ONM' or that they 'stabilize the fusion of the INM and ONM' is not necessarily supported by our analysis.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationThe Nup35 dimer is critical during early NPC biogenesis.
“It strongly suggests that the Nup35 dimer, which is critical during early NPC biogenesis (39), functions as an architectural organizer for the IR membrane coat in a horizontal direction along the membrane plane.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [39]
Not checked in the free run.
May combine two claims.
InterpretationreasoningAladin-NDC1 likely further associates with Gp210, which arches between spokes in the NE lumen.
“Aladin-NDC1 likely further associates with Gp210, which arches between spokes in the NE lumen.”
Quote in the paperNot a substantial claimClassified as probably not a substantial claim.
InterpretationcitationThe complete model of the human NPC could be in reach by integrating data from complementary techniques that can address flexible proteins, such as super-resolution microscopy, FRET, and site-specific labeling.
“the complete model of the human NPC could be in reach by integrating data from complementary techniques that can address flexible proteins, such as super-resolution microscopy, FRET, and site-specific labeling (18).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [18]
Not checked in the free run.
The paper relies on this without support.
Proximity labeling mass spectrometry with BirA-tagged Aladin reliably identifies the most prominently enriched interactors of Aladin.
“We confirmed this interaction using proximity labeling mass spectrometry with BirA-tagged Aladin and identified NDC1 and Nup35 as the most prominently enriched interactors (Fig. S12).”
The paper relies on this without support.
The X-ray structures provided by the Hoelz laboratory are accurate.
“The X-ray structures were provided to us by the Hoelz laboratory (33,34) and were not used as input for the modeling procedure.”
The paper relies on this without support.
Predicted atomic structures traditionally exhibited inaccuracies that limited their use for detailed near-atomic model building in low-resolution EM maps.
“Predicted atomic structures traditionally exhibited various inaccuracies, limiting their usage for detailed near-atomic model building in low-resolution EM maps.”
The paper relies on this without support.
The previous model of the human NPC scaffold included 16 Nups and accounted for 35 MDa (46% of the scaffold molecular weight).
“in comparison to 16 Nups and 35 MDa (46% of the scaffold) of the previous model”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Accessing accurate protein structures paves the way for an enhanced understanding of protein function, providing tools for modulating or engineering proteins.
“Accessing accurate protein structures paves the way for an enhanced understanding of protein function, providing researchers with the tools necessary for modulating these proteins or engineering new ones (8–10).”
From AlphaFold Protein Structure Database in 2024: providing structure coverage for over 214 million protein sequences (2024) · cites this paper as [9]
The Introduction and Discussion and conclusions (page not specified in our copy) show that accurate structural models reveal functions of nuclear-pore proteins and enable further analyses. They do not say that the models provide tools for modulating proteins or engineering new ones. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Inner-ring diameters are smaller than the channel they surround
MinorThe stated inner-ring diameters of 42 Å and 54 Å are 4.2 and 5.4 nm, respectively. Neither can surround the paper's stated 40-50 nm-wide transport channel; the diameter units appear inconsistent.
“The dilated, in cellulo NPC exhibits the IR diameter of 54 Å in comparison to 42 Å in the constricted state”
“Each ring comprises eight spokes that surround a 40 to 50 nm-wide transport channel (5,6).”
Cites
Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482 · see citing works
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952 · see citing works
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Molecular dynamics with coupling to an external bath
Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 30,626 · see citing works
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
Abraham, M. J., Murtola, T., Schulz, R., Páll, S., Smith, J. C., Hess, B., & Lindahl, E. (2015) · SoftwareX · doi:10.1016/j.softx.2015.06.001 · Cited by 27,190 · see citing works
Polymorphic transitions in single crystals: A new molecular dynamics method
Parrinello, M., & Rahman, A. (1981) · Journal of Applied Physics · doi:10.1063/1.328693 · Cited by 19,668 · see citing works
Canonical sampling through velocity rescaling
Bussi, G., Donadio, D., & Parrinello, M. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2408420 · Cited by 18,034 · see citing works
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320 · see citing works
Overview of the <i>CCP</i> 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353 · see citing works
Inference of macromolecular assemblies from crystalline state.
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,189 · see citing works
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works
Accurate prediction of protein structures and interactions using a 3-track network
Baek, M., DiMaio, F., Anishchenko, I., Dauparas, J., Ovchinnikov, S., Lee, G. R., Wang, J., Cong, Q., Kinch, L. N., Schaeffer, R. D., et al. (2021) · doi:10.1101/2021.06.14.448402 · Cited by 5,542 · see citing works
The MARTINI Force Field: Coarse Grained Model for Biomolecular Simulations
Marrink, . J., Risselada, H. J., Yefimov, S., Tieleman, D. P., & de Vries, A. H. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp071097f · Cited by 5,527 · see citing works
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446 · see citing works
UCSF ChimeraX: Meeting modern challenges in visualization and analysis
Goddard, T. D., Huang, C. C., Meng, E. C., Pettersen, E. F., Couch, G. S., Morris, J. H., & Ferrin, T. E. (2018) · Protein Science · doi:10.1002/pro.3235 · Cited by 5,267 · see citing works
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,926 · see citing works
MDAnalysis: A toolkit for the analysis of molecular dynamics simulations
Michaud‐Agrawal, N., Denning, E. J., Woolf, T. B., & Beckstein, O. (2011) · Journal of Computational Chemistry · doi:10.1002/jcc.21787 · Cited by 4,549 · see citing works
Comparative Protein Structure Modeling Using MODELLER
Webb, B., & Šali, A. (2016) · Current Protocols in Bioinformatics · doi:10.1002/cpbi.3 · Cited by 4,349 · see citing works
The PSIPRED protein structure prediction server
McGuffin, L. J., Bryson, K., & Jones, D. T. (2000) · Bioinformatics · doi:10.1093/bioinformatics/16.4.404 · Cited by 3,841 · see citing works
Protein complex prediction with AlphaFold-Multimer
Evans, R., O’Neill, M., Pritzel, A., Antropova, N., Senior, A., Green, T., Žídek, A., Bates, R., Blackwell, S., Yim, J., et al. (2021) · doi:10.1101/2021.10.04.463034 · Cited by 3,808 · see citing works
TM-align: a protein structure alignment algorithm based on the TM-score
Zhang, Y. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki524 · Cited by 3,774 · see citing works
Real-space refinement in PHENIX for cryo-EM and crystallography
Afonine, P., Poon, B., Read, R. J., Sobolev, O., Terwilliger, T., Urzhumtsev, A., & Adams, P. (2018) · bioRxiv · doi:10.1107/s2059798318006551 · Cited by 3,057 · see citing works
Highly accurate protein structure prediction for the human proteome
Tunyasuvunakool, K., Adler, J., Wu, Z., Green, T., Zielinski, M., Žídek, A., Bridgland, A., Cowie, A., Meyer, C., Laydon, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03828-1 · Cited by 3,025 · cited 3× · see citing works
“The structures of all individual NUPs and selected subcomplexes were modeled using AlphaFold (26) or downloaded from AlphaFold Database (60).”
