Recombinant Human Protein disulfide-isomerase (P4HB)

1. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase. PMID:29191937
2. Overexpression of HIF-1alpha and P4HB is associated with poor prognosis in patients with gastric cancer. PMID:29904245
3. 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. PMID:29207176
4. 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. PMID:29521097
5. P4HB promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition. PMID:28052026
6. 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 PMID:28109047
7. 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. PMID:28598864
8. DIA1 was robustly secreted by physiological levels of arterial laminar shear in endothelial cells and supported alpha 5 integrin thiol oxidation. PMID:28034831
9. Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates. PMID:28364042
10. a mechanism of dual Ero1alpha regulation by dynamic redox interactions between PDI and the two Ero1alpha flexible loops that harbor the regulatory cysteines. PMID:27703014
11. analysis of how redox affects human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol PMID:28257787
12. These findings improve our understanding of PDI-protected aggregation of wild-type alpha-Syn and its H50Q familial mutant. PMID:27142583
13. Association of P4HB polymorphisms with sporadic amyotrophic lateral sclerosis susceptibility in the Chinese Han population. PMID:26000911
14. the effect of the endoplasmic reticulum chaperone protein disulfide isomerase (PDI) on beta-cell dysfunction, was examined. PMID:26607804
15. Amyotrophic lateral sclerosis-linked PDIA1 mutations disrupt motor neuron connectivity. PMID:26869642
16. direct binding of PDIA1 to VWF, is reported. PMID:26670633
17. 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. PMID:25575667
18. Cole-Carpenter syndrome is caused by a specific de novo mutation in P4HB that impairs the disulfide isomerase activity of protein disulfide isomerase. PMID:25683117
19. 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 PMID:25258311
20. 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. PMID:24549644
21. Elevated P4HB expression is associated with temozolomide resistance in malignant glioma. PMID:23444257
22. ). The results suggest that P4HB is a modifier gene inamyotrophic lateral sclerosis susceptibility and may represent a potential therapeutic target for amyotrophic lateral sclerosis . PMID:23337974
23. A mixed disulfide complex was formed with the catalytic domain A1 from human PDI consistent with a model for cotranslational oxidative protein folding wherein PDI acts as a placeholder that is relieved by the pairing of cysteines caused by substrate folding. PMID:23141538
24. TPM4, PDIA and SRC8 were also localized to the trophoblast cells, further highlighting the importance of these cytoskeletal remodelling proteins in early pregnancy PMID:21373848
25. these data revealed a redox-regulated chaperone function of PDI in delivering antigenic peptides from TAP to MHC-I. PMID:21299467
26. Functional PDI is rapidly secreted from human umbilical vein endothelial cells in culture upon activation with thrombin or after laser-induced stimulation. PMID:20668226
27. domain c is required for the stabilization and maintenance of the chaperone function of PDI under extreme conditions PMID:15358778
28. data indicate that binding sites in three PDI domains, a, b', and a', contribute to efficient C-P4H tetramer assembly PMID:15590633
29. PDI can be S-nitrosated and PDI-SNO can be denitrosated by PDI suggesting that this enzyme could be intimately involved in the transport of intracellular NO equivalents to the cell surface. PMID:15611098
30. Data show that protein disulfide isomerase can switch its conformation from dimer to tetramer in its functions as a foldase. PMID:15695804

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HGNC: 8548

UNIGENE: Hs.464336

KEGG: hsa:5034

STRING: 9606.ENSP00000327801

OMIM: 112240