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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Thioredoxin domain containing 15

disulfide isomerase
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Top mentioned proteins: alpha-Synuclein, CAN, Thioredoxin, V1a, fibrillin-1
Papers on disulfide isomerase
Peri/Epicellular Protein Disulfide Isomerase Sustains Vascular Lumen Caliber Through an Anticonstrictive Remodeling Effect.
Laurindo et al., São Paulo, Brazil. In Hypertension, Feb 2016
We hypothesized that the cell-surface pool of the endoplasmic reticulum redox chaperone protein disulfide isomerase-A1 (peri/epicellular=pecPDI), which is known to support thrombosis, also regulates disease-associated vascular architecture.
The Membrane Topology of Vitamin K Epoxide Reductase is conserved between Human Isoforms and the Bacterial Enzyme.
Bulleid et al., Glasgow, United Kingdom. In Biochem J, Feb 2016
Our results provide a resolution to the membrane topology controversy and support previous results suggesting a role for members of the ER protein disulfide isomerase family in recycling VKOR.
Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.
da Silva Neto et al., São Paulo, Brazil. In Free Radic Res, Feb 2016
PDI enzymes and DsbC are endowed with disulfide isomerase activity, which is related with their tetra-domain architecture.
Immunomodulation mediated through Leishmania donovani protein disulfide isomerase by eliciting CD8(+) T-cell in cured visceral leishmaniasis subjects and identification of its possible HLA class-1 restricted T-cell epitopes.
Bimal et al., Patna, India. In J Biomol Struct Dyn, Feb 2016
UNASSIGNED: Protein disulfide isomerase is one of the key enzymes essential for the survival of Leishmania donovani in the host.
Extracellular Thiol Isomerases and Their Role in Thrombus Formation.
Furie et al., Boston, United States. In Antioxid Redox Signal, Feb 2016
SIGNIFICANCE: The mammalian endoplasmic reticulum (ER) houses a large family of twenty thioredoxin-like proteins of which protein disulfide isomerase (PDI) is the archetypal member.
Protein disulfide isomerase A3-specific Th1 effector cells infiltrate colon cancer tissue of patients with circulating anti-protein disulfide isomerase A3 autoantibodies.
Novelli et al., Torino, Italy. In Transl Res, Jan 2016
Two-dimensional Western blotting (2D-WB) and mass spectrometry analysis revealed a strong reactivity of this serum against protein disulfide isomerase A3 (PDIA3).
Combined ligand-observe (19)F and protein-observe (15)N,(1)H-HSQC NMR suggests phenylalanine as the key Δ-somatostatin residue recognized by human protein disulfide isomerase.
Howard et al., Canterbury, United Kingdom. In Sci Rep, Dec 2015
Human protein disulphide isomerase (hPDI) is an endoplasmic reticulum (ER) based isomerase and folding chaperone.
Protein Disulfide Isomerase in Thrombosis.
Hogg et al., Sydney, Australia. In Semin Thromb Hemost, Oct 2015
Protein disulfide isomerase (PDI) is a 57-kDa oxidoreductase that facilitates cysteine thiol reactions inside and outside the cell.
Physiological, pathological, and structural implications of non-enzymatic protein-protein interactions of the multifunctional human transglutaminase 2.
Fésüs et al., Debrecen, Hungary. In Cell Mol Life Sci, Aug 2015
It is a multifunctional protein having several well-defined enzymatic (GTP binding and hydrolysis, protein disulfide isomerase, and protein kinase activities) and non-enzymatic (multiple interactions in protein scaffolds) functions.
Protein disulfide isomerase and Nox: new partners in redox signaling.
Lopes et al., São Paulo, Brazil. In Curr Pharm Des, 2014
Protein disulfide isomerase (PDI) is a thiol oxidoreductase member of the thioredoxin family that has multiple roles in cellular function.
IRE1α-XBP1s induces PDI expression to increase MTP activity for hepatic VLDL assembly and lipid homeostasis.
Kaufman et al., Los Angeles, United States. In Cell Metab, 2012
The defect in VLDL assembly is, at least in part, due to decreased microsomal triglyceride-transfer protein (MTP) activity resulting from reduced protein disulfide isomerase (PDI) expression.
Cell surface thiol isomerases may explain the platelet-selective action of S-nitrosoglutathione.
Gordge et al., London, United Kingdom. In Nitric Oxide, 2011
Increased surface thiol isomerase activity on platelets, compared with cells of the vascular wall, may explain the platelet-selective actions of S-nitrosoglutathione and help define its antithrombotic potential
Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer.
Reinisch et al., New Haven, United States. In Immunity, 2009
The structure revealed that tapasin interacts with both ERp57 catalytic domains, accounting for the stability of the heterodimer, and provided an example of a protein disulfide isomerase family member interacting with substrate.
Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system.
Johnson et al., College Station, United States. In Cell, 2007
The retrotranslocation kinetics of nonglycosylated pro-alpha factor were not significantly altered by replacing all lumenal proteins with only protein disulfide isomerase or all cytosolic proteins with only PA700, the 19S regulatory particle of the 26S proteasome.
The complex route to MHC class I-peptide complexes.
Neefjes et al., Southampton, United Kingdom. In Cell, 2006
In this issue of Cell, Park et al. (2006) show that peptide loading gets a helping hand from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidoreductase activity.
Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing.
Ahn et al., Seoul, South Korea. In Cell, 2006
Here, we identify protein disulfide isomerase (PDI), an enzyme critical to the formation of correct disulfide bonds in proteins, as a component of the peptide-loading complex.
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