Affinage

MND1

Meiotic nuclear division protein 1 homolog · UniProt Q9BWT6

Length
205 aa
Mass
23.8 kDa
Annotated
2026-06-10
33 papers in source corpus 26 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MND1 is a meiotic and somatic homologous-recombination cofactor that functions exclusively as a stable heterodimer with HOP2/PSMC3IP to license recombinase-mediated strand invasion (PMID:11940665, PMID:15249670). Within the complex, MND1 is the primary recombinase-interaction subunit while HOP2 provides the dominant DNA-binding activity, together forming a bipartite stimulator that physically engages both RAD51 and DMC1 and enhances their strand-exchange activity up to 35-fold (PMID:15834424, PMID:17639080). The heterodimer stabilizes the recombinase-ssDNA presynaptic filament and promotes capture of duplex DNA to drive synaptic complex formation, mechanistically by condensing dsDNA and by inducing conformational changes in RAD51 that reprogram its nucleotide and DNA-binding properties, acting as a molecular trigger of strand exchange (PMID:17639081, PMID:21112301, PMID:24943459). During homology search the HOP2-MND1 complex codiffuses with the DMC1-ssDNA presynaptic complex, clamping ssDNA-dsDNA junctions and maintaining an expanded DNA bubble for sequence alignment, and serves as a fidelity switch that suppresses illegitimate recombination between microhomologous sequences through its recombinase-filament interaction surface (PMID:39463417, PMID:41746729). Structurally the heterodimer is a curved, V-shaped rod built around central coiled-coil/leucine-zipper interfaces with terminal winged-helix DNA-binding domains and a helical bundle that docks onto the recombinase nucleofilament (PMID:24150939, PMID:25740648). Beyond meiosis, MND1 acts in somatic cells to promote repair of two-ended DSBs in G2 phase, localizing to RAD51-coated resected ssDNA, supporting alternative lengthening of telomeres, and its loss confers PARP-inhibitor and IR sensitivity through abrogated D-loop formation (PMID:25820426, PMID:37195379, PMID:37163373). In cancer cells MND1 expression and HR function are reinforced by an E2F1 transcriptional feedback loop and by recruitment of USP5 to deubiquitinate and stabilize RAD51, while O-GlcNAcylation at Thr121 controls its stability and nuclear retention (PMID:33734616, PMID:41668200, PMID:42236675).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2002 High

    Establishing that Mnd1 acts as a chromatin-bound partner of Hop2 defined the basic functional unit and tied it to meiotic chromosome pairing and DSB repair.

    Evidence Co-IP, null-mutant genetics, and chromosome spreads in S. cerevisiae meiotic cells

    PMID:11940665

    Open questions at the time
    • No biochemical activity assigned to the complex
    • Molecular mechanism of pairing not resolved
  2. 2004 High

    Reconstitution showed the Hop2-Mnd1 heterodimer is a stable DNA-binding entity that stimulates Dmc1 D-loop activity, converting a genetic interaction into a biochemical mechanism for interhomolog recombination.

    Evidence In vitro strand assimilation assay, size-exclusion chromatography, and double-mutant epistasis

    PMID:15120066 PMID:15249670

    Open questions at the time
    • Which subunit binds DNA vs recombinase unresolved
    • Mechanism of filament stimulation unknown
  3. 2005 High

    Demonstrating the heterodimer stimulates both Rad51 and Dmc1 and that Mnd1 association abolishes Hop2's intrinsic recombinase activity revealed that complex formation reprograms subunit function.

    Evidence D-loop assays, Co-IP, and quantitative recombinase stimulation assays with mouse proteins

    PMID:15834424 PMID:16407260

    Open questions at the time
    • Structural basis of conformational change not defined
    • Step in recombination affected not yet dissected
  4. 2006 High

    Domain mapping and genetics located the interaction and DNA-binding interfaces and showed the complex designates DSBs for crossover versus noncrossover outcomes, linking biochemistry to recombination fate.

