Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility

Journal of Biological Chemistry

Volumn 288, Issue 9, 2013, Pages 6130-6139

  Fredrickson, Eric K ^a   Gallagher, Pamela S ^a   Candadai, Sarah V Clowes ^a   Gardner, Richard G ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

BUDDING YEASTS; HYDROPHOBIC RESIDUES; MISFOLDED PROTEINS; MISFOLDING; NUCLEAR PROTEINS; PROTEASOMES; PROTEIN QUALITY CONTROL; SUBSTRATE RECOGNITION; UBIQUITIN-PROTEIN LIGASES;

HYDROPHOBICITY; QUALITY CONTROL; SUBSTRATES;

PROTEINS;

NUCLEAR PROTEIN; PROTEIN SAN1; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ARTICLE; CELLULAR DISTRIBUTION; FUNGAL STRAIN; HYDROPHOBICITY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN TARGETING; SIGNAL TRANSDUCTION; SOLUBILITY;

HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; NUCLEAR PROTEINS; PROTEIN FOLDING; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SOLUBILITY; UBIQUITIN-PROTEIN LIGASES;

EID: 84874772986     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.406710     Document Type: Article

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