Condensin extrudes DNA loops in steps up to hundreds of base pairs that are generated by ATP binding events
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Abstract
The condensin SMC protein complex organizes chromosomal structure by extruding loops of DNA. Its ATP-dependent motor mechanism remains unclear but likely involves steps associated with large conformational changes within the ∼50 nm protein complex. Here, using high-resolution magnetic tweezers, we resolve single steps in the loop extrusion process by individual yeast condensins. The measured median step sizes range between 20–40 nm at forces of 1.0–0.2 pN, respectively, comparable with the holocomplex size. These large steps show that, strikingly, condensin typically reels in DNA in very sizeable amounts with ∼200 bp on average per single extrusion step at low force, and occasionally even much larger, exceeding 500 bp per step. Using Molecular Dynamics simulations, we demonstrate that this is due to the structural flexibility of the DNA polymer at these low forces. Using ATP-binding-impaired and ATP-hydrolysis-deficient mutants, we find that ATP binding is the primary step-generating stage underlying DNA loop extrusion. We discuss our findings in terms of a scrunching model where a stepwise DNA loop extrusion is generated by an ATP-binding-induced engagement of the hinge and the globular domain of the SMC complex.
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In vitro experiments of yeast condensin observed loop extrusion by SMC complexes at rates up to 600 bp/s, with individual step sizes having a median around 200 bp.
“The step size of roughly 200 bp, and step frequency of 1 per 0.4 seconds, are based on values observed from in vitro experiments of yeast condensin, where the rate of loop extrusion by SMC complexes was observed to take place at rates up to 600 bp/s, with individual step sizes of the complex having a median around 200 bp.25”
From Bringing the genetically minimal cell to life on a computer in 4D (2026) · cites this paper as [25]
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Structure-function relationships of SMC protein complexes for DNA loop extrusion
Lee, H., Noh, H., & Ryu, J. (2021) · Korean Society for Structural Biology · doi:10.34184/kssb.2021.9.1.1 · Cited by 15 · cited 1× · see citing works
“By contrast, our result that ATP binding is the step-generating process is in good agreement with cryo-EM results on cohesin (20,21,55,56) and with AFM data on condensin that showed a transition from an extended state to a hinge-engaged state upon ATP binding (18).”
Self-citationJanissen, R., Eslami-Mossallam, B., Artsimovitch, I., Depken, M., & Dekker, N. (2020) · doi:10.1016/j.bpj.2019.11.2974 · Cited by 5 · cited 1×
“Using this technique, we were able to measure up to 300 DNA tethers simultaneously at a frame rate of 50 Hz, which provides large data sets suited for statistically robust analysis (23, 26, 35).”
Self-citation
Flagged first, then by citations
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Cited by
Sorted by citations
CTCF is a DNA-tension-dependent barrier to cohesin-mediated loop extrusion
Davidson, I. F., Barth, R., Zaczek, M., van der Torre, J., Tang, W., Nagasaka, K., Janissen, R., Kerssemakers, J. W. J., Wutz, G., Dekker, C., et al. (2023) · Nature · doi:10.1038/s41586-023-05961-5 · Cited by 190 · see citing works
Self-citationGenome control by SMC complexes
Hoencamp, C., & Rowland, B. D. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00609-8 · Cited by 138 · see citing works
The Smc5/6 complex is a DNA loop-extruding motor
Pradhan, B., Kanno, T., Igarashi, M. U., Loke, M. S., Baaske, M. D., Wong, J. S. K., Jeppsson, K. E., Björkegren, C., & Kim, E. (2023) · Nature · doi:10.1038/s41586-023-05963-3 · Cited by 136 · see citing works
SMC complexes can traverse physical roadblocks bigger than their ring size
Pradhan, B., Barth, R., Kim, E., Davidson, I., Bauer, B. W., van Laar, T., Yang, W., Ryu, J.-K., van der Torre, J., Peters, J., et al. (2021) · bioRxiv · doi:10.1101/2021.07.15.452501 · Cited by 124
“To avoid imposing additional tension within the DNA by the side flow, which can slow down or stall loop extrusion (Ganji et al., 2018; Je-Kyung et al., 2021), most roadblock experiments were performed without side flow (Figure 1D).”
