Recombinant Human Protein disulfide-isomerase A2 (PDIA2)

1. Galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface. PMID: 28810662
2. PDI overexpression is associated with Multiple Myeloma. PMID: 27197150
3. Tissue factor-regulated vascular smooth cell migration and microvessel formation is under the control of the ER-protein PDIA2. PMID: 25631539
4. It was found that PDI interacts with dengue virus nonstructural protein 1 (NS1) intracellularly as well as on the surface in the lipid raft domain. PMID: 25664880
5. Data show that cell surface disulfide isomerase (PDI) expression and function regulate the capacity of natriuretic peptides to generate cyclic guanosine monophosphate (cGMP) through interaction with their receptors. PMID: 25419565
6. The redox-regulated open/closed conformational switch of hPDI endows the protein with versatile target-binding capacities for its enzymatic and chaperone functions. PMID: 22657537
7. These results indicate that BPA, a widely distributed and potentially harmful chemical, inhibits Ero1-PDI-mediated disulfide bond formation. PMID: 25122773
8. PDI appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin via a redox-dependent mechanism. PMID: 24415753
9. Data indicate that protein disulfide isomerase (PDI) and ERp44 dynamically localize Ero1alpha and peroxiredoxin 4 in early secretory compartment (ESC). PMID: 23979138
10. GPx7 is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys mechanism in which GSH and PDI are alternative substrates. PMID: 23454490
11. Human major histocompatibility complex class 1 antigens (HLA-A,B,C) are potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation. PMID: 23167757
12. Data indicate that apoptosis induced by misfolded PrP proteins could be regulated by protein disulfide isomerase (PDI) via mitochondrial dysfunction. PMID: 22685557
13. The hydrogen bond, formed between the 3-hydroxyl group of Estradiol (E(2)) (donor) and pancreas-specific protein disulfide isomerase's His278 (acceptor), is indispensable for its binding. PMID: 21080683
14. PDI is required to support Nox1/redox and GTPase-dependent VSMC migration. PMID: 22773830
15. PDI exhibits unfoldase activity for proinsulin, increasing retention of proinsulin within the ER of pancreatic beta-cells PMID: 22105075
16. Data show that diabetic patients had a greater number of transferase-mediated dUTP nick-end labeling-positive cells than nondiabetic patients despite a greater myocardial protein disulfide isomerase (PDI)expression suggesting altered PDI function. PMID: 21637911
17. surface-associated PDI is an important regulator of coagulation factor ligation to thrombin-stimulated platelets and of subsequent feedback activation of platelet thrombin generation PMID: 21929690
18. mechanistic insights into the redox-regulated chaperone activity of human PDI. PMID: 22090031
19. the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1alpha. PMID: 21757736
20. tein disulfide isomerase redox-dependent association with p47(phox): evidence for an organizer role in leukocyte NADPH oxidase activation. PMID: 21791598
21. Protein disulfide isomerase blocks CEBPA translation and is up-regulated during the unfolded protein response in acute myeloid leukemia. PMID: 21471526
22. PDI knockdown-induced cell death is cell-line-dependent and involves apoptosis in MCF-7 cells. PMID: 21297336
23. PDI is a major target of post-streptococcal autoimmunity. PMID: 20886095
24. These results suggest that PDI could be a therapeutic target to prevent ER stress in neuronal cells in Alzheimer disease. PMID: 20550946
25. PDI has a role in regulating tissue factor that involves FVIIa activity [review] PMID: 20163832
26. Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3. PMID: 20562109
27. Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance. PMID: 20516074
28. new mechanism for PDI contribution to coagulation on endothelial cells, namely, the regulation of PS exposure, where PDI acts as a negative regulator of coagulation PMID: 20448108
29. Among target genes of XBP-1, expression of protein disulfide isomerase (PDI), but not glucose- regulated protein 78 (GRP78), was increased in AD PMID: 20368688
30. an appropriate Ero1alpha-PDI ratio is critical for regulating the binding-release cycle of CTA1 by PDI during retro-translocation, and PDI's redox state has a role in targeting it to the retro-translocon PMID: 20130085
31. Selective expression of pancreas-specific protein disulfide-isomerase confers strong protection against heat shock and oxidative-stress-induced cell death. PMID: 20423326
32. The absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer. PMID: 19821078
33. A haplotype within the AXIN1-PDIA2 locus (p-value of 2.926x10(-06)) and a haplotype within the Endoglin gene (p-value of 5.881x10(-04)) were found to be strongly associated with bicuspid aortic valve PMID: 20098615
34. The b domain of human PDI tends to form homodimers - both in isolation and in other contexts. This tendency is moderated by the adjacent x region, which can bind to a surface patch on the b domain. PMID: 19844948
35. Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring. PMID: 11968009
36. role of association with ubiquilin in the endoplasmic reticulum in stress-induced apoptotic cell death PMID: 12095988
37. dissociation of PDI from substrates observed in the presence of glutathione disulfide can be explained by competition for the peptide-binding site on PDI PMID: 12485997
38. PDI has a role in conferring resistance to apoptosis under hypoxia and a potential role in the oxygen-sensing apparatus PMID: 12766950
39. study of the principal substrate binding site of PDI PMID: 14684740
40. Low resolution structure of the entire PDI molecule in solution has been determined for the first time by the small angle X-ray scattering technique PMID: 16407203
41. PDI stabilizes a peptide-receptive site by regulating oxidation state of the disulfide bond in MHC peptide-binding groove, an essential function for selecting optimal peptides; link between thiol-based redox regulation & antigen processing established PMID: 17055437
42. These data indicate that cytosolic PDI is a substrate of caspase-3 and -7, and that it has an anti-apoptotic action. PMID: 17978580
43. Study shows that SUMF1 interacts with protein disulfide isomerase (PDI) and ERp44, two thioredoxin family members residing in the early secretory pathway, and with ERGIC-53, a lectin that shuttles between the ER and the Golgi. PMID: 18508857
44. Platelet microparticle-associated PDI promotes platelet aggregation and inactivates insulin. PMID: 18691554
45. The x region of PDI can adopt alternative conformations during the functional cycle of PDI action and that these are linked to the ability of PDI to interact with folding substrates. PMID: 18801374
46. a role for both GRP78 and PDI in insulin biosynthesis, although an excess of PDI disrupts normal proinsulin processing. PMID: 19103594
47. structures and functions of human PDIp are redox-regulated through formation of an inter-subunit disulfide bond between two cysteine-4 residues PMID: 19150607
48. the solution structure of the second and third domains of human protein disulfide isomerase (b and b', respectively) by triple-resonance NMR spectroscopy and molecular modeling PMID: 19187238
49. PDIp can also serve as an effective modulator of the cellular levels and biological actions of endogenous estrogens in the pancreas where estrogen receptors alpha and beta and PDIp are co-present. PMID: 19429457
50. The b' domain of PDI contributes to binding unfolded proteins; its structure is stabilized by the b domain. PMID: 19636846

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HGNC: 14180

OMIM: 608012

KEGG: hsa:64714

STRING: 9606.ENSP00000219406

UniGene: Hs.66581