Affinage

RAD51

DNA repair protein RAD51 homolog 1 · UniProt Q06609

Round 2 corrected
Length
339 aa
Mass
37.0 kDa
Annotated
2026-04-28
130 papers in source corpus 58 papers cited in narrative 58 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RAD51 is a RecA-family recombinase that assembles ATP-dependent helical nucleoprotein filaments on single-stranded DNA to catalyze homology search and strand exchange, forming the central enzymatic activity of homologous recombination repair of DNA double-strand breaks, replication fork reversal, and nascent DNA protection (PMID:7988572, PMID:8929543, PMID:25733714, PMID:37104614). Filament nucleation on RPA-coated ssDNA is rate-limited and overcome by BRCA2, which chaperones preassembled RAD51 onto ssDNA, blocks RAD51 ATP hydrolysis to stabilize the active filament, and targets RAD51 to ssDNA over dsDNA (PMID:20729832, PMID:36976771, PMID:12442171); filament dynamics are further tuned by stimulatory cofactors (Rad54, HOP2-MND1, RAD51 paralogs, MMS22L-TONSL) and antagonists (Srs2, RADX, BLM) that respectively stabilize or dismantle filaments (PMID:12205100, PMID:24943459, PMID:12748644, PMID:33453169, PMID:27797818). Multiple post-translational modifications regulate RAD51 chromatin loading and activity, including Chk1-mediated T309 phosphorylation, TOPBP1/PLK1-mediated S14 phosphorylation, TOPORS-dependent SUMOylation at K57/K70, CDK-dependent phosphorylation of BRCA2-S3291 that gates the BRCA2–RAD51 interaction across the cell cycle, and PRDX1-maintained reduction of the redox-sensitive C319 residue (PMID:15665856, PMID:26811421, PMID:35061896, PMID:15800615, PMID:36058112).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1994 High

    Identifying RAD51 as a functional human RecA homolog resolved whether eukaryotes possess a dedicated strand-exchange recombinase: purified human RAD51 bound DNA, hydrolyzed ATP, unwound duplexes, and formed helical nucleoprotein filaments.

    Evidence Protein purification, ATPase assay, topological unwinding, electron microscopy of filaments

    PMID:7988572

    Open questions at the time
    • No strand exchange demonstrated yet
    • Cofactor requirements unknown
    • No in vivo functional proof
  2. 1996 High

    Demonstrating that human RAD51 catalyzes ATP-dependent homologous pairing and strand exchange in vitro established the core enzymatic activity of the protein, while revealing that its intrinsic rate is much lower than RecA and requires accessory factors for extensive heteroduplex formation.

    Evidence In vitro strand exchange assay with purified hRAD51 and RPA

    PMID:8929543 PMID:9012806

    Open questions at the time
    • Identity of required accessory factors unknown
    • Relationship between ATP hydrolysis and strand exchange kinetics unclear
  3. 1997 High

    Discovery of direct BRCA2–RAD51 and BRCA1–RAD51 interactions placed the hereditary breast cancer tumor suppressors in the homologous recombination pathway, with BRCA2's BRC repeats providing the molecular interface to RAD51.

    Evidence Co-immunoprecipitation, yeast two-hybrid mapping of BRC motifs to RAD51 residues 98–339, BRCA2-null mouse embryo phenotyping

    PMID:9008167 PMID:9126738 PMID:9405383

    Open questions at the time
    • How BRCA2 mechanistically promotes RAD51 activity unknown
    • Full-length BRCA2 not yet purified
    • BRCA1's direct role vs. indirect scaffolding unclear
  4. 1998 High

    ATP/Mg²⁺-induced conformational switching of RAD51 and its accumulation at UV-damaged chromatin during S phase established that RAD51 adopts a catalytically competent conformation upon nucleotide binding and functions in the context of DNA replication.

    Evidence Circular dichroism spectroscopy, equilibrium dialysis, UV microirradiation with BrdU fractionation

    PMID:10908572 PMID:9718317

    Open questions at the time
    • Structural basis of conformational change unknown
    • Whether RAD51 foci represent active filaments unclear
  5. 2000 High

    Placing γ-H2AX upstream of RAD51 focus formation and identifying RAD51 paralog complexes (RAD51B/C/D, XRCC2/3) defined the signaling hierarchy: PI-3 kinase–dependent H2AX phosphorylation is required for RAD51 recruitment, and paralog sub-complexes act as mediators.

    Evidence Wortmannin inhibition of γ-H2AX abolishes RAD51 foci; yeast two/three-hybrid and baculovirus co-expression of paralog complexes

    PMID:10749867 PMID:10959836

    Open questions at the time
    • Direct mechanism by which paralogs load RAD51 unknown
    • Paralog complex stoichiometry undefined
  6. 2002 High

    Crystal structure of the BRC repeat–RAD51 complex revealed that BRC mimics the RAD51 protomer–protomer interface, explaining how BRCA2 controls filament assembly; concurrently, RPA's postsynaptic role in stabilizing strand exchange products and Rad54's ATP-dependent cooperation with RAD51 were mechanistically dissected.

    Evidence X-ray crystallography of BRC–RAD51; in vitro strand exchange with RPA deproteinization controls; Rad54 supercoiling/branch migration assays

    PMID:12169690 PMID:12205100 PMID:12442171

    Open questions at the time
    • Full-length BRCA2 not structurally resolved
    • How individual BRC repeats differ in function unclear
    • Rad54's in vivo contribution to branch migration not tested
  7. 2003 High

    Discovery that Srs2 helicase dismantles RAD51 presynaptic filaments established the first anti-recombination mechanism targeting RAD51 directly, providing a framework for understanding how inappropriate recombination is prevented.

    Evidence In vitro reconstitution with purified Srs2 and Rad51; filament disruption assay

    PMID:12748644

    Open questions at the time
    • Human Srs2 functional ortholog not identified
    • Whether Rad52 can counteract Srs2 unknown
  8. 2005 High

    Multiple regulatory inputs were identified: CDK phosphorylation of BRCA2-S3291 gates RAD51 binding across the cell cycle, Chk1 phosphorylation of RAD51-T309 is required for damage-induced focus formation, and MDC1 retains RAD51 on chromatin—collectively establishing that RAD51 is regulated by checkpoint kinases, CDK, and chromatin adaptor proteins.

    Evidence Phospho-specific antibodies, cell-cycle fractionation, in vitro kinase assays, siRNA, RAD51-T309A mutagenesis, MDC1 FHA-domain mapping

    PMID:15665856 PMID:15800615 PMID:16186822

    Open questions at the time
    • Interplay between T309 and S14 phosphorylation not explored
    • Whether CDK-BRCA2-S3291 is the sole cell-cycle switch unclear
  9. 2010 High

    Purification of full-length BRCA2 finally demonstrated its direct biochemical mechanism: BRCA2 nucleates RAD51 filaments by targeting RAD51 to ssDNA, displacing RPA, and blocking RAD51's ATP hydrolysis to stabilize the active filament; concurrently, DNA fiber analysis separated RAD51's fork restart function from its HR repair function.

