Affinage

MND1

Meiotic nuclear division protein 1 homolog · UniProt Q9BWT6

Length
205 aa
Mass
23.8 kDa
Annotated
2026-04-28
35 papers in source corpus 26 papers cited in narrative 27 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MND1 is an obligate subunit of the HOP2–MND1 heterodimer that functions as a central cofactor for RAD51/DMC1 recombinase-mediated homologous recombination in both meiotic and somatic cells. The complex, assembled through coiled-coil interactions into a V-shaped rod with winged-helix domains at one end, operates through a bipartite mechanism: it stabilizes recombinase–ssDNA presynaptic filaments and promotes capture of duplex DNA for synaptic complex formation, while also inducing conformational changes in RAD51 that activate its ATPase and strand-exchange activities (PMID:15834424, PMID:17639081, PMID:17639080, PMID:24943459, PMID:25740648). HOP2–MND1 codiffuses with DMC1–ssDNA filaments to clamp ssDNA–dsDNA junctions during homology search, enforces recombination fidelity by suppressing illegitimate strand exchange between substrates sharing only microhomology, and in meiosis promotes interhomolog bias for crossover formation (PMID:41746729, PMID:39463417, PMID:15120066, PMID:16581767). In somatic G2 cells, MND1 localizes to two-ended DSBs in a resection-dependent manner, stimulates homology-directed repair, and its depletion causes toxic RAD51 focus accumulation and sensitivity to PARP inhibitors and ionizing radiation; MND1 protein stability and nuclear retention are additionally regulated by O-GlcNAcylation at Thr121 (PMID:37195379, PMID:37163373, PMID:41668200).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2002 High

    Discovery that Mnd1 forms a stable complex with Hop2 and that both are required for meiotic chromosome pairing and DSB repair established the heterodimer as a functional unit in meiotic recombination.

    Evidence Co-IP from yeast meiotic extracts, chromosome spreads, and null mutant analysis in budding yeast

    PMID:11940665

    Open questions at the time
    • Biochemical activity of the complex unknown
    • Mechanism of action on recombinases not addressed
    • Whether the complex functions in somatic cells untested
  2. 2004 High

    Reconstitution of Hop2–Mnd1 stimulation of Dmc1 strand assimilation in vitro, combined with epistasis placing both genes in the DMC1 pathway, established that the heterodimer is a direct biochemical cofactor for recombinase-mediated strand invasion and acts specifically to promote interhomolog recombination.

    Evidence In vitro D-loop assays with purified yeast proteins, DNA-binding assays, genetic epistasis with RED1/HOP1 suppressors in budding yeast

    PMID:15120066 PMID:15249670

    Open questions at the time
    • Whether the complex acts on Rad51 as well as Dmc1 unknown
    • Structural basis of the interaction unresolved
    • Mechanism of stimulation (presynaptic vs synaptic) not dissected
  3. 2005 High

    Demonstration that mammalian Hop2–Mnd1 stimulates both Rad51 and Dmc1 D-loop activity up to 35-fold, and that Mnd1 generates a new recombinase-interaction interface within the heterodimer, revealed the complex as a general recombination cofactor rather than a Dmc1-specific factor.

    Evidence Co-IP and in vitro D-loop assays with purified mouse Hop2, Mnd1, Rad51, and Dmc1

    PMID:15834424

    Open questions at the time
    • Which step of strand exchange is stimulated (filament stability vs DNA capture) not resolved
    • Whether species-specific Dmc1/Rad51 selectivity exists unclear
  4. 2006 High

    Domain dissection showed that coiled-coil motifs mediate Hop2–Mnd1 heterodimerization while C-terminal regions are essential for DNA binding; in vivo, the complex was shown to be required specifically for Dmc1-mediated crossover formation and noncrossover designation.

    Evidence Mutagenesis of coiled-coil domains, analytical ultracentrifugation, in vitro D-loop assays with mouse proteins; physical recombination assays (Southern blots) and epistasis in yeast

    PMID:16407260 PMID:16581767 PMID:16675459

    Open questions at the time
    • Atomic structure not yet available
    • Whether Mnd1's N-terminus contributes to DNA binding unresolved
    • Mechanism of noncrossover designation unclear
  5. 2007 High

    Mechanistic dissection revealed that Hop2–Mnd1 acts through a bipartite mechanism — stabilizing the recombinase–ssDNA presynaptic filament and facilitating duplex DNA capture for synaptic complex formation — with Mnd1 as the primary Rad51-interacting subunit and Hop2 as the primary DNA-binding subunit.

