Cited by 355Nuclear Structure and FunctionProtein Structure and DynamicsEnzyme Structure and Function

AI-based structure prediction empowers integrative structural analysis of human nuclear pores

Open access
Mosalaganti, Shyamal, Obarska-Kosinska, Agnieszka, Siggel, Marc, Taniguchi, Reiya, Turoňová, Beata, Zimmerli, Christian E., Buczak, Katarzyna, Schmidt, Florian H. +6 more·2022·Science

Published 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

Crossref · 10.1126/science.abm9506

Cites

138 of 138 references verified0 citation errors · 0 not checkable

Statistics

Nothing to recompute.

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
  • May combine two claims. 25
  • Classified as probably not a substantial claim. 4
  • May combine two claims.

    Findingown data

    Within 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 claim
  • May combine two claims.

    Findingown data

    The 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
  • May combine two claims.

    Findingcitation

    Two 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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingown data

    Applying 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 claim
  • May combine two claims.

    Findingown data

    In 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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingown data

    The 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 data

    AlphaFold/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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingown data

    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.

    “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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingreasoning

    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.

    “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 claim
  • May combine two claims.

    Findingown data

    The 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 claim
  • May combine two claims.

    Findingnone given

    The 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 claim
  • May combine two claims.

    Interpretationown data

    Microsecond-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
  • May combine two claims.

    Interpretationown data

    The 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 claim
  • Probably not a substantial claim: may not pass S2 (checkable).

    Interpretationreasoning

    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.

    “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 claim
  • May combine two claims.

    Premisecitation

    Aladin 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.

    Interpretationreasoning

    The 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 claim
  • Probably not a substantial claim: may not pass S3 (load-bearing).

    Premisecitation

    Recent 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.

    Interpretationreasoning

    Together 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 claim
  • May combine two claims.

    Interpretationown data

    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.

    “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 claim
  • Probably not a substantial claim: may not pass S3 (load-bearing).

    Premisecitation

    The 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.

    Interpretationreasoning

    Aladin-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 claim
  • Classified as probably not a substantial claim.

    Interpretationcitation

    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.

    “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.

29 of 29
  • 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”
4 of 4

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

    Minor

    The 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.

1 of 1

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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
Venue
Science
Published
2022-06-10
Volume
376
Issue
6598
Pages
eabm9506-eabm9506
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W4282936228
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
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

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