    Evidence Full-length BRCA2 purification with in vitro strand exchange, filament stability, and RPA displacement assays; DNA fiber assay in XRCC3-mutant and siRAD51 cells

    PMID:20188668 PMID:20729832

    Open questions at the time
    • Whether BRCA2 forms a stoichiometric or catalytic complex with RAD51 unclear
    • Structural basis of BRCA2 blocking ATP hydrolysis unknown
  10. 2015 High

    RAD51-mediated replication fork reversal was established as a global cellular response to genotoxic stress, and RAD51 paralog complexes were shown to remodel presynaptic filaments into an 'open' conformation that facilitates strand exchange, defining the structural output of paralog action.

    Evidence EM of replication fork architecture in human cells after RAD51 depletion; single-molecule FRET and EM of RFS-1/RIP-1 filament remodeling in C. elegans

    PMID:25733714 PMID:26186187

    Open questions at the time
    • Whether human RAD51B-C or RAD51C-XRCC3 remodel filaments analogously unknown
    • Specific RAD51 domains required for fork reversal not mapped
  11. 2018 High

    RADX was identified as a ssDNA-binding antagonist of RAD51 at stalled forks, and Rad52 was shown to protect Rad51 filaments from Srs2 disruption—together establishing that the balance between filament stabilizers and destabilizers determines fork protection versus degradation.

    Evidence DNA fiber assays across BRCA1/2- and FA-deficient backgrounds with RADX silencing; separation-of-function Rad52 mutants with Srs2 disruption assay in vitro and in vivo

    PMID:29985128 PMID:30021152

    Open questions at the time
    • Whether RADX acts identically at DSB-associated ssDNA unclear
    • Human RAD52's filament-protective role not directly tested
  12. 2021 High

    Mechanistic dissection of RADX revealed it directly binds ATP-bound RAD51 and stimulates its ATPase to destabilize filaments; MMS22L-TONSL was shown to limit RAD51 dsDNA binding to promote productive ssDNA filament formation; and conditional RAD51 knockout in mice demonstrated essential roles in spermatogonial maintenance and meiotic crossover formation.

    Evidence In vitro ATPase/strand exchange with RADX and RAD51; iPOND and reconstitution with MMS22L-TONSL; Vasa-Cre and UBC-CreERT2 conditional knockouts in mouse germ cells

    PMID:27797818 PMID:33453169 PMID:35292640

    Open questions at the time
    • RADX structural basis of RAD51 interaction unknown
    • MMS22L-TONSL mechanism of ssDNA selectivity not structurally explained
  13. 2022 High

    Two new regulatory layers were discovered: TOPORS SUMOylates RAD51 at K57/K70 downstream of ATM to promote chromatin loading and BRCA2 interaction, and PRDX1 maintains RAD51-C319 in a reduced state required for DNA binding, establishing redox and SUMO control of filament competence.

    Evidence SUMO modification assays with TOPORS, SUMOylation-deficient RAD51-K57R/K70R mutants, HR reporter; sulfenylation probes, PRDX1-deficient cells, RAD51-C319 mutagenesis, molecular dynamics

    PMID:35061896 PMID:36058112

    Open questions at the time
    • Interplay between SUMOylation and phosphorylation of RAD51 not characterized
    • Whether C319 oxidation occurs under physiological oxidative stress in vivo not established
  14. 2023 High

    Cryo-EM structures resolved how BRCA2's TR2 motif braces adjacent RAD51 protomers across the filament interface and how RAD51 Loop2 residues V273/D274 enforce mismatch intolerance during strand exchange; in vivo imaging revealed nucleus-spanning RAD51 filaments that undergo Rad54/Srs2-modulated compaction-extension cycles to conduct homology search; and RAD51 strand exchange activity was shown to bypass the CMG helicase at stalled forks to initiate fork reversal.

    Evidence Cryo-EM of BRCA2-TR2–RAD51 and RAD51/DMC1–DNA complexes; live-cell single-molecule imaging of tagged Rad51 filaments; auxin-inducible CMG depletion with EM and fiber assays

    PMID:34871438 PMID:37104614 PMID:37605042 PMID:37919288

    Open questions at the time
    • Full cryo-EM structure of BRCA2-loaded RAD51 filament not yet available
    • How filament compaction-extension is coordinated with chromatin architecture unknown
    • Structural basis of CMG bypass not resolved
  15. 2024 High

    RAD51 was found to specifically recognize and protect abasic sites in ssDNA from MRE11-RAD50 nucleolytic cleavage, expanding its fork-protection function beyond simple ssDNA coating to lesion-specific shielding of damaged replication intermediates.

    Evidence Cryo-EM of RAD51 on abasic DNA, Xenopus egg extract fork protection assays, human cell experiments with APE1/MRE11 cleavage readouts

    PMID:39178838

    Open questions at the time
    • Whether other DNA lesion types are similarly recognized by RAD51 unknown
    • In vivo frequency and genomic distribution of abasic-site protection events not determined

Open questions

Synthesis pass · forward-looking unresolved questions
  • A comprehensive structural model of full-length BRCA2 bound to a complete RAD51 nucleoprotein filament during active strand exchange remains unresolved, as does the precise mechanism by which RAD51 filament dynamics are spatially coordinated with chromatin topology and replication fork architecture in mammalian cells.
  • No full-length BRCA2–RAD51 filament structure available
  • Structural basis of RAD51's CMG bypass mechanism unresolved
  • How multiple PTMs are integrated in space and time during a single repair event is unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140657 ATP-dependent activity 5 GO:0003677 DNA binding 4 GO:0140097 catalytic activity, acting on DNA 4
Localization
GO:0005634 nucleus 5 GO:0005694 chromosome 4
Pathway
R-HSA-73894 DNA Repair 7 R-HSA-69306 DNA Replication 5 R-HSA-1474165 Reproduction 2 R-HSA-1640170 Cell Cycle 2
Partners
BRCA1BRCA2HELQMMS22LRAD52RAD54LRADXTOPORS
Complex memberships
BRCA1-BRCA2-RAD51 complexRAD51 nucleoprotein filament

