A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein

EMBO Journal

Volumn 17, Issue 20, 1998, Pages 5964-5973

  Breitschopf, Kristin ^a   Bengal, Eyal ^a   Ziv, Tamar ^a   Admon, Arie ^a   Ciechanover, Aaron ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

MyoD; N terminus; Proteolysis; Ubiquitin

Indexed keywords

HELIX LOOP HELIX PROTEIN; LYSINE; MYOD PROTEIN; PROTEASOME; TRANSACTIVATOR PROTEIN; UBIQUITIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CHEMICAL MODIFICATION; CONJUGATION; EUKARYOTIC CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ADENOSINE TRIPHOSPHATE; ANIMALS; CELLS, CULTURED; COS CELLS; LYSINE; MYOD PROTEIN; PEPTIDE FRAGMENTS; PLASMIDS; RADIOACTIVE TRACERS; TRANSFECTION; UBIQUITINS;

EID: 0032531925     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.20.5964     Document Type: Article

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