Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin

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

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915

WebLogo: A Sequence Logo Generator: Figure 1Preprint

Crooks, G. E., Hon, G. C., Chandonia, J., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,418

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 11,626

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

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix

Liebschner, D., Afonine, P. V., Baker, M. L., Bunkóczi, G., Chen, V. B., Croll, T. I., Hintze, B., Hung, L.-W., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 7,953

MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496

COSMIC: the Catalogue Of Somatic Mutations In Cancer

Tate, J. G., Bamford, S., Jubb, H. C., Sondka, Z., Beare, D. M., Bindal, N., Boutselakis, H., Cole, C. G., Creatore, C., Dawson, E., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1015 · Cited by 4,867

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 4,759

MolProbity: More and better reference data for improved all‐atom structure validation

Williams, C. J., Headd, J. J., Moriarty, N. W., Prisant, M. G., Videau, L. L., Deis, L. N., Verma, V., Keedy, D. A., Hintze, B. J., Chen, V. B., et al. (2018) · Protein Science · doi:10.1002/pro.3330 · Cited by 4,599

ClinVar: improving access to variant interpretations and supporting evidence

Landrum, M. J., Lee, J. M., Benson, M., Brown, G. R., Chao, C., Chitipiralla, S., Gu, B., Hart, J., Hoffman, D., Jang, W., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1153 · Cited by 4,196

Accurate proteome-wide missense variant effect prediction with AlphaMissense

Cheng, J., Novati, G., Pan, J., Bycroft, C., Žemgulytė, A., Applebaum, T., Pritzel, A., Wong, L. H., Zielinski, M., Sargeant, T., et al. (2023) · Science · doi:10.1126/science.adg7492 · Cited by 2,163

Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs

Bepler, T., Morin, A., Rapp, M., Brasch, J., Shapiro, L. S., Noble, A. J., & Berger, B. (2019) · Nature Methods · doi:10.1038/s41592-019-0575-8 · Cited by 1,620

New tools for automated cryo-EM single-particle analysis in RELION-4.0

Kimanius, D., Dong, L., Sharov, G., Nakane, T., & Scheres, S. H. W. (2021) · Biochemical Journal · doi:10.1042/bcj20210708 · Cited by 1,029

A distinct replication fork protection pathway connects Fanconi anemia tumor suppressors to RAD51-BRCA1/2

Schlacher, K., Wu, H., & Jasin, M. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.015 · Cited by 936

A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis

Zivanov, J., Nakane, T., & Scheres, S. H. W. (2018) · IUCrJ · doi:10.1107/s205225251801463x · Cited by 879

Purified human BRCA2 stimulates RAD51-mediated recombination

Jensen, R. B., Carreira, A., & Kowalczykowski, S. C. (2010) · Nature · doi:10.1038/nature09399 · Cited by 715

Insights into DNA recombination from the structure of a RAD51–BRCA2 complex

Pellegrini, L., Yu, D. S., Lo, T., Anand, S., Lee, M., Blundell, T. L., & Venkitaraman, A. R. (2002) · Nature · doi:10.1038/nature01230 · Cited by 704

Human Rad51 Protein Promotes ATP-Dependent Homologous Pairing and Strand Transfer Reactions In Vitro

Baumann, P., Benson, F. E., & West, S. C. (1996) · Cell · doi:10.1016/s0092-8674(00)81394-x · Cited by 689

RecA homologs Dmc1 and Rad51 interact to form multiple nuclear complexes prior to meiotic chromosome synapsis

Bishop, D. K. (1994) · Cell · doi:10.1016/0092-8674(94)90038-8 · Cited by 480

Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA.

Benson, F. E., Stasiak, A., & West, S. C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06914.x · Cited by 455

Disruption of Mouse RAD54 Reduces Ionizing Radiation Resistance and Homologous Recombination

Essers, J., Hendriks, R. W., Swagemakers, S. M. A., Troelstra, C., de Wit, J., Bootsma, D., Hoeijmakers, J. H. J., & Kanaar, R. (1997) · Cell · doi:10.1016/s0092-8674(00)80199-3 · Cited by 435

Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase

Yin, J., Straight, P. D., McLoughlin, S. M., Zhou, Z., Lin, A. J., Golan, D. E., Kelleher, N. L., Kolter, R., & Walsh, C. T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507705102 · Cited by 408