MethodThe MARTINI Coarse-Grained Force Field: Extension to Proteins
Monticelli, L., Kandasamy, S. K., Périole, X., Larson, R. G., Tieleman, D. P., & Marrink, . J. (2008) · Journal of Chemical Theory and Computation · doi:10.1021/ct700324x · Cited by 2,491 · see citing works
Transport Between the Cell Nucleus and the Cytoplasm
Görlich, D., & Kutay, U. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.607 · Cited by 2,025 · see citing works
Croll, T. (2018) · Acta Crystallographica Section D: Structural Biology · doi:10.1107/s2059798318002425 · Cited by 1,934 · see citing works
No evidence that carotenoid pigments boost either immune or antioxidant defenses in a songbird
Koch, R. E., Kavazis, A. N., Hasselquist, D., Hood, W. R., Zhang, Y., Toomey, M. B., & Hill, G. E. (2018) · Nature Communications · doi:10.1038/s41467-018-02974-x · Cited by 1,924 · see citing works
Wassenaar, T. A., Ingólfsson, H. I., Böckmann, R. A., Tieleman, D. P., & Marrink, S. J. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00209 · Cited by 1,174 · see citing works
Mariani, V., Biasini, M., Barbato, A., & Schwede, T. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt473 · Cited by 1,138 · see citing works
Improved prediction of protein-protein interactions using AlphaFold2
Bryant, P., Pozzati, G., & Elofsson, A. (2021) · doi:10.1101/2021.09.15.460468 · Cited by 1,025 · see citing works
Hagen, W. J. H., Wan, W., & Briggs, J. A. G. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.06.007 · Cited by 812 · see citing works
Self-citationAutomated tilt series alignment and tomographic reconstruction in IMOD
Mastronarde, D. N., & Held, S. R. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.07.011 · Cited by 790 · see citing works
fdrtool: a versatile R package for estimating local and tail area-based false discovery rates
Strimmer, K. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn209 · Cited by 723 · see citing works
Detecting Rhythms in Time Series with RAIN
Thaben, P. F., & Westermark, P. O. (2014) · Journal of Biological Rhythms · doi:10.1177/0748730414553029 · Cited by 709 · see citing works
Périole, X., Cavalli, M., Marrink, . J., & Ceruso, M. A. (2009) · Journal of Chemical Theory and Computation · doi:10.1021/ct9002114 · Cited by 703 · see citing works
The nuclear pore complex: understanding its function through structural insight
Beck, M., & Hurt, E. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.147 · Cited by 680 · see citing works
Self-citationA structural biology community assessment of AlphaFold2 applications
Akdel, M., Pires, D. E. V., Pardo, E. P., Jänes, J., Zalevsky, A. O., Mészáros, B., Bryant, P., Good, L. L., Laskowski, R. A., Pozzati, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00849-w · Cited by 675 · see citing works
Pupko, T., Bell, R. E., Mayrose, I., Glaser, F., & Ben‐Tal, N. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.suppl_1.s71 · Cited by 635 · see citing works
The nuclear pore complex: bridging nuclear transport and gene regulation
Strambio‐De‐Castillia, C., Niepel, M., & Rout, M. P. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2928 · Cited by 595 · see citing works
Visualizing the molecular sociology at the HeLa cell nuclear periphery
Mahamid, J., Pfeffer, S., Schaffer, M., Villa, E., Danev, R., Cuellar, L. K., Förster, F. G., Hyman, A. A., Plitzko, J. M., & Baumeister, W. P. (2016) · Science · doi:10.1126/science.aad8857 · Cited by 561 · see citing works
Computed structures of core eukaryotic protein complexes
Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542 · see citing works
Structures of core eukaryotic protein complexes
Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S., et al. (2021) · doi:10.1101/2021.09.30.462231 · Cited by 541 · see citing works
The Structure of the Nuclear Pore Complex
Hoelz, A., Debler, E., & Blobel, G. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060109-151030 · Cited by 525 · see citing works
Castaño‐Díez, D., Kudryashev, M., Arheit, M., & Stahlberg, H. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.12.017 · Cited by 511 · see citing works
Integrative structure and functional anatomy of a nuclear pore complex
Kim, S. J., Fernández-Martı́nez, J., Nudelman, I., Shi, Y., Zhang, W., Raveh, B., Herricks, T., Slaughter, B. D., Hogan, J. A., Upla, P., et al. (2018) · Nature · doi:10.1038/nature26003 · Cited by 469 · see citing works
Nakane, T., Kimanius, D., Lindahl, E. R., & Scheres, S. H. W. (2018) · eLife · doi:10.7554/elife.36861 · Cited by 450 · see citing works
The Structure of the Nuclear Pore Complex (An Update)
Lin, D. H., & Hoelz, A. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011901 · Cited by 449 · see citing works
In situ structural analysis of the human nuclear pore complex
von Appen, A., Kosiński, J., Sparks, L., Ori, A., DiGuilio, A. L., Vollmer, B., Mackmull, M., Banterle, N., Parca, L., Kastritis, P. L., et al. (2015) · Nature · doi:10.1038/nature15381 · Cited by 411 · see citing works
Self-citationComponents of Coated Vesicles and Nuclear Pore Complexes Share a Common Molecular Architecture
Devos, D. P., Dokudovskaya, S., Alber, F., Williams, R., Chait, B. T., Šali, A., & Rout, M. P. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020380 · Cited by 390 · see citing works
Applying and improving AlphaFold at CASP14
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26257 · Cited by 370 · see citing works
Integrated Structural Analysis of the Human Nuclear Pore Complex Scaffold
Bui, K. H., von Appen, A., DiGuilio, A. L., Ori, A., Sparks, L., Mackmull, M., Bock, T., Hagen, W. J. H., Andrés‐Pons, A., Glavy, J. S., et al. (2013) · Cell · doi:10.1016/j.cell.2013.10.055 · Cited by 351 · see citing works
Self-citationCone-shaped HIV-1 capsids are transported through intact nuclear pores
Žíla, V., Margiotta, E., Turoňová, B., Müller, T. G., Zimmerli, C. E., Mattei, S., Allegretti, M., Börner, K., Rada, J., Müller, B., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.025 · Cited by 333 · see citing works
Self-citationNuclear pores dilate and constrict in cellulo
Zimmerli, C. E., Allegretti, M., Rantos, V., Goetz, S. K., Obarska-Kosińska, A., Zagoriy, I., Halavatyi, A. A., Hummer, G., Mahamid, J., Kosiński, J., et al. (2021) · Science · doi:10.1126/science.abd9776 · Cited by 320 · see citing works
Self-citationHigh‐accuracy protein structure prediction in <scp>CASP14</scp>
Pereira, J., Simpkin, A. J., Hartmann, M. D., Rigden, D. J., Keegan, R. M., & Lupas, A. N. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26171 · Cited by 314 · see citing works
Ori, A., Banterle, N., Iskar, M., Andrés‐Pons, A., Escher, C., Bui, K. H., Sparks, L., Solis‐Mezarino, V., Rinner, O., Peer Bork, B., et al. (2013) · Molecular Systems Biology · doi:10.1038/msb.2013.4 · Cited by 308 · see citing works
Self-citationMolecular architecture of the inner ring scaffold of the human nuclear pore complex
Kosiński, J., Mosalaganti, S., von Appen, A., Teimer, R., DiGuilio, A. L., Wan, W., Bui, K. H., Hagen, W. J. H., Briggs, J. A. G., Glavy, J. S., et al. (2016) · Science · doi:10.1126/science.aaf0643 · Cited by 303 · see citing works