Evidence

Reading pass · 58 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 Human RAD51 protein binds single- and double-stranded DNA, exhibits DNA-dependent ATPase activity, underwinds duplex DNA in an ATP-dependent reaction, and forms helical nucleoprotein filaments on nicked duplex DNA resembling RecA/yeast Rad51 filaments, establishing it as a functional RecA homolog. Protein purification, ATPase assay, topological unwinding assay, electron microscopy The EMBO journal High 7988572
1996 Human RAD51 promotes ATP-dependent homologous pairing and strand exchange reactions in vitro; joint molecule formation requires ATP hydrolysis and DNA homology and is stimulated by RPA; hRad51 initiates strand exchange but requires additional proteins for extensive heteroduplex formation. In vitro strand exchange assay with purified proteins, ATP hydrolysis measurement Cell High 8929543
1997 Human RAD51 (HsRad51) promotes homologous pairing and strand exchange at rates less than 1/10 those of RecA; in the presence of ATP-γ-S, HsRad51 forms stable presynaptic complexes and promotes renaturation but not strand exchange or homologous pairing with duplex DNA, suggesting homologous pairing and strand exchange are more closely linked to ATP hydrolysis in HsRad51 than in RecA. In vitro recombination assays, ATP hydrolysis assays, stoichiometry of DNA binding Proceedings of the National Academy of Sciences of the United States of America High 9012806
1997 BRCA1 colocalizes with RAD51 in discrete nuclear foci during S phase and the two proteins co-immunoprecipitate; BRCA1 residues 758–1064 form RAD51-containing complexes in vitro; both proteins associate with developing synaptonemal complexes in meiotic cells, indicating a functional interaction in DNA repair and recombination. Co-immunoprecipitation, immunofluorescence co-localization, in vitro binding, meiotic chromosome spreads Cell High 9008167
1997 RAD51 interacts specifically with the eight BRC motifs encoded in exon 11 of BRCA2; RAD51 residues 98–339 are sufficient to interact with the 59-residue minimal conserved BRC motif, mapping the molecular interface between RAD51 and BRCA2. Yeast two-hybrid, biochemical deletion analysis The Journal of biological chemistry High 9405383
1997 BRCA2 protein physically interacts with RAD51 during mouse embryogenesis; Brca2-deficient embryos show developmental arrest and radiation hypersensitivity mediated by RAD51, indicating BRCA2 is an essential cofactor in RAD51-dependent repair of double-strand breaks. Co-immunoprecipitation, mouse knockout, radiation sensitivity assay Nature High 9126738
1998 ATP and Mg2+ binding induces a conformational change in Rad51 detected by circular dichroism spectroscopy, producing a more structured state; this active conformation is required for DNA binding; ATP-γ-S also stabilizes activity but AMP-PNP does not, and DNA significantly increases Rad51's affinity for ATP. Equilibrium dialysis (nucleotide binding), circular dichroism spectroscopy, thermal inactivation assay Biochemistry High 9718317
1998 BRCA2 gene product forms in vivo complexes with both p53 and RAD51 as a nuclear phosphoprotein; exogenous BRCA2 inhibits p53 transcriptional activity and RAD51 co-expression enhances this effect, placing BRCA2 at the intersection of cell cycle control and DNA repair via RAD51. Co-immunoprecipitation in vivo, nuclear fractionation, transcriptional reporter assay Proceedings of the National Academy of Sciences of the United States of America Medium 9811893
1998 RAD51 accumulates at sites of UV-induced DNA damage in human S-phase cells and is preferentially associated with postreplicative (rather than actively replicating) chromatin, demonstrating that RAD51 redistribution to damaged chromatin occurs from pre-existing S-phase foci. UV microirradiation, BrdU/IdU dual-label fractionation, immunofluorescence microscopy The Journal of cell biology High 10908572
2000 Human RAD51 paralogs XRCC2, XRCC3, RAD51B, RAD51C, and RAD51D form simultaneous protein interactions; yeast three-hybrid experiments show several pairs interact concurrently (e.g., RAD51B enhances RAD51C binding to XRCC3 and RAD51D); baculovirus co-expression confirms multi-subunit complex formation, suggesting these paralogs assemble into one or more complexes. Yeast two-hybrid, yeast three-hybrid, His-tag pull-down from baculovirus co-expression The Journal of biological chemistry High 10749867
2000 Gamma-H2AX phosphorylation after DNA double-strand breaks is necessary for recruitment of RAD51 (and RAD50, BRCA1) to nuclear foci; wortmannin (PI-3 kinase inhibitor) prevents gamma-H2AX formation and abolishes RAD51 focus formation, placing PI-3 kinase signaling and H2AX upstream of RAD51 recruitment. Immunofluorescence, wortmannin inhibition, laser-induced DSBs in human cells Current biology : CB High 10959836
2000 Mammalian Rad51 and Rad52 co-localize in distinct nuclear foci upon DNA damage in murine cells expressing GFP-Rad52; cells expressing GFP-Rad52 show increased survival and increased Rad51 foci, indicating Rad52 is limiting for Rad51-mediated repair and the two proteins function together in the DNA damage response. GFP-Rad52 live-cell imaging, immunofluorescence, survival assay EMBO reports Medium 11256631
2001 BRCA2 plays a dual role in regulating RAD51: BRC3 and BRC4 repeats block RAD51 nucleoprotein filament formation; cancer-associated BRC3 mutations abolish this effect; additionally, BRCA2 controls nuclear import of RAD51, with a cancer-associated BRCA2 truncation causing defective nuclear RAD51 localization. In vitro filament formation assays, nuclear transport assays, cancer mutation analysis Molecular cell High 11239456
2001 HsRad51 is required for triplex-induced intermolecular recombination between plasmid targets in human cell-free extracts; depletion of HsRad51 with specific antibodies diminishes triplex-induced recombination and supplementation with purified HsRad51 restores it. Cell-free extract reconstitution, antibody depletion, purified protein supplementation The Journal of biological chemistry Medium 11278954
2002 Crystal structure of a BRC repeat–RAD51 RecA-homology domain complex reveals that the BRC repeat mimics the RAD51 oligomerization interface, enabling BRCA2 to control RAD51 nucleoprotein filament assembly; cancer-associated BRC mutations disrupt predicted RAD51 contacts. X-ray crystallography, structure-guided mutational analysis Nature High 12442171
