Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-L

FEBS Journal

Volumn 283, Issue 1, 2016, Pages 157-172

  Hosokawa, Nobuko ^a   Wada, Ikuo ^b  

^a KYOTO UNIVERSITY   (Japan)

^b FUKUSHIMA MEDICAL UNIVERSITY   (Japan)

Author keywords

endoplasmic reticulum; ER associated degradation; HRD1 ubiquitin ligase complex; membrane protein; SEL1L protein

Indexed keywords

ALPHA 1 ANTITRYPSIN; MEMBRANE PROTEIN; PROTEIN SEL1L; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE HRD1; UNCLASSIFIED DRUG; PROTEIN; SEL1L PROTEIN, HUMAN; SYVN1 PROTEIN, HUMAN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TRANSPORT; PROTEIN UNFOLDING; REGULATORY MECHANISM; CHEMISTRY; ENDOPLASMIC RETICULUM; METABOLISM; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE;

ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; HUMANS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; UBIQUITIN-PROTEIN LIGASES;

EID: 84954369024     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13564     Document Type: Article

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