ArticleNucleic acids research2006
RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Genome-wide association study of cocaine self-administration behavior in Heterogeneous Stock rats.Nature communications · 2026Article
- Disruption of meiotic double-strand break dynamics provokes germline human infertility in both sexes.Journal of assisted reproduction and genetics · 2026Article
- RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phosphoregulation of RAD51AP1 function in homology-directed repair.bioRxiv : the preprint server for biology · 2025Article
- A single-nucleus transcriptomic atlas of primate testicular aging reveals exhaustion of the spermatogonial stem cell reservoir and loss of Sertoli cell homeostasis.Protein & cell · 2023Article
- RAD51AP2 is required for efficient meiotic recombination between X and Y chromosomes.Science advances · 2022Article
- NUCKS1 promotes RAD54 activity in homologous recombination DNA repair.The Journal of cell biology · 2020Article
- Two distinct pathways of pregranulosa cell differentiation support follicle formation in the mouse ovary.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Unified single-cell analysis of testis gene regulation and pathology in five mouse strains.eLife · 2019Article
- Review
- Article
- NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability.Nucleic acids research · 2015Article
- RAD51AP1-deficiency in vertebrate cells impairs DNA replication.DNA repair · 2014Article
- Homologous recombination and its regulation.Nucleic acids research · 2012Review
- Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in homologous DNA repair.The Journal of biological chemistry · 2012Article
- RAD51-associated protein 1 (RAD51AP1) interacts with the meiotic recombinase DMC1 through a conserved motif.The Journal of biological chemistry · 2011Article
- Molecular basis for enhancement of the meiotic DMC1 recombinase by RAD51 associated protein 1 (RAD51AP1).Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Cellular redistribution of Rad51 in response to DNA damage: novel role for Rad51C.The Journal of biological chemistry · 2009Article
- Promotion of homologous recombination and genomic stability by RAD51AP1 via RAD51 recombinase enhancement.Molecular cell · 2007Article
- A novel homozygous loss-of-function mutation inAsian journal of andrologyArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Many interacting proteins regulate and/or assist the activities of RAD51, a recombinase which plays a critical role in both DNA repair and meiotic recombination. Yeast two-hybrid screening of a human testis cDNA library revealed a new protein, RAD51AP2 (RAD51 Associated Protein 2), that interacts strongly with RAD51. A full-length cDNA clone predicts a novel vertebrate-specific protein of 1159 residues, and the RAD51AP2 transcript was observed only in meiotic tissue (i.e. adult testis and fetal ovary), suggesting a meiotic-specific function for RAD51AP2. In HEK293 cells the interaction of RAD51 with an ectopically-expressed recombinant large fragment of RAD51AP2 requires the C-terminal 57 residues of RAD51AP2. This RAD51-binding region shows 81% homology to the C-terminus of RAD51AP1/PIR51, an otherwise totally unrelated RAD51-binding partner that is ubiquitously expressed. Analyses using truncations and point mutations in both RAD51AP1 and RAD51AP2 demonstrate that these proteins use the same structural motif for RAD51 binding. RAD54 shares some homology with this RAD51-binding motif, but this homologous region plays only an accessory role to the adjacent main RAD51-interacting region, which has been narrowed here to 40 amino acids. A novel protein, RAD51AP2, has been discovered that interacts with RAD51 through a C-terminal motif also present in RAD51AP1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.