CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity
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منابع مشابه
The disulfide isomerase ERp72 supports arterial thrombosis in mice.
Several CGHC motif-containing disulfide isomerases support thrombosis. We here report that endoplasmic reticulum protein 72 (ERp72), with 3 CGHC redox-active sites (ao, a, and a'), supports thrombosis. We generated a new conditional knockout mouse model and found that Tie2-Cre/ERp72fl/fl mice with blood and endothelial cells lacking ERp72 had prolonged tail bleeding times and decreased platelet...
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The endoplasmic reticulum (ER) resident protein, ER60, is a member of the protein disulfide-isomerase family and contains two copies of the internal thioredoxin motif, CGHC. Previously, ER60 was identified as a cysteine protease and named ER-60 protease (Urade, R., Nasu, M., Moriyama, T., Wada, K., and Kito, M. (1992) J. Biol. Chem. 267, 15152-15159; Urade, R., and Kito, M. (1992) FEBS Lett. 31...
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Essentials ERp72 is a thiol isomerase enzyme. ERp72 levels increase at the platelet surface during platelet activation. We generated a humanized monoclonal antibody which blocks ERp72 enzyme activity (anti-ERp72). Anti-ERp72 inhibits platelet functional responses and thrombosis. SUMMARY Background Within the endoplasmic reticulum, thiol isomerase enzymes modulate the formation and rearrangeme...
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in this work, a novel and fast method for direct analysis of volatile compounds (davc) of medicinal plants has been developed by holding a filament from different parts of a plant in the gc injection port. the extraction and analysis of volatile components of a small amount of plant were carried out in one-step without any sample preparation. after optimization of temperature, extraction time a...
Cyclophilin40 isomerase activity is regulated by a temperature-dependent allosteric interaction with Hsp90
Cyclophilin 40 (Cyp40) comprises an N-terminal cyclophilin domain with peptidyl-prolyl isomerase (PPIase) activity and a C-terminal tetratricopeptide repeat (TPR) domain that binds to the C-terminal-EEVD sequence common to both heat shock protein 70 (Hsp70) and Hsp90. We show in the present study that binding of peptides containing the MEEVD motif reduces the PPIase activity by ∼30%. CD and flu...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1993
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1993.tb17821.x