    Evidence In vitro filament stability assays, synaptic complex assays, protein interaction mapping with purified mouse proteins; cross-species reconstitution with S. pombe and Arabidopsis orthologs

    PMID:17426123 PMID:17639080 PMID:17639081 PMID:17937504

    Open questions at the time
    • Structural basis of the V-shape and DNA-binding sites unresolved
    • Single-molecule dynamics of the interaction unknown
    • How duplex capture leads to strand invasion mechanistically unclear
  6. 2013 High

    SAXS and EM revealed the V-shaped architecture of the heterodimer and identified three distinct DNA-binding sites — two N-terminal dsDNA-binding sites (one on each subunit) for synaptic complex assembly and one C-terminal ssDNA-binding site on Hop2 for filament stabilization — providing a structural framework for the bipartite mechanism.

    Evidence Small-angle X-ray scattering, electron microscopy, deletion analysis with in vitro DNA-binding and strand exchange assays

    PMID:24150939

    Open questions at the time
    • Atomic-resolution structure not yet determined
    • How the three binding sites coordinate during strand exchange unknown
  7. 2014 High

    Hop2–Mnd1 was shown to act as a molecular trigger inducing conformational changes in RAD51 that enhance ATP interaction, modify DNA-binding specificity, and enable strand exchange even without divalent cations, establishing allosteric activation of the recombinase as a key mechanism.

    Evidence In vitro strand exchange, nucleotide binding, and DNA-binding competition assays with RAD51 mutants

    PMID:24943459

    Open questions at the time
    • Structural basis of the conformational change in RAD51 not visualized
    • Whether DMC1 undergoes analogous conformational changes unknown
  8. 2015 High

    Crystal structure of Hop2–Mnd1 revealed a curved rod of three leucine zippers with winged-helix domains that can perturb DNA base pairing and a helical bundle that interfaces with the Dmc1 filament; disease-associated mutations in the C-terminal recombinase-interaction regions diminished stimulation of both RAD51 and DMC1, linking structure to function and disease.

    Evidence X-ray crystallography with deletion analysis; Co-IP, mutagenesis, and strand exchange assays including the HOP2 p.del201Glu ovarian dysgenesis mutation

    PMID:25740648 PMID:25820426

    Open questions at the time
    • Structure of the complex bound to recombinase filament not determined
    • Whether winged-helix DNA destabilization is essential in vivo untested
  9. 2018 High

    Single-molecule DNA curtain imaging quantified that yeast Hop2–Mnd1 binds Dmc1–ssDNA filaments rapidly and with high specificity (no detectable binding to Rad51–ssDNA or RPA–ssDNA), providing a biophysical basis for the differential regulation of Dmc1 versus Rad51 in yeast meiosis.

    Evidence Single-molecule DNA curtains with real-time fluorescence imaging of yeast proteins

    PMID:30420424

    Open questions at the time
    • Whether mammalian Hop2–Mnd1 shows similar Dmc1 specificity at the single-molecule level untested
    • How specificity is encoded structurally unknown
  10. 2023 High

    Multiple studies established that MND1–HOP2 functions in somatic cells: MND1 localizes to two-ended DSBs in G2 phase dependent on end resection, its depletion causes toxic RAD51 foci and PARPi/IR sensitivity, and smFRET revealed Hop2–Mnd1 enhances Dmc1 filament nucleation at ss/dsDNA junctions — a mechanism distinct from Swi5–Sfr1.

    Evidence Live-cell imaging, CRISPR KO with functional assays and rescue by wild-type but not D-loop-defective mutant; smFRET and tethered particle motion with purified proteins

    PMID:37163373 PMID:37195379 PMID:37395447

    Open questions at the time
    • Whether MND1 somatic function is HOP2-independent in any context unclear
    • How MND1 distinguishes two-ended from one-ended DSBs mechanistically unknown
    • Relative contributions of Dmc1 nucleation enhancement vs filament stabilization in vivo unresolved
  11. 2024 High

    Hop2–Mnd1 was demonstrated to act as a fidelity switch that stimulates recombination with homologous substrates while suppressing illegitimate recombination between substrates sharing only microhomology; separation-of-function analysis showed that suppression of illegitimate recombination requires Dmc1 filament interaction but not DNA binding.

