Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop

Molecular and Cellular Biology

Volumn 21, Issue 1, 2001, Pages 88-99

  Garrett, S ^a   Barton, W A ^a   Knights, R ^a   Jin, P ^a   Morgan, D O ^a   Fisher, R P ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 2; SERINE;

ARTICLE; CATALYSIS; COMPLEX FORMATION; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; T LYMPHOCYTE ACTIVATION; TEMPERATURE SENSITIVE MUTANT;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACULOVIRIDAE; CDC2 PROTEIN KINASE; CDC2-CDC28 KINASES; CELL CYCLE; CONSENSUS SEQUENCE; CYCLIN-DEPENDENT KINASE 2; CYCLIN-DEPENDENT KINASES; CYCLINS; ENZYME ACTIVATION; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHOPEPTIDES; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

METAZOA;

EID: 0034747803     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.1.88-99.2001     Document Type: Article

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