Self-citationA hold-and-feed mechanism drives directional DNA loop extrusion by condensin
Shaltiel, I. A., Datta, S., Lecomte, L., Hassler, M., Kschonsak, M., Bravo, S., Stober, C., Ormanns, J., Eustermann, S., & Haering, C. H. (2022) · Science · doi:10.1126/science.abm4012 · Cited by 112 · see citing works
A walk through the SMC cycle: From catching DNAs to shaping the genome
Oldenkamp, R., & Rowland, B. D. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.006 · Cited by 68 · see citing works
Nomidis, S. K., Carlon, E., Gruber, S., & Marko, J. (2022) · bioRxiv · doi:10.1093/nar/gkac268 · Cited by 48 · see citing works
“Recent observations of large ATP hydrolysis-independent contractions of SMCC-DNA complexes (54) are likely looking at the DNA segment capture process rather than protein conformational change.”
BackgroundResultInfluentialSMC motor proteins extrude DNA asymmetrically and can switch directions
Barth, R., Davidson, I. F., van der Torre, J., Taschner, M., Gruber, S., Peters, J.-M., & Dekker, C. (2025) · Cell · doi:10.1016/j.cell.2024.12.020 · Cited by 40 · see citing works
Self-citationA unified model for cohesin function in sister chromatid cohesion and chromatin loop formation
Uhlmann, F. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.005 · Cited by 44 · see citing works
Bringing the genetically minimal cell to life on a computer in 4D
Thornburg, Z. R., Maytin, A., Kwon, J., Brier, T. A., Gilbert, B. R., Fu, E., Gao, Y.-L., Quenneville, J., Wu, T., Li, H., et al. (2026) · Cell · doi:10.1016/j.cell.2026.02.009 · Cited by 44 · see citing works
Structural biology of SMC complexes across the tree of life
Burmann, F., & Löwe, J. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102598 · Cited by 29 · see citing works
Loop extrusion rules: the next generation.
Corsi, F., Rusch, E., & Goloborodko, A. (2023) · Current Opinion in Genetics and Development · doi:10.1016/j.gde.2023.102061 · Cited by 27 · see citing works
All eukaryotic SMC proteins induce a twist of −0.6 at each DNA loop extrusion step
Janissen, R., Barth, R., Davidson, I., Taschner, M., Gruber, S., Peters, J.-M., & Dekker, C. (2024) · bioRxiv · doi:10.1126/sciadv.adt1832 · Cited by 26 · see citing works
“Using MT, we previously determined that ATP binding (i.e., not ATP hydrolysis) is the step-generating event during the DNA loop extrusion cycle of yeast condensin ( 28 ).”
InfluentialSelf-citationCan DyeCycling break the photobleaching limit in single-molecule FRET?
Vermeer, B., & Schmid, S. (2022) · Nano Research · doi:10.1007/s12274-022-4420-5 · Cited by 25 · see citing works
“1 Transcription and translation machineries The central dogma of molecular biology – DNA is transcribed into RNA, RNA is translated into proteins – is rife with dynamic heterogeneity [89].”
BackgroundCondensin pinches a short negatively supercoiled DNA loop during each round of ATP usage
Martínez‐García, B., Dyson, S., Segura, J., Ayats-Fraile, A., Cutts, E., Gutiérrez-Escribano, P., Aragón, L., & Roca, J. (2022) · The EMBO Journal · doi:10.15252/embj.2022111913 · Cited by 23 · see citing works
Dynamics of chromosome organization in a minimal bacterial cell
Gilbert, B. R., Thornburg, Z. R., Brier, T. A., Stevens, J. A., Grünewald, F., Stone, J. E., Marrink, S. J., & Luthey-Schulten, Z. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1214962 · Cited by 19 · see citing works
“For this study we made the simplifying assumption that only intra-strand motion is permitted ( p unbind = 0), which has been used in other studies (Ryu et al., 2021), but the software is capable of simulating inter-strand motion.”