Measurement of atom resolvability in cryo-EM maps with Q-scores

Pintilie, G. D., Zhang, K., Su, Z., Li, S., Schmid, M. F., & Chiu, W. (2020) · Nature Methods · doi:10.1038/s41592-020-0731-1 · Cited by 404

BRCA1–BARD1 promotes RAD51-mediated homologous DNA pairing

Zhao, W., Steinfeld, J. B., Liang, F., Chen, X., Maranon, D. G., Jian Ma, C., Kwon, Y., Rao, T., Wang, W., Sheng, C., et al. (2017) · Nature · doi:10.1038/nature24060 · Cited by 393

The consequences of Rad51 overexpression for normal and tumor cells

Klein, H. L. (2008) · DNA repair · doi:10.1016/j.dnarep.2007.12.008 · Cited by 357

Rad51 overexpression promotes alternative double-strand break repair pathways and genome instability

Richardson, C. A., Stark, J. M., Ommundsen, M., & Jasin, M. (2004) · Oncogene · doi:10.1038/sj.onc.1207098 · Cited by 255

Microtubule Disassembly by ATP-Dependent Oligomerization of the AAA Enzyme Katanin

Hartman, J. J., & Vale, R. D. (1999) · Science · doi:10.1126/science.286.5440.782 · Cited by 232

Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing

Puchades, C., Rampello, A. J., Shin, M., Giuliano, C. J., Wiseman, R. L., Glynn, S. E., & Lander, G. C. (2017) · Science · doi:10.1126/science.aao0464 · Cited by 223

Structural basis of homologous recombination

Sun, Y., McCorvie, T. J., Yates, L. A., & Zhang, X. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03365-1 · Cited by 175

Srs2 Disassembles Rad51 Filaments by a Protein-Protein Interaction Triggering ATP Turnover and Dissociation of Rad51 from DNA

Antony, E., Tomko, E. J., Xiao, Q., Krejčí, L., Lohman, T. M., & Ellenberger, T. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.05.026 · Cited by 170

Analysis of AlphaMissense data in different protein groups and structural context

Tordai, H., Torres, O., Csepi, M., Padányi, R., Lukács, G. L., & Hegedűs, T. (2024) · Scientific Data · doi:10.1038/s41597-024-03327-8 · Cited by 158

Rad51 Paralogs Remodel Pre-synaptic Rad51 Filaments to Stimulate Homologous Recombination

Taylor, M. R. G., Špı́rek, M., Chaurasiya, K. R., Ward, J. D., Carzaniga, R., Yu, X., Egelman, E. H., Collinson, L., Rueda, D., Krejčí, L., et al. (2015) · Cell · doi:10.1016/j.cell.2015.06.015 · Cited by 156

Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange

Xu, J., Zhao, L., Xu, Y., Zhao, W., Sung, P., & Wang, H. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3336 · Cited by 155

Recombination activities of HsDmc1 protein, the meiotic human homolog of RecA protein

Li, Z., Golub, E. I., Gupta, R. C., & Radding, C. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11221 · Cited by 142

Mechanism for remodelling of the cell cycle checkpoint protein MAD2 by the ATPase TRIP13

Alfieri, C., Chang, L., & Barford, D. (2018) · Nature · doi:10.1038/s41586-018-0281-1 · Cited by 128

The AAA+ superfamily: a review of the structural and mechanistic principles of these molecular machines

Khan, Y. A., White, K. I., & Brünger, A. T. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1979460 · Cited by 128

Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase

Monroe, N., Han, H., Shen, P. S., Sundquist, W. I., & Hill, C. P. (2017) · eLife · doi:10.7554/elife.24487 · Cited by 120

Multi-invasions Are Recombination Byproducts that Induce Chromosomal Rearrangements

Piazza, A., Wright, W. D., & Heyer, W. (2017) · Cell · doi:10.1016/j.cell.2017.06.052 · Cited by 119

FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination

Fernandes, J. B., Duhamel, M., Seguéla-Arnaud, M., Froger, N., Girard, C., Choinard, S., Solier, V., De Winne, N., De Jaeger, G., Gevaert, K., et al. (2018) · PLOS Genetics · doi:10.1371/journal.pgen.1007317 · Cited by 116 · cited 3×

FIGNL1-containing protein complex is required for efficient homologous recombination repair

Yuan, J., & Chen, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220662110 · Cited by 109

Katanin spiral and ring structures shed light on power stroke for microtubule severing

Zehr, E. A., Szyk, A., Piszczek, G., Szczęsna, E., Zuo, X., & Roll‐Mecak, A. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3448 · Cited by 106

