Grp78, Grp94, and Grp170 interact with α1-antitrypsin mutants that are retained in the endoplasmic reticulum

American Journal of Physiology - Gastrointestinal and Liver Physiology

Volumn 289, Issue 3 52-3, 2005, Pages

  Schmidt, Bela Z ^a   Perlmutter, David H ^a  

^a CHILDREN S HOSPITAL OF PITTSBURGH   (United States)

Author keywords

1 antitrypsin deficiency; Endoplasmic reticulum quality control; Endoplasmic reticulum retention; Molecular chaperones

Indexed keywords

ALPHA 1 ANTITRYPSIN; CALCIMYCIN; CALNEXIN; CHAPERONE; GLUCOSE REGULATED PROTEIN 170; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; GLUCOSYLTRANSFERASE; TUNICAMYCIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE;

ALPHA 1 ANTITRYPSIN DEFICIENCY; ANIMAL CELL; ARTICLE; CHRONIC HEPATITIS; CONTROLLED STUDY; CROSS LINKING; ENDOPLASMIC RETICULUM; GENETIC ENGINEERING; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IMMUNOPRECIPITATION; LIVER CELL; LIVER CELL CARCINOMA; NONHUMAN; PRIORITY JOURNAL; PROTEIN POLYMERIZATION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; SUCROSE DENSITY GRADIENT CENTRIFUGATION;

ALPHA 1-ANTITRYPSIN; ALPHA 1-ANTITRYPSIN DEFICIENCY; CELL CULTURE TECHNIQUES; ENDOPLASMIC RETICULUM; FIBROBLASTS; GLYCOPROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; MUTATION; SOLUBILITY;

EID: 24044535062     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.00237.2004     Document Type: Article

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