InfluentialDNA packaging by molecular motors: from bacteriophage to human chromosomes
Prevo, B., & Earnshaw, W. C. (2024) · Nature reviews genetics · doi:10.1038/s41576-024-00740-y · Cited by 14 · see citing works
“Indeed, steps of up to >500 bp (>170 nm) have been observed 187 .”
Fluidification of entangled polymers by loop extrusion
Conforto, F., Fosado, Y. A. G., & Michieletto, D. (2024) · Physical Review Research · doi:10.1103/physrevresearch.6.033160 · Cited by 15 · see citing works
“We expect that considering interchain loop extrusion [34, 59] and bridging [35] may drastically influence our results, eventually decreasing the mobility of the polymers and thus increasing the viscoelasticity of the solution.”
BackgroundSelf-citationSMC motor proteins extrude DNA asymmetrically and contain a direction switchPreprint
Barth, R., Davidson, I., van der Torre, J., Taschner, M., Gruber, S., Peters, J.-M., & Dekker, C. (2023) · bioRxiv · doi:10.1101/2023.12.21.572892 · Cited by 14 · see citing works
“All three are capable of manipulating DNA via an ATP-dependent process called DNA loop extrusion 2 – 10 , where loops are created and enlarged stepwise by ATP-binding events to the SMC complex 9,11 .”
BackgroundSelf-citationCohesin supercoils DNA during loop extrusion
Davidson, I., Barth, R., Horn, S., Janissen, R., Nagasaka, K., Wutz, G., Stocsits, R. R., Bauer, B. W., Dekker, C., & Peters, J.-M. (2024) · bioRxiv · doi:10.1101/2024.03.22.586228 · Cited by 13
“Key steps in the loop extrusion cycle are the ATP-driven engagement of cohesin’s ATPase heads, resulting in ~15 pN force generation ( 18 ), DNA translocation (~100-200 bp/step ( 19, 48 )) and subsequent DNA clamping.”
Self-citationHigh-speed AFM imaging reveals DNA capture and loop extrusion dynamics by cohesin-NIPBL
Kaur, P., Lu, X., Xu, Q. K., Irvin, E. M., Pappas, C., Zhang, H., Finkelstein, I. J., Shi, Z., Tao, Y. J., Yu, H., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105296 · Cited by 15 · see citing works
“It is known that tension on DNA reduces the DNA loop extrusion step size (48).”
BackgroundMethodInfluentialTelomeres stall DNA loop extrusion by condensin.
Analikwu, B. T., Deshayes, A., van der Torre, J., Guérin, T. M., Katan, A., Béneut, C., Barth, R., Phipps, J., Scolari, V., Veaute, X., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115900 · Cited by 12 · see citing works
Self-citationTwo CTCF motifs impede cohesin-mediated DNA loop extrusion
Barth, R., Janissen, R., Muras, L., van der Torre, J., Litos, G., van der Sluis, E. O., van den Berg, A., Davidson, I., Peters, J.-M., & Dekker, C. (2025) · bioRxiv · doi:10.1101/2025.01.26.634934 · Cited by 12
“56 In brief, 1.5 kbp-long dsDNA was tethered between the glass surface and magnetic bead as described above and a force of 0.3 pN or 1 pN was applied.”