    Evidence Coiled-coil/C-terminal mutagenesis, analytical ultracentrifugation, and physical recombination assays in yeast

    PMID:16581767 PMID:16675459

    Open questions at the time
    • How crossover designation is mechanistically enforced unknown
  5. 2007 High

    Mechanistic dissection separated the complex's action into filament stabilization and dsDNA capture, and assigned the DNA-binding role to Hop2 and the recombinase-interaction role to Mnd1, defining the bipartite stimulation model.

    Evidence In vitro synaptic complex and strand-exchange assays with domain-swap/deletion mutants; cross-species comparison

    PMID:17426123 PMID:17639080 PMID:17639081

    Open questions at the time
    • Physical structure of the complex on the filament not yet determined
    • Basis of species-specific recombinase preference unclear
  6. 2010 High

    Single-molecule biophysics identified dsDNA condensation as a discrete physical mechanism underlying synapsis stimulation, providing a tangible step for how the complex promotes homology pairing.

    Evidence Optical tweezers and fluorescence microscopy DNA condensation assays

    PMID:21112301

    Open questions at the time
    • How condensation couples to recombinase-mediated synapsis in vivo unknown
  7. 2014 High

    Defining how HOP2-MND1 alters RAD51 nucleotide cofactor and DNA-binding behavior recast the complex as an allosteric trigger that switches the recombinase between filament-loading and homology-search modes.

    Evidence In vitro strand exchange and nucleotide-binding assays with RAD51 K133A mutant

    PMID:24943459

    Open questions at the time
    • Atomic-level basis of RAD51 conformational change not resolved
  8. 2015 High

    Structural and somatic-function studies produced a V-shaped/curved-rod architecture with multiple DNA-binding sites and extended the complex's role to RAD51-dependent ALT telomere maintenance, including a disease-linked HOP2 variant.

    Evidence SAXS, EM, XL-MS, crystallography, deletion mutagenesis, and cell-based ALT assays

    PMID:24150939 PMID:25740648 PMID:25820426 PMID:26535604

    Open questions at the time
    • High-resolution structure of complex bound to the nucleofilament missing
    • Open vs closed conformational switching not functionally tested in vivo
  9. 2018 High

    Single-molecule binding kinetics demonstrated yeast Hop2-Mnd1 binds Dmc1-ssDNA filaments specifically and transiently but not Rad51 or RPA filaments, refining the targeting specificity of the complex.

    Evidence DNA curtain single-molecule imaging with quantitative kinetics and Rad51/RPA negative controls

    PMID:30420424

    Open questions at the time
    • Yeast Dmc1-specificity contrasts with mouse/human dual specificity; reconciliation unresolved
  10. 2021 Medium

    Cell-based studies established a somatic HR role: MND1 localizes to resected, RAD51-coated two-ended DSBs in G2, and an E2F1/MND1 feedback loop couples its expression to cell-cycle progression in cancer.

    Evidence siRNA/CRISPR depletion, DSB localization imaging, cell-cycle analysis, Co-IP, ChIP, and luciferase reporter assays

    PMID:33734616 PMID:37195379

    Open questions at the time
    • Whether somatic MND1 acts via the same biochemical mechanism as in meiosis not directly shown
    • E2F1/KLF6 axis evidence from single lab
  11. 2023 High

    Single-molecule and synthetic-lethality studies pinpointed how MND1 accelerates Dmc1 filament nucleation and showed that its loss causes PARPi/IR sensitivity through abrogated D-loop formation, establishing therapeutic relevance.

    Evidence smFRET and TPM filament-assembly assays; genome-scale CRISPR screens with separation-of-function PSMC3IP rescue

    PMID:37163373 PMID:37395447

    Open questions at the time
    • Mechanism of toxic RAD51 foci accumulation upon depletion not fully defined
  12. 2024 High

    Defining HOP2-MND1 as a sequence-fidelity switch revealed that the complex suppresses microhomology-driven illegitimate recombination via its recombinase-filament interface independent of DNA binding, adding a quality-control function.

    Evidence In vitro strand exchange with defined homologous/mismatch/microhomology substrates and separation-of-function mutants

    PMID:39463417

    Open questions at the time
    • Whether the fidelity function operates in vivo not directly tested
  13. 2026 Medium

    Single-molecule, live-cell, and post-translational studies clarified the homology-search mechanism (codiffusion and junction clamping), additional RAD51-stabilizing routes (USP5), and O-GlcNAc control of MND1 stability/localization.

