Gene Review:
PDIA4 - protein disulfide isomerase family A,...
Homo sapiens
Synonyms:
ER protein 70, ER protein 72, ERP70, ERP72, ERp-72, ...
- HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. Schaiff, W.T., Hruska, K.A., McCourt, D.W., Green, M., Schwartz, B.D. J. Exp. Med. (1992)
- Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation. Forster, M.L., Sivick, K., Park, Y.N., Arvan, P., Lencer, W.I., Tsai, B. J. Cell Biol. (2006)
- Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. Soldà, T., Garbi, N., Hämmerling, G.J., Molinari, M. J. Biol. Chem. (2006)
- Novel covalent chaperone complexes associated with human chorionic gonadotropin beta subunit folding intermediates. Feng, W., Bedows, E., Norton, S.E., Ruddon, R.W. J. Biol. Chem. (1996)
- An antibody that binds a neutrophil membrane protein, ERp72, primes human neutrophils for enhanced oxidative metabolism in response to formyl-methionyl-leucyl-phenylalanine. Implications for ERp72 in the signal transduction pathway for neutrophil priming. Weisbart, R.H. J. Immunol. (1992)
- Competitive inhibition of a set of endoplasmic reticulum protein genes (GRP78, GRP94, and ERp72) retards cell growth and lowers viability after ionophore treatment. Li, X.A., Lee, A.S. Mol. Cell. Biol. (1991)
- Accumulation and degradation in the endoplasmic reticulum of a truncated ER-60 devoid of C-terminal amino acid residues. Urade, R., Kusunose, M., Moriyama, T., Higasa, T., Kito, M. J. Biochem. (2000)
- Serum antibodies from halothane hepatitis patients react with the rat endoplasmic reticulum protein ERp72. Pumford, N.R., Martin, B.M., Thomassen, D., Burris, J.A., Kenna, J.G., Martin, J.L., Pohl, L.R. Chem. Res. Toxicol. (1993)
- Isolation of ERp72 from guinea pig term placentae using heparin Sepharose affinity chromatography. Bonifacio, M.D., Steeves, T., Saunders, D.M., Sinosich, M.J. Biochem. Mol. Biol. Int. (1995)
- Molecular characterization and expression of an alfalfa protein with sequence similarity to mammalian ERp72, a glucose-regulated endoplasmic reticulum protein containing active site sequences of protein disulphide isomerase. Shorrosh, B.S., Dixon, R.A. Plant J. (1992)
- ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. Mazzarella, R.A., Srinivasan, M., Haugejorden, S.M., Green, M. J. Biol. Chem. (1990)
- The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing. Feng, W., Matzuk, M.M., Mountjoy, K., Bedows, E., Ruddon, R.W., Boime, I. J. Biol. Chem. (1995)
- Trefoil factor 1 (TFF1/pS2) deficiency activates the unfolded protein response. Torres, L.F., Karam, S.M., Wendling, C., Chenard, M.P., Kershenobich, D., Tomasetto, C., Rio, M.C. Mol. Med. (2002)
- Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state. Linnik, K.M., Herscovitz, H. J. Biol. Chem. (1998)