Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells

Nature Cell Biology

Volumn 18, Issue 7, 2016, Pages 765-776

  Lee, Jin Gu ^a   Takahama, Shokichi ^b,d   Zhang, Guofeng ^c   Tomarev, Stanislav I ^b   Ye, Yihong ^a,d  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL EYE INSTITUTE   (United States)

^c NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING   (United States)

^d KUMAMOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROTEASOME; PROTEIN BINDING; PROTEINASE; USP19 PROTEIN, HUMAN;

ARTICLE; AUTOPHAGOSOME; CATALYSIS; CELL ENCAPSULATION; ENDOPLASMIC RETICULUM; ENDOSOME; EVOLUTIONARY ADAPTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN HOMEOSTASIS; PROTEIN MISFOLDING; PROTEIN PROCESSING; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEOMICS; SIGNAL TRANSDUCTION; UBIQUITINATION; CYTOSOL; DEFICIENCY; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; HUMAN; METABOLISM; PHYSIOLOGY; PROCEDURES; PROTEIN FOLDING; PROTEIN TRANSPORT;

CYTOSOL; ENDOPEPTIDASES; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; HUMANS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN TRANSPORT; PROTEOMICS;

EID: 84976515858     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb3372     Document Type: Article

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