Self-citationAsarnow, D. E., Palovcak, E. J., & Cheng, Y. (2019) · Figshare · doi:10.5281/zenodo.3576630 · Cited by 275 · see citing works
Amlacher, S., Sarges, P., Flemming, D., van Noort, V., Kunze, R., Devos, D. P., Arumugam, M., Bork, P., & Hurt, E. (2011) · Cell · doi:10.1016/j.cell.2011.06.039 · Cited by 269 · see citing works
Architecture of the symmetric core of the nuclear pore
Lin, D. H., Stuwe, T., Schilbach, S., Rundlet, E. J., Perriches, T., Mobbs, G. W., Fan, Y., Thierbach, K., Huber, F. M., Collins, L. N., et al. (2016) · Science · doi:10.1126/science.aaf1015 · Cited by 266 · see citing works
Structure and Assembly of the Nuclear Pore Complex
Hampoelz, B., Andrés‐Pons, A., Kastritis, P. L., & Beck, M. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115308 · Cited by 261 · see citing works
Self-citationRasala, B. A., Orjalo, A. V., Shen, Z., Briggs, S. P., & Forbes, D. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608484103 · Cited by 250 · see citing works
Turoňová, B., Schur, F. K. M., Wan, W., & Briggs, J. A. G. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.07.007 · Cited by 248 · see citing works
Self-citationAsarnow, D., Palovcak, E., & Cheng, Y. (2019) · Figshare · doi:10.5281/zenodo.3576629 · Cited by 241 · see citing works
The cellular environment shapes the nuclear pore complex architecture
Schuller, A. P., Wojtynek, M., Mankus, D. V., Tatlı, M., Kronenberg‐Tenga, R., Regmi, S. G., Dip, P. V., Lytton‐Jean, A. K. R., Brignole, E. J., Dasso, M., et al. (2021) · Nature · doi:10.1038/s41586-021-03985-3 · Cited by 236 · see citing works
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
Wozniak, R. W., Bartnik, E., & Blobel, G. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.6.2083 · Cited by 228 · see citing works
Mansfeld, J., Güttinger, S., Hawryluk-Gara, L. A., Panté, N., Mall, M., Galy, V., Haselmann, U., Mühlhäusser, P., Wozniak, R. W., Mattaj, I. W., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.02.015 · Cited by 221 · see citing works
Nuclear pore proteins and the control of genome functionsPreprint
Ibarra, A., & Hetzer, M. W. (2015) · Genes & Development · doi:10.1101/gad.256495.114 · Cited by 198 · see citing works
The Human Nuclear Pore Complex as Revealed by Cryo-Electron Tomography
Maimon, T., Elad, N., Dahan, I., & Medalia, O. (2012) · Structure · doi:10.1016/j.str.2012.03.025 · Cited by 196 · see citing works
Simulation of FUS Protein Condensates with an Adapted Coarse-Grained Model
Benayad, Z., von Bülow, S., Stelzl, L., & Hummer, G. (2020) · bioRxiv · doi:10.1021/acs.jctc.0c01064 · Cited by 189 · see citing works
Self-citationIn-cell architecture of the nuclear pore and snapshots of its turnover
Allegretti, M., Zimmerli, C. E., Rantos, V., Wilfling, F., Ronchi, P., Fung, H. K. H., Lee, C., Hagen, W. J. H., Turoňová, B., Karius, K., et al. (2020) · Nature · doi:10.1038/s41586-020-2670-5 · Cited by 181 · see citing works
Self-citationExcessive aggregation of membrane proteins in the Martini model
Javanainen, M., Martinez‐Seara, H., & Vattulainen, I. (2017) · PLoS ONE · doi:10.1371/journal.pone.0187936 · Cited by 179 · see citing works
Mukherjee, S., & Zhang, Y. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp318 · Cited by 178 · see citing works
Gall, J. G. (1967) · The Journal of Cell Biology · doi:10.1083/jcb.32.2.391 · Cited by 176 · see citing works
The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome
Cronshaw, J. M., & Matunis, M. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031047100 · Cited by 173 · see citing works
Structure and Assembly of the Nup84p Complex
Siniossoglou, S., Lutzmann, M., Santos-Rosa, H., Leonard, K., Mueller, S., Aebi, U., & Hurt, E. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.1.41 · Cited by 168 · see citing works
Architecture of the cytoplasmic face of the nuclear pore
Bley, C. J., Nie, S., Mobbs, G. W., Petrovic, S., Gres, A. T., Liu, X., Mukherjee, S., Harvey, S. C., Huber, F. M., Lin, D. H., et al. (2022) · Science · doi:10.1126/science.abm9129 · Cited by 158 · see citing works
Stafstrom, J. P., & Staehelin, L. A. (1984) · PubMed · Cited by 156 · see citing works
Grandi, P., Dang, T., Pané, N., Shevchenko, A., Mann, M., Forbes, D. J., & Hurt, E. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.10.2017 · Cited by 155 · see citing works
Vollmer, B., Lorenz, M., Moreno-Andrés, D., Bodenhöfer, M., Magistris, P. D., Astrinidis, S. A., Schooley, A., Floetenmeyer, M., Leptihn, S., & Antonin, W. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.04.027 · Cited by 142 · see citing works
Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance
Onischenko, E. A., Stanton, L. H., Madrid, A. S., Kieselbach, T., & Weis, K. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810030 · Cited by 142 · see citing works
In situ architecture of the algal nuclear pore complex
Mosalaganti, S., Kosiński, J., Albert, S., Schaffer, M., Strenkert, D., Salomé, P. A., Merchant, S., Plitzko, J. M., Baumeister, W. P., Engel, B. D., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04739-y · Cited by 140 · see citing works
Self-citationThe Dynamic Nature of the Nuclear Envelope
Magistris, P. D., & Antonin, W. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.073 · Cited by 134 · see citing works
Architecture of the fungal nuclear pore inner ring complex
Stuwe, T., Bley, C. J., Thierbach, K., Petrovic, S., Schilbach, S., Mayo, D. J., Perriches, T., Rundlet, E. J., Jeon, Y. E., Collins, L. N., et al. (2015) · Science · doi:10.1126/science.aac9176 · Cited by 130 · see citing works
Nuclear pore complexes and regulation of gene expression
Raı́ces, M., & D’Angelo, M. A. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.12.006 · Cited by 127 · see citing works
A Fence-like Coat for the Nuclear Pore Membrane
Debler, E., Ma, Y., Seo, H., Hsia, K., Noriega, T. R., Blobel, G., & Hoelz, A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.12.001 · Cited by 122 · see citing works
A structural biology community assessment of AlphaFold 2 applications
Akdel, M., Pires, D. E. V., Porta Pardo, E., Jänes, J., Zalevsky, A. O., Mészáros, B., Bryant, P., Good, L. L., Laskowski, R. A., Pozzati, G., et al. (2021) · doi:10.1101/2021.09.26.461876 · Cited by 122 · see citing works
Interactome Mapping Reveals the Evolutionary History of the Nuclear Pore Complex
Obado, S. O., Brillantes, M., Uryu, K., Zhang, W., Ketaren, N. E., Chait, B. T., Field, M. C., & Rout, M. P. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002365 · Cited by 115 · see citing works
Architecture of the linker-scaffold in the nuclear pore
Petrovic, S., Samanta, D., Perriches, T., Bley, C. J., Thierbach, K., Brown, B., Nie, S., Mobbs, G. W., Stevens, T. A., Liu, X., et al. (2022) · Science · doi:10.1126/science.abm9798 · Cited by 114 · see citing works
Landscape of nuclear transport receptor cargo specificity
Mackmull, M., Klaus, B., Heinze, I., Chokkalingam, M., Beyer, A., Russell, R. B., Ori, A., & Beck, M. (2017) · Molecular Systems Biology · doi:10.15252/msb.20177608 · Cited by 108 · see citing works
