Lysine 188 substitutions convert the pattern of proteasome activation by REGγ to that of REGs α and β

EMBO Journal

Volumn 20, Issue 13, 2001, Pages 3359-3369

  Li, Jun ^a   Gao, Xiaolin ^a   Ortega, Joaquin ^b   Nazif, Tamim ^c   Joss, Lisa ^a   Bogyo, Matthew ^c   Steven, Alasdair C ^b   Rechsteiner, Martin ^a  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^b NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Affinity labeling; Chimera; Enzyme specificity; Mutagenesis

Indexed keywords

PROTEASOME; PROTEIN REG ALPHA; PROTEIN REG BETA; PROTEIN REG GAMMA; PROTEIN SUBUNIT; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTIGENS, SURFACE; AUTOANTIGENS; CALCIUM-BINDING PROTEINS; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; ENZYME ACTIVATION; LITHOSTATHINE; LYSINE; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; PHOSPHOPROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 0035796464     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.13.3359     Document Type: Article

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