DNA loop extrusion by human cohesin

A 3D Map of the Human Genome at Kilobase Resolution Reveals Principles of Chromatin Looping

Rao, S. S. P., Huntley, M. H., Durand, N. C., Stamenova, E. K., Bochkov, I. D., Robinson, J. T., Sanborn, A. L., Machol, I., Omer, A. D., Lander, E. S., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.021 · Cited by 9,212 · see citing works

Topological domains in mammalian genomes identified by analysis of chromatin interactions

Dixon, J. R., Selvaraj, S., Yue, F., Kim, A., Li, Y., Shen, Y., Hu, M., Liu, J. S., & Ren, B. (2012) · Nature · doi:10.1038/nature11082 · Cited by 6,829 · see citing works

Double nicking by RNA-guided CRISPR Cas9 for enhanced genome editing specificity

Ran, F. A., Hsu, P. D., Lin, C.-Y., Gootenberg, J. S., Konermann, S., Trevino, A. E., Scott, D. A., Inoue, A., Matoba, S., Zhang, Y., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.021 · Cited by 3,299 · see citing works

Spatial partitioning of the regulatory landscape of the X-inactivation centre

Nora, E. P., Lajoie, B. R., Schulz, E. G., Giorgetti, L., Okamoto, I., Servant, N., Piolot, T., van Berkum, N. L., Meisig, J., Sedat, J., et al. (2012) · Nature · doi:10.1038/nature11049 · Cited by 2,895 · see citing works

Formation of chromosomal domains by loop extrusion

Fudenberg, G., Imakaev, M., Lu, C., Goloborodko, A., Abdennur, N., & Mirny, L. A. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.085 · Cited by 2,003 · see citing works

Cohesin Loss Eliminates All Loop Domains

Rao, S. S. P., Huang, S.-C., Glenn St Hilaire, B., Engreitz, J. M., Perez, E. M., Kieffer-Kwon, K.-R., Sanborn, A. L., Johnstone, S. E., Bascom, G. D., Bochkov, I. D., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.026 · Cited by 1,883 · see citing works

Chromatin extrusion explains key features of loop and domain formation in wild-type and engineered genomes

Sanborn, A. L., Rao, S. S. P., Huang, S.-C., Durand, N. C., Huntley, M. H., Jewett, A. I., Bochkov, I. D., Chinnappan, D., Cutkosky, A., Li, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1518552112 · Cited by 1,730 · see citing works

Two independent modes of chromatin organization revealed by cohesin removal

Schwarzer, W., Abdennur, N., Goloborodko, A., Pekowska, A., Fudenberg, G., Loe-Mie, Y., Fonseca, N. A., Huber, W., Haering, C. H., Mirny, L., et al. (2017) · Nature · doi:10.1038/nature24281 · Cited by 1,196 · see citing works

Cohesin mediates transcriptional insulation by CCCTC-binding factor

Wendt, K. S., Yoshida, K., Itoh, T., Bando, M., Koch, B., Schirghuber, E., Tsutsumi, S., Nagae, G., Ishihara, K., Mishiro, T., et al. (2008) · Nature · doi:10.1038/nature06634 · Cited by 1,193 · see citing works

Cohesins Functionally Associate with CTCF on Mammalian Chromosome Arms

Parelho, V., Hadjur, S., Spivakov, M., Leleu, M., Sauer, S., Gregson, H. C., Jarmuz, A., Canzonetta, C., Webster, Z., Nesterova, T., et al. (2008) · Cell · doi:10.1016/j.cell.2008.01.011 · Cited by 900 · see citing works

Topologically associating domains and chromatin loops depend on cohesin and are regulated by CTCF, WAPL, and PDS5 proteins

Wutz, G., Várnai, C., Nagasaka, K., Cisneros, D. A., Stocsits, R. R., Tang, W., Schoenfelder, S., Jessberger, G., Muhar, M., Hossain, M. J., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201798004 · Cited by 864 · see citing works

Disseminating the genome: joining, resolving, and separating sister chromatids during mitosis and meiosis