Self-citationDimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly
Vollmer, B., Schooley, A., Sachdev, R., Eisenhardt, N., Schneider, A. M., Sieverding, C., Madlung, J., Gerken, U., Macek, B., & Antonin, W. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.256 · Cited by 104 · see citing works
Integrative structure modeling with the Integrative Modeling Platform
Webb, B., Viswanath, S., Bonomi, M., Pellarin, R., Greenberg, C. H., Saltzberg, D. J., & Šali, A. (2017) · Protein Science · doi:10.1002/pro.3311 · Cited by 104 · see citing works
Linker Nups connect the nuclear pore complex inner ring with the outer ring and transport channel
Fischer, J., Teimer, R., Amlacher, S., Kunze, R., & Hurt, E. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3084 · Cited by 103 · see citing works
Atomic Structure of the Y-Complex of the Nuclear Pore
Kelley, K., Knockenhauer, K., Kabachinski, G., & Schwartz, T. (2015) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.2998 · Cited by 99 · see citing works
iAlign: a method for the structural comparison of protein–protein interfaces
Gao, M., & Skolnick, J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq404 · Cited by 98 · see citing works
Postmitotic nuclear pore assembly proceeds by radial dilation of small membrane openings
Otsuka, S., Steyer, A. M., Schorb, M., Hériché, J.-K., Hossain, M. J., Sethi, S., Kueblbeck, M., Schwab, Y., Beck, M., & Ellenberg, J. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0001-9 · Cited by 90 · see citing works
Self-citationThe Multiple Faces of Disordered Nucleoporins
Lemke, E. A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.01.002 · Cited by 86 · see citing works
Structural Basis of the Nic96 Subcomplex Organization in the Nuclear Pore Channel
Schrader, N., Stelter, P., Flemming, D., Kunze, R., Hurt, E., & Vetter, I. R. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.10.022 · Cited by 83 · see citing works
Molecular architecture of the Nup84–Nup145C–Sec13 edge element in the nuclear pore complex lattice
Brohawn, S. G., & Schwartz, T. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1713 · Cited by 82 · see citing works
Architecture of the yeast Elongator complex
Daudén, M. I., Kosiński, J., Kolaj‐Robin, O., Desfosses, A., Ori, A., Faux, C., Hoffmann, N. A., Onuma, O. F., Breunig, K. D., Beck, M., et al. (2016) · EMBO Reports · doi:10.15252/embr.201643353 · Cited by 80 · see citing works
Self-citationOn wakefulness fluctuations as a source of BOLD functional connectivity dynamics
Haimovici, A., Tagliazucchi, E., Balenzuela, P., & Laufs, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-06389-4 · Cited by 80 · see citing works
Structural and functional analysis of mRNA export regulation by the nuclear pore complex
Lin, D. H., Correia, A. R., Cai, S. W., Huber, F. M., Jette, C. A., & Hoelz, A. (2018) · Nature Communications · doi:10.1038/s41467-018-04459-3 · Cited by 76 · see citing works
The Triple A Syndrome Is Due to Mutations in ALADIN, a Novel Member of the Nuclear Pore Complex
Huebner, A., Kaindl, A. M., Knobeloch, K., Petzold, H. A., Mann, P., & Koehler, K. (2004) · Endocrine Research · doi:10.1081/erc-200044138 · Cited by 73 · see citing works
Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex
Bilokapić, S., & Schwartz, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205151109 · Cited by 72 · see citing works
Nup53 interaction with Ndc1 and Nup155 are required for nuclear pore complex assembly
Eisenhardt, N., Redolfi, J., & Antonin, W. (2013) · Journal of Cell Science · doi:10.1242/jcs.141739 · Cited by 69 · see citing works
Molecular dynamics simulations of carbon nanotube porins in lipid bilayers
Vögele, M., Köfinger, J., & Hummer, G. (2018) · Faraday Discussions · doi:10.1039/c8fd00011e · Cited by 68 · see citing works
Self-citationMolecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex
Zhang, Y., Li, S., Zeng, C., Huang, G., Zhu, X., Wang, Q., Wang, K., Zhou, Q., Yan, C., Zhang, W., et al. (2020) · Cell Research · doi:10.1038/s41422-020-0320-y · Cited by 64 · see citing works
Fifty Years of Nuclear Pores and Nucleocytoplasmic Transport Studies
Floch, A. G., Palancade, B., & Doye, V. (2014) · Methods in cell biology · doi:10.1016/b978-0-12-417160-2.00001-1 · Cited by 59 · see citing works
BUMPy: A Model-Independent Tool for Constructing Lipid Bilayers of Varying Curvature and Composition
Boyd, K. J., & May, E. R. (2018) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.8b00765 · Cited by 59 · see citing works
Structure of a trimeric nucleoporin complex reveals alternate oligomerization states
Nagy, V. Á., Hsia, K., Debler, E., Kampmann, M., Davenport, A. M., Blobel, G., & Hoelz, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909373106 · Cited by 58 · see citing works
Huang, G., Zhang, Y., Zhu, X., Zeng, C., Wang, Q., Zhou, Q., Tao, Q., Liu, M., Lei, J., Yan, C., et al. (2020) · Cell Research · doi:10.1038/s41422-020-0319-4 · Cited by 57 · see citing works
Integrative structural modeling of macromolecular complexes using Assembline
Rantos, V., Karius, K., & Kosiński, J. (2021) · Nature Protocols · doi:10.1038/s41596-021-00640-z · Cited by 57 · see citing works
Yoshida, K., Seo, H., Debler, E., Blobel, G., & Hoelz, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112846108 · Cited by 56 · see citing works
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex
Upla, P., Kim, S. J., Sampathkumar, P., Dutta, K., Cahill, S. M., Chemmama, I. E., Williams, R., Bonanno, J. B., Rice, W. J., Stokes, D. L., et al. (2017) · Structure · doi:10.1016/j.str.2017.01.006 · Cited by 55 · see citing works
The flexibility and dynamics of the tubules in the endoplasmic reticulum
Georgiades, P., Allan, V., Wright, G. D., Woodman, P. G., Udommai, P., Chung, M. A., & Waigh, T. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-16570-4 · Cited by 55 · see citing works
Integrative Structural Biology in the Era of Accurate Structure Prediction
Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53 · see citing works
Co-translational assembly orchestrates competing biogenesis pathways
Seidel, M., Becker, A., Pereira, F. M., Landry, J. J. M., de Azevedo, N. T. D., Fusco, C. M., Kaindl, E., Romanov, N., Baumbach, J., Langer, J. D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28878-5 · Cited by 52 · see citing works
Self-citationKind, B., Koehler, K., Lorenz, M., & Huebner, A. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.09.080 · Cited by 48 · see citing works
Carbon Nanotubes Mediate Fusion of Lipid Vesicles
Bhaskara, R. M., Linker, S. M., Vögele, M., Köfinger, J., & Hummer, G. (2017) · ACS Nano · doi:10.1021/acsnano.6b05434 · Cited by 45 · see citing works
Self-citationKosova, B., Panté, N., Rollenhagen, C., & Hurt, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22646 · Cited by 43 · see citing works
Modeling Biological Complexes Using Integrative Modeling Platform
Saltzberg, D. J., Greenberg, C. H., Viswanath, S., Chemmama, I. E., Webb, B., Pellarin, R., Echeverria, I., & Šali, A. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9608-7_15 · Cited by 39 · see citing works