FBH1 Helicase Disrupts RAD51 Filaments in Vitro and Modulates Homologous Recombination in Mammalian Cells

Šimandlová, J., Zagelbaum, J., Payne, M., Chu, W. K., Shevelev, I., Hanada, K., Chatterjee, S., Reid, D. A., Liu, Y., Janščák, P., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.484493 · Cited by 103

Swi2/Snf2-Related Translocases Prevent Accumulation of Toxic Rad51 Complexes during Mitotic Growth

Shah, P. P., Zheng, X., Epshtein, A., Carey, J. N., Bishop, D. K., & Klein, H. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.028 · Cited by 100

Overlapping Mechanisms Promote Postsynaptic RAD-51 Filament Disassembly during Meiotic Double-Strand Break Repair

Ward, J. D., Muzzini, D. M., Petalcorin, M. I. R., Martínez-Pérez, E., Martin, J. S., Plevani, P., Cassata, G., Marini, F., & Boulton, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.026 · Cited by 97

Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease

Puchades, C., Ding, B., Song, A. S., Wiseman, R. L., Lander, G. C., & Glynn, S. E. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.016 · Cited by 96

Mechanism of replication origin melting nucleated by CMG helicase assembly

Lewis, J. S., Gross, M. H., Sousa, J. S., Henrikus, S. S., Greiwe, J. F., Nans, A., Diffley, J. F. X., & Costa, A. (2022) · Nature · doi:10.1038/s41586-022-04829-4 · Cited by 96

The AAA+ ATPase TRIP13 remodels HORMA domains through N‐terminal engagement and unfolding

Ye, Q., Kim, D. H., Dereli, I., Rosenberg, S., Hagemann, G., Herzog, F., Tóth, A., Cleveland, D. W., & Corbett, K. D. (2017) · The EMBO Journal · doi:10.15252/embj.201797291 · Cited by 91

The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets

Han, H., Monroe, N., Sundquist, W. I., Shen, P. S., & Hill, C. P. (2017) · eLife · doi:10.7554/elife.31324 · Cited by 88

Structure and function of the RAD51B–RAD51C–RAD51D–XRCC2 tumour suppressor

Greenhough, L. A., Liang, C., Beláň, O., Kunzelmann, S., Maslen, S., Rodrigo-Brenni, M. C., Anand, R., Skehel, M. J., Boulton, S. J., & West, S. C. (2023) · Nature · doi:10.1038/s41586-023-06179-1 · Cited by 86

Minichromosome maintenance helicase activity is controlled by N- and C-terminal motifs and requires the ATPase domain helix-2 insert

Jenkinson, E. R., & Chong, J. P. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509297103 · Cited by 86

Two distinct conformational states define the interaction of human RAD51‐ATP with single‐stranded DNA

Brouwer, I., Moschetti, T., Candelli, A., Garcin, E. B., Modesti, M., Pellegrini, L., Wuite, G. J. L., & Peterman, E. J. G. (2018) · The EMBO Journal · doi:10.15252/embj.201798162 · Cited by 82

A fork in the road: Where homologous recombination and stalled replication fork protection part ways

Tye, S., Ronson, G. E., & Morris, J. R. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.07.004 · Cited by 80

Genome-wide phenotype analysis in ES cells by regulated disruption of Bloom's syndrome gene

Yusa, K., Horie, K., Kondoh, G., Kouno, M., Maeda, Y., Kinoshita, T., & Takeda, J. (2004) · Nature · doi:10.1038/nature02646 · Cited by 76

Single-molecule analysis reveals cooperative stimulation of Rad51 filament nucleation and growth by mediator proteins

Beláň, O., Barroso, C., Kaczmarczyk, A. P., Anand, R., Federico, S., O’Reilly, N., Newton, M. D., Mäeots, M.-E., Enchev, R. I., Martínez-Pérez, E., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.020 · Cited by 75

Human RAD51 paralogue SWSAP1 fosters RAD51 filament by regulating the anti-recombinase FIGNL1 AAA+ ATPase

MATSUZAKI, K., Kondo, S., Ishikawa, T., & Shinohara, A. (2019) · Nature Communications · doi:10.1038/s41467-019-09190-1 · Cited by 74

Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules

Zehr, E. A., Szyk, A., Szczęsna, E., & Roll‐Mecak, A. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.10.010 · Cited by 74