Nasmyth, K. (2001) · Annual Review of Genetics · doi:10.1146/annurev.genet.35.102401.091334 · Cited by 805 · see citing works

The cohesin release factor WAPL restricts chromatin loop extension

Haarhuis, J. H. I., van der Weide, R. H., Blomen, V. A., Yáñez-Cuna, J. O., Amendola, M., van Ruiten, M. S., Krijger, P. H. L., Teunissen, H., Medema, R. H., van Steensel, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.04.013 · Cited by 793 · see citing works

Real-time imaging of DNA loop extrusion by condensin

Ganji, M., Shaltiel, I. A., Bisht, S., Kim, E., Kalichava, A., Haering, C. H., & Dekker, C. (2018) · Science · doi:10.1126/science.aar7831 · Cited by 793 · see citing works

Cohesin’s binding to chromosomes depends on a separate complex consisting of Scc2 and Scc4 proteins

Ciosk, R., Shirayama, M., Shevchenko, A., Tanaka, T., Toth, A., Shevchenko, A., & Nasmyth, K. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80420-7 · Cited by 755 · see citing works

Cohesin relocation from sites of chromosomal loading to places of convergent transcription

Lengronne, A., Katou, Y., Mori, S., Yokobayashi, S., Kelly, G. P., Itoh, T., Watanabe, Y., Shirahige, K., & Uhlmann, F. (2004) · Nature · doi:10.1038/nature02742 · Cited by 588 · see citing works

Self-organization of domain structures by DNA-loop-extruding enzymes

Alipour, E., & Marko, J. F. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks925 · Cited by 540 · see citing works

SMC complexes: from DNA to chromosomes

Uhlmann, F. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.30 · Cited by 524 · see citing works

The cohesin ring concatenates sister DNA molecules

Haering, C. H., Farcas, A.-M., Arumugam, P., Metson, J., & Nasmyth, K. (2008) · Nature · doi:10.1038/nature07098 · Cited by 494 · see citing works

Cohesin is positioned in mammalian genomes by transcription, CTCF and Wapl

Busslinger, G. A., Stocsits, R. R., van der Lelij, P., Axelsson, E., Tedeschi, A., Galjart, N., & Peters, J.-M. (2017) · Nature · doi:10.1038/nature22063 · Cited by 468 · see citing works

Characterization of Vertebrate Cohesin Complexes and Their Regulation in Prophase

Sumara, I., Vorlaufer, E., Gieffers, C., Peters, B. H., & Peters, J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.4.749 · Cited by 414 · see citing works

Condensin and cohesin display different arm conformations with characteristic hinge angles

Anderson, D. E., Losada, A., Erickson, H., & Hirano, T. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200111002 · Cited by 378 · see citing works

A mechanism of cohesin‐dependent loop extrusion organizes zygotic genome architecture

Gassler, J., Brandão, H. B., Imakaev, M., Flyamer, I. M., Ladstätter, S., Bickmore, W. A., Peters, J., Mirny, L. A., & Tachibana, K.-E. K. (2017) · The EMBO Journal · doi:10.15252/embj.201798083 · Cited by 363 · see citing works

Wapl is an essential regulator of chromatin structure and chromosome segregation

Tedeschi, A., Wutz, G., Huet, S., Jaritz, M., Wuensche, A., Schirghuber, E., Davidson, I. F., Tang, W., Cisneros, D. A., Bhaskara, V., et al. (2013) · Nature · doi:10.1038/nature12471 · Cited by 359 · see citing works

Compaction and segregation of sister chromatids via active loop extrusion

Goloborodko, A. A., Imakaev, M., Marko, J. F., & Mirny, L. A. (2016) · eLife · doi:10.7554/elife.14864 · Cited by 317 · see citing works

SMC1: an essential yeast gene encoding a putative head-rod-tail protein is required for nuclear division and defines a new ubiquitous protein family.