    Evidence Single-molecule reconstitution and tracking with human proteins, GFP-MND1 live-cell imaging, Co-IP, in vitro glycosylation, and T121A mutagenesis

    PMID:41668200 PMID:41746729 PMID:42236675 PMID:bio_10.1101_2025.03.01.640932

    Open questions at the time
    • O-GlcNAc and USP5 findings are single-lab/cancer-context
    • Live-cell MND1 filament study is a preprint
    • Integration of O-GlcNAc regulation with meiotic function unaddressed

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the in vitro biochemical and structural mechanisms of HOP2-MND1 quantitatively control recombination outcome (crossover designation, fidelity, telomere maintenance) within intact cells, and how somatic post-translational regulation integrates with the core recombinase mechanism, remains open.
  • No high-resolution structure of the complex bound to a recombinase nucleofilament
  • In vivo test of the fidelity-switch function lacking
  • Reconciliation of species-specific recombinase specificity unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 5 GO:0003677 DNA binding 4 GO:0060090 molecular adaptor activity 2
Localization
GO:0005634 nucleus 3 GO:0005694 chromosome 2
Pathway
R-HSA-1474165 Reproduction 3 R-HSA-1640170 Cell Cycle 2 R-HSA-73894 DNA Repair 2
Partners
DMC1E2F1KLF6OGTPSMC3IPRAD51USP5
Complex memberships
HOP2-MND1 (PSMC3IP-MND1) heterodimer

