CtIP maintains stability at common fragile sites and inverted repeats by end resection-independent endonuclease activity.
Wang, Hailong; Li, Yongjiang; Truong, Lan N; Shi, Linda Z; Hwang, Patty Yi-Hwa; He, Jing; Do, Johnny; Cho, Michael Jeffrey; Li, Hongzhi; Negrete, Alejandro; Shiloach, Joseph; Berns, Michael W; Shen, Binghui; Chen, Longchuan; Wu, Xiaohua.
; 54(6): 1012-21, 2014 Jun 19.
Artigo em Inglês | MEDLINE | ID: mdl-24837675
Regulation of DNA-end resection by hnRNPU-like proteins promotes DNA double-strand break signaling and repair.
Nuclear pores protect genome integrity by assembling a premitotic and Mad1-dependent anaphase inhibitor.
Nbs1 Converts the Human Mre11/Rad50 Nuclease Complex into an Endo/Exonuclease Machine Specific for Protein-DNA Adducts.
USP4 Auto-Deubiquitylation Promotes Homologous Recombination.
PTIP associates with Artemis to dictate DNA repair pathway choice.
Catalytic and noncatalytic roles of the CtIP endonuclease in double-strand break end resection.
The ubiquitin E3 ligase TRIM31 promotes aggregation and activation of the signaling adaptor MAVS through Lys63-linked polyubiquitination.
FRA2A is a CGG repeat expansion associated with silencing of AFF3.
Phosphorylated CtIP Functions as a Co-factor of the MRE11-RAD50-NBS1 Endonuclease in DNA End Resection.
A mechanism of cohesin-dependent loop extrusion organizes zygotic genome architecture.