2002 Human Rad54 promotes transient strand separation in duplex DNA via ATP hydrolysis-driven DNA supercoiling; its ATPase, supercoiling, and strand-opening activities are greatly stimulated by interaction with hRad51; hRad51 and hRad54 functionally cooperate in the homologous DNA pairing reaction. In vitro ATPase assay, DNA supercoiling assay, strand opening assay, homologous pairing assay with purified proteins The Journal of biological chemistry High 12205100
2002 FANCD2 co-localizes with RAD51 in S-phase-specific nuclear foci upon DNA damage; monoubiquitination of FANCD2 is required for this co-localization and for normal cell-cycle progression after mitomycin C exposure, placing FANCD2 in the same S-phase repair pathway as RAD51. Immunofluorescence co-localization, cell-cycle fractionation, FA mutant cell analysis Blood Medium 12239151
2002 RPA stabilizes RAD51-generated DNA pairing intermediates in a critical postsynaptic role during strand exchange; RPA binds the displaced strand to stabilize pairing, whereas its presynaptic role in facilitating filament formation is minimal under conditions that minimize ssDNA secondary structure. In vitro strand exchange assay with purified Rad51 and RPA, deproteinization controls The Journal of biological chemistry High 12169690
2003 Yeast DNA helicase Srs2 binds Rad51, possesses robust ssDNA-stimulated ATPase activity, and at catalytic quantities causes severe inhibition of Rad51-mediated recombination by dislodging Rad51 from ssDNA, thereby dismantling the presynaptic filament. In vitro ATPase assay, Rad51 filament disruption assay, pulldown Nature High 12748644
2003 Rad52 forms complexes with Rad51, RPA, and Rad59; Rad51-Rad52-Rad59 and RPA-Rad52-Rad59 complexes depend on Rad52 for formation; the N-terminal Rad52 self-interaction domain is required for Rad59 interaction, implicating distinct Rad52 complexes in conservative and single-strand annealing recombination pathways. Co-immunoprecipitation, two-hybrid, in vitro binding DNA repair Medium 13679150
2005 RAD51 focus formation in response to ionizing radiation is dependent on BRCA2 and the five RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, XRCC3), whereas spontaneous S-phase RAD51 foci form without requiring these factors, revealing two distinct modes of RAD51 nuclear focus assembly. Immunofluorescence in paralog/BRCA2-deficient cell lines, DNA damage-induced focus assay Philosophical transactions of the Royal Society of London. Series B, Biological sciences High 15065660
2005 BRCA2 BRC repeats (BRC3/BRC4) at low concentrations bind and form stable complexes with RAD51-DNA nucleoprotein filaments; BRC3 contacts the N-terminal domain of RAD51 while BRC4 contacts the nucleotide-binding core, demonstrating nonequivalent and distinct binding modes within the filament. Electron microscopy of RAD51-DNA filaments with BRC peptides, cryo-EM image reconstruction Proceedings of the National Academy of Sciences of the United States of America High 15937124
2005 CDK-mediated phosphorylation of BRCA2 at serine 3291 during late cell cycle blocks the C-terminal BRCA2–RAD51 interaction; this phosphorylation is low in S phase when recombination is active and increases toward mitosis; DNA damage decreases S3291 phosphorylation to re-enable RAD51 binding, providing a molecular switch for recombination regulation. Phospho-specific antibody, cell-cycle fractionation, in vitro kinase assay, co-immunoprecipitation Nature High 15800615
2005 Chk1 interacts with RAD51 and phosphorylates RAD51 on Thr309 in a Chk1-dependent manner; loss of Chk1 by siRNA or chemical inhibition abolishes RAD51 focus formation after hydroxyurea; a phosphorylation-deficient RAD51(T309A) mutant causes hydroxyurea hypersensitivity, establishing Chk1 as a regulator of RAD51-mediated homologous recombination repair. Co-immunoprecipitation, phospho-specific antibody, siRNA, chemical inhibitors, RAD51-T309A mutant phenotyping Nature cell biology High 15665856
2005 BRCA2 and BRCA1 form a stable biochemical complex that co-localizes with RAD51 at replication sites after hydroxyurea or UV damage in S-phase cells and on synaptonemal complexes in meiosis, placing both tumor suppressors together in the same RAD51-mediated repair pathway. Co-immunoprecipitation, immunofluorescence co-localization, meiotic chromosome spreads Molecular cell High 9774970
2005 MDC1 directly interacts with RAD51 through its forkhead-associated (FHA) domain; MDC1 knockdown impairs RAD51 focus formation after ionizing radiation, reduces nuclear and chromatin-bound RAD51, and increases RAD51 protein degradation, indicating MDC1 retains RAD51 in chromatin to facilitate homologous recombination. Co-immunoprecipitation, siRNA knockdown, chromatin fractionation, immunofluorescence Nature structural & molecular biology High 16186822
2006 The L1 loop residue Tyr232 of human RAD51 is critical for DNA binding; alanine or conservative tryptophan substitution significantly decreases DNA-binding ability without affecting protein folding or salt-induced ATPase; fluorescence spectroscopy confirms L1 and L2 loops are positioned near the DNA-binding site. Site-directed mutagenesis, gel retardation assay, DNA-dependent ATPase assay, fluorescence spectroscopy The FEBS journal High 16780572
2007 Both Rad51 ATPase activity and Rad54 ATPase activity are required for efficient Rad51 turnover from dsDNA (product dissociation); the Rad54 ATPase is stimulated by partial Rad51 filaments on dsDNA; the Rad51-K191R Walker-box mutant has increased filament stability and defective dsDNA binding, demonstrating that Rad51's own ATPase activity is needed for normal presynaptic and postsynaptic filament dynamics. In vitro ATPase kinetics, electron microscopy of filaments, Walker-box mutant analysis Nucleic acids research High 17567608
2008 Human Rad51 specifically inhibits Rad52-mediated annealing of complementary ssDNA in an ATP-dependent manner via a direct Rad51–Rad52 interaction; the Rad51 nucleoprotein filament is more inhibitory than free Rad51; Rad59 partially restores Rad52-dependent annealing in the presence of Rad51, suggesting Rad51 channels repair toward strand invasion over annealing. In vitro ssDNA annealing assay, protein interaction analysis, ATP dependency experiments The Journal of biological chemistry High 18337252
2008 Human Rad51 stimulates branch migration activity of human Rad54 through specific protein–protein interactions; the active (ATP-bound) Rad51 filament conformation is more stimulatory than the inactive form; this stimulation is evolutionarily conserved (also seen with yeast proteins), indicating Rad51 allosterically regulates Rad54's branch migration function. In vitro branch migration assay, protein–protein interaction analysis, yeast and human protein comparison The Journal of biological chemistry High 18617519