    Evidence In vitro D-loop and strand exchange assays with separation-of-function mutants and single-molecule imaging

    PMID:39463417

    Open questions at the time
    • Whether this fidelity function operates in somatic HR not tested
    • Structural basis for discrimination between homologous and microhomologous substrates unknown
  12. 2026 High

    Single-molecule imaging of human proteins showed HOP2–MND1 codiffuses with the DMC1–ssDNA presynaptic complex, clamping ssDNA–dsDNA junctions and maintaining an expanded DNA bubble to enable homology recognition, defining the DMC1–HOP2–MND1 assembly as the functional homology search unit; separately, O-GlcNAcylation at MND1 Thr121 was shown to stabilize the protein and maintain its nuclear localization for DSB repair.

    Evidence Single-molecule imaging on DNA tightropes with purified human proteins; site-directed mutagenesis, in vitro glycosylation, subcellular fractionation, and γH2AX quantification in breast cancer cells

    PMID:41668200 PMID:41746729

    Open questions at the time
    • How the migrating bubble is resolved upon homology recognition is unknown
    • Whether O-GlcNAcylation regulates MND1 in meiotic cells untested
    • Structure of the codiffusing DMC1–HOP2–MND1 complex on DNA not determined

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include the high-resolution cryo-EM structure of the HOP2–MND1 complex bound to a recombinase–DNA filament, the mechanism by which MND1 distinguishes two-ended from one-ended DSBs in somatic cells, and whether the recombination fidelity function operates during mitotic HR.
  • No structure of the ternary HOP2–MND1–recombinase–DNA complex
  • Mechanism of two-ended vs one-ended DSB selectivity unknown
  • In vivo significance of fidelity switching in somatic HR untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003677 DNA binding 6 GO:0098772 molecular function regulator activity 5 GO:0008092 cytoskeletal protein binding 2
Localization
GO:0005634 nucleus 3 GO:0005694 chromosome 3
Pathway
R-HSA-73894 DNA Repair 7 R-HSA-1474165 Reproduction 5 R-HSA-1640170 Cell Cycle 2
Partners
DMC1KLF6OGTPSMC3IPRAD51RAD54LTKT
Complex memberships
HOP2–MND1 heterodimer