InfluentialSelf-citationActive Loop Extrusion guides DNA-Protein Condensation
Takaki, R., Savich, Y., Brugués, J., & Jülicher, F. (2024) · bioRxiv · doi:10.1101/2024.07.03.601883 · Cited by 12
Chromosome compaction is triggered by an autonomous DNA-binding module within condensin
Pastic, A., Nosella, M. L., Kochhar, A., Liu, Z. H., Forman-Kay, J. D., & D’Amours, D. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114419 · Cited by 13 · see citing works
Barth, R., Pradhan, B., Kim, E., Davidson, I. F., van der Torre, J., Peters, J., & Dekker, C. (2023) · Scientific Reports · doi:10.1038/s41598-023-35359-2 · Cited by 19 · see citing works
Self-citationInterphase chromatin biophysics and mechanics: new perspectives and open questions
Coulon, A. (2024) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2024.102296 · Cited by 16 · see citing works
Telomere protein arrays stall DNA loop extrusion by condensinPreprint
Analikwu, B. T., Deshayes, A., van der Torre, J., Guérin, T. M., Katan, A., Béneut, C., Barth, R., Phipps, J., Scolari, V., Veaute, X., et al. (2023) · bioRxiv · doi:10.1101/2023.10.29.564563 · Cited by 10 · see citing works
“%) of the encounters, which prompts us to hypothesize that condensin can occasionally grab even beyond the longest 93 nm array, in accordance with our previous measurements of the step sizes that showed that condensin occasionally makes steps larger than its ~40 nm diameter 53,54 .”
BackgroundResultSelf-citationCurrent working models of SMC-driven DNA-loop extrusion
Moon, K.-W., & Ryu, J. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220898 · Cited by 11 · see citing works
Self-citationFeng, C., Wang, J., & Chu, X. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad042 · Cited by 12 · see citing works
“However, since the loop extrusion process is characterized as ATP-dependent ( Ryu et al., 2022 ) , the results that these equilibrium models are sufficient for inducing the formation of experimentally consistent chromatin loops are quite puzzling.”
Zooming into Disease at the Nanoscale: High-Speed Atomic Force Microscopy in Biomedical Discovery
Lim, K., & Wong, R. W.-C. (2026) · ACS Nano · doi:10.1021/acsnano.5c20737 · Cited by 8 · see citing works
Cohesin supercoils DNA during loop extrusion
Davidson, I. F., Barth, R., Nagasaka, K., Tang, W., Wutz, G., Horn, S., Janissen, R., Stocsits, R. R., Chlosta, E., Bauer, B. W., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115856 · Cited by 24 · see citing works
Self-citationSMC-mediated chromosome organization: Does loop extrusion explain it all?
Hirano, T., & Kinoshita, K. (2024) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2024.102447 · Cited by 10 · see citing works
Genome organization across scales: mechanistic insights from in vitro reconstitution studies
Oberbeckmann, E., & Oudelaar, A. M. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230883 · Cited by 7 · see citing works
Piveteau, V., Dupont, C., Salari, H., Dumont, A., Savocco, J., Jost, D., & Piazza, A. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00748-6 · Cited by 13 · see citing works
“…the ability to extrude DNA loops in vitro presumably via a conserved mechanism (Ganji et al, 2018; Davidson et al, 2019; Kim et al, 2019; Kong et al, 2020; Kim et al, 2020; Gol fi er et al, 2020; Pradhan et al, 2022; Shaltiel et al, 2022; Ryu et al, 2022; Pradhan et al, 2023; Janissen et al, 2024).”
Condensin loop extrusion properties, roadblocks, and role in homology search in S. cerevisiae
Piveteau, V., Dupont, C., Salari, H., Dumont, A., Savocco, J., Jost, D., & Piazza, A. (2026) · bioRxiv · doi:10.1101/2024.09.12.612585 · Cited by 6
“…to extrude DNA loops in vitro presumably via a conserved mechanism (Ganji et al , 2018; Davidson et al , 2019; Kim et al , 2019; Kong et al , 2020; Kim et al , 2020; Golfier et al , 2020; Pradhan et al , 2022; Shaltiel et al , 2022; Ryu et al , 2022; Pradhan et al , 2023; Janissen et al , 2024).”
Yamauchi, M., Brandani, G., Terakawa, T., & Takada, S. (2025) · bioRxiv · doi:10.1101/2024.04.29.591782 · Cited by 6
Measuring molecular forces inside living cells using magnetic tweezers
Kongari, A., & Molodtsov, M. (2025) · Biophysical Reviews · doi:10.1007/s12551-025-01349-z · Cited by 5 · see citing works
Bonato, A., Jang, J., Kim, D., Moon, K.-W., Michieletto, D., & Ryu, J. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf725 · Cited by 7 · see citing works
Self-citationMotorized chromosome models of mitotic chromosome folding
Cao, Z., Du, C., Hou, Z., & Wolynes, P. G. (2025) · Nature Communications · doi:10.1038/s41467-025-66025-y · Cited by 4 · see citing works
“These values correspond to an apparent extrusion rate of 1-2 kbp/s, which is comparable to the experimental values 1 – 3 kbp/s 34 – 36, 40 , 58 We choose the shown representative structure as the reference.”
