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    PDIA2 protein disulfide isomerase family A member 2 [ Homo sapiens (human) ]

    Gene ID: 64714, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PDIA2 has a dual function in promoting androgen deprivation therapy induced venous thrombosis events and castrate resistant prostate cancer progression.

    PDIA2 has a dual function in promoting androgen deprivation therapy induced venous thrombosis events and castrate resistant prostate cancer progression.
    Li Y, Lv L, Ye M, Xie N, Fazli L, Wang Y, Wang W, Yang S, Ni Q, Chen J, Guo X, Zhao Y, Xue G, Sha J, Dong X, Zhang L.

    05/29/2024
    Protein Disulfide Isomerase A2 Is Correlated with Immune Infiltrates and Is a Novel Prognostic Biomarker in Glioma Patients.

    Protein Disulfide Isomerase A2 Is Correlated with Immune Infiltrates and Is a Novel Prognostic Biomarker in Glioma Patients.
    Ma ZG, Liu YX, Zou N, Huang Z, Wang M, Li T, Zhou J, Chen LG.

    01/4/2024
    The involvement of PDIA2 gene in the progression of renal cell carcinoma is potentially through regulation of JNK signaling pathway.

    The involvement of PDIA2 gene in the progression of renal cell carcinoma is potentially through regulation of JNK signaling pathway.
    Fang H, Peng Z, Tan B, Peng N, Li B, He D, Xu M, Yang Z.

    08/30/2023
    De-dimerization of PTB is catalyzed by PDI and is involved in the regulation of p53 translation.

    De-dimerization of PTB is catalyzed by PDI and is involved in the regulation of p53 translation.
    Gong FX, Zhan G, Han R, Yang Z, Fu X, Xiao R., Free PMC Article

    11/6/2021
    Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide-isomerase relay when protein folding capacity is exceeded.

    Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide-isomerase relay when protein folding capacity is exceeded.
    Moilanen A, Ruddock LW., Free PMC Article

    01/16/2021
    Galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface.

    Galectin-9 binds to O-glycans on protein disulfide isomerase.
    Schaefer K, Webb NE, Pang M, Hernandez-Davies JE, Lee KP, Gonzalez P, Douglass MV, Lee B, Baum LG., Free PMC Article

    04/28/2018
    PDI overexpression is associated with Multiple Myeloma.

    Novel Protein Disulfide Isomerase Inhibitor with Anticancer Activity in Multiple Myeloma.
    Vatolin S, Phillips JG, Jha BK, Govindgari S, Hu J, Grabowski D, Parker Y, Lindner DJ, Zhong F, Distelhorst CW, Smith MR, Cotta C, Xu Y, Chilakala S, Kuang RR, Tall S, Reu FJ.

    07/29/2017
    Tissue factor-regulated vascular smooth cell migration and microvessel formation is under the control of the ER-protein PDIA2.

    Protein disulphide-isomerase A2 regulated intracellular tissue factor mobilisation in migrating human vascular smooth muscle cells.
    Peña E, Arderiu G, Badimon L.

    03/26/2016
    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.

    Protein disulfide isomerase mediates dengue virus entry in association with lipid rafts.
    Diwaker D, Mishra KP, Ganju L, Singh SB.

    12/26/2015
    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.

    Cell surface protein disulfide isomerase regulates natriuretic peptide generation of cyclic guanosine monophosphate.
    Pan S, Chen HH, Correia C, Dai H, Witt TA, Kleppe LS, Burnett JC Jr, Simari RD., Free PMC Article

    07/25/2015
    The redox-regulated open/closed conformational switch of hPDI endows the protein with versatile target-binding capacities for its enzymatic and chaperone functions.

    Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase.
    Wang C, Li W, Ren J, Fang J, Ke H, Gong W, Feng W, Wang CC.

    12/20/2014
    These results indicate that BPA, a widely distributed and potentially harmful chemical, inhibits Ero1-PDI-mediated disulfide bond formation.

    Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.
    Okumura M, Kadokura H, Hashimoto S, Yutani K, Kanemura S, Hikima T, Hidaka Y, Ito L, Shiba K, Masui S, Imai D, Imaoka S, Yamaguchi H, Inaba K., Free PMC Article

    12/20/2014
    PDI appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin via a redox-dependent mechanism.