Strunnikov, A. V., Larionov, V., & Koshland, D. E. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.123.6.1635 · Cited by 312 · see citing works

Biochemical reconstitution of topological DNA binding by the cohesin ring

Murayama, Y., & Uhlmann, F. (2013) · Nature · doi:10.1038/nature12867 · Cited by 307 · see citing works

<i>Bacillus subtilis</i> SMC complexes juxtapose chromosome arms as they travel from origin to terminus

Wang, X., Brandão, H. B., Le, T. B. K., Laub, M. T., & Rudner, D. Z. (2017) · Science · doi:10.1126/science.aai8982 · Cited by 293 · see citing works

The condensin complex is a mechanochemical motor that translocates along DNA

Terakawa, T., Bisht, S., Eeftens, J., Dekker, C., Haering, C., & Greene, E. (2017) · Science · doi:10.1126/science.aan6516 · Cited by 269 · see citing works

Rapid movement and transcriptional re-localization of human cohesin on DNA

Davidson, I. F., Goetz, D., Zaczek, M. P., Molodtsov, M. I., Huis in 't Veld, P. J., Weissmann, F., Litos, G., Cisneros, D. A., Ocampo‐Hafalla, M., Ladurner, R., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201695402 · Cited by 246 · see citing works

Control of inducible gene expression links cohesin to hematopoietic progenitor self-renewal and differentiation

Cuartero, S., Weiss, F. D., Dharmalingam, G., Guo, Y., Ing-Simmons, E., Masella, S., Robles-Rebollo, I., Xiao, X., Wang, Y.-F., Barozzi, I., et al. (2018) · Nature Immunology · doi:10.1038/s41590-018-0184-1 · Cited by 210 · see citing works

Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl–Pds5 and Sgo1

Shintomi, K., & Hirano, T. (2009) · Genes &amp; Development · doi:10.1101/gad.1844309 · Cited by 203 · see citing works

Recruitment of Xenopus Scc2 and cohesin to chromatin requires the pre-replication complex

Takahashi, T. S., Yiu, P., Chou, M. F., Gygi, S. P., & Walter, J. C. (2004) · Nature Cell Biology · doi:10.1038/ncb1177 · Cited by 201 · see citing works

Characterization of a DNA exit gate in the human cohesin ring

Veld, P. J. H. I. ’., Herzog, F., Ladurner, R., Davidson, I. F., Piric, S., Kreidl, E., Bhaskara, V., Aebersold, R. H., & Peters, J. (2014) · Science · doi:10.1126/science.1256904 · Cited by 189 · see citing works

Scc2 Is a Potent Activator of Cohesin’s ATPase that Promotes Loading by Binding Scc1 without Pds5

Petela, N. J., Gligoris, T. G., Metson, J., Lee, B., Voulgaris, M., Hu, B., Kikuchi, S., Chapard, C., Chen, W., Rajendra, E., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.022 · Cited by 187 · see citing works

The fundamental role of chromatin loop extrusion in physiological V(D)J recombination

Zhang, Y., Zhang, X., Ba, Z., Liang, Z., Dring, E. W., Hu, H., Lou, J., Kyritsis, N., Zurita, J., Shamim, M. S., et al. (2019) · Nature · doi:10.1038/s41586-019-1547-y · Cited by 160 · see citing works

Mechanism of APC/C CDC20 activation by mitotic phosphorylation

Qiao, R., Weissmann, F., Yamaguchi, M., Brown, N. G., VanderLinden, R. T., Imre, R., Jarvis, M. A., Brunner, M. R., Davidson, I. F., Litos, G., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604929113 · Cited by 143 · see citing works

The Cohesin Ring Uses Its Hinge to Organize DNA Using Non-topological as well as Topological Mechanisms

Srinivasan, M., Scheinost, J. C., Petela, N. J., Gligoris, T. G., Wissler, M. F., Ogushi, S., Collier, J., Voulgaris, M., Kurze, A., Chan, K., et al. (2018) · Cell · doi:10.1016/j.cell.2018.04.015 · Cited by 142 · see citing works

Crystal structure of the cohesin loader Scc2 and insight into cohesinopathy

Kikuchi, S., Borek, D., Otwinowski, Z., Tomchick, D. R., & Yu, H. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611333113 · Cited by 122 · see citing works

Evolution of condensin and cohesin complexes driven by replacement of Kite by Hawk proteins