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 Mnd1 forms a complex with Hop2 (co-immunoprecipitation from meiotic cell extracts) and localizes to chromatin throughout meiotic prophase; this localization requires Hop2. The complex promotes meiotic chromosome pairing and DSB repair in S. cerevisiae. Co-immunoprecipitation, genetic analysis (null mutant phenotype), chromosome spreads/localization Molecular and cellular biology High 11940665
2004 Hop2 and Mnd1 form a stable heterodimer with higher affinity for double-stranded than single-stranded DNA, and this heterodimer stimulates the strand assimilation (D-loop) activity of Dmc1 in vitro. Genetic double-mutant analysis places HOP2, MND1, and DMC1 in the same pathway for homologous chromosome juxtaposition. In vitro biochemical reconstitution (strand assimilation assay), size-exclusion chromatography, genetic epistasis (double mutant analysis) Proceedings of the National Academy of Sciences of the United States of America High 15249670
2004 In S. cerevisiae, Mnd1 is specifically required for DSB repair using the homologous chromosome (interhomolog repair); deletion of RED1 or HOP1 suppresses mnd1Δ arrest by permitting sister-chromatid repair. Mnd1 localizes to chromatin as foci independently of DSB formation, axial element formation, SC formation, and does not colocalize with Rad51, suggesting it facilitates chromatin accessibility for strand invasion rather than being recruited to repair sites. Genetic epistasis (double mutant suppression), chromosome spreads, immunofluorescence localization Current biology : CB Medium 15120066
2005 Mouse Hop2 alone can form D-loops, but this activity is abrogated upon association with Mnd1. The Hop2-Mnd1 heterodimer physically interacts with both Rad51 and Dmc1 recombinases and stimulates their strand invasion activity up to 35-fold. D-loop formation assay, co-immunoprecipitation, in vitro recombinase stimulation assay Nature structural & molecular biology High 15834424
2006 The Hop2-Mnd1 heterodimer (but not individual proteins) stimulates Dmc1-mediated strand invasion. Interaction with Mnd1 induces conformational changes in Hop2 that abrogate Hop2's intrinsic recombinase activity and create a new interface for Dmc1 interaction. Coiled-coil motifs in both Hop2 and Mnd1 are essential for their mutual interaction, and a C-terminal region of both proteins is required for DNA binding and single-strand annealing. In vitro D-loop assay, mutagenesis (coiled-coil deletions, C-terminal deletions, point mutation), analytical ultracentrifugation The Journal of biological chemistry High 16675459
2006 Mnd1/Hop2 in S. cerevisiae is required for Dmc1-mediated crossover recombination. In mnd1 rad51 double mutants, crossover recombination is restored (through Dmc1 alone), but noncrossover recombination remains absent, revealing a role for Mnd1/Hop2 in designating DSBs for noncrossover recombination. Epistasis analysis supports a model in which Mnd1/Hop2 ensures Dmc1-mediated strand invasion between homologs. Genetic epistasis (double mutant analysis: mnd1 rad51, hop2 rad51, mnd1 rad17), physical recombination assays Molecular and cellular biology Medium 16581767
2006 Human TBPIP/Hop2-Mnd1 complex stimulates Dmc1- and Rad51-mediated DNA strand exchange and preferentially binds three-stranded DNA branch structures mimicking strand-exchange intermediates. In vitro strand exchange assay, DNA-binding assays (gel shift with branched DNA substrates), protein purification The Journal of biological chemistry High 16407260
2007 Hop2-Mnd1 acts on two distinct steps to stimulate Dmc1-mediated homologous pairing: (1) stabilization of the Dmc1-ssDNA nucleoprotein filament, and (2) facilitation of dsDNA capture by the Dmc1-ssDNA filament, enabling synaptic complex formation on long duplex DNAs. In vitro reconstitution (strand invasion, synaptic complex formation assays on long duplexes), biochemical dissection of reaction steps Genes & development High 17639081
2007 In the Hop2-Mnd1 complex, Hop2 is the major DNA-binding subunit while Mnd1 is the primary Rad51-interaction entity. Hop2-Mnd1 stabilizes the Rad51-ssDNA nucleoprotein filament and enhances the ability of the Rad51-ssDNA filament to capture duplex DNA, revealing a bipartite stimulation mechanism. In vitro reconstitution (strand exchange, D-loop assays), domain-swap and deletion mutant analysis, DNA-binding assays Genes & development High 17639080
