Mammalian OS-9 Is Upregulated in Response to Endoplasmic Reticulum Stress and Facilitates Ubiquitination of Misfolded Glycoproteins

Journal of Molecular Biology

Volumn 385, Issue 4, 2009, Pages 1032-1042

  Alcock, Felicity ^a   Swanton, Eileithyia ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

endoplasmic reticulum; ERAD; N glycosylation; quality control; ubiquitination

Indexed keywords

CELL PROTEIN; GLYCOPROTEIN; OS 9 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CELL STRUCTURE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; ENDOPLASMIC RETICULUM STRESS; GLYCOSYLATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN TRANSPORT; RNA INTERFERENCE; SIGNAL TRANSDUCTION; UBIQUITINATION; UPREGULATION;

MAMMALIA;

EID: 58149336774     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.11.045     Document Type: Article

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