Regulation of the Src family kinase Lck by Hsp90 and ubiquitination

Molecular and Cellular Biology

Volumn 24, Issue 13, 2004, Pages 5667-5676

  Giannini, Ana ^a   Bijlmakers, Marie José ^a  

^a GUY S HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE LCK; PROTEIN TYROSINE KINASE; SERINE; T LYMPHOCYTE RECEPTOR; TYROSINE;

ANIMAL CELL; ARTICLE; BINDING SITE; CELL STRAIN COS7; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME STABILITY; HUMAN; HUMAN CELL; MOLECULAR INTERACTION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; RECEPTOR UPREGULATION; SRC HOMOLOGY DOMAIN; T LYMPHOCYTE; UBIQUITINATION;

ANIMALS; CELLS, CULTURED; ENZYME INHIBITORS; ENZYME STABILITY; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LYMPHOCYTE ACTIVATION; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); MICE; MUTATION, MISSENSE; PHOSPHORYLATION; PROTEIN BINDING; T-LYMPHOCYTES; TRANSFECTION; UBIQUITIN;

ANIMALIA;

EID: 2942744500     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.13.5667-5676.2004     Document Type: Article

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