Anisotropic scrunching of SMC with a baton-pass mechanism
Moon, K.-W., Kim, D.-G., & Ryu, J. (2024) · Communications Biology · doi:10.1038/s42003-024-06557-z · Cited by 5 · see citing works
“Moreover, molecular dynamic simulations sup-portedthescrunchingmodelbyassumingconformationalchangesfromthehinge-releasedtohinge-engagedshapes(shownas26nmfromtheheadto thehinge) 28 – 30 .”
InfluentialSelf-citationKolbin, D., Walker, B., Hult, C., Stanton, J., Adalsteinsson, D., Forest, M. G., & Bloom, K. (2023) · Genes · doi:10.3390/genes14122193 · Cited by 4 · see citing works
“Single-molecule in vitro experiments tracked con-densins on DNA sheets, demonstrating their ability to unidirectionally translocate along DNA [66] and to extrude and stabilize loops in the presence of ATP [65,68].”
BackgroundLagunov, T., Gridina, M., Nurislamov, A., Kulikova, T., Maslova, A., Konstantinov, V., Popov, A., Krasikova, A., & Fishman, V. (2026) · bioRxiv · doi:10.1093/nar/gkag316 · Cited by 3 · see citing works
Current Advances in Genome Modeling Across Length Scales
Schultz, E. R., Kaplan, J. L., Wu, Y., Kyhl, S., Willett, R., & de Pablo, J. D. (2025) · WIREs Computational Molecular Science · doi:10.1002/wcms.70024 · Cited by 3 · see citing works
“…experiments using molecular tweezers in conjunction with molecular dynamics simulations are also being used to characterize the properties of loop extrusion complexes, including the forces generated, the size of individual extrusion steps, and the properties of CTCF barriers [265, 266].”
Koide, H., Kodera, N., Takada, S., & Terakawa, T. (2024) · bioRxiv · doi:10.1101/2024.12.16.628603 · Cited by 3
Valdés, A., & Haering, C. (2024) · Biochemical Society Transactions · doi:10.1042/bst20240650 · Cited by 3 · see citing works
Corticosteroid‐induced chromatin loop dynamics at the FKBP5 gene
Wang, C., Manders, F., Groh, L., Oldenkamp, R., & Logie, C. (2023) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.15064 · Cited by 3 · see citing works
Loops are geometric catalysts for DNA integration
Battaglia, C., & Michieletto, D. (2023) · bioRxiv · doi:10.1093/nar/gkae484 · Cited by 3 · see citing works
“Beyond classic enhancer-promoter interactions ( 45 ), several new mechanisms of loop formation have been identified recently, for instance those mediated by CTCF ( 43 ) ( ∼ 0.1–1 Mb), cohesin ( 46 ,47 ) and condensin ( 48–50 ) ( ∼ 1–10 kb).”
BackgroundInfluentialSelf-citationCTCF is a DNA-tension-dependent barrier to cohesin-mediated DNA loop extrusionPreprint
Davidson, I., Barth, R., Zaczek, M., van der Torre, J., Tang, W., Nagasaka, K., Janissen, R., Kerssemakers, J., Wutz, G., Dekker, C., et al. (2022) · bioRxiv · doi:10.1101/2022.09.08.507093 · Cited by 3 · see citing works
Self-citationTheory of chromosome structural dynamics by processive loop extrusion.