Membrane-Elasticity Model of Coatless Vesicle Budding Induced by ESCRT Complexes
Różycki, B., Bouřa, E., Hurley, J. H., & Hummer, G. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002736 · Cited by 38 · see citing works
Self-citationAssessment of protein–protein interfaces in cryo-EM derived assemblies
Malhotra, S., Joseph, A. P., Thiyagalingam, J., & Topf, M. (2021) · Nature Communications · doi:10.1038/s41467-021-23692-x · Cited by 37 · see citing works
Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex
Huang, G., Zhan, X., Zeng, C., Zhu, X., Liang, K., Zhao, Y., Wang, P., Wang, Q., Zhou, Q., Tao, Q., et al. (2022) · Cell Research · doi:10.1038/s41422-021-00610-w · Cited by 36 · see citing works
On the Octagonal Structure of the Nuclear Pore Complex: Insights from Coarse-Grained Models
Wolf, C. B., & Mofrad, M. R. K. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.130336 · Cited by 35 · see citing works
The transmembrane nucleoporin NDC1 is required for targeting of ALADIN to nuclear pore complexes
Yamazumi, Y., Kamiya, A., Nishida, A., Nishihara, A., Iemura, S.-I., Natsume, T., & Akiyama, T. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.096 · Cited by 34 · see citing works
Tai, L., Zhu, Y., Ren, H., Huang, X., Zhang, C., & Sun, F. (2022) · Protein & Cell · doi:10.1007/s13238-021-00895-y · Cited by 32 · see citing works
Cho, A., Yang, K., Bae, Y., Bahk, Y. Y., Kim, E., Lee, H., Kim, J. K., Park, W.-S., Rhim, H., Choi, S. Y., et al. (2009) · Experimental & Molecular Medicine · doi:10.3858/emm.2009.41.6.043 · Cited by 31 · see citing works
Magistris, P. D., Tatarek‐Nossol, M., Dewor, M., & Antonin, W. (2018) · Journal of Cell Science · doi:10.1242/jcs.208538 · Cited by 29 · see citing works
Structural evolution of the membrane-coating module of the nuclear pore complex
Liu, X., Mitchell, J. M., Wozniak, R. W., Blobel, G., & Fan, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214557109 · Cited by 23 · see citing works
Beck, M., Mosalaganti, S., & Kosiński, J. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.07.012 · Cited by 22 · see citing works
Self-citationInteraction of Nup53 with Ndc1 and Nup155 is required for nuclear pore complex assembly
Eisenhardt, N., Redolfi, J., & Antonin, W. (2014) · Max Planck Institute for Plasma Physics · Cited by 19 · see citing works
Assessing the accuracy of contact and distance predictions in CASP14
Ruiz-Serra, V., Pontes, C., Milanetti, E., Kryshtafovych, A., Lepore, R., & Valencia, A. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26248 · Cited by 13 · see citing works
turonova/novaSTA: Advanced particle analysis
Turonova (2020) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.3973622 · Cited by 9 · see citing works
Co-translational assembly counteracts promiscuous interactionsPreprint
Seidel, M., Becker, A., Pereira, F. M., Landry, J. J. M., de Azevedo, N. T. D., Fusco, C. M., Kaindl, E., Baumbach, J., Langer, J. D., Schuman, E. M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.13.452229 · Cited by 4 · see citing works
Self-citationSpatial proteomics: from tissue organization to protein function
Buczak, K. (2019) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00025909 · Cited by 1 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Accurate structure prediction of biomolecular interactions with AlphaFold 3
Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861 · see citing works
“Accurate models of biological complexes are critical to our understanding of cellular functions and for the rational design of therapeutics 2–4 , 9 .”
BackgroundColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works
Varadi, M., Bertoni, D., Magana, P., Paramval, U., Pidruchna, I., Radhakrishnan, M., Tsenkov, M., Nair, S., Mirdita, M., Yeo, J., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkad1011 · Cited by 2,052 · see citing works
Tian, H., Zhao, L., Yunfang, L., & Wei, W. (2023) · Technological Forecasting and Social Change · doi:10.1016/j.techfore.2023.122732 · Cited by 265 · see citing works
Protein structure predictions to atomic accuracy with AlphaFold
Jumper, J., & Hassabis, D. (2022) · Nature Methods · doi:10.1038/s41592-021-01362-6 · Cited by 265 · see citing works
Bridging structural and cell biology with cryo-electron microscopy
Nogales, E., & Mahamid, J. (2024) · Nature · doi:10.1038/s41586-024-07198-2 · Cited by 207 · see citing works
Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold
Fontana, P., Dong, Y., Pi, X., Tong, A. B., Hecksel, C. W., Wang, L., Fu, T.-M., Bustamante, C., & Wu, H. (2022) · Science · doi:10.1126/science.abm9326 · Cited by 195 · see citing works
Nuclear transport proteins: structure, function and disease relevance
Yang, Y., Guo, L., Chen, L., Gong, B., Jia, D., & Sun, Q. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01649-4 · Cited by 190 · see citing works
AlphaFold2 structures guide prospective ligand discovery
Lyu, J., Kapolka, N. J., Gumpper, R. H., Alon, A., Wang, L., Jain, M. K., Barros-Álvarez, X., Sakamoto, K., Kim, Y., DiBerto, J. F., et al. (2024) · Science · doi:10.1126/science.adn6354 · Cited by 182 · see citing works
Easy and accurate protein structure prediction using ColabFold
Kim, G., Lee, S., Karin, E. L., Kim, H., Moriwaki, Y., Ovchinnikov, S., Steinegger, M., & Mirdita, M. (2024) · Nature Protocols · doi:10.1038/s41596-024-01060-5 · Cited by 167 · see citing works
AlphaPulldown—a python package for protein–protein interaction screens using AlphaFold-Multimer
Yu, D., Chojnowski, G., Rosenthal, M., & Kosinski, J. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btac749 · Cited by 162 · see citing works
Architecture of the cytoplasmic face of the nuclear pore
Bley, C. J., Nie, S., Mobbs, G. W., Petrovic, S., Gres, A. T., Liu, X., Mukherjee, S., Harvey, S. C., Huber, F. M., Lin, D. H., et al. (2022) · Science · doi:10.1126/science.abm9129 · Cited by 158 · see citing works
Molecular dynamics simulation of an entire cell
Stevens, J. A., Grünewald, F., van Tilburg, P. A. M., König, M., Gilbert, B. R., Brier, T. A., Thornburg, Z. R., Luthey-Schulten, Z., & Marrink, S. J. (2023) · Frontiers in Chemistry · doi:10.3389/fchem.2023.1106495 · Cited by 156 · see citing works
“…hundreds of millions of atoms, include dynamic models of a photosynthetic chromatophore vesicle (Singharoy et al., 2019), the nuclear core complex (Mosalaganti et al., 2022), the membranes of a mitochondrion (Pezeshkian et al., 2020), the bacterial cytoplasm (Yu et al., 2016), and a virus…”
BackgroundWhat's next for AlphaFold and the AI protein-folding revolution
Callaway, E. (2022) · Nature · doi:10.1038/d41586-022-00997-5 · Cited by 146 · see citing works
Burley, S. K., Berman, H. M., Duarte, J. M., Feng, Z., Flatt, J. W., Hudson, B. P., Lowe, R., Peisach, E., Piehl, D. W., Rose, Y., et al. (2022) · Biomolecules · doi:10.3390/biom12101425 · Cited by 144 · see citing works
AlphaFold2 protein structure prediction: Implications for drug discovery
Borkakoti, N., & Thornton, J. M. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102526 · Cited by 137 · see citing works
