Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 15, 2014, Pages 5544-5549

  Unverdorben, Pia ^a   Beck, Florian ^a   Sledz, Pawel ^a   Schweitzer, Andreas ^a   Pfeifer, Günter ^a   Plitzko, Jürgen M ^a   Baumeister, Wolfgang ^a   Förster, Friedrich ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Conformational Switching; Proteolysis; Proteostasis; Quality Control

Indexed keywords

26S PROTEASOME; AAA ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE GAMMAS; PROTEASOME; PROTEIN; RPN1 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; DENSITY; PRIORITY JOURNAL; PROTEIN DEGRADATION; UBIQUITINATION;

CONFORMATIONAL SWITCHING; PROTEOLYSIS; PROTEOSTASIS; QUALITY CONTROL;

CRYOELECTRON MICROSCOPY; DATABASES, FACTUAL; IMAGE PROCESSING, COMPUTER-ASSISTED; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PROTEASOME ENDOPEPTIDASE COMPLEX;

EID: 84898807479     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1403409111     Document Type: Article

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