2009 Human PSF directly interacts with RAD51 via its N-terminal region and modulates RAD51 activity in a concentration-dependent manner: PSF enhances RAD51-mediated homologous pairing and strand exchange at low RAD51 concentrations but inhibits these activities at optimal RAD51 concentrations, suggesting dual regulatory roles. Co-immunoprecipitation/pulldown, in vitro homologous pairing assay, strand exchange assay, deletion analysis Nucleic acids research Medium 19447914
2010 Purified full-length BRCA2 binds RAD51 and stimulates RAD51-mediated recombination by: (1) targeting RAD51 to ssDNA over dsDNA, (2) enabling RAD51 to displace RPA from ssDNA, and (3) stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. BRCA2 does not directly catalyze ssDNA annealing. Full-length BRCA2 purification, in vitro strand exchange assay, filament stability assay, RPA displacement assay Nature High 20729832
2010 RAD51 mediates two distinct replication responses: stalled replication forks (HU short-term) are restarted in a RAD51-dependent, XRCC3-dependent manner without triggering HR; collapsed forks (prolonged HU) undergo RAD51-dependent HR repair without apparent restart, showing that restart and repair represent distinct RAD51 pathways. DNA fiber assay, siRNA knockdown, XRCC3 mutant cells, RAD51 focus formation Molecular cell High 20188668
2011 In budding yeast, Rad51 is phosphorylated on Ser192 primarily by the checkpoint kinase Mec1 in response to DNA damage; Rad51-S192A or S192E mutations confer DNA damage hypersensitivity and HR defects; Ser192 is required for Rad51 ATPase activity and DNA binding in vitro but not for multimer formation. Mass spectrometry phosphosite identification, in vitro kinase assay, HR assay, ATPase assay, DNA binding assay EMBO reports High 21738226
2014 HOP2-MND1 heterodimer acts as a 'molecular trigger' of RAD51 by inducing conformational changes that enhance RAD51's interaction with nucleotide cofactors, modify DNA-binding specificity, enable strand exchange without divalent metal ions, offset K133A ATP-binding mutation defects, restrict dsDNA binding during filament formation, and promote dsDNA binding during homology search. In vitro strand exchange assay, nucleotide binding assay, ssDNA/dsDNA binding assay with HOP2-MND1 and mutant RAD51 Nature communications High 24943459
2015 RAD51-mediated replication fork reversal is a global response to diverse genotoxic treatments in human cells; electron microscopy of replication fork architecture shows uncoupling and reversal are frequent; RAD51 is present at replication forks independently of breakage; fork reversal is RAD51-dependent and antagonized by PARP/RECQ1-regulated restart. Electron microscopy of replication fork architecture, siRNA depletion, EM quantification of fork reversal The Journal of cell biology High 25733714
2015 The C. elegans Rad51 paralog complex RFS-1/RIP-1 binds and remodels pre-synaptic RAD-51-ssDNA filaments into a stabilized, 'open,' flexible conformation in which ssDNA is more accessible and RAD-51 dissociation rate is reduced; Walker-box mutations in RFS-1 abolish filament remodeling and fail to stimulate strand exchange, demonstrating remodeling is essential for paralog function. Single-molecule FRET, electron microscopy, in vitro strand exchange assay, Walker-box mutagenesis Cell High 26186187
2016 TOPBP1 promotes PLK1 kinase-mediated phosphorylation of RAD51 at serine 14, a modification required for RAD51 recruitment to chromatin and focus formation; TOPBP1 BRCT domains 7/8 are essential for RAD51 foci; TOPBP1 depletion abrogates RAD51 chromatin loading without affecting upstream resection or RPA loading. siRNA screen, phospho-specific antibody, in vitro kinase assay, chromatin fractionation, BRCT mutants The Journal of cell biology High 26811421
2016 The MMS22L-TONSL heterodimer localizes to replication forks, associates with RPA-coated ssDNA, and directly interacts with RAD51 via MMS22L; recombinant MMS22L-TONSL limits RAD51 assembly on dsDNA, stimulating RAD51-ssDNA filament formation and strand exchange; MMS22L-RAD51 interaction is required for proper RAD51 focus assembly and HR-mediated fork restart. Co-immunoprecipitation, in vitro strand exchange assay with purified proteins, mutant cell analysis, iPOND replication fork proteomics The EMBO journal High 27797818
2017 Human RAD52 binds tightly to RPA-ssDNA complexes and inhibits RPA turnover; during presynaptic complex assembly, RAD51 displaces most RAD52-RPA from ssDNA; once RAD51 is assembled, it restricts new RAD52 binding events, revealing reciprocal regulation between RAD51 and RAD52 at the presynaptic filament. Single-molecule imaging, ssDNA curtains, TIRF microscopy The Journal of biological chemistry High 28551686
2017 Srs2 is a processive translocase that strips Rad51 monomers from ssDNA at ~50 monomers/second; Srs2 is recruited to RPA clusters embedded within Rad51 filaments; multi-Srs2 arrays form via iterative loading; Srs2 disrupts heteroduplex DNA joints through two alternative pathways, establishing the mechanism of Srs2-mediated anti-recombination. Single-molecule fluorescence imaging (ssDNA curtains), TIRF microscopy Cell reports High 29241544
2018 RADX antagonizes RAD51 at stalled replication forks by competing with RAD51 for ssDNA binding; silencing RADX restores fork protection in BRCA1/2-, FANCA-, FANCD2-, or BOD1L-deficient cells; RADX overexpression causes fork degradation dependent on MRE11 and DNA2 and fork reversal, establishing that the RAD51/RADX balance determines stalled fork fate. DNA fiber assay, siRNA, RADX overexpression, iPOND, fork protection assays Cell reports High 30021152
2018 In budding yeast, Rad52–Rad51 protein interaction is dispensable for Rad51 filament formation and gene conversion but is essential for protecting Rad51 filaments against dissociation by Srs2 DNA translocase, revealing a filament-protection function of Rad52–Rad51 association independent of mediator activity. Rad52 interaction-deficient mutants, in vitro Srs2-disruption assay, in vivo gene conversion assay, electron microscopy eLife High 29985128
2018 Rad51 and Dmc1 have an intrinsic ability to self-segregate in mixed filaments on ssDNA, even without accessory proteins; Dmc1 stabilizes adjacent Rad51 filament segments, suggesting the two meiotic recombinases form spatially distinct but cross-stabilizing filament domains. Single-molecule imaging (ssDNA curtains), co-visualization of labeled Rad51 and Dmc1 The Journal of biological chemistry High 29382724