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 Mnd1 forms a stable complex with Hop2 (co-immunoprecipitation from meiotic cell extracts); Mnd1 localizes to chromatin throughout meiotic prophase in a Hop2-dependent manner; together they promote meiotic chromosome pairing and DSB repair in budding yeast. Co-immunoprecipitation, chromosome spreads, genetic analysis of null mutants Molecular and cellular biology High 11940665
2004 Saccharomyces cerevisiae 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 epistasis places HOP2, MND1, and DMC1 in the same pathway for homologous chromosome juxtaposition. In vitro strand assimilation assay, DNA-binding assays, double-mutant epistasis analysis Proceedings of the National Academy of Sciences of the United States of America High 15249670
2004 In budding yeast, Mnd1 specifically promotes DSB repair using the homologous chromosome as template; deletion of RED1 or HOP1 suppresses mnd1Δ arrest, indicating Mnd1 acts within the interhomolog bias pathway. Mnd1 localizes to chromatin as foci independently of DSB formation and does not colocalize with Rad51. Genetic epistasis (double mutants), chromosome spreads, immunofluorescence localization Current biology : CB High 15120066
2005 Mouse Hop2-Mnd1 heterodimer physically interacts with both Rad51 and Dmc1 recombinases and stimulates their D-loop (strand invasion) activity up to 35-fold; Hop2 alone can form D-loops but this activity is abrogated upon association with Mnd1, which instead generates a new interface that stimulates recombinase activity. Co-immunoprecipitation, in vitro D-loop assay with purified proteins Nature structural & molecular biology High 15834424
2006 Human TBPIP/Hop2-Mnd1 complex stimulates Dmc1- and Rad51-mediated strand exchange and preferentially binds three-stranded DNA branch structures mimicking strand-exchange intermediates. In vitro strand exchange assay, DNA-binding assay with purified human proteins The Journal of biological chemistry High 16407260
2006 Interaction of mouse Mnd1 with Hop2 through coiled-coil motifs is essential for heterodimer formation; coiled-coil motifs in both proteins are required for their mutual interaction, and a C-terminal region of both proteins is necessary for DNA binding and single-strand annealing by the heterodimer. Mnd1 alone has no D-loop or Dmc1-stimulation activity; only the Hop2-Mnd1 complex stimulates Dmc1. In vitro D-loop assay, DNA binding assay, mutagenesis of coiled-coil domains, analytical ultracentrifugation The Journal of biological chemistry High 16675459
2006 In budding yeast, Mnd1/Hop2 is required for Dmc1-mediated crossover recombination; mnd1 rad51 double mutants restore crossover (but not noncrossover) recombination, indicating Mnd1/Hop2 ensures Dmc1-mediated stable strand invasion between homologous chromosomes and is specifically required for designation of DSBs for noncrossover recombination. Genetic epistasis (double mutants), physical recombination assays (Southern blots for joint molecules and crossovers) Molecular and cellular biology High 16581767
2007 Hop2-Mnd1 stimulates Dmc1 through two mechanistically distinct steps: (1) stabilizing the Dmc1-ssDNA nucleoprotein filament (presynaptic step) and (2) facilitating capture of duplex DNA by the Dmc1-ssDNA filament to promote synaptic complex formation on long duplex DNAs. In vitro homologous pairing assay, synaptic complex assay, Dmc1-ssDNA filament stability assay with purified mouse proteins Genes & development High 17639081
2007 In the Hop2-Mnd1 heterodimer, Hop2 is the major DNA-binding subunit while Mnd1 is the prominent Rad51 interaction entity; Hop2-Mnd1 stabilizes the Rad51-ssDNA nucleoprotein filament and enhances the ability of this filament to capture duplex DNA for synaptic complex formation — a bipartite mechanism. In vitro Rad51-ssDNA filament stability assay, duplex DNA capture assay, protein interaction mapping with purified subunits Genes & development High 17639080
2007 S. pombe Hop2-Mnd1 binds ssDNA ends of 3'-tailed DNA, promotes renaturation of complementary ssDNA, catalyzes strand exchange with short oligonucleotides, and stimulates spDmc1-dependent strand exchange; mouse Hop2 or Hop2-Mnd1 stimulates both hRad51 and hDmc1, revealing species-specific differences in recombinase specificity. Electron microscopy, in vitro strand exchange assay, strand invasion assay with purified S. pombe and mouse proteins Nucleic acids research High 17426123
2007 In Arabidopsis, AtMND1 loading onto meiotic chromosomes depends exclusively on AHP2 (the Hop2 homolog); the AtMND1-AHP2 complex directly interacts with AtRAD51 and AtDMC1 in vitro; AtDMC1 foci accumulate in the Atmnd1 mutant indicating MND1 promotes productive Dmc1 activity; genetic epistasis shows AtMND1 is needed for AtRAD51-dependent AtDMC1 focus formation but AtXRCC3 is not. Chromosome spreads, immunolocalization, in vitro protein interaction assays, genetic epistasis in double mutants PLoS genetics High 17937504
2010 Hop2-Mnd1 heterodimer condenses double-stranded DNA into bright condensates via a concentration-dependent, reversible mechanism visible by single-molecule optical tweezers and fluorescence microscopy; neither Hop2 nor Mnd1 alone can mediate condensation; this DNA condensation activity is proposed to stimulate the synapsis phase of strand invasion. Single-molecule optical tweezers, video fluorescence microscopy Biophysical journal High 21112301
2013 Hop2-Mnd1 is a V-shaped heterodimer (by SAXS and EM) harboring three distinct DNA-binding sites: N-terminal dsDNA-binding functions of both Hop2 and Mnd1 cooperate to mediate synaptic complex assembly, while ssDNA binding by the Hop2 C-terminus stabilizes the Dmc1-ssDNA filament. Small-angle X-ray scattering, electron microscopy, deletion analysis, in vitro DNA-binding and strand exchange assays Nucleic acids research High 24150939
2014 HOP2-MND1 acts as a 'molecular trigger' that induces conformational changes in RAD51, enhancing its interaction with nucleotide cofactors (ATP), modifying its DNA-binding specificity (restricting dsDNA binding during loading, promoting dsDNA binding during homology search), and enabling RAD51 strand exchange even without divalent metal ions or with ATP-binding mutations (K133A). In vitro strand exchange assay, nucleotide binding assay, DNA-binding competition assay, mutagenesis Nature communications High 24943459