Wells, J. N., Gligoris, T. G., Nasmyth, K., & Marsh, J. A. (2017) · Current Biology · doi:10.1016/j.cub.2016.11.050 · Cited by 113 · see citing works

Absolute quantification of cohesin, CTCF and their regulators in human cells

Holzmann, J., Politi, A. Z., Nagasaka, K., Hantsche-Grininger, M., Walther, N., Koch, B., Fuchs, J., Dürnberger, G., Tang, W., Ladurner, R., et al. (2019) · eLife · doi:10.7554/elife.46269 · Cited by 109 · see citing works

Scc2/Nipbl hops between chromosomal cohesin rings after loading

Rhodes, J., Mazza, D., Nasmyth, K., & Uphoff, S. (2017) · eLife · doi:10.7554/elife.30000 · Cited by 99 · see citing works

Structure and function of cohesin's Scc3/SA regulatory subunit

Roig, M. B., Löwe, J., Chan, K.-L., Beckouët, F., Metson, J., & Nasmyth, K. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.08.015 · Cited by 91 · see citing works

Pds5 promotes cohesin acetylation and stable cohesin–chromosome interaction

Vaur, S., Feytout, A., Vazquez, S., & Javerzat, J. (2012) · EMBO Reports · doi:10.1038/embor.2012.72 · Cited by 60 · see citing works

Scc2 counteracts a Wapl-independent mechanism that releases cohesin from chromosomes during G1

Srinivasan, M., Petela, N. J., Scheinost, J. C., Collier, J., Voulgaris, M., Roig, M. B., Beckouët, F., Hu, B., & Nasmyth, K. (2019) · eLife · doi:10.7554/elife.44736 · Cited by 48 · see citing works

Expressing Multi-subunit Complexes Using biGBac

Weissmann, F., & Peters, J. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7759-8_21 · Cited by 32 · see citing works

The Self-Organizing Genome: Principles of Genome Architecture and Function

Misteli, T. (2020) · Cell · doi:10.1016/j.cell.2020.09.014 · Cited by 706 · see citing works

Genome folding through loop extrusion by SMC complexes

Davidson, I. F., & Peters, J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00349-7 · Cited by 507 · see citing works

Dynamics of CTCF- and cohesin-mediated chromatin looping revealed by live-cell imaging

Gabriele, M., Brandão, H. B., Grosse-Holz, S., Jha, A., Dailey, G. M., Cattoglio, C., Hsieh, T.-H. S., Mirny, L., Zechner, C., & Hansen, A. S. (2022) · Science · doi:10.1126/science.abn6583 · Cited by 506 · see citing works

The molecular basis and disease relevance of non-homologous DNA end joining

Zhao, B., Rothenberg, E., Ramsden, D. A., & Lieber, M. R. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00297-8 · Cited by 389 · see citing works

Mechanisms of enhancer action: the known and the unknown

Panigrahi, A., & O’Malley, B. W. (2021) · Genome biology · doi:10.1186/s13059-021-02322-1 · Cited by 351 · see citing works

Loop extrusion as a mechanism for formation of DNA damage repair foci

Arnould, C., Rocher, V., Finoux, A.-L., Clouaire, T., Li, K., Zhou, F., Caron, P., Mangeot, P. E., Ricci, E. P., Mourad, R., et al. (2021) · Nature · doi:10.1038/s41586-021-03193-z · Cited by 341 · see citing works

Epigenetic regulation of T cell exhaustion

Belk, J. A., Dániel, B., & Satpathy, A. T. (2022) · Nature Immunology · doi:10.1038/s41590-022-01224-z · Cited by 334 · see citing works

The relationship between genome structure and function

Oudelaar, A. M., & Higgs, D. R. (2021) · Nature Reviews Genetics · doi:10.1038/s41576-020-00303-x · Cited by 304 · see citing works

Cohesin and CTCF control the dynamics of chromosome folding

Mach, P., Kos, P. I., Zhan, Y., Cramard, J., Gaudin, S., Tünnermann, J., Marchi, E., Eglinger, J., Zuin, J., Kryzhanovska, M., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01232-7 · Cited by 269 · see citing works