2007 S. pombe Hop2-Mnd1 stimulates spDmc1-dependent strand exchange and strand invasion, and promotes renaturation of complementary ssDNA and strand exchange with short oligonucleotides. Mouse Hop2 or mHop2-Mnd1 stimulates both hRad51 and hDmc1, whereas spHop2-Mnd1 is specific for spDmc1, revealing evolutionary divergence in recombinase specificity. In vitro strand exchange assay, co-immunoprecipitation, two-hybrid analysis, electron microscopy Nucleic acids research High 17426123
2010 The Hop2-Mnd1 heterodimer condenses double-stranded DNA via formation of a DNA condensate, in a concentration-dependent and reversible manner. Neither Hop2 nor Mnd1 alone can mediate condensation. Hop2-Mnd1/Dmc1/ssDNA nucleoprotein filaments also condense dsDNA, and the concentration dependence parallels that of DNA strand exchange, suggesting DNA condensation is a key mechanistic step in synapsis stimulation. Single-molecule optical tweezers, video fluorescence microscopy, DNA condensation assays Biophysical journal High 21112301
2013 Small angle X-ray scattering (SAXS) and electron microscopy reveal that Hop2-Mnd1 is a V-shaped heterodimer with three distinct DNA binding sites. The N-terminal dsDNA-binding functions of Hop2 and Mnd1 cooperate for synaptic complex assembly, while ssDNA binding by the Hop2 C-terminus stabilizes the Dmc1-ssDNA filament. Small angle X-ray scattering (SAXS), electron microscopy, deletion mutagenesis, in vitro strand invasion assay Nucleic acids research High 24150939
2014 HOP2-MND1 induces conformational changes in RAD51 that alter its basic properties: it enhances RAD51 interaction with nucleotide cofactors, modifies RAD51 DNA-binding specificity to stimulate strand exchange, enables RAD51 strand exchange without divalent metal ions required for ATP binding, and offsets the K133A ATP-binding mutation. During nucleoprotein formation HOP2-MND1 helps load RAD51 onto ssDNA while restricting dsDNA binding; during homology search it promotes dsDNA binding by removing ssDNA inhibition. HOP2-MND1 is described as a 'molecular trigger' of RAD51 strand exchange. In vitro strand exchange assay, nucleotide-binding assays, RAD51 conformation assays, mutagenesis (K133A) Nature communications High 24943459
2015 Crystal structure of Hop2-Mnd1 reveals a curved rod-like structure with three leucine zippers and two kinked junctions, with juxtaposed winged-helix domains at one end and a helical bundle at the other. Deletion analysis shows the helical bundle is sufficient for interacting with the Dmc1-ssDNA nucleofilament. Molecular modeling suggests the curved rod fits into the helical groove of the nucleofilament and that winged-helix domain DNA binding likely perturbs base pairing to facilitate strand invasion. X-ray crystallography, deletion mutagenesis, molecular modeling Nucleic acids research High 25740648
2015 Hop2-Mnd1 is expressed in somatic tissues and primary human fibroblasts where it functions with Rad51 to repair damaged telomeres via the alternative lengthening of telomeres (ALT) mechanism. Both Hop2 and Mnd1 C-terminal regions interact with RAD51 (and DMC1); ATP enhances the Hop2-Mnd1–RAD51 interaction. The HOP2 p.del201Glu mutation (present in an XX ovarian dysgenesis patient) diminishes association and functional synergy with RAD51 and DMC1. Co-immunoprecipitation, mutagenesis (C-terminal deletion and patient variant), in vitro strand invasion assay, cell-based ALT assay Nucleic acids research High 25820426
2015 Cross-linking mass spectrometry (XL-MS) of plant HOP2-MND1 reveals that the major interaction site is in the central coiled-coil domains, and the complex adopts an open colinear parallel arrangement with flexible C-terminal capping helices suggesting a closed conformation also exists in solution. Chemical cross-linking mass spectrometry (XL-MS), protein threading, protein-protein docking Journal of proteome research Medium 26535604
2018 Using single-molecule DNA curtain imaging, yeast Hop2-Mnd1 binds rapidly to Dmc1-ssDNA filaments with high affinity and remains bound for ~1.3 min. No association was detected between Hop2-Mnd1 and Rad51-ssDNA or RPA-ssDNA filaments, demonstrating Dmc1-specific binding. Single-molecule imaging (DNA curtains), quantitative binding kinetics The Journal of biological chemistry High 30420424
2021 MND1 in somatic (cancer) cells localizes to DSBs, stimulates HR repair, and is specifically active in G2 phase but not S phase. MND1 is not involved in repair of replication-associated one-ended DSBs, but specifically promotes repair of two-ended DSBs induced by IR or chemotherapeutic drugs. MND1 localization to DSBs depends on DNA end resection and occurs through binding to RAD51-coated ssDNA. Loss-of-function (siRNA/CRISPR depletion), immunofluorescence (localization to DSBs), cell cycle analysis, epistasis with RAD51 and resection factors Molecular oncology Medium 37195379
