Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: One for soluble Z variant of human α-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ

Molecular Biology of the Cell

Volumn 17, Issue 1, 2006, Pages 203-212

  Kruse, Kristina B ^a   Brodsky, Jeffrey L ^b   McCracken, Ardythe A ^a  

^a UNIVERSITY OF NEVADA   (United States)

^b UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; CARBOXYPEPTIDASE C; MUTANT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE;

ARTICLE; ATG6 GENE; AUTOPHAGY; CELL VACUOLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ERAD GENE; FUNGUS MUTANT; GENE; GENE IDENTIFICATION; GENE OVEREXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN TARGETING; QUALITY CONTROL; SOLUBILITY; TRANS GOLGI NETWORK; VPS30 GENE; YEAST;

ALPHA 1-ANTITRYPSIN; ENDOPLASMIC RETICULUM; GENE DELETION; HUMANS; PROTEIN BINDING; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE PROTEINS; SOLUBILITY; VESICULAR TRANSPORT PROTEINS;

FUNGI;

EID: 30044436220     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-09-0779     Document Type: Article

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