Identification of Src Phosphorylation Sites in the Catenin p120 ctn

Journal of Biological Chemistry

Volumn 276, Issue 30, 2001, Pages 28006-28013

  Mariner, Deborah J ^a   Anastasiadis, Panos ^a   Keilhack, Heike ^b   Böhmer, Frank D ^b   Wang, Jue ^a   Reynolds, Albert B ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; CELLS; ENZYME KINETICS; PHYSIOLOGY;

PHOSPHORYLATION;

ENZYMES;

CADHERIN; CATENIN; EPIDERMAL GROWTH FACTOR; MUTANT PROTEIN; PHENYLALANINE; PROTEIN P120; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SHP 1; TYROSINE; UNCLASSIFIED DRUG; CADHERIN ASSOCIATED SRC SUBSTRATE P120; CADHERIN-ASSOCIATED SRC SUBSTRATE P120; CELL ADHESION MOLECULE; GLUTATHIONE TRANSFERASE; PERVANADATE; PHOSPHOPROTEIN; PROTEIN KINASE P60; VANADIC ACID;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CELL JUNCTION; CELL TRANSFORMATION; CONTROLLED STUDY; CYTOPLASM; EMBRYO; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MUTATION; NONHUMAN; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; ANIMAL; CELL LINE; CELL STRAIN COS1; CHEMISTRY; DOMINANT GENE; GENE DELETION; GENETIC TRANSFECTION; METABOLISM; NUCLEOTIDE SEQUENCE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SERODIAGNOSIS; SITE DIRECTED MUTAGENESIS; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING;

ANIMALS; BINDING SITES; BLOTTING, WESTERN; CELL ADHESION MOLECULES; CELL LINE; COS CELLS; CYTOPLASM; DNA MUTATIONAL ANALYSIS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; EPIDERMAL GROWTH FACTOR; GENE DELETION; GENES, DOMINANT; GLUTATHIONE TRANSFERASE; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENYLALANINE; PHOSPHOPROTEINS; PHOSPHORYLATION; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS PP60(C-SRC); TRANSFECTION; TYROSINE; VANADATES;

EID: 0035958886     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102443200     Document Type: Article

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