Cao, Z.-Y., Du, C., Hou, Z.-H., & Wolynes, P. (2026) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2609796123 · Cited by 2 · see citing works
Condensin I but not Condensin II is crucial for mitotic chromosome mechanics
Nielsen, C. F., Witt, H., Ridolfi, A., Kempers, B., Chameau, E. M. J., van der Smagt, S., Sitz, J., Barišić, M., Peterman, E. J. G., Wuite, G., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72825-7 · Cited by 2
Yeast condensin acts as a transient intermolecular crosslinker in entangled DNA
Conforto, F., Valdés, A., Vanderlinden, W., & Michieletto, D. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkag044 · Cited by 2 · see citing works
“SMCs are expected to have a significant impact on the dynamics of chromosomes in cells, however it is challenging to precisely quantify it experimentally.”
Self-citationSMC modulates ParB engagement in segregation complexes in streptomyces
Pawlikiewicz, K., Strzałka, A., Majkowski, M., Duława-Kobeluszczyk, J., Szafran, M., & Jakimowicz, D. (2024) · bioRxiv · doi:10.1038/s41467-025-64044-3 · Cited by 2
“Moreover, it is also demonstrated that ParB and SMC form a complex involving their CTP-binding and joint domains, respectively.”
Torsional Mechanics of Circular DNA
Singh, G., Hong, Y., Inman, J. T., Sethna, J., & Wang, M. D. (2024) · bioRxiv · doi:10.1101/2024.10.08.617281 · Cited by 2
Zhegalova, I., Ulianov, S., Galitsyna, A., Pletenev, I., Tsoy, O., Luzhin, A. V., Vasiluev, P., Bulavko, E. S., Ivankov, D., Gavrilov, A., et al. (2024) · bioRxiv · doi:10.1101/2024.06.12.598618 · Cited by 2 · see citing works
“ATP binding is required for cohesin loading onto DNA 81 , and ATP hydrolysis is required for the extrusion progression 73 .”
BackgroundLeishIF4E2 is a cap‐binding protein that plays a role in Leishmania cell cycle progression
Baron, N., Purushotham, R., Pullaiahgari, D., Bose, P., Zarivach, R., & Shapira, M. (2023) · The FASEB Journal · doi:10.1096/fj.202301665r · Cited by 8 · see citing works
Making Mitotic Chromosomes in a Test Tube
Shintomi, K. (2022) · Epigenomes · doi:10.3390/epigenomes6030020 · Cited by 2 · see citing works
Loop Extrusion Reversal by Condensin Motor is Mediated by Catch Bonds
Dey, A., Shi, G., Takaki, R., & Thirumalai, D. (2026) · bioRxiv · doi:10.64898/2026.05.01.722258 · Cited by 1
“We estimated that in the experiment [25] t ≈ 50 s under the condition of F = 0 .”
InfluentialGu, C., Takada, S., Brandani, G. B., & Terakawa, T. (2024) · doi:10.1101/2024.09.17.613402 · Cited by 1 · see citing works
DNA capture and loop extrusion dynamics by cohesin-NIPBLPreprint
Kaur, P., Shi, Z.-B., Lu, X.-T., Zhang, H.-S., Finkelstein, I., Tao, Y., Yu, H.-T., & Wang, H. (2022) · bioRxiv · doi:10.1101/2022.08.18.504320 · Cited by 1 · see citing works
“A recent magnetic tweezers study of condensin with a resolution of ~10 nm revealed a broad distribution of DNA looping step sizes (47).”
BackgroundUnderstanding the role of chromatin accessibility and compaction on loop extrusion dynamicsPreprint
Pellet, N., Pastrana, C. L., Delamarre, A., D'Asaro, D., Bernard, P., & Jost, D. (2026) · bioRxiv · doi:10.64898/2026.10.12.758711
“In particular, we monitor the progression of the LEF hinge along chromatin by assuming that it occurs by consecutive stochastic jumps ∆ x sampled from a Gamma-like distribution p (∆ x ) at a given rate k 0 , as observed in vitro [31], and is hindered by the presence of roadblocks [40](Fig.”