2020 RADX condenses RPA-coated ssDNA filaments via higher-order assemblies that can capture ssDNA in trans; RADX blocks RPA displacement by RAD51 and prevents RAD51 loading on ssDNA, establishing RADX as an ssDNA condensation protein that inhibits RAD51 filament formation. Single-molecule imaging of RADX on RPA-ssDNA, TIRF microscopy, RAD51 loading assay Nucleic acids research High 32621611
2021 RADX directly and selectively interacts with ATP-bound RAD51, stimulates RAD51 ATP hydrolysis, and destabilizes RAD51 nucleofilaments, inhibiting strand exchange and D-loop formation; RADX ssDNA-binding capability plus its RAD51 interaction are both required for maintaining replication fork elongation and stability; BRCA2 can overcome RADX-mediated RAD51 inhibition. In vitro strand exchange assay, ATPase assay, RAD51 filament stability assay, DNA fiber assay, RADX–RAD51 interaction mapping Molecular cell High 33453169
2021 HELQ helicase activity is strongly stimulated by RAD51 (which forms a complex with HELQ) during DNA unwinding; conversely, RPA inhibits HELQ unwinding but stimulates a previously unappreciated HELQ DNA strand annealing activity; HELQ can capture RPA-bound DNA strands and displace RPA to facilitate annealing. In vitro helicase and annealing assays, single-molecule imaging, biochemical co-complex analysis Nature High 34937945
2021 The HsRAD51B-HsRAD51C heterodimer forms stable complexes on ssDNA and partially stabilizes the HsRAD51 nucleoprotein filament against BLM-mediated disruption; it stimulates HsRAD51-mediated D-loop formation in the presence of RPA but does not facilitate HsRAD51 nucleation on RPA-coated ssDNA, placing RAD51B-C function downstream of BRCA2 in filament stabilization during the presynaptic phase. In vitro filament stability assay, D-loop assay, ssDNA binding assay with purified proteins DNA repair Medium 23810717
2021 Conditional knockout of RAD51 in mouse germ cells (Vasa-Cre) causes spermatogonial loss and Sertoli cell-only syndrome; inducible adult knockout causes meiotic DSB accumulation, reduced pachytene spermatocytes, and fewer crossovers, establishing an essential role for RAD51 in spermatogonial maintenance and meiotic DSB repair. Conditional mouse knockout (Vasa-Cre and UBC-CreERT2), γH2AX staining, crossover quantification Cell death discovery High 35292640
2022 TOPORS acts as a SUMO E3 ligase for RAD51, SUMOylating RAD51 at lysines 57 and 70 in response to DNA damage; SUMOylation is facilitated by ATM-induced phosphorylation of TOPORS at Thr515; SUMOylation-deficient RAD51 (K57R/K70R) reduces chromatin loading, RAD51 focus formation, and association with BRCA2, impairing HR repair. SUMO modification assay, phospho-specific antibody, SUMOylation-deficient mutants, co-immunoprecipitation, HR reporter assay Nucleic acids research High 35061896
2022 RAD51 Cys319 is a redox-sensitive residue regulated by PRDX1; oxidation of Cys319 (sulfenylation) impairs irradiation-induced RAD51 focus formation and HR; PRDX1 maintains Cys319 in a reduced state; molecular dynamics simulations show that oxidized Cys319 causes dissociation of DNA from the RAD51 filament. Phospho/sulfenylation probes, PRDX1-deficient cells, RAD51-C319 mutagenesis, molecular dynamics simulation, PARP inhibitor sensitivity Redox biology High 36058112
2023 Cryo-EM structure of the BRCA2 TR2 motif bound to the human RAD51 nucleoprotein filament reveals TR2 binds across the protomer interface, acting as a brace for adjacent RAD51 molecules; TR2 targets an acidic-patch motif on RAD51 that also serves as a recruitment hub for recombination mediators in fission yeast. Cryo-electron microscopy, structure-guided mutagenesis Nature communications High 37919288
2023 Cryo-EM structures of human RAD51-DNA and DMC1-DNA complexes reveal that the Loop2 region (containing ssDNA and complementary strand binding residues) differs between RAD51 and DMC1; RAD51 residues V273 and D274 (vs. P274 and G275 in DMC1) are key determinants of mismatch intolerance during strand exchange, explaining RAD51's high fidelity compared to DMC1's mismatch tolerance. Cryo-EM structure determination, molecular dynamics simulation, single-molecule FRET, mutagenesis Nucleic acids research High 34871438
2023 RAD51 uses its strand exchange activity to bypass the replicative helicase (CMG) that remains bound at stalled replication forks; when CMG is unloaded, RAD51 is no longer required for fork reversal; RAD51 creates a parental DNA duplex behind the helicase that DNA translocases then use as substrate for branch migration to generate a reversed fork. Auxin-inducible degron to acutely deplete CMG, DNA fiber assay, EM of replication forks, RAD51 strand exchange mutants Science (New York, N.Y.) High 37104614
2023 BRCA2 chaperones a short preassembled RAD51 filament onto RPA-coated ssDNA; a dimer of RAD51 is the minimal unit for spontaneous nucleation but growth self-terminates below diffraction limit; BRCA2 accelerates RAD51 nucleation to rates approaching binding to naked ssDNA, eliminating the kinetic barrier imposed by RPA. Single-molecule microfluidics with full-length BRCA2, direct visualization of RAD51 filament assembly on RPA-ssDNA Proceedings of the National Academy of Sciences of the United States of America High 36976771
2023 Human centromeres harbor enrichment of DNA breaks that occur during both proliferation and quiescence; centromere DNA breaks in quiescent cells are resolved by the RAD51 recombinase, which safeguards functional centromere specification. Single-cell imaging of DNA breaks at repetitive centromere regions, RAD51 depletion, centromere function assay Molecular cell Medium 36702125
2023 Functionally tagged Rad51 in budding yeast forms exceedingly long nucleoprotein filaments spanning the entire nucleus after DSB induction; filaments adopt dynamic compaction-extension cycles modulated by Rad54 (promoting compaction) and Srs2 (promoting extension/disassembly); biophysical modeling shows this dynamics constitutes a robust homology search strategy. Live-cell single-molecule imaging with functional tagged Rad51, biophysical modeling, DSB induction Nature structural & molecular biology High 37605042
2024 RAD51 nucleofilaments specifically recognize and protect abasic sites in ssDNA (which increase RAD51's DNA association rate); in the absence of BRCA2 or RAD51, abasic ssDNA gaps accumulate making replicating DNA sensitive to APE1; RAD51 assembled on abasic DNA prevents cleavage by the MRE11-RAD50 complex, suppressing replication fork breakage. Cryo-EM of RAD51 on abasic DNA, Xenopus egg extract assays, human cell experiments, APE1/MRE11 cleavage assays Molecular cell High 39178838

