Base-CP proteasome can serve as a platform for stepwise lid formation

Bioscience Reports

Volumn 35, Issue , 2015, Pages

  Yu, Zanlin ^a   Livnat Levanon, Nurit ^a   Kleifeld, Oded ^b   Mansour, Wissam ^a   Nakasone, Mark A ^a   Castaneda, Carlos A ^c   Dixon, Emma K ^c   Fushman, David ^c   Reis, Noa ^a   Pick, Elah ^d   Glickman, Michael H ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^b MONASH UNIVERSITY   (Australia)

^c UNIVERSITY OF HAIFA   (Israel)

^d University of Maryland   (United States)

Author keywords

19S regulatory particle; 20S core particle; 26S proteasome; Base; Lid; MPN; PCI; rpn11 m1

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEASOME; REGULATORY PARTICLE NON ATPASE 11; REGULATORY PARTICLE NON ATPASE 8; UNCLASSIFIED DRUG; ATP DEPENDENT 26S PROTEASE; PROTEINASE; RPN11 PROTEIN, S CEREVISIAE; RPN6 PROTEIN, S CEREVISIAE; RPN8 PROTEIN, S CEREVISIAE; RPN9 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME STABILITY; FUNGAL STRAIN; IN VITRO STUDY; MITOCHONDRION; MUTANT; NONHUMAN; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN SUBUNIT; YEAST; CHEMISTRY; GENE SILENCING; GENETICS; METABOLISM; MOLECULAR MODEL; MUTATION; PROTEIN DOMAIN;

EUKARYOTA;

ENDOPEPTIDASES; GENE SILENCING; MODELS, MOLECULAR; MUTATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN DOMAINS; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84929472388     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20140173     Document Type: Article

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