Mustache: multi-scale detection of chromatin loops from Hi-C and Micro-C maps using scale-space representation

Roayaei Ardakany, A., Gezer, H. T., Lonardi, S., & Ay, F. (2020) · Genome Biology · doi:10.1186/s13059-020-02167-0 · Cited by 250 · see citing works

Transcription shapes 3D chromatin organization by interacting with loop extrusion

Banigan, E. J., Tang, W., van den Berg, A. A., Stocsits, R. R., Wutz, G., Brandão, H. B., Busslinger, G. A., Peters, J., & Mirny, L. A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210480120 · Cited by 216 · see citing works

Cryo-EM structure of the human cohesin-NIPBL-DNA complex

Shi, Z.-B., Gao, H.-S., Bai, X.-C., & Yu, H.-T. (2020) · Science · doi:10.1126/science.abb0981 · Cited by 196 · see citing works

Molecular basis of CTCF binding polarity in genome folding

Nora, E. P., Caccianini, L., Fudenberg, G., So, K., Kameswaran, V., Nagle, A., Uebersohn, A., Hajj, B., Saux, A. L., Coulon, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19283-x · Cited by 206 · see citing works

Chromosome Conformation Capture and Beyond: Toward an Integrative View of Chromosome Structure and Function

McCord, R. P., Kaplan, N., & Giorgetti, L. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.021 · Cited by 204 · see citing works

Chromatin arranges in chains of mesoscale domains with nanoscale functional topography independent of cohesin

Miron, E., Oldenkamp, R., Brown, J. M., Pinto, D. M. S., Xu, C. S., Faria, A. R., Shaban, H. A., Rhodes, J. D. P., Innocent, C., de Ornellas, S., et al. (2020) · Science Advances · doi:10.1126/sciadv.aba8811 · Cited by 200 · see citing works

Cohesin and condensin extrude DNA loops in a cell cycle-dependent manner

Golfier, S., Quail, T., Kimura, H., & Brugués, J. (2020) · eLife · doi:10.7554/elife.53885 · Cited by 184 · see citing works

Regulation of single-cell genome organization into TADs and chromatin nanodomains

Szabo, Q., Donjon, A., Jerković, I., Papadopoulos, G. L., Cheutin, T., Bonev, B., Nora, E. P., Bruneau, B. G., Bantignies, F., & Cavalli, G. (2020) · Nature Genetics · doi:10.1038/s41588-020-00716-8 · Cited by 184 · see citing works

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

Enhancer selectivity in space and time: from enhancer–promoter interactions to promoter activation

Yang, J. H., & Hansen, A. S. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00710-6 · Cited by 191 · see citing works

CTCF mediates dosage- and sequence-context-dependent transcriptional insulation by forming local chromatin domains

Huang, H., Zhu, Q., Jussila, A., Han, Y., Bintu, B., Kern, C., Conte, M., Zhang, Y., Bianco, S., Chiariello, A. M., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00863-6 · Cited by 187 · see citing works

Primary Role of the Nucleosome

Kornberg, R. D., & Lorch, Y. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.020 · Cited by 178 · see citing works

ESCO1 and CTCF enable formation of long chromatin loops by protecting cohesinSTAG1 from WAPL

Wutz, G., Ladurner, R., Hilaire, B. G. S., Stocsits, R. R., Nagasaka, K., Pignard, B., Sanborn, A. L., Tang, W., Várnai, C., Ivanov, M. P., et al. (2020) · eLife · doi:10.7554/elife.52091 · Cited by 167 · see citing works

Cohesin-Dependent and -Independent Mechanisms Mediate Chromosomal Contacts between Promoters and Enhancers

Thiecke, M. J., Wutz, G., Muhar, M., Tang, W., Bevan, S., Malysheva, V., Stocsits, R., Neumann, T., Zuber, J., Fraser, P., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107929 · Cited by 177 · see citing works

Enhancer–promoter contact formation requires RNAPII and antagonizes loop extrusion

Zhang, S., Übelmesser, N., Barbieri, M., & Papantonis, A. (2023) · Nature Genetics · doi:10.1038/s41588-023-01364-4 · Cited by 165 · see citing works

