Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding

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

Volumn 107, Issue 5, 2010, Pages 2001-2006

  Hagai, Tzachi ^a   Levy, Yaakov ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Coarse grained simulations; Posttranslational modifications; Protein degradation; Protein folding ubiquitination

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR 2D; UBIQUITIN;

ARTICLE; IN VIVO STUDY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; THERMODYNAMICS; THERMOSTABILITY; UBIQUITINATION;

BIOPHYSICAL PHENOMENA; CYCLIN-DEPENDENT KINASE INHIBITOR P19; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEINS; THERMODYNAMICS; UBIQUITIN; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITINATION;

EUKARYOTA;

EID: 76649123968     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0912335107     Document Type: Article

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