DNA binding and RAD51 engagement by the BRCA2 C-terminus orchestrate DNA repair and replication fork preservation

Kwon, Y., Rösner, H. I., Zhao, W., Selemenakis, P., He, Z., Kawale, A. S., Katz, J. N., Rogers, C. M., Neal, F. E., Shabestari, A. B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36211-x · Cited by 67

An allosteric network in spastin couples multiple activities required for microtubule severing

Sandate, C. R., Szyk, A., Zehr, E. A., Lander, G. C., & Roll‐Mecak, A. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0257-3 · Cited by 64

Mechanism of Vps4 hexamer function revealed by cryo-EM

Su, M., Guo, E. Z., Ding, X., Li, Y., Tarrasch, J. T., Brooks, C. L., Xu, Z., & Skiniotis, G. (2017) · Science Advances · doi:10.1126/sciadv.1700325 · Cited by 57

Structural insights into BCDX2 complex function in homologous recombination

Rawal, Y., Jia, L., Meir, A., Zhou, S., Kaur, H., Ruben, E. A., Kwon, Y., Bernstein, K. A., Jasin, M., Taylor, A. B., et al. (2023) · Nature · doi:10.1038/s41586-023-06219-w · Cited by 57

Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction

Wang, L., Myasnikov, A. G., Pan, X., & Walter, P. (2020) · eLife · doi:10.7554/elife.54031 · Cited by 55

A new class of ultrafine anaphase bridges generated by homologous recombination

Chan, Y. W., & West, S. C. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1515555 · Cited by 51

FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51 dynamics

Stok, C., Tsaridou, S., van den Tempel, N., Everts, M., Wierenga, E., Bakker, F. J., Kok, Y. P., Alves, I. T., Jae, L. T., Raas, M. W. D., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112668 · Cited by 37

Cryo-EM structures of RAD51 assembled on nucleosomes containing a DSB site

Shioi, T., Hatazawa, S., Oya, E., Hosoya, N., Kobayashi, W., Ogasawara, M., Kobayashi, T., Takizawa, Y., & Kurumizaka, H. (2024) · Nature · doi:10.1038/s41586-024-07196-4 · Cited by 37

FIGNL1 AAA+ ATPase remodels RAD51 and DMC1 filaments in pre-meiotic DNA replication and meiotic recombination

Ito, M., Furukohri, A., Matsuzaki, K., Fujita, Y., Toyoda, A., & Shinohara, A. (2023) · Nature Communications · doi:10.1038/s41467-023-42576-w · Cited by 32

Mechanism of AAA+ ATPase-mediated RuvAB–Holliday junction branch migration

Wald, J., Fahrenkamp, D., Goessweiner‐Mohr, N., Lugmayr, W., Ciccarelli, L., Vesper, O., & Marlovits, T. C. (2022) · Nature · doi:10.1038/s41586-022-05121-1 · Cited by 31

Rad51 filament dynamics and its antagonistic modulators

Carver, A., & Zhang, X. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.06.012 · Cited by 27

RAD51-associated Protein 1 (RAD51AP1) Interacts with the Meiotic Recombinase DMC1 through a Conserved Motif

Dunlop, M. H., Dray, E. V., Zhao, W., Tsai, M.-S., Wiese, C., Schild, D., & Sung, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.290015 · Cited by 23

FIGNL1-FIRRM is essential for meiotic recombination and prevents DNA damage-independent RAD51 and DMC1 loading

Zainu, A., Dupaigne, P., Bouchouika, S., Cau, J., Clément, J. A. J., Auffret, P., Ropars, V., Charbonnier, J., de Massy, B., Mercier, R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51458-8 · Cited by 22

FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association to promote viability after replication stress

Tischler, J. D., Tsuchida, H., Bosire, R., Oda, T. T., Park, A., & Adeyemi, R. O. (2024) · Nature Communications · doi:10.1038/s41467-024-45139-9 · Cited by 17

DNA helicases in homologous recombination repair

Branzei, D., & Szakál, B. (2021) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2021.06.009 · Cited by 15

FIRRM cooperates with FIGNL1 to promote RAD51 disassembly during DNA repair

Carpio, E. P., Dessapt, J., Beneyton, A., Sacre, L., Bérubé, M.-A., Villot, R., Lavoie, É. G., Coulombe, Y., Blondeau, A., Boulais, J., et al. (2023) · Science Advances · doi:10.1126/sciadv.adf4082 · Cited by 15