Source papers

Stage 0 corpus · 130 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 A human protein-protein interaction network: a resource for annotating the proteome. Cell 1704 16169070
2000 A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Current biology : CB 1685 10959836
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
1997 Association of BRCA1 with Rad51 in mitotic and meiotic cells. Cell 1278 9008167
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
1997 Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2. Nature 917 9126738
2008 Resistance to therapy caused by intragenic deletion in BRCA2. Nature 830 18264088
2012 A distinct replication fork protection pathway connects Fanconi anemia tumor suppressors to RAD51-BRCA1/2. Cancer cell 796 22789542
2015 Homologous-recombination-deficient tumours are dependent on Polθ-mediated repair. Nature 740 25642963
2007 Large-scale mapping of human protein-protein interactions by mass spectrometry. Molecular systems biology 733 17353931
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2010 Hydroxyurea-stalled replication forks become progressively inactivated and require two different RAD51-mediated pathways for restart and repair. Molecular cell 693 20188668
2006 Control of BRCA2 cellular and clinical functions by a nuclear partner, PALB2. Molecular cell 677 16793542
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
1996 Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell 585 8929543
2001 Role of BRCA2 in control of the RAD51 recombination and DNA repair protein. Molecular cell 573 11239456
2015 Rad51-mediated replication fork reversal is a global response to genotoxic treatments in human cells. The Journal of cell biology 568 25733714
2002 Insights into DNA recombination from the structure of a RAD51-BRCA2 complex. Nature 561 12442171
2010 Purified human BRCA2 stimulates RAD51-mediated recombination. Nature 553 20729832
2010 Germline mutations in breast and ovarian cancer pedigrees establish RAD51C as a human cancer susceptibility gene. Nature genetics 543 20400964
2005 The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair. Nature cell biology 539 15665856
2003 DNA helicase Srs2 disrupts the Rad51 presynaptic filament. Nature 521 12748644
1998 Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells. Molecular cell 500 9774970
1993 Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA. Nature genetics 466 8358431
1998 XRCC2 and XRCC3, new human Rad51-family members, promote chromosome stability and protect against DNA cross-links and other damages. Molecular cell 454 9660962
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
1997 RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2. The Journal of biological chemistry 432 9405383
1994 Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. The EMBO journal 405 7988572
2002 S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51. Blood 386 12239151
2005 CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair. Nature 380 15800615
1998 Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins. Nature 359 9590697
2018 RPA and RAD51: fork reversal, fork protection, and genome stability. Nature structural & molecular biology 283 29807999
2005 The RAD51 gene family, genetic instability and cancer. Cancer letters 281 15723711
2008 The consequences of Rad51 overexpression for normal and tumor cells. DNA repair 279 18243065
1997 Activities of human recombination protein Rad51. Proceedings of the National Academy of Sciences of the United States of America 229 9012806
1998 The BRCA2 gene product functionally interacts with p53 and RAD51. Proceedings of the National Academy of Sciences of the United States of America 223 9811893
2007 HDAC inhibitor PCI-24781 decreases RAD51 expression and inhibits homologous recombination. Proceedings of the National Academy of Sciences of the United States of America 190 18042714
2020 RAD51 Gene Family Structure and Function. Annual review of genetics 183 32663049
1998 Isolation and characterisation of the RAD51 and DMC1 homologs from Arabidopsis thaliana. Molecular & general genetics : MGG 172 9520262
2000 Rad51 accumulation at sites of DNA damage and in postreplicative chromatin. The Journal of cell biology 170 10908572
2000 Evidence for simultaneous protein interactions between human Rad51 paralogs. The Journal of biological chemistry 159 10749867
1997 Rad51 immunocytology in rat and mouse spermatocytes and oocytes. Chromosoma 157 9254722
2012 The recombinases DMC1 and RAD51 are functionally and spatially separated during meiosis in Arabidopsis. The Plant cell 147 22589466
1999 A surfeit of RAD51-like genes? Trends in genetics : TIG 141 10322480
1997 Elevated recombination in immortal human cells is mediated by HsRAD51 recombinase. Molecular and cellular biology 121 9372947
2002 Homologous DNA pairing by human recombination factors Rad51 and Rad54. The Journal of biological chemistry 118 12205100
2015 Rad51 Paralogs Remodel Pre-synaptic Rad51 Filaments to Stimulate Homologous Recombination. Cell 115 26186187
2005 BRCA2 BRC motifs bind RAD51-DNA filaments. Proceedings of the National Academy of Sciences of the United States of America 109 15937124
2005 RAD51, genomic stability, and tumorigenesis. Cancer letters 101 15670890
2005 MDC1 interacts with Rad51 and facilitates homologous recombination. Nature structural & molecular biology 101 16186822
2018 RAD-ical New Insights into RAD51 Regulation. Genes 100 30551670
2001 Triplex-induced recombination in human cell-free extracts. Dependence on XPA and HsRad51. The Journal of biological chemistry 97 11278954
2004 RAD51 localization and activation following DNA damage. Philosophical transactions of the Royal Society of London. Series B, Biological sciences 94 15065660
2020 Role of Rad51 and DNA repair in cancer: A molecular perspective. Pharmacology & therapeutics 90 32001312
2018 RADX Modulates RAD51 Activity to Control Replication Fork Protection. Cell reports 84 30021152
2009 Overexpression of RAD51 suppresses recombination defects: a possible mechanism to reverse genomic instability. Nucleic acids research 81 19942681
2000 Coordinated response of mammalian Rad51 and Rad52 to DNA damage. EMBO reports 75 11256631
2016 The MMS22L-TONSL heterodimer directly promotes RAD51-dependent recombination upon replication stress. The EMBO journal 73 27797818
2023 RAD51 bypasses the CMG helicase to promote replication fork reversal. Science (New York, N.Y.) 72 37104614
2011 Brca2, Rad51 and Mre11: performing balancing acts on replication forks. DNA repair 69 21900052
2008 Rad51 protein controls Rad52-mediated DNA annealing. The Journal of biological chemistry 69 18337252
2007 Rad51 and Rad54 ATPase activities are both required to modulate Rad51-dsDNA filament dynamics. Nucleic acids research 69 17567608
2005 Role of recA/RAD51 family proteins in mammals. Acta medica Okayama 69 15902993
2002 The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein A. The Journal of biological chemistry 69 12169690
2016 TOPBP1 regulates RAD51 phosphorylation and chromatin loading and determines PARP inhibitor sensitivity. The Journal of cell biology 67 26811421
2006 Interaction between Arabidopsis Brca2 and its partners Rad51, Dmc1, and Dss1. Plant physiology 66 16415210
