How a disordered ubiquitin ligase maintains order in nuclear protein homeostasis

Nucleus

Volumn 2, Issue 4, 2011, Pages 264-270

  Rosenbaum, Joel C ^a   Gardner, Richard G ^a  

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

Author keywords

Intrinsic disorder; Proteasome; Protein quality control; San1; Ubiquitin; Ubiquitin ligase; Unstructured

Indexed keywords

CHAPERONE; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 70; NUCLEAR PROTEIN; PROTEIN SAN1; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; BINDING KINETICS; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL NUCLEUS; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; GENETIC TRANSCRIPTION; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN HOMEOSTASIS; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN QUALITY CONTROL; PROTEIN STRUCTURE; QUALITY CONTROL; REVIEW; STEADY STATE; STRUCTURE ANALYSIS; UBIQUITINATION; YEAST CELL;

EID: 83455179425     PISSN: 19491034     EISSN: 19491042     Source Type: Journal    
DOI: 10.4161/nucl.2.4.16118     Document Type: Review

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