The FLIP-FIGNL1 complex regulates the dissociation of RAD51/DMC1 in homologous recombination and replication fork restart

Zhang, Q., Fan, J., Xu, W., Cao, H., Qiu, C. J., Xiong, Y., Zhao, H., Wang, Y., Huang, J., & Yu, C. Y. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad596 · Cited by 14

C1orf112 teams up with FIGNL1 to facilitate RAD51 filament disassembly and DNA interstrand cross-link repair

Zhou, Z., Yang, H., Liang, X., Zhou, T., Zhang, T., Yang, Y., Wang, J., & Wang, W. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112907 · Cited by 14

Human AAA+ ATPase FIGNL1 suppresses RAD51-mediated ultra-fine bridge formation

Matsuzaki, K., Shinohara, A., & Shinohara, M. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae263 · Cited by 12

A chemical genetics approach to examine the functions of AAA proteins

Cupido, T., Jones, N. H., Grasso, M. J., Pisa, R., & Kapoor, T. M. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00575-9 · Cited by 10

Interhomolog Homologous Recombination in Mouse Embryonic Stem Cells

Vanoli, F., Prakash, R., White, T., & Jasin, M. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0644-5_10 · Cited by 4

The FIGNL1-FIRRM complex is required to complete meiotic recombination in the mouse and prevents massive DNA damage-independent RAD51 and DMC1 loadingPreprint

Zainu, A., Pauline, D., Bouchouika, S., Cau, J., Clément, J. A. J., Auffret, P., Ropars, V., Charbonnier, J., de Massy, B., Mercier, R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.17.541096 · Cited by 4

Irinotecan alleviates chemoresistance to anthracyclines through the inhibition of AARS1-mediated BLM lactylation and homologous recombination repair

Li, X., Zhang, C., Mei, Y., Zhong, W., Fan, W. Q., Liu, L., Feng, Z., Bai, X., Liu, C., Xiao, M., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02302-y · Cited by 53

Structural mechanism of strand exchange by the RAD51 filament

Joudeh, L. I., Appleby, R. E., Maman, J. D., & Pellegrini, L. (2025) · eLife · doi:10.7554/elife.107114 · Cited by 24

A Metformin-Based Multifunctional Nanoplatform as a DNA Damage Amplifier for Maximized Radio-Immunotherapy to Overcome Radiotherapy Resistance

He, S., Huang, Y., Liu, J., Liu, H., Chen, Y., Zou, T., Sun, J., Wang, W.-Z., Wei, H., & Yu, C. (2025) · ACS Nano · doi:10.1021/acsnano.4c18627 · Cited by 20

RAD51-mediated homologous recombination is a pro-tumour driver pathway

López, B. S. (2025) · Oncogene · doi:10.1038/s41388-025-03583-x · Cited by 17

Cryo–electron microscopic visualization of RAD51 filament assembly and end-capping by XRCC3-RAD51C-RAD51D-XRCC2

Greenhough, L. A., Galanti, L., Liang, C., Boulton, S. J., & West, S. C. (2025) · Science · doi:10.1126/science.aea1546 · Cited by 15

Extensive homologous recombination safeguards oocyte genome integrity in mammals

Cao, H., Qiu, C., Fang, A., Shang, J., Xu, W., He, L., Duan, X., Zhang, Q., & Yu, C. Y. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1304 · Cited by 9

FIGNL1 inhibits homologous recombination in BRCA2 deficient cells by dissociating RAD51 filaments

Kuthethur, R., Safa Nasrin, V. Z., Sengodan, S. K., Fonseca, C., Braunshier, S., Nagar, N., Acharya, A., Wang, X., Theil, A. F., Ibini, O., et al. (2025) · Science · doi:10.1126/science.adt1210 · Cited by 9

The expanding roles of homologous recombination proteins in genome stability

Sassi, L., Marroquin, A. M., Waked, S., Ardizzoia, A., & Costanzo, V. (2026) · The EMBO Journal · doi:10.1038/s44318-025-00673-0 · Cited by 7

Distinct roles of RECQL5 in RAD51-mediated fork reversal and transcription elongation

Nagraj, T., Sahoo, S., Kadupatil, S., & Nagaraju, G. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1019 · Cited by 6

Subunit specialization in AAA+ proteins and substrate unfolding during transcription complex remodeling

Gao, F., Ye, F., Jovanovic, M., Buck, M., & Zhang, X. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2425868122 · Cited by 4

