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Human PDI Protein expressed in Escherichia coli (E. coli) - ABIN413737
Pendurthi, Ghosh, Mandal, Rao: Tissue factor activation: is disulfide bond switching a regulatory mechanism? in Blood 2007
Show all 2 Pubmed References
Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase.
Overexpression of HIF-1alpha and P4HB is associated with poor prognosis in patients with gastric cancer.
Study demonstrated that the expression of P4HB is frequently upregulated at the mRNA and protein levels in diffuse gliomas. Its high expression was significantly correlated with high Ki-67, more TP53 mutations and poor survival outcome. These findings imply that high expression of P4HB plays an important role in diffuse glioma progression.
identify a potent and selective PDIA1 inhibitor, KSC-34, with 30-fold selectivity for the a site over the a' site. KSC-34 displays time-dependent inhibition of PDIA1 reductase activity in vitro with a kinact/ KI of 9.66 x 10(3) M(-1) s(-1) and is selective for PDIA1 over other members of the PDI family, and other cellular cysteine-containing proteins.
P4HB promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition.
analysis of antiplatelet activity of CxxC through binding to Cys400 in the PDI a0 domain, which can be further exploited as a model for sitedriven antithrombotic agent development
Current findings indicate that thiol isomerase-mediated disulfide bond modification in receptors and plasma proteins is an important layer of control of thrombosis and vascular function more generally.
DIA1 was robustly secreted by physiological levels of arterial laminar shear in endothelial cells and supported alpha 5 integrin thiol oxidation.
Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.
a mechanism of dual Ero1alpha regulation by dynamic redox interactions between PDI and the two Ero1alpha flexible loops that harbor the regulatory cysteines.
analysis of how redox affects human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol
These findings improve our understanding of PDI-protected aggregation of wild-type alpha-Syn and its H50Q familial mutant.
Association of P4HB polymorphisms with sporadic amyotrophic lateral sclerosis susceptibility in the Chinese Han population.
the effect of the endoplasmic reticulum chaperone protein disulfide isomerase (PDI) on beta-cell dysfunction, was examined.
Amyotrophic lateral sclerosis-linked PDIA1 mutations disrupt motor neuron connectivity.
direct binding of PDIA1 to VWF, is reported.
Selective sequestration of PDI1A in a calcium depletion-mediated complex with the abundant chaperone calreticulin attenuates the effective concentration of this major lumenal thiol oxidant.
Cole-Carpenter syndrome is caused by a specific de novo mutation in P4HB that impairs the disulfide isomerase activity of protein disulfide isomerase.
PDI has a role as a competent regulator and a specific substrate of Ero1alpha govern efficient and faithful oxidative protein folding and maintain the ER redox homeostasis
The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 A resolution revealed that the formation of dimers occludes the substrate binding site.
Rotavirus-protein disulfide isomerase interaction was demonstrated in vitro as well as inMA104 cells and intestinal villi from suckling mice.
This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.
cellular thyroid hormone-binding protein
, collagen prolyl 4-hydroxylase beta
, glutathione-insulin transhydrogenase
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide
, prolyl 4-hydroxylase subunit beta
, protein disulfide isomerase family A, member 1
, protein disulfide isomerase-associated 1
, protein disulfide isomerase/oxidoreductase
, protein disulfide-isomerase
, protocollagen hydroxylase
, thyroid hormone-binding protein p55
, ER protein 59
, endoplasmic reticulum resident protein 59
, protein disulfide isomerase
, Protein disulfide isomerase (Prolyl 4-hydroxylase, beta polypeptide)
, PDI (E.C.220.127.116.11)
, cellular thyroid hormone binding protein
, prolyl 4-hydroxylase beta polypeptide
, prolyl 4-hydroxylase, beta subunit
, Cellular thyroid hormone-binding protein
, Prolyl 4-hydroxylase subunit beta
, multifunctional thyroid hormone binding protein
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide (protein disulfide isomerase-associated 1)
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide (protein disulfide isomerase; thyroid hormone binding protein p55)
, retina cognin
, protein disulphide isomerase PDI
, prolyl 4-hydroxylase, beta polypeptide