USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism.

Knobel, Philip A

USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism. [electronic resource] - Molecular and cellular biology Jun 2014 - 2062-74 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

1098-5549

10.1128/MCB.00197-14 doi


Animals
Apoptosis--genetics
Ataxia Telangiectasia Mutated Proteins--metabolism
B-Lymphocytes--cytology
Cell Cycle Proteins--metabolism
Cell Line
Checkpoint Kinase 2--metabolism
DNA Breaks, Double-Stranded
DNA Damage
DNA Repair--genetics
DNA-Binding Proteins
Genomic Instability
HEK293 Cells
Humans
Immunoglobulin Class Switching--immunology
Intracellular Signaling Peptides and Proteins--genetics
M Phase Cell Cycle Checkpoints
Mice
Mice, Inbred C57BL
Neoplasms--genetics
Nuclear Proteins--metabolism
RNA Interference
RNA, Small Interfering
S Phase Cell Cycle Checkpoints--genetics
Signal Transduction--genetics
Thymocytes--immunology
Tumor Suppressor p53-Binding Protein 1
Ubiquitin Thiolesterase--genetics