RAD51AP1 is a versatile RAD51 modulator

Kuhlen, L., Argunhan, B., Liang, P., Zhong, J., Masino, L., & Zhang, X. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2514728122 · Cited by 4

Structures and mechanisms of AAA+ protein complexes in DNA processing

Carver, A., Zhang, B., & Zhang, X. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103056 · Cited by 4

FIGNL1 hexamer dissociates RAD51-filament: a new mechanism

Kumar, R. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.01.002 · Cited by 3

FIGNL1 inhibits homologous recombination in BRCA2 deficient cells by dissociating RAD51 filamentsPreprint

Kuthethur, R., Acharya, A., Sengodan, S. K., Fonseca, C., Nagar, N., Safa Nasrin, V. Z., Ibini, O., Manolika, E. M., de Koning, K., Braunshier, S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.03.621741 · Cited by 2

A regulatory adaptor for RAD51’s AAA+ unfoldase promotes homologous recombination–mediated DNA repair and genome stability

Zhou, T., Pang, M., Liang, X., Zhou, Z., Yang, H., Cui, Y., Yu, S. J., Liang, L., Wang, P., Chen, Y., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2531632123 · Cited by 1

Reviewer #2 (Public review): Structural mechanism of strand exchange by the RAD51 filament

(2025) · eLife · doi:10.7554/elife.107114.1.sa2

Structural mechanism of strand exchange by the RAD51 filamentPreprint

Joudeh, L. I., Appleby, R. E., Maman, J. D., & Pellegrini, L. (2025) · eLife · doi:10.7554/elife.107114.1

Structural mechanism of strand exchange by the RAD51 filamentPreprint

Joudeh, L. I., Appleby, R. E., Maman, J. D., & Pellegrini, L. (2025) · eLife · doi:10.7554/elife.107114.2

Age-dependent accumulation of RAD51 on non-damaged chromosomes prevents chromosome segregation in mammalian oocytesPreprint

Ito, M., Soeda, S., Kondo, T., Furukohri, A., 梶谷, み., Ogata, R., Ohsugi, M., & Shinohara, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.18.712809

SIK2 drives cisplatin chemoresistance in BRAF-wild-type anaplastic thyroid cacner by phosphorylating AURKB to activate RAD51- dependent homologous recombinationPreprint

Sun, Z., Liang, M., Liu, X., Zhu, H., Zhang, J., Hu, P., Lin, B., Liang, X., Zhang, Z., Li, R., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9364108/v1

Mass Photometry Analysis of Membrane Proteins in Detergent Micelles

Cortiella-Valls, N., Cester, E., & Pérez, C. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5186-5_7

Distinct functions of mammalian RAD51 paralogs in genome maintenance

Dwivedi, H. K., Bhattacharya, D., Kadupatil, S., & Nagaraju, G. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250440

Distinct ways by which Srs2 helicase and Rrp1 translocase shape Rad51–DNA interactions in fission yeast

Misiorna, D., Dziadkowiec, D., & Kramarz, K. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag978

Temporal tuning of actin nucleation by the repurposed DNA repair complex RAD51/fignl1 encodes distinct axon guidance decisionsPreprint

Zerkoune, S., Zagar, Y., Delaroche, J., Danicka, J., Vougny, J., Uthayasuthan, S., Aureille, J., Roche, F., Haantjes, R., Gomez-Bravo, C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.17.759799

FIGNL1 hexamer dissociates RAD51-filament: a new mechanism

Kumar, R. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.01.002 · Cited by 3

Human AAA+ ATPase FIGNL1 suppresses RAD51-mediated ultra-fine bridge formation

Matsuzaki, K., Shinohara, A., & Shinohara, M. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae263 · Cited by 12

Structural and biochemical studies of RAD51 filament modulators

Carver, A. (2023) · doi:10.25560/130979

C1orf112 teams up with FIGNL1 to facilitate RAD51 filament disassembly and DNA interstrand cross-link repair

Zhou, Z., Yang, H., Liang, X., Zhou, T., Zhang, T., Yang, Y., Wang, J., & Wang, W. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112907 · Cited by 14

Human RAD51 paralogue SWSAP1 fosters RAD51 filament by regulating the anti-recombinase FIGNL1 AAA+ ATPase

MATSUZAKI, K., Kondo, S., Ishikawa, T., & Shinohara, A. (2019) · Nature Communications · doi:10.1038/s41467-019-09190-1 · Cited by 74