Visualizing the disordered nuclear transport machinery in situ
Yu, M., Heidari, M., Mikhaleva, S., Tan, P. S., Mingu, S., Ruan, H., Reinkemeier, C. D., Obarska-Kosińska, A., Siggel, M., Beck, M., et al. (2023) · Nature · doi:10.1038/s41586-023-05990-0 · Cited by 136 · see citing works
Self-citationThe impact of AlphaFold Protein Structure Database on the fields of life sciences
Váradi, M., & Velankar, S. S. (2022) · PROTEOMICS · doi:10.1002/pmic.202200128 · Cited by 132 · see citing works
Bringing Structure to Cell Biology with Cryo-Electron Tomography
Young, L. N., & Villa, E. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111622-091327 · Cited by 131 · see citing works
Architecture of the linker-scaffold in the nuclear pore
Petrovic, S., Samanta, D., Perriches, T., Bley, C. J., Thierbach, K., Brown, B., Nie, S., Mobbs, G. W., Stevens, T. A., Liu, X., et al. (2022) · Science · doi:10.1126/science.abm9798 · Cited by 114 · see citing works
Selective degradation of multimeric proteins by TRIM21-based molecular glue and PROTAC degraders
Lu, P., Cheng, Y., Xue, L., Ren, X., Xu, X., Chen, C., Cao, L., Li, J., Wu, Q., Sun, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.10.015 · Cited by 114 · see citing works
Cryo-electron tomography on focused ion beam lamellae transforms structural cell biology
Berger, C., Premaraj, N., Ravelli, R. B. G., Knoops, K., López‐Iglesias, C., & Peters, P. J. (2023) · Nature Methods · doi:10.1038/s41592-023-01783-5 · Cited by 113 · see citing works
iU-ExM: nanoscopy of organelles and tissues with iterative ultrastructure expansion microscopy
Louvel, V., Haase, R., Mercey, O., Laporte, M. H., Eloy, T., Baudrier, É., Fortun, D., Soldati‐Favre, D., Hamel, V., & Guichard, P. (2023) · Nature Communications · doi:10.1038/s41467-023-43582-8 · Cited by 110 · see citing works
McCafferty, C. L., Klumpe, S., Amaro, R. E., Kukulski, W., Collinson, L., & Engel, B. D. (2024) · Cell · doi:10.1016/j.cell.2024.01.005 · Cited by 109 · see citing works
Translation dynamics in human cells visualized at high resolution reveal cancer drug action
Xing, H., Taniguchi, R., Khusainov, I. S., Kreysing, J. P., Welsch, S., Turoňová, B., & Beck, M. (2023) · Science · doi:10.1126/science.adh1411 · Cited by 104 · see citing works
Self-citationRice, G., Wagner, T., Stabrin, M., Sitsel, O., Prumbaum, D., & Raunser, S. (2023) · Nature Methods · doi:10.1038/s41592-023-01878-z · Cited by 98 · see citing works
Passage of the HIV capsid cracks the nuclear pore
Kreysing, J. P., Heidari, M., Žíla, V., Cruz-León, S., Obarska-Kosińska, A., Laketa, V., Rohleder, L., Welsch, S., Köfinger, J., Turoňová, B., et al. (2025) · Cell · doi:10.1016/j.cell.2024.12.008 · Cited by 98 · see citing works
Self-citationAlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function
Laurents, D. V. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.906437 · Cited by 95 · see citing works
The molecular architecture of the nuclear basket
(2024) · doi:10.1016/j.cell.2024.07.020 · Cited by 94 · see citing works
Structure and dynamics in drug discovery
Wei, H., & McCammon, J. A. (2024) · npj Drug Discovery. · doi:10.1038/s44386-024-00001-2 · Cited by 94 · see citing works
MINSTED nanoscopy enters the Ångström localization range
Weber, M., von der Emde, H., Leutenegger, M., Gunkel, P., Sambandan, S., Khan, T. A., Keller-Findeisen, J., Cordes, V. C., & Hell, S. W. (2023) · Nature Biotechnology · doi:10.1038/s41587-022-01519-4 · Cited by 94 · see citing works
High-confidence 3D template matching for cryo-electron tomography
Cruz-León, S., Majtner, T., Hoffmann, P. C., Kreysing, J. P., Kehl, S., Tuijtel, M. W., Schaefer, S. L., Geißler, K., Beck, M., Turoňová, B., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47839-8 · Cited by 89 · see citing works
Self-citationTargeting SLC transporters: small molecules as modulators and therapeutic opportunities
Schlessinger, A., Zatorski, N., Hutchinson, K., & Colas, C. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.05.011 · Cited by 87 · see citing works
Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex
Zhu, X., Huang, G., Zeng, C., Zhan, X., Liang, K., Xu, Q., Zhao, Y., Wang, P., Wang, Q., Zhou, Q., et al. (2022) · Science · doi:10.1126/science.abl8280 · Cited by 86 · see citing works
The HIV capsid mimics karyopherin engagement of FG-nucleoporins
Dickson, C. F., Hertel, S., Tuckwell, A., Li, N., Ruan, J., Al-Izzi, S. C., Ariotti, N., Sierecki, E., Gambin, Y., Morris, R. G., et al. (2024) · Nature · doi:10.1038/s41586-023-06969-7 · Cited by 85 · see citing works
Chemistry Nobel goes to developers of AlphaFold AI that predicts protein structures
Callaway, E. (2024) · Nature · doi:10.1038/d41586-024-03214-7 · Cited by 85 · see citing works
HIV-1 capsids enter the FG phase of nuclear pores like a transport receptor
Fu, L., Weiskopf, E. N., Akkermans, O., Swanson, N. A., Cheng, S., Schwartz, T., & Görlich, D. (2024) · Nature · doi:10.1038/s41586-023-06966-w · Cited by 81 · see citing works
AlphaFold two years on: Validation and impact
Kovalevskiy, O. V., Mateos-Garcia, J. C., & Tunyasuvunakool, K. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315002121 · Cited by 81 · see citing works
Pragmatic Coarse-Graining of Proteins: Models and Applications
Borges-Araújo, L., Patmanidis, I., Singh, A. P., Santos, L. H., Sieradzan, A. K., Vanni, S., Czaplewski, C. R., Pantano, S., Shinoda, W., Monticelli, L., et al. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.3c00733 · Cited by 78 · see citing works
Enhanced Protein-Protein Interaction Discovery via AlphaFold-MultimerPreprint
Kim, A., Hu, Y., Comjean, A., Rodiger, J., Mohr, S. E., & Perrimon, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.19.580970 · Cited by 76 · see citing works
Critical Assessment of Methods for Predicting the 3D Structure of Proteins and Protein Complexes
Wodak, S. J., Vajda, S., Lensink, M. F., Kozakov, D., & Bates, P. A. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-102622-084607 · Cited by 71 · see citing works
Deep learning for protein structure prediction and design—progress and applications
Jänes, J., & Beltrão, P. (2024) · Molecular Systems Biology · doi:10.1038/s44320-024-00016-x · Cited by 71 · see citing works
Understanding the cell: Future views of structural biology
Beck, M., Covino, R., Hänelt, I., & Müller-McNicoll, M. (2024) · Cell · doi:10.1016/j.cell.2023.12.017 · Cited by 71 · see citing works
Self-citationHasanzadeh, A., Hamblin, M. R., Kiani, J., Noori, H., Hardie, J. M., Karimi, M., & Shafiee, H. (2022) · Nano Today · doi:10.1016/j.nantod.2022.101665 · Cited by 69 · see citing works
A quantitative map of nuclear pore assembly reveals two distinct mechanisms
Otsuka, S., Tempkin, J. O. B., Zhang, W., Politi, A. Z., Rybina, A., Hossain, M. J., Kueblbeck, M., Callegari, A., Koch, B., Morero, N. R., et al. (2023) · Nature · doi:10.1038/s41586-022-05528-w · Cited by 69 · see citing works
Chen, C., Zhan, Y., Wang, T., Wang, Y., Gao, K., Wu, J., Wang, J., Qiu, J., & Tan, D. (2024) · Nature Communications · doi:10.1038/s41467-024-53371-6 · Cited by 69 · see citing works