2021 MND1 competitively binds to KLF6 tumor suppressor, protecting E2F1 from KLF6-induced transcriptional repression; E2F1 in turn activates MND1 transcription by binding to its promoter, forming a positive feedback loop that regulates cell cycle progression in lung adenocarcinoma cells. Co-immunoprecipitation, chromatin immunoprecipitation (ChIP), dual-luciferase reporter assay, mass spectrometry Cancer communications (London, England) Medium 33734616
2023 Using smFRET and tethered particle motion experiments, Hop2-Mnd1 enhances Dmc1 filament assembly on ssDNA by increasing the Dmc1 nucleation binding rate (at ss/dsDNA junctions), whereas Swi5-Sfr1 reduces the dissociation rate during nucleation. The two complexes act via distinct, additive mechanisms on Dmc1 filament assembly. Single-molecule FRET (smFRET), tethered particle motion (TPM), order-of-addition experiments Nucleic acids research High 37395447
2023 Depletion of MND1 (or PSMC3IP/HOP2) causes PARP inhibitor sensitivity and ionizing radiation sensitivity in mitotic cells, causes accumulation of toxic RAD51 foci, and impairs homology-directed DNA repair. These effects are independent of the ALT telomere pathway. Epistasis with BRCA1/BRCA2 defects suggests the mechanism is abrogated D-loop formation. A PSMC3IP p.Glu201del mutant with defective D-loop activity fails to reverse PARPi sensitivity, unlike wild-type PSMC3IP. Genome-scale CRISPR screens, siRNA depletion, immunofluorescence (RAD51 foci), HR reporter assays, rescue with wild-type vs. mutant PSMC3IP, epistasis analysis Cell reports High 37163373
2024 Hop2-Mnd1 acts as a DNA sequence fidelity switch for Dmc1: it upregulates Dmc1 activity on fully homologous and mismatch-containing substrates, but suppresses illegitimate DNA strand exchange between substrates with only microhomology. Separation-of-function variants show that suppression of illegitimate recombination requires the Dmc1-filament interaction surface of Hop2-Mnd1 but not its DNA-binding activity. In vitro strand exchange assays with defined substrates, separation-of-function mutant analysis Nature communications High 39463417
2026 O-GlcNAcylation of MND1 at Thr121 (by OGT) stabilizes MND1 protein and promotes its nuclear localization in breast cancer cells. T121A mutagenesis reduces MND1 stability and nuclear retention, impairs MND1-mediated DSB repair, and elevates persistent pH2AX levels. O-GlcNAc on T121 modulates the MND1-HOP2 interaction; loss of this modification augments MND1-HOP2 binding and causes structural perturbation of the complex. Immunoprecipitation, in vitro glycosylation assay, site-directed mutagenesis (T121A), OGT/OGA inhibitors, subcellular fractionation, pH2AX quantification Breast cancer research : BCR Medium 41668200
2026 In breast cancer cells, MND1 promotes HR repair by recruiting USP5 to deubiquitinate and stabilize RAD51. E2F1 transcriptionally activates MND1 by binding its promoter and inducing promoter hypomethylation, establishing an E2F1/MND1/USP5/RAD51 feedback loop. Co-immunoprecipitation, luciferase reporter assay, bisulfite sequencing PCR, in vitro/in vivo functional assays Cell death & disease Medium 42236675
2026 Using single-molecule imaging, human DMC1-ssDNA presynaptic complex employs a diffusion-based mechanism to search for homologous DNA. HOP2-MND1 codiffuses with the presynaptic complex, clamping ssDNA-dsDNA junctions and maintaining an expanded DNA bubble to enable homology recognition, compensating for absence of free DMC1 and enabling strand exchange. HOP2-MND1 and DMC1 together constitute a functional homology search unit. Single-molecule imaging (fluorescence), in vitro reconstitution with human proteins, single-molecule tracking Proceedings of the National Academy of Sciences of the United States of America High 41746729
2025 GFP-MND1 in living human cells forms long filamentous structures on ssDNA several hours after DSB formation; these filaments are highly dynamic, explore nuclear space, and resolve over time. Resolution of MND1 filaments depends on RAD54L (known for homology search/strand invasion), and loss of cohesin also inhibits filament resolution, placing MND1 in an active HR intermediate resolvable by RAD54L. Live-cell single-molecule imaging (GFP-MND1), genetic epistasis (RAD54L and cohesin depletion), fluorescence microscopy bioRxivpreprint Medium bio_10.1101_2025.03.01.640932

