ArticleNucleic acids research2000
Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
What it found
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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
103 citing papers in PubMed, 268 citations in OpenAlex.
- Energetically equivalent structural transitions in the Rad17-Rad9-Hus1-Rad1-Rhino complex underlie the sequential progression from activation through maintenance to inactivation of the ATR-dependent DNA damage response.Nucleic acids research · 2026Article
- Structures of 9-1-1 DNA checkpoint clamp loading at gaps from start to finish and ramification on biology.Cell reports · 2023Article
- Structures of 9-1-1 DNA checkpoint clamp loading at gaps from start to finish and ramification to biology.bioRxiv : the preprint server for biology · 2023Article
- DNA is loaded through the 9-1-1 DNA checkpoint clamp in the opposite direction of the PCNA clamp.Nature structural & molecular biology · 2022Article
- Critical role of SMG7 in activation of the ATR-CHK1 axis in response to genotoxic stress.Scientific reports · 2021Article
- The Role of Nitric Oxide in Cancer: Master Regulator or NOt?International journal of molecular sciences · 2020Review
- Preserving salivary gland physiology against genotoxic damage - the Tousled way.Oral diseases · 2018Review
- Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017Review
- Article
- Recovery from the DNA Replication Checkpoint.Genes · 2016Review
- The effects of nonyl phenoxypolyethoxyl ethanol on cell damage pathway gene expression in SK-NSH cells.The Korean journal of internal medicine · 2015Article
- Association of the Rad9-Rad1-Hus1 checkpoint clamp with MYH DNA glycosylase and DNA.DNA repair · 2015Article
- Visualization of the physical and functional interaction between hMYH and hRad9 by Dronpa bimolecular fluorescence complementation.BMC molecular biology · 2014Article
- The N-terminus of Mcm10 is important for interaction with the 9-1-1 clamp and in resistance to DNA damage.Nucleic acids research · 2014Article
- OsHUS1 facilitates accurate meiotic recombination in rice.PLoS genetics · 2014Article
- Interaction of apurinic/apyrimidinic endonuclease 2 (Apn2) with Myh1 DNA glycosylase in fission yeast.DNA repair · 2014Article
- Role of the checkpoint clamp in DNA damage response.Biomolecules · 2013Article
- Tousled-like kinase-dependent phosphorylation of Rad9 plays a role in cell cycle progression and G2/M checkpoint exit.PloS one · 2013Article
- Similarities and differences between "uncapped" telomeres and DNA double-strand breaks.Chromosoma · 2012Review
- Article
43 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The repair of damaged DNA is coupled to the completion of DNA replication by several cell cycle checkpoint proteins, including, for example, in fission yeast Rad1(Sp), Hus1(Sp), Rad9(Sp) and Rad17(Sp). We have found that these four proteins are conserved with protein sequences throughout eukaryotic evolution. Using computational techniques, including fold recognition, comparative modeling and generalized sequence profiles, we have made high confidence structure predictions for the each of the Rad1, Hus1 and Rad9 protein families (Rad17(Sc), Mec3(Sc) and Ddc1(Sc) in budding yeast, respectively). Each of these families was found to share a common protein fold with that of PCNA, the sliding clamp protein that tethers DNA polymerase to its template. We used previously reported genetic and biochemical data for these proteins from yeast and human cells to predict a heterotrimeric PCNA-like ring structure for the functional Rad1/Rad9/Hus1 complex and to determine their exact order within it. In addition, for each individual protein family, contact regions with neighbors within the PCNA-like ring were identified. Based on a molecular model for Rad17(Sp), we concluded that members of this family, similar to the subunits of the RFC clamp-loading complex, are capable of coupling ATP binding with conformational changes required to load a sliding clamp onto DNA. This model substantiates previous findings regarding the behavior of Rad17 family proteins upon DNA damage and within the RFC complex of clamp-loading proteins.
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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.