Conserved ATRMec1 phosphorylation-independent activation of Chk1 by single amino acid substitution in the GD domain

Cell Cycle

Volumn 8, Issue 11, 2009, Pages 1788-1793

  Pereira, Elizabeth ^a   Chen, Yinhuai ^b   Sanchez, Yolanda ^a,c  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^c NONE   (United States)

Author keywords

ATR; Checkpoint kinases; DNA damage; DNA replication; Rad9; S phase checkpoint; Saccharomyces cerevisiae

Indexed keywords

ATR PROTEIN; CHECKPOINT KINASE 1; GADOLINIUM; ATR PROTEIN, HUMAN; CELL CYCLE PROTEIN; PROTEIN KINASE; PROTEIN RAD9; PROTEIN SERINE THREONINE KINASE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME REGULATION; GENE MUTATION; HUMAN; HUMAN CELL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; AMINO ACID SEQUENCE; BINDING SITE; CELL LINE; CHEMISTRY; DNA DAMAGE; DNA REPLICATION; ENZYME ACTIVE SITE; GENETICS; HELA CELL; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYTIC DOMAIN; CELL CYCLE PROTEINS; CELL LINE; DNA DAMAGE; DNA REPLICATION; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 66749149044     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.8.11.8737     Document Type: Article

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