    Protein disulfide isomerase directly interacts with β-actin Cys374 and regulates cytoskeleton reorganization.
    Sobierajska K, Skurzynski S, Stasiak M, Kryczka J, Cierniewski CS, Swiatkowska M., Free PMC Article

    04/26/2014
    Data indicate that protein disulfide isomerase (PDI) and ERp44 dynamically localize Ero1alpha and peroxiredoxin 4 in early secretory compartment (ESC).

    Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.
    Kakihana T, Araki K, Vavassori S, Iemura S, Cortini M, Fagioli C, Natsume T, Sitia R, Nagata K., Free PMC Article

    12/14/2013
    GPx7 is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys mechanism in which GSH and PDI are alternative substrates.

    Protein disulfide isomerase and glutathione are alternative substrates in the one Cys catalytic cycle of glutathione peroxidase 7.
    Bosello-Travain V, Conrad M, Cozza G, Negro A, Quartesan S, Rossetto M, Roveri A, Toppo S, Ursini F, Zaccarin M, Maiorino M.

    08/10/2013
    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.

    N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
    Walker AK, Soo KY, Levina V, Talbo GH, Atkin JD.

    03/2/2013
    Data indicate that apoptosis induced by misfolded PrP proteins could be regulated by protein disulfide isomerase (PDI) via mitochondrial dysfunction.

    Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity.
    Wang SB, Shi Q, Xu Y, Xie WL, Zhang J, Tian C, Guo Y, Wang K, Zhang BY, Chen C, Gao C, Dong XP., Free PMC Article

    12/8/2012
    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.

    Characterization of the estradiol-binding site structure of human pancreas-specific protein disulfide isomerase: indispensable role of the hydrogen bond between His278 and the estradiol 3-hydroxyl group.
    Fu XM, Wang P, Zhu BT., Free PMC Article

    12/8/2012
    PDI is required to support Nox1/redox and GTPase-dependent VSMC migration.

    Protein disulfide isomerase is required for platelet-derived growth factor-induced vascular smooth muscle cell migration, Nox1 NADPH oxidase expression, and RhoGTPase activation.
    Pescatore LA, Bonatto D, Forti FL, Sadok A, Kovacic H, Laurindo FR., Free PMC Article

    11/24/2012
    PDI exhibits unfoldase activity for proinsulin, increasing retention of proinsulin within the ER of pancreatic beta-cells

    Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells.
    Rajpal G, Schuiki I, Liu M, Volchuk A, Arvan P., Free PMC Article

    05/12/2012
    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.

    Altered oxido-reductive state in the diabetic heart: loss of cardioprotection due to protein disulfide isomerase.
    Toldo S, Boccellino M, Rinaldi B, Seropian IM, Mezzaroma E, Severino A, Quagliuolo L, Van Tassell BW, Marfella R, Paolisso G, Rossi F, Natarajan R, Voelkel N, Abbate A, Crea F, Baldi A., Free PMC Article

    03/31/2012
    surface-associated PDI is an important regulator of coagulation factor ligation to thrombin-stimulated platelets and of subsequent feedback activation of platelet thrombin generation

    Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding.
    Jurk K, Lahav J, VAN Aken H, Brodde MF, Nofer JR, Kehrel BE.

    03/17/2012
    mechanistic insights into the redox-regulated chaperone activity of human PDI.

    Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'.
    Wang C, Yu J, Huo L, Wang L, Feng W, Wang CC., Free PMC Article

    03/3/2012
    the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1alpha.

    Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.
    Araki K, Nagata K., Free PMC Article

    11/26/2011
    tein disulfide isomerase redox-dependent association with p47(phox): evidence for an organizer role in leukocyte NADPH oxidase activation.

    Protein disulfide isomerase redox-dependent association with p47(phox): evidence for an organizer role in leukocyte NADPH oxidase activation.
    de A Paes AM, Veríssimo-Filho S, Guimarães LL, Silva AC, Takiuti JT, Santos CX, Janiszewski M, Laurindo FR, Lopes LR.

    11/19/2011
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