2015 Crystal structure of Hop2-Mnd1 reveals a curved rod-like structure consisting of three leucine zippers and two kinked junctions with juxtaposed winged-helix domains at one end and a helical bundle at the other; the helical bundle is sufficient for interacting with the Dmc1-ssDNA nucleofilament; the winged-helix domains bind DNA in a manner likely to perturb base pairing, facilitating strand invasion. X-ray crystallography, deletion analysis, molecular modeling Nucleic acids research High 25740648
2015 Both Hop2 and Mnd1 C-terminal regions are involved in RAD51 interaction; ATP enhances the Hop2-Mnd1/RAD51 interaction; mutations in these domains (including the HOP2 p.del201Glu ovarian dysgenesis mutation) diminish association with and functional stimulation of both RAD51 and DMC1; Hop2-Mnd1 also functions in somatic cells to repair damaged telomeres via alternative lengthening of telomeres with Rad51. Co-immunoprecipitation, in vitro strand exchange assay, site-directed mutagenesis Nucleic acids research High 25820426
2015 Cross-linking mass spectrometry of plant HOP2-MND1 reveals the major interaction site is in the central coiled-coil domains; the complex adopts an open, colinear parallel arrangement of HOP2 and MND1 with conformational flexibility at the C-terminal capping helices. Chemical cross-linking combined with mass spectrometry (XL-MS), protein threading and docking for modeling Journal of proteome research Medium 26535604
2018 Using single-molecule DNA curtains imaging, yeast Hop2-Mnd1 binds rapidly to Dmc1-ssDNA filaments with high affinity and remains bound ~1.3 min before dissociating; it shows high specificity for Dmc1 filaments with no detectable association with Rad51-ssDNA or RPA-ssDNA, providing quantitative basis for differential regulation of Dmc1 vs. Rad51. Single-molecule DNA curtains, real-time fluorescence imaging The Journal of biological chemistry High 30420424
2021 In lung adenocarcinoma cells, MND1 competitively binds to tumor suppressor KLF6, protecting E2F1 from KLF6-induced transcriptional repression; E2F1 in turn activates MND1 transcription by binding its promoter, forming a positive feedback loop that regulates cell cycle progression. Co-immunoprecipitation, ChIP assay, dual-luciferase reporter assay, mass spectrometry Cancer communications (London, England) Medium 33734616
2023 MND1 localizes to DSBs in somatic (mitotic) cells where it stimulates homologous recombination repair; its localization depends on DNA end resection and occurs through direct binding to RAD51-coated ssDNA; MND1 is specifically active in G2 phase and is required for repair of two-ended DSBs (IR, chemotherapy) but not replication-associated one-ended DSBs. Live-cell imaging, subcellular fractionation, CRISPR knockout functional assays, IR sensitivity assay, cell-cycle staging Molecular oncology High 37195379
2023 Depletion of MND1 (or its partner PSMC3IP/HOP2) in mitotic cells causes accumulation of toxic RAD51 foci after DNA damage, impairs homology-directed repair, and confers sensitivity to PARP inhibitors and ionizing radiation; the PSMC3IP p.Glu201del D-loop-defective mutant cannot rescue PARPi sensitivity, whereas wild-type PSMC3IP can, placing MND1/PSMC3IP function upstream of D-loop formation in mitotic HR. CRISPR screen, depletion/rescue experiments, RAD51 focus quantification, HR reporter assay, PARPi and IR sensitivity assays Cell reports High 37163373
2023 Using smFRET and tethered particle motion, Hop2-Mnd1 enhances Dmc1 filament assembly on ssDNA by increasing the binding rate (nucleation rate) of Dmc1 at ss/dsDNA junctions, acting through prior DNA binding to recruit Dmc1; this is mechanistically distinct from Swi5-Sfr1, which reduces Dmc1 dissociation rate during nucleation. Single-molecule FRET (smFRET), tethered particle motion, order-of-addition experiments Nucleic acids research High 37395447
2023 In gastric cancer cells, MND1 directly binds to transketolase (TKT) (identified by Co-IP and mass spectrometry); this interaction activates the PI3K/AKT signaling axis and enhances glucose uptake and lactate production; FOXA1 directly binds the MND1 promoter to inhibit its transcription. Co-immunoprecipitation, mass spectrometry, luciferase reporter assay, ChIP Cancer cell international Medium 37817120
2024 Hop2-Mnd1 acts as a DNA sequence fidelity switch: it upregulates Dmc1 activity with fully homologous or mismatch-containing substrates but suppresses illegitimate recombination between substrates with only microhomology; separation-of-function variants show that suppression of illegitimate recombination requires the Dmc1 filament interaction of Hop2-Mnd1 but not its DNA-binding activity. In vitro D-loop/strand exchange assay with separation-of-function mutants, single-molecule imaging Nature communications High 39463417
2026 O-GlcNAcylation of MND1 at Thr121 (catalyzed by OGT) stabilizes MND1 protein, maintains its nuclear localization, and is required for MND1-mediated DSB repair in breast cancer cells; T121A mutation reduces protein stability, impairs nuclear retention, elevates persistent pH2AX, and augments MND1-HOP2 interaction, perturbing the complex structure. Site-directed mutagenesis, immunoprecipitation, in vitro glycosylation assay, subcellular fractionation, pH2AX quantification, OGT/OGA inhibitor treatment Breast cancer research : BCR Medium 41668200
2026 Single-molecule imaging reveals that human DMC1-ssDNA presynaptic complexes search for homologous DNA by diffusion, generating a migrating DNA bubble; HOP2-MND1 codiffuses with the presynaptic complex, clamping the ssDNA-dsDNA junctions and maintaining an expanded DNA bubble to enable homology recognition — defining DMC1 together with HOP2-MND1 as a functional homology search unit. Single-molecule imaging of purified human proteins on DNA tightropes Proceedings of the National Academy of Sciences of the United States of America High 41746729
2025 GFP-MND1 forms long, dynamic filamentous structures in living human cells hours after DSB formation; these filaments explore nuclear space and resolve in a RAD54L-dependent manner; cohesin loss inhibits filament resolution, consistent with a role for cohesin in HR. Live-cell fluorescence imaging of GFP-MND1, genetic depletion of RAD54L and cohesin bioRxivpreprint Medium