InfluentialJang, J., Higashi, T. L., Tang, M., Kim, C., Kinoshita, Y., Myeong, H., Lee, J., Nishiyama, T., Cho, W., Uhlmann, F., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag850
Self-citationHu, T., Song, X., & Luo, Z. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2607976123
Kim, H., Kim, D.-G., Ha, S., Jang, J., Vitorino, F. N. D. L., Gongora, J. M., Kim, W., Oh, Y., Park, G., Kang, H., et al. (2026) · Molecules and Cells · doi:10.1016/j.molcel.2026.06.021
Self-citationHSV-1 origin binding protein UL9 forms intermolecular DNA tethers and intramolecular DNA loops
Meier, A., Vuckovic, J., Girvan, P., Jalal, A. S. B., Cutts, E., Brophy, T., Ambrose, B., & Rueda, D. S. (2026) · Nature Communications · doi:10.1038/s41467-026-74361-w
Chromosome segregation in a minimal bacterial cell driven by SMC protein complexes
Maytin, A. K., Gilbert, B. R., & Luthey-Schulten, Z. (2026) · Protein Science · doi:10.1002/pro.70604
Effects of Extruder Dynamics and Noise on Simulated Chromatin Contact Probability Curves
Konstantinov, V., Shadskiy, A., & Lagunov, T. (2026) · bioRxiv · doi:10.1101/2025.06.09.658566
“This mechanistic foundation (discrete spatial stepping coupled with DNA wrapping) supports our coarse-grained representation of extrusion as a sequence of bead-displacement events in our simulations.”
InfluentialContact networks encode the ATP-induced dynamic structural asymmetry of condensin head domains
Xu, C., & Chu, X. (2025) · The Journal of Chemical Physics · doi:10.1063/5.0295393
Condensin I confers Stiffness and Centromeric Cohesion to Mitotic Chromosomes
Nielsen, C. F., Witt, H., Ridolfi, A., Kempers, B., Chameau, E. M. J., van der Smagt, S., Barišić, M., Peterman, E. J. G., Wuite, G., & Hickson, I. (2025) · bioRxiv · doi:10.1101/2025.04.29.651176
“Condensins have been shown to be very sensitive to even relatively low forces, with measurements showing that loop extrusion ceases at forces above 1 pN 31,32 .”
Meier, A., Vuckovic, J., Girvan, P., Cutts, E., Brophy, T., Ambrose, B., & Rueda, D. S. (2024) · bioRxiv · doi:10.1101/2024.10.30.621104
“5A ), as described 28,29 .”
Motor domain of condensin and step formation in extruding loop of DNA
Chou, Y.-C. (2024) · Journal of biological physics (Print) · doi:10.1007/s10867-024-09661-7
“The expected value of the step size may be evaluated from where C is a normalization constant and can evaluated by comparing between the average value of the measured step size distribution [34] and the calculated one from Eq.”
Influential
- Authors
- Ryu, J.-K., Rah, S.-H., Janissen, R., Kerssemakers, J. W. J., Bonato, A., Michieletto, D., & Dekker, C.
- Affiliations
- Delft University of Technology (NL)
- University of Edinburgh (GB)
- Institute of Genetics and Cancer (GB)
- Corresponding author
- Dekker, Cees
- ORCID
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2021-12-24
- Volume
- 50
- Issue
- 2
- Pages
- 820-832
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC8789078
- OpenAlex
- W3209917808
- Cited by
- 87
- References
- 63
- Citations by year
- 2026: 14 · 2025: 25 · 2024: 17 · 2023: 16 · 2022: 9 · 2021: 5 · 2020: 1
- FWCI
- 5.13
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, cc-by)
- Research Repository (Delft University of Technology) (submittedVersion, cc-by-nc)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Funders
- European Research Council (883684, 947918)
- Marie Sklodowska-Curie (753002)
- Royal Society
- Topics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- condensin, SMC complex, DNA loop extrusion, ATP binding, motor mechanism, step size, chromatin organization, magnetic tweezers
- MeSH terms
- Adenosine Triphosphatases, Chromatin, DNA-Binding Proteins, DNA, Fungal, Nucleic Acid Conformation, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Multiprotein Complexes
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.
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 ›
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