Genetically encoded multimeric tags for subcellular protein localization in cryo-EM
Fung, H. K. H., Hayashi, Y., Salo, V. T., Babenko, A., Zagoriy, I., Brunner, A. H., Ellenberg, J., Müller, C. W., Cuylen‐Haering, S., & Mahamid, J. (2023) · Nature Methods · doi:10.1038/s41592-023-02053-0 · Cited by 64 · see citing works
Benchmarking all-atom biomolecular structure prediction with FoldBench
Xu, S. Y., Feng, Q., Qiao, L., Wu, H., Shen, T., Cheng, Y., Zheng, S., & Sun, S. (2025) · Nature Communications · doi:10.1038/s41467-025-67127-3 · Cited by 64 · see citing works
The Nuclear Pore Complex: Birth, Life, and Death of a Cellular Behemoth
Dultz, E., Wojtynek, M., Medalia, O., & Onischenko, E. A. (2022) · Cells · doi:10.3390/cells11091456 · Cited by 63 · see citing works
Structure and Function of the Nuclear Pore ComplexPreprint
Petrovic, S., Mobbs, G. W., Bley, C. J., Nie, S., Patke, A., & Hoelz, A. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041264 · Cited by 58 · see citing works
Overview of AlphaFold2 and breakthroughs in overcoming its limitations
Wang, L., Wen, Z., Liu, S.-W., Zhang, L., Finley, C., Lee, H., & Fan, H. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2024.108620 · Cited by 53 · see citing works
EMBL’s European Bioinformatics Institute (EMBL-EBI) in 2022
Thakur, M., Bateman, A. G., Brooksbank, C., Freeberg, M., Harrison, M., Hartley, M., Keane, T., Kleywegt, G. J., Leach, A. R., Levchenko, M., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1098 · Cited by 52 · see citing works
mdCATH: A Large-Scale MD Dataset for Data-Driven Computational Biophysics
Mirarchi, A., Toni Giorgino, A., & Fabritiis, G. D. (2024) · Scientific Data · doi:10.1038/s41597-024-04140-z · Cited by 52 · see citing works
Nuclear pores safeguard the integrity of the nuclear envelope
Taniguchi, R., Orniacki, C., Kreysing, J. P., Žíla, V., Zimmerli, C. E., Böhm, S., Turoňová, B., Kräusslich, H., Doye, V., & Beck, M. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01648-3 · Cited by 50 · see citing works
Self-citationDeep learning for protein complex structure prediction
Bryant, P. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102529 · Cited by 49 · see citing works
On the nuclear pore complex and its emerging role in cellular mechanotransduction
Matsuda, A., & Mofrad, M. R. K. (2022) · APL Bioengineering · doi:10.1063/5.0080480 · Cited by 44 · see citing works
Hudait, A., & Voth, G. A. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313737121 · Cited by 44 · see citing works
Structural determinants of co-translational protein complex assembly
Mallik, S., Venezian, J., Lobov, A., Heidenreich, M., Garcia-Seisdedos, H., Yeates, T. O., Shiber, A., & Levy, E. D. (2025) · Cell · doi:10.1016/j.cell.2024.11.013 · Cited by 42 · see citing works
Nuclear pore permeability and fluid flow are modulated by its dilation state
Hoffmann, P. C., Kim, H., Obarska-Kosińska, A., Kreysing, J. P., Andino-Frydman, E. Y., Cruz-León, S., Margiotta, E., Cernikova, L., Kosiński, J., Turoňová, B., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.038 · Cited by 42 · see citing works
Self-citationGomes, P. D. S. F. C., Gomes, D. E. B., & Bernardi, R. C. (2022) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2022.983306 · Cited by 42 · see citing works
Burley, S. K., Berman, H. M., Chiu, W., Dai, W., Flatt, J. W., Hudson, B. P., Kaelber, J. T., Khare, S. D., Kulczyk, A., Lawson, C. L., et al. (2022) · Biophysical Reviews · doi:10.1007/s12551-022-01013-w · Cited by 41 · see citing works
The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Shen, Q., Kumari, S., Xu, C., Jang, S., Shi, J., Burdick, R. C., Levintov, L., Xiong, Q., Wu, C., Devarkar, S. C., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2202815120 · Cited by 41 · see citing works
Structural biology: A golden era
Carugo, O., & Djinović‐Carugo, K. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002187 · Cited by 40 · see citing works
Artificial intelligence in small molecule drug discovery from 2018 to 2023: Does it really work?
Lv, Q., Zhou, F., Liu, X., & Zhi, L. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106894 · Cited by 38 · see citing works
A functional map of the human intrinsically disordered proteome
Pritišanac, I., Alderson, T. R., Kolarić, Đ., Zarin, T., Xie, S., Lu, A. X., Alam, A., Maqsood, A., Youn, J., Forman-Kay, J. D., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2604562123 · Cited by 37 · see citing works
Challenges in bridging the gap between protein structure prediction and functional interpretation
Varadi, M., Tsenkov, M., & Velankar, S. (2025) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26614 · Cited by 36 · see citing works
Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex
Huang, G., Zhan, X., Zeng, C., Zhu, X., Liang, K., Zhao, Y., Wang, P., Wang, Q., Zhou, Q., Tao, Q., et al. (2022) · Cell Research · doi:10.1038/s41422-021-00610-w · Cited by 36 · see citing works
Nuclear export of pre-60S particles through the nuclear pore complex
Li, Z., Chen, S., Zhao, L., Huang, G., Xu, H., Yang, X., Wang, P., Gao, N., & Sui, S. (2023) · Nature · doi:10.1038/s41586-023-06128-y · Cited by 36 · see citing works
Label-free visual proteomics: Coupling MS- and EM-based approaches in structural biology
Klykov, O. V., Kopylov, M., Carragher, B. O., Heck, A. J. R., Noble, A. J., & Scheltema, R. A. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.12.027 · Cited by 36 · see citing works
Hou, Z., Shen, Y., Fronik, S., Shen, J., Shi, J., Xu, J., Chen, L., Hardenbrook, N. J., Thompson, C., Neumann, S., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02054-z · Cited by 35 · see citing works
A combinatorial approach to uncover an additional Integrator subunit
Offley, S. R., Pfleiderer, M. M., Zucco, A. J., Fraudeau, A., Welsh, S. A., Rażew, M., Galej, W. P., & Gardini, A. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112244 · Cited by 35 · see citing works
Zhao, J., Yu, X., Shentu, X., & Li, D. (2024) · Cell and Tissue Research · doi:10.1007/s00441-024-03878-7 · Cited by 34 · see citing works
Structure, function and assembly of nuclear pore complexes
Petrovic, S., Mobbs, G. W., & Hoelz, A. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00881-w · Cited by 34 · see citing works
Unbreaking Assemblies in Molecular Simulations with Periodic Boundaries
Bruininks, B. M. H., Wassenaar, T. A., & Vattulainen, I. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c01574 · Cited by 33 · see citing works
A Perspective on the Prospective Use of AI in Protein Structure Prediction
Versini, R., Sritharan, S., Fas, B. A., Tubiana, T., Aimeur, S., Henri, J., Erard, M., Nüße, O., Andréani, J., Baaden, M., et al. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01361 · Cited by 33 · see citing works
Analysing protein complexes in plant science: insights and limitation with AlphaFold 3
Lin, P.-Y., Huang, S.-C., Chen, K.-L., Huang, Y., Liao, C.-Y., Lin, G.-J., Lee, H., & Chen, P. (2025) · Botanical studies · doi:10.1186/s40529-025-00462-2 · Cited by 34 · see citing works
Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD
Khalil, B., Linsenmeier, M., Smith, C. L., Shorter, J., & Rossoll, W. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00698-1 · Cited by 32 · see citing works
Structural Biology of RNA and Protein‐RNA Complexes after AlphaFold3
Hennig, J. (2025) · ChemBioChem · doi:10.1002/cbic.202401047 · Cited by 32 · see citing works
Hepatitis B Virus Capsid: The Core in Productive Entry and Covalently Closed Circular DNA Formation
Mendenhall, M. A., Hong, X., & Hu, J. (2023) · Viruses · doi:10.3390/v15030642 · Cited by 31 · see citing works
Open data and algorithms for open science in AI-driven molecular informatics
Brinkhaus, H. O., Rajan, K., Schaub, J., Zielesny, A., & Steinbeck, C. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102542 · Cited by 29 · see citing works
Varadi, M., Bordin, N., Orengo, C., & Velankar, S. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102543 · Cited by 29 · see citing works
Nonlinear dynamics in MEMS systems: Overcoming pull-in challenges and exploring innovative solutions
He, C., Cui, Y., He, J., Buhe, E., Bai, Q., Xu, Q., Ma, J., Alsolami, A. A., & Gao, M. (2025) · Journal of low frequency noise, vibration and active control · doi:10.1177/14613484251385061 · Cited by 29 · see citing works
Structural ensembles of disordered proteins from hierarchical chain growth and simulation
Pietrek, L. M., Stelzl, L. S., & Hummer, G. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102501 · Cited by 29 · see citing works
Self-citationAssessing the Martini 3 protein model: A review of its path and potential
Borges-Araújo, L., Pereira, G. P., Valério, M., & Souza, P. C. T. (2024) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2024.141014 · Cited by 29 · see citing works
Target identification and assessment in the era of AI
Pun, F. W., Podolskiy, D. I., Izumchenko, E., Mortlock, A. A., Oprea, T. I., Scheibye‐Knudsen, M., Fortney, K., Morgen, E. K., Ren, F., & Zhavoronkov, A. A. (2026) · Nature Reviews Drug Discovery · doi:10.1038/s41573-026-01412-8 · Cited by 28 · see citing works
Stewart, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052578 · Cited by 28 · see citing works
The impact of AlphaFold2 on experimental structure solution
Edich, M., Briggs, D. C., Kippes, O., Gao, Y., & Thorn, A. (2022) · Faraday Discussions · doi:10.1039/d2fd00072e · Cited by 28 · see citing works
The endoplasmic reticulum connects to the nucleus by constricted junctions that mature after mitosis
Bragulat-Teixidor, H., Ishihara, K., Szücs, G. M., & Otsuka, S. (2024) · EMBO Reports · doi:10.1038/s44319-024-00175-w · Cited by 27 · see citing works
Advances in cryo-ET data processing: meeting the demands of visual proteomics
Watson, A. J., & Bartesaghi, A. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102861 · Cited by 27 · see citing works
Emerging frontiers in protein structure prediction following the AlphaFold revolution
Rennie, M. L., & Oliver, M. R. (2025) · Journal of The Royal Society Interface · doi:10.1098/rsif.2024.0886 · Cited by 27 · see citing works
Structure of the nuclear pore complex goes atomic
Huang, G., Zeng, C., & Shi, Y. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102523 · Cited by 27 · see citing works
Docking a flexible basket onto the core of the nuclear pore complex
Stankunas, E., & Köhler, A. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01484-x · Cited by 26 · see citing works
Quantitative Cryo-Electron Tomography
Navarro, P. P. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.934465 · Cited by 26 · see citing works
The augmin complex architecture reveals structural insights into microtubule branching
Župa, E., Würtz, M., Neuner, A., Hoffmann, T., Rettel, M., Böhler, A., Vermeulen, B. J. A., Eustermann, S., Schiebel, E., & Pfeffer, S. (2022) · Nature Communications · doi:10.1038/s41467-022-33228-6 · Cited by 26 · see citing works
Váradi, M., Anyango, S., Appasamy, S. D., Armstrong, D. R., Bage, M., Berrisford, J. M., Choudhary, P., Bertoni, D., Deshpande, M., Leines, G. D., et al. (2022) · Protein Science · doi:10.1002/pro.4439 · Cited by 26 · see citing works
Mesoscale simulations: An indispensable approach to understand biomembranes
Duncan, A. L., & Pezeshkian, W. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.02.017 · Cited by 26 · see citing works
Implications of a multiscale structure of the yeast nuclear pore complex
Akey, C. W., Echeverria, I., Ouch, C., Nudelman, I., Shi, Y., Wang, J., Chait, B. T., Šali, A., Fernández-Martı́nez, J., & Rout, M. P. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.08.025 · Cited by 26 · see citing works
Rush, C., Jiang, Z., Tingey, M., Feng, F., & Yang, W. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1245939 · Cited by 26 · see citing works
Maurer, V. J., Siggel, M., & Kosiński, J. (2024) · SoftwareX · doi:10.1016/j.softx.2024.101636 · Cited by 26 · see citing works
Self-citation
- Authors
- Mosalaganti, S., Obarska-Kosinska, A., Siggel, M., Taniguchi, R., Turoňová, B., Zimmerli, C. E., Buczak, K., Schmidt, F. H., Margiotta, E., Mackmull, M.-T., Hagen, W. J. H., Hummer, G., Kosinski, J., & Beck, M.
- Affiliations
- University of Michigan (US)
- Department of Molecular Sociology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.
- Max Planck Institute of Biophysics (DE)
- European Molecular Biology Laboratory (DE)
- Goethe University Frankfurt (DE)
- Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
- Corresponding author
- Mosalaganti, Shyamal
- Siggel, Marc
- Hummer, Gerhard
- Beck, Martin
- ORCID
- Venue
- Science
- Published
- 2022-06-10
- Volume
- 376
- Issue
- 6598
- Pages
- eabm9506-eabm9506
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W4282936228
- Semantic Scholar
- edb8a6b7f93e3b6dfead2bd3859ff492e2ac564d
- Cited by
- 355
- References
- 135
- Citations by year
- 2026: 55 · 2025: 81 · 2024: 80 · 2023: 85 · 2022: 51 · 2021: 2 · 2012: 1
- FWCI
- 24.25
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Desy Publications Database (Deutsches Elektronen-Synchrotron DESY) (publishedVersion)
- Institute of Science and Technology Austria (submittedVersion)
- Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) (submittedVersion, cc-by-nc-nd)
- Funders
- European Molecular Biology Laboratory
- Bundesministerium für Bildung und Forschung (FKZ 031L0100)
- Max-Planck-Gesellschaft
- H2020 European Research Council (724349)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- nuclear pore complex, nucleoporins, integrative structural modeling, scaffold architecture, intrinsically disordered proteins, conformational dynamics, nuclear transport, nuclear envelope, protein-protein interaction network
- MeSH terms
- Artificial Intelligence, Humans, Cryoelectron Microscopy, Active Transport, Cell Nucleus, Nuclear Pore, Nuclear Pore Complex Proteins, Proteomics, Molecular Dynamics Simulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Claims read by deepseek-v4.1-flash under definition version 3 (extract-v3) on 2026-10-10.
Classified by jev-1.13-20260917 (gold-guideline-v0.2) on 2026-10-10.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review