Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain

Biochemical Journal

Volumn 381, Issue 1, 2004, Pages 275-285

  Rinaldi, Teresa ^a   Pick, Elah ^b   Gambadoro, Alessia ^a   Zilli, Stefania ^a   Maytal Kivity, Vered ^b   Frontali, Laura ^a   Glickman, Michael H ^b  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

Deubiquitination; Mitochondria; MPN (Mpr1, Pad1, N terminal) domain; Proteasome; Rpn11; Ubiquitin

Indexed keywords

BIODEGRADATION; MORPHOLOGY; MUTAGENESIS; PROTEINS;

POLYUBIQUITIN CHAINS; PROTEASOMES; PROTEOLYSIS;

BIOCHEMISTRY;

PROTEASOME;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL CYCLE; CELL FUNCTION; CELL STRUCTURE; GENE MUTATION; GENETIC COMPLEMENTATION; MITOCHONDRION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN MOTIF; WILD TYPE;

ACETYLTRANSFERASES; CARBOXY-LYASES; CATALYTIC DOMAIN; ENDOPEPTIDASES; GENETIC COMPLEMENTATION TEST; MITOCHONDRIA; PEPTIDE HYDROLASES; PEPTIDE MAPPING; PEPTIDES; PHENOTYPE; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN;

CHIMAERIFORMES;

EID: 3142723187     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040008     Document Type: Article

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