ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex

Science

Volumn 308, Issue 5721, 2005, Pages 551-554

  Lee, Ji Hoon ^a   Paull, Tanya T ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; ANIMAL CELL CULTURE; DNA; MOLECULES; PROTEINS; SENSORS;

ATAXIA-TELANGIECTASIA MUTATED (ATM); CELLULAR TARGETS; MAMMALIAN CELLS; MRE11-RAD50-NBS1 (MRN) COMPLEX;

ENZYMES;

ATM PROTEIN; CHECKPOINT KINASE 2; DOUBLE STRANDED DNA; MRE11 PROTEIN; PROTEIN P53; RAD50 PROTEIN; SINGLE STRANDED DNA;

BIOCHEMISTRY; GENETICS;

APOPTOSIS; ARTICLE; AUTOPHOSPHORYLATION; DIMERIZATION; DNA DAMAGE; DNA REPAIR; DNA STRAND BREAKAGE; ENZYME ACTIVATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING;

AMINO ACID SUBSTITUTION; CELL CYCLE PROTEINS; CELL LINE; DIMERIZATION; DNA; DNA DAMAGE; DNA REPAIR; DNA REPAIR ENZYMES; DNA, SINGLE-STRANDED; DNA-BINDING PROTEINS; ENZYME ACTIVATION; HUMANS; MUTATION; NUCLEAR PROTEINS; NUCLEIC ACID CONFORMATION; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT PROTEINS; SERINE; SIGNAL TRANSDUCTION; TRANSFECTION; TUMOR SUPPRESSOR PROTEINS;

ATAXIA; ATAXIA TELANGIECTASIA; MAMMALIA;

EID: 17644409069     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1108297     Document Type: Article

References (21)

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21. Molecular interaction data have been deposited in the Biomolecular Interaction Network Database (BIND) with accession codes 216020 to 216045. We thank M. Kastan and R. Abraham for expression constructs; D. Ramsden, M. Gellert, and M. O'Dea for Rag1/Rag2 protein; S. Stevens for technical advice; members of the Paull lab for their help; and R. Rothstein for a helpful word. This work was supported by NIH (grant