2020 RAD51: Beyond the break. Seminars in cell & developmental biology 61 32938550
2021 HELQ is a dual-function DSB repair enzyme modulated by RPA and RAD51. Nature 58 34937945
2009 Human PSF binds to RAD51 and modulates its homologous-pairing and strand-exchange activities. Nucleic acids research 58 19447914
2019 Activation of Oncogenic Super-Enhancers Is Coupled with DNA Repair by RAD51. Cell reports 57 31618627
2010 Single-molecule imaging brings Rad51 nucleoprotein filaments into focus. Trends in cell biology 56 20299221
2021 Efficient embryonic homozygous gene conversion via RAD51-enhanced interhomolog repair. Cell 54 34043941
2023 Centromeres as universal hotspots of DNA breakage, driving RAD51-mediated recombination during quiescence. Molecular cell 51 36702125
2016 A radiosensitizing effect of RAD51 inhibition in glioblastoma stem-like cells. BMC cancer 51 27495836
1999 Chlorambucil induction of HsRad51 in B-cell chronic lymphocytic leukemia. Clinical cancer research : an official journal of the American Association for Cancer Research 49 10473103
2017 Human RAD52 interactions with replication protein A and the RAD51 presynaptic complex. The Journal of biological chemistry 48 28551686
2011 Regulation of Rad51 function by phosphorylation. EMBO reports 48 21738226
2006 Roles of the human Rad51 L1 and L2 loops in DNA binding. The FEBS journal 48 16780572
2021 Inhibiting homologous recombination by targeting RAD51 protein. Biochimica et biophysica acta. Reviews on cancer 47 34332021
2014 HOP2-MND1 modulates RAD51 binding to nucleotides and DNA. Nature communications 44 24943459
2001 Identification and characterisation of a RAD51 gene from Leishmania major. Molecular and biochemical parasitology 42 11420107
2018 BET Inhibition Induces HEXIM1- and RAD51-Dependent Conflicts between Transcription and Replication. Cell reports 41 30463005
2017 Dissociation of Rad51 Presynaptic Complexes and Heteroduplex DNA Joints by Tandem Assemblies of Srs2. Cell reports 41 29241544
2021 Regulation of RAD51 at the Transcriptional and Functional Levels: What Prospects for Cancer Therapy? Cancers 39 34208195
2003 The Rad52-Rad59 complex interacts with Rad51 and replication protein A. DNA repair 39 13679150
2021 Mechanisms of distinctive mismatch tolerance between Rad51 and Dmc1 in homologous recombination. Nucleic acids research 36 34871438
2011 Genomic evolution in Barrett's adenocarcinoma cells: critical roles of elevated hsRAD51, homologous recombination and Alu sequences in the genome. Oncogene 36 21423218
2021 Homologous recombination, cancer and the 'RAD51 paradox'. NAR cancer 35 34316706
1998 Proteolytic cleavage of HsRad51 during apoptosis. FEBS letters 34 9607320
2024 RAD51 protects abasic sites to prevent replication fork breakage. Molecular cell 32 39178838
2023 Structural basis for stabilisation of the RAD51 nucleoprotein filament by BRCA2. Nature communications 32 37919288
2022 TOPORS-mediated RAD51 SUMOylation facilitates homologous recombination repair. Nucleic acids research 31 35061896
2021 RADX controls RAD51 filament dynamics to regulate replication fork stability. Molecular cell 31 33453169
2018 Rad52-Rad51 association is essential to protect Rad51 filaments against Srs2, but facultative for filament formation. eLife 29 29985128
2018 Jab1/Cops5 contributes to chemoresistance in breast cancer by regulating Rad51. Cellular signalling 29 30244171
2010 Knockdown of Rad51 expression induces radiation- and chemo-sensitivity in osteosarcoma cells. Medical oncology (Northwood, London, England) 29 20625943
2023 BRCA2 chaperones RAD51 to single molecules of RPA-coated ssDNA. Proceedings of the National Academy of Sciences of the United States of America 28 36976771
2013 XRCC3 and RAD51 expression are associated with clinical factors in breast cancer. PloS one 27 23977219
2021 RAD51 paralog function in replicative DNA damage and tolerance. Current opinion in genetics & development 25 34311385
2019 Roles of RAD51 and RTEL1 in telomere and rDNA stability in Physcomitrella patens. The Plant journal : for cell and molecular biology 25 30834585
2011 Expression and regulation of RAD51 mediate cellular responses to chemotherapeutics. Biochemical pharmacology 25 22222428
2020 CtBP1 transactivates RAD51 and confers cisplatin resistance to breast cancer cells. Molecular carcinogenesis 23 32124501
2017 A cell-penetrating antibody inhibits human RAD51 via direct binding. Nucleic acids research 23 29036688
2023 In vivo tracking of functionally tagged Rad51 unveils a robust strategy of homology search. Nature structural & molecular biology 22 37605042
2022 Cannabidiol inhibits RAD51 and sensitizes glioblastoma to temozolomide in multiple orthotopic tumor models. Neuro-oncology advances 22 35356807
2022 Redox regulation of RAD51 Cys319 and homologous recombination by peroxiredoxin 1. Redox biology 22 36058112
2022 RAD51 paralogs: Expanding roles in replication stress responses and repair. Current opinion in pharmacology 22 36343481
2019 Calcitriol Prevents RAD51 Loss and cGAS-STING-IFN Response Triggered by Progerin. Proteomics 22 31834988
2015 RAD51, XRCC3, and XRCC2 mutation screening in Finnish breast cancer families. SpringerPlus 22 25918678
2014 Regulation of Rad51 promoter. Cell cycle (Georgetown, Tex.) 22 24781030
2008 Rad51 protein stimulates the branch migration activity of Rad54 protein. The Journal of biological chemistry 22 18617519
2023 FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51 dynamics. Cell reports 21 37347663
2006 Variation in the RAD51 gene and familial breast cancer. Breast cancer research : BCR 21 16762046
2003 Genetic and cytological characterization of the RecA-homologous proteins Rad51 and Dmc1 of Schizosaccharomyces pombe. Current genetics 21 12955454
2018 Spontaneous self-segregation of Rad51 and Dmc1 DNA recombinases within mixed recombinase filaments. The Journal of biological chemistry 20 29382724
2023 Noncanonical Roles of RAD51. Cells 19 37190078
2020 RADX condenses single-stranded DNA to antagonize RAD51 loading. Nucleic acids research 19 32621611
2013 The HsRAD51B-HsRAD51C stabilizes the HsRAD51 nucleoprotein filament. DNA repair 19 23810717
2022 RAD51 is essential for spermatogenesis and male fertility in mice. Cell death discovery 18 35292640
2019 MiR-34s negatively regulate homologous recombination through targeting RAD51. Archives of biochemistry and biophysics 18 30951682
1998 Identification and characterization of the RAD51 gene from the ciliate Tetrahymena thermophila. Nucleic acids research 18 9628914
1998 Interaction of Rad51 with ATP and Mg2+ induces a conformational change in Rad51. Biochemistry 18 9718317
2023 ssDNA accessibility of Rad51 is regulated by orchestrating multiple RPA dynamics. Nature communications 17 37391417
2023 Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes. Nature communications 17 37798272
2021 RAD54 is essential for RAD51-mediated repair of meiotic DSB in Arabidopsis. PLoS genetics 17 34003859
2015 Caffeine inhibits gene conversion by displacing Rad51 from ssDNA. Nucleic acids research 17 26019181
2013 BLM and RAD51 genes polymorphism and susceptibility to breast cancer. Pathology oncology research : POR 17 23404160
2024 Bleomycin induces senescence and repression of DNA repair via downregulation of Rad51. Molecular medicine (Cambridge, Mass.) 16 38649802