ArticleBiophysical journal2018
MutSγ-Induced DNA Conformational Changes Provide Insights into Its Role in Meiotic Recombination.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 29 citations in OpenAlex.
- Multiscale Conformational Dynamics of DNA Holliday Junctions Modulated by Ion Concentration: Insights from Fluorescence Correlation Spectroscopy and Time-Resolved Anisotropy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Mms4 chromosomal association reveals functional relationships between meiotic crossover pathways in budding yeast.PLoS genetics · 2026Article
- The DNA mismatch repair protein Msh4 is essential for meiosis of male but not for female in zebrafish.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026Article
- Integrated analysis of lncRNA-miRNA-mRNA networks reveals stage-specific molecular regulation of oogenesis in Chinese alligator (Alligator sinensis).BMC genomics · 2026Article
- Mechanism and potential therapeutic strategies of genetic abnormalities involved in deoxyribonucleic acid double-strand breaks leading to the development of human non-obstructive azoospermia.Reproductive biology and endocrinology : RB&E · 2026Review
- HEIP1 orchestrates pro-crossover protein activity during mammalian meiosis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genetic and functional analysis reveals novel mutations in meiotic genes underlying non-obstructive azoospermia.Journal of assisted reproduction and genetics · 2025Article
- Proximity labeling reveals new functional relationships between meiotic recombination proteins in S. cerevisiae.PLoS genetics · 2024Article
- Site-Specific Investigation of DNA Holliday Junction Dynamics and Structure with 6-Methylisoxanthopterin, a Fluorescent Guanine Analog.bioRxiv : the preprint server for biology · 2024Article
- The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024Review
- The DNA helicase FANCJ (BRIP1) functions in double strand break repair processing, but not crossover formation during prophase I of meiosis in male mice.PLoS genetics · 2024Article
- The DNA helicase FANCJ (BRIP1) functions in Double Strand Break repair processing, but not crossover formation during Prophase I of meiosis in male mice.bioRxiv : the preprint server for biology · 2023Article
- Site-specific investigation of DNA Holliday Junction dynamics and structure with 6-Methylisoxanthopterin, a fluorescent guanine analog.Trends in photochemistry & photobiology · 2023Article
- Integration Host Factor Binds DNA Holliday Junctions.International journal of molecular sciences · 2022Article
- Robust designation of meiotic crossover sites by CDK-2 through phosphorylation of the MutSγ complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- DNA repair, recombination, and damage signaling.Genetics · 2022Review
- Article
- Expanded roles for the MutL family of DNA mismatch repair proteins.Yeast (Chichester, England) · 2021Review
- A novel function for CDK2 activity at meiotic crossover sites.PLoS biology · 2020Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In many organisms, MutSγ plays a role in meiotic recombination, facilitating crossover formation between homologous chromosomes. Failure to form crossovers leads to improper segregation of chromosomes and aneuploidy, which in humans result in infertility and birth defects. To improve current understanding of MutSγ function, this study investigates the binding affinities and structures of MutSγ in complex with DNA substrates that model homologous recombination intermediates. For these studies, we overexpressed and isolated from Escherichia coli the yeast MutSγ protein Saccharomyces cerevisiae (Sc) Msh4-Msh5. Sc Msh4-Msh5 binds Holliday junction (HJ)-like substrates, 3' overhangs, single-stranded (ss) forks, and the displacement loop with nanomolar affinity. The weakest binding affinities are detected for an intact duplex and open-junction construct. Similar to the human protein, Sc Msh4-Msh5 exhibits the highest affinity for the HJ with a K
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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.