Source papers

Stage 0 corpus · 35 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 99 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
2007 The interplay of RecA-related proteins and the MND1-HOP2 complex during meiosis in Arabidopsis thaliana. PLoS genetics 93 17937504
2004 Mnd1 is required for meiotic interhomolog repair. Current biology : CB 76 15120066
2006 The Arabidopsis thaliana MND1 homologue plays a key role in meiotic homologous pairing, synapsis and recombination. Journal of cell science 67 16763194
2006 Molecular activities of meiosis-specific proteins Hop2, Mnd1, and the Hop2-Mnd1 complex. The Journal of biological chemistry 64 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
2013 Sufficient amounts of functional HOP2/MND1 complex promote interhomolog DNA repair but are dispensable for intersister DNA repair during meiosis in Arabidopsis. The Plant cell 42 24363313
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) 28 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 The Hop2-Mnd1 Complex and Its Regulation of Homologous Recombination. Biomolecules 6 37189409
2023 MND1 and PSMC3IP control PARP inhibitor sensitivity in mitotic cells. Cell reports 5 37163373
2021 Genetic network and gene set enrichment analyses identify MND1 as potential diagnostic and therapeutic target gene for lung adenocarcinoma. Scientific reports 4 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
2025 MND1 Promotes the Proliferation of Prostate Cancer Cell Via the CCNB1/p53 Signaling Pathway. Current cancer drug targets 0 40353402