A point mutation in the FAT domain constitutively increases the kinase activity of Rad3ATR and bypasses the requirement for 9-1-1 phosphorylation to activate the DNA replication checkpoint.

Saved in:
Bibliographic Details
Title: A point mutation in the FAT domain constitutively increases the kinase activity of Rad3ATR and bypasses the requirement for 9-1-1 phosphorylation to activate the DNA replication checkpoint.
Authors: Dev K; Department of Pharmacology and Toxicology, Boonshoft School of Medicine, Wright State University, Dayton, Ohio, United States of America., Rider SD Jr; Department of Pharmacology and Toxicology, Boonshoft School of Medicine, Wright State University, Dayton, Ohio, United States of America., Singh B; Department of Pharmacology and Toxicology, Boonshoft School of Medicine, Wright State University, Dayton, Ohio, United States of America., Saini A; Department of Pharmacology and Toxicology, Boonshoft School of Medicine, Wright State University, Dayton, Ohio, United States of America., Xu YJ; Department of Pharmacology and Toxicology, Boonshoft School of Medicine, Wright State University, Dayton, Ohio, United States of America.
Source: PLoS genetics [PLoS Genet] 2026 Jun 22; Vol. 22 (6), pp. e1012213. Date of Electronic Publication: 2026 Jun 22 (Print Publication: 2026).
Publication Type: Journal Article
Journal Info: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101239074 Publication Model: eCollection Cited Medium: Internet ISSN: 1553-7404 (Electronic) Linking ISSN: 15537390 NLM ISO Abbreviation: PLoS Genet Subsets: MEDLINE
Database: MEDLINE Ultimate
Full text is not displayed to guests.
Description
ISSN:1553-7404
DOI:10.1371/journal.pgen.1012213