Source papers

Stage 0 corpus · 33 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in meiotic recombination. Nature structural & molecular biology 144 15834424
2002 The Mnd1 protein forms a complex with hop2 to promote homologous chromosome pairing and meiotic double-strand break repair. Molecular and cellular biology 120 11940665
2007 Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous pairing. Genes & development 101 17639081
2007 Bipartite stimulatory action of the Hop2-Mnd1 complex on the Rad51 recombinase. Genes & development 100 17639080
2004 Heterodimeric complexes of Hop2 and Mnd1 function with Dmc1 to promote meiotic homolog juxtaposition and strand assimilation. Proceedings of the National Academy of Sciences of the United States of America 94 15249670
2004 Mnd1 is required for meiotic interhomolog repair. Current biology : CB 76 15120066
2006 Molecular activities of meiosis-specific proteins Hop2, Mnd1, and the Hop2-Mnd1 complex. The Journal of biological chemistry 65 16675459
2013 Mechanistic insights into the role of Hop2-Mnd1 in meiotic homologous DNA pairing. Nucleic acids research 51 24150939
2006 Stimulation of DNA strand exchange by the human TBPIP/Hop2-Mnd1 complex. The Journal of biological chemistry 49 16407260
2015 Significance of ligand interactions involving Hop2-Mnd1 and the RAD51 and DMC1 recombinases in homologous DNA repair and XX ovarian dysgenesis. Nucleic acids research 45 25820426
2014 HOP2-MND1 modulates RAD51 binding to nucleotides and DNA. Nature communications 44 24943459
2015 Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination. Nucleic acids research 43 25740648
2007 Stimulation of fission yeast and mouse Hop2-Mnd1 of the Dmc1 and Rad51 recombinases. Nucleic acids research 39 17426123
2006 Mnd1/Hop2 facilitates Dmc1-dependent interhomolog crossover formation in meiosis of budding yeast. Molecular and cellular biology 39 16581767
2015 Comprehensive Cross-Linking Mass Spectrometry Reveals Parallel Orientation and Flexible Conformations of Plant HOP2-MND1. Journal of proteome research 35 26535604
2021 Meiotic nuclear divisions 1 (MND1) fuels cell cycle progression by activating a KLF6/E2F1 positive feedback loop in lung adenocarcinoma. Cancer communications (London, England) 29 33734616
2010 Hop2-Mnd1 condenses DNA to stimulate the synapsis phase of DNA strand exchange. Biophysical journal 24 21112301
2018 Dynamic interactions of the homologous pairing 2 (Hop2)-meiotic nuclear divisions 1 (Mnd1) protein complex with meiotic presynaptic filaments in budding yeast. The Journal of biological chemistry 19 30420424
2013 Expression analysis of MND1/GAJ, SPATA22, GAPDHS and ACR genes in testicular biopsies from non-obstructive azoospermia (NOA) patients. Reproductive biology and endocrinology : RB&E 18 23675907
2023 FOXA1/MND1/TKT axis regulates gastric cancer progression and oxaliplatin sensitivity via PI3K/AKT signaling pathway. Cancer cell international 14 37817120
2023 MND1 enables homologous recombination in somatic cells primarily outside the context of replication. Molecular oncology 12 37195379
2015 Entamoeba histolytica Dmc1 Catalyzes Homologous DNA Pairing and Strand Exchange That Is Stimulated by Calcium and Hop2-Mnd1. PloS one 9 26422142
2023 Hop2-Mnd1 and Swi5-Sfr1 stimulate Dmc1 filament assembly using distinct mechanisms. Nucleic acids research 8 37395447
2019 A predicted deleterious allele of the essential meiosis gene MND1, present in ~ 3% of East Asians, does not disrupt reproduction in mice. Molecular human reproduction 8 31393579
2023 MND1 and PSMC3IP control PARP inhibitor sensitivity in mitotic cells. Cell reports 7 37163373
2023 The Hop2-Mnd1 Complex and Its Regulation of Homologous Recombination. Biomolecules 6 37189409
2021 Genetic network and gene set enrichment analyses identify MND1 as potential diagnostic and therapeutic target gene for lung adenocarcinoma. Scientific reports 5 33941804
2024 Hop2-Mnd1 functions as a DNA sequence fidelity switch in Dmc1-mediated DNA recombination. Nature communications 2 39463417
2024 Integrative Pan-Cancer Analysis Reveals the Oncogenic Role of MND1 and Validation of MND1's Role in Breast Cancer. Journal of inflammation research 1 39051055
2026 O-GlcNAcylation regulates the DNA damage repair function of MND1 in breast cancer. Breast cancer research : BCR 0 41668200
2026 HOP2-MND1 chaperones a diffusing DMC1-ssDNA complex to survey dsDNA for homology recognition during meiotic recombination. Proceedings of the National Academy of Sciences of the United States of America 0 41746729
2026 MND1 reduces breast cancer chemosensitivity by promoting RAD51-mediated homologous recombination repair. Cell death & disease 0 42236675
2025 MND1 Promotes the Proliferation of Prostate Cancer Cell Via the CCNB1/p53 Signaling Pathway. Current cancer drug targets 0 40353402

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