The base of the proteasome regulatory particle exhibits chaperone-like activity

Nature Cell Biology

Volumn 1, Issue 4, 1999, Pages 221-226

  Braun, Beate C ^a   Glickman, Michael ^b   Kraft, Regine ^c   Dahlmann, Burkhardt ^d   Kloetzel, Peter M ^a   Finley, Daniel ^e   Schmidt, Marion ^a,e  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^b TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^c MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^d LEIBNIZ CENTER FOR DIABETES RESEARCH AT HEINRICH HEINE UNIVERSITY DÜSSELDORF   (Germany)

^e HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; CITRATE SYNTHASE; CYSTEINE PROTEINASE; ENZYME ACTIVATOR; MULTIENZYME COMPLEX; PROTEASOME; UBIQUITIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HUMAN; IN VITRO STUDY; METABOLISM; MOLECULAR GENETICS; PROTEIN FOLDING; PROTEIN RENATURATION; SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CITRATE (SI)-SYNTHASE; CYSTEINE ENDOPEPTIDASES; ENZYME REACTIVATORS; HUMANS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN FOLDING; PROTEIN RENATURATION; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY; UBIQUITINS;

EID: 0033176770     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/12043     Document Type: Article

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