Ornithine decarboxylase-antizyme is rapidly degraded through a mechanism that requires functional ubiquitin-dependent proteolytic activity

European Journal of Biochemistry

Volumn 269, Issue 4, 2002, Pages 1316-1322

  Gandre, Shilpa ^a   Bercovich, Zippi ^a   Kahana, Chaim ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Antizyme; Ornithine decarboxylase; Polyamines; Proteasome; Protein degradation

Indexed keywords

ANTIZYME; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; MG 115; ORNITHINE DECARBOXYLASE; PROTEASOME INHIBITOR; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CODON; CONTROLLED STUDY; ENZYME DEGRADATION; ENZYME METABOLISM; ENZYME STABILITY; HUMAN; HUMAN CELL; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RETICULOCYTE LYSATE;

ANIMALS; MICE; ORNITHINE DECARBOXYLASE; PEPTIDE HYDROLASES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEINS; UBIQUITIN;

ANIMALIA; MAMMALIA;

EID: 0036183476     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.02774.x     Document Type: Article

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