Bridging-induced phase separation induced by cohesin SMC protein complexes

Ryu, J., Bouchoux, C., Liu, H. W., Kim, E., Minamino, M., de Groot, R., Katan, A. J., Bonato, A., Marenduzzo, D., Michieletto, D., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe5905 · Cited by 163 · see citing works

WAPL maintains a cohesin loading cycle to preserve cell-type-specific distal gene regulation

Liu, N. Q., Maresca, M., van den Brand, T., Braccioli, L., Schijns, M. M. G. A., Teunissen, H., Bruneau, B. G., Nora, E. P., & de Wit, E. (2021) · Nature Genetics · doi:10.1038/s41588-020-00744-4 · Cited by 162 · see citing works

Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA

Kong, M., Cutts, E., Pan, D., Beuron, F., Kaliyappan, T., Xue, C., Morris, E. P., Musacchio, A., Vannini, A., & Greene, E. C. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.026 · Cited by 156 · see citing works

Building regulatory landscapes reveals that an enhancer can recruit cohesin to create contact domains, engage CTCF sites and activate distant genes

Rinzema, N. J., Sofiadis, K., Tjalsma, S. J. D., Verstegen, M. J. A. M., Oz, Y., Valdes-Quezada, C., Felder, A.-K., Filipovska, T., van der Elst, S., de Andrade dos Ramos, Z., et al. (2022) · Nature Structural &amp; Molecular Biology · doi:10.1038/s41594-022-00787-7 · Cited by 166 · see citing works

3D enhancer-promoter interactions and multi-connected hubs: Organizational principles and functional roles

Uyehara, C. M., & Apostolou, E. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112068 · Cited by 143 · see citing works

Simple biochemical features underlie transcriptional activation domain diversity and dynamic, fuzzy binding to Mediator

Sanborn, A. L., Yeh, B. T., Feigerle, J. T., Hao, C. V., Townshend, R. J. L., Aiden, E. L., Dror, R. O., & Kornberg, R. D. (2021) · eLife · doi:10.7554/elife.68068 · Cited by 158 · see citing works

Cohesin mediates DNA loop extrusion by a “swing and clamp” mechanism

Bauer, B. W., Davidson, I., Canena, D., Wutz, G., Tang, W., Litos, G., Horn, S., Hinterdorfer, P., & Peters, J. (2021) · Cell · doi:10.1016/j.cell.2021.09.016 · Cited by 142 · see citing works

Loop extrusion: theory meets single-molecule experiments

Banigan, E. J., & Mirny, L. A. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.04.011 · Cited by 160 · see citing works

Hi-C analyses with GENOVA: a case study with cohesin variants

van der Weide, R. H., van den Brand, T., Haarhuis, J. H. I., Teunissen, H., Rowland, B. D., & de Wit, E. (2021) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqab040 · Cited by 161 · see citing works

A Structure-Based Mechanism for DNA Entry into the Cohesin Ring

Higashi, T. L., Eickhoff, P., Sousa, J. S., Locke, J., Nans, A., Flynn, H. R., Snijders, A. P., Papageorgiou, G., O’Reilly, N., Chen, Z. A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.013 · Cited by 146 · see citing works

MCM complexes are barriers that restrict cohesin-mediated loop extrusion

Dequeker, B. J. H., Scherr, M. J., Brandão, H. B., Gassler, J., Powell, S. T., Gáspár, I., Flyamer, I. M., Lalic, A., Tang, W., Stocsits, R. R., et al. (2022) · Nature · doi:10.1038/s41586-022-04730-0 · Cited by 149 · see citing works

Chromosome organization by one-sided and two-sided loop extrusion

Banigan, E. J., van den Berg, A. A., Brandão, H. B., Marko, J. F., & Mirny, L. A. (2020) · eLife · doi:10.7554/elife.53558 · Cited by 146 · see citing works

Genome 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

Wapl repression by Pax5 promotes V gene recombination by Igh loop extrusion

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The Smc5/6 complex is a DNA loop-extruding motor

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