The cadherin cytoplasmic domain is unstructured in the absence of β-catenin. A possible mechanism for regulating cadherin turnover

Journal of Biological Chemistry

Volumn 276, Issue 15, 2001, Pages 12301-12309

  Huber, Andrew H ^a   Stewart, Daniel B ^a   Laurents, Douglas V ^a   Nelson, W James ^a   Weis, William I ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CYTOLOGY; FLUORESCENCE; NUCLEAR MAGNETIC RESONANCE; PROTEINS;

CELL ADHESION; PROTEOLYSIS;

BIOCHEMISTRY;

ACTIN; ALPHA CATENIN; BETA CATENIN; CADHERIN; MEMBRANE PROTEIN; PROTEASOME; TRYPTOPHAN; UBIQUITIN; CTNNB1 PROTEIN, HUMAN; CYTOSKELETON PROTEIN; PRIMER DNA; RECOMBINANT PROTEIN; TRANSACTIVATOR PROTEIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; CELL ADHESION; CELL JUNCTION; CIRCULAR DICHROISM; COMPLEX FORMATION; CYTOSKELETON; ELECTRICITY; FLUORESCENCE; IONIC STRENGTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; ANIMAL; CHEMISTRY; CYTOPLASM; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY; SPECTROFLUOROMETRY;

ANIMALIA; MURINAE;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BETA CATENIN; CADHERINS; CELL ADHESION; CIRCULAR DICHROISM; CYTOPLASM; CYTOSKELETAL PROTEINS; DNA PRIMERS; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE; TRANS-ACTIVATORS;

EID: 0035853847     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010377200     Document Type: Article

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