Results 11 to 20 of about 3,285 (194)
Thioredoxin‐interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress [PDF]
EMBO Molecular Medicine, 2014 The endoplasmic reticulum (ER) is responsible for protein folding, modification, and trafficking. Accumulation of unfolded or misfolded proteins represents the condition of ER stress and triggers the unfolded protein response (UPR), a key mechanism ...
Samuel Lee +10 more
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The human protein disulfide isomerase gene family [PDF]
Human Genomics, 2012 Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known ...
Galligan James J, Petersen Dennis R
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Downregulated miR-181a alleviates H2O2-induced oxidative stress and cellular senescence by targeting PDIA6 in human foreskin fibroblasts [PDF]
Anais Brasileiros de Dermatologia, 2023 Background Oxidative stress is strongly associated with cellular senescence. Numerous studies have indicated that microRNAs (miRNAs) play a critical part in cellular senescence.
Yan Huang +5 more
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Plants, 2022 Switchgrass rust caused by Puccinia novopanici (P. novopanici) has the ability to significantly affect the biomass yield of switchgrass, an important biofuel crop in the United States. A comparative genome analysis of P.
Raja Sekhar Nandety +6 more
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Autodegradation of Protein Disulfide Isomerase [PDF]
Bioscience, Biotechnology, and Biochemistry, 1999 Protein disulfide isomerase (PDI) and its degradation products were found in HepG2, COS-1, and CHO-K1 cells. Whether or not the products were formed through autodegradation of PDI was examined, since PDI contains the CGHC motif, which is the active center of proteolytic activity in ER-60 protease.
R, Urade +4 more
openaire +2 more sources
PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly
Molecules, 2020 Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the ...
Jiahui Fu +3 more
doaj +1 more source
Protein disulfide isomerase in cardiovascular disease [PDF]
Experimental & Molecular Medicine, 2020 AbstractProtein disulfide isomerase (PDI) participates in the pathogenesis of numerous diseases. Increasing evidence indicates that intravascular cell-derived PDI plays an important role in the initiation and progression of cardiovascular diseases, including thrombosis and vascular inflammation.
Bei Xiong +3 more
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FEBS Open Bio, 2014 Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
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Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation [PDF]
, 2008 The activation of initiator protein tissue factor (TF) is likely to be a crucial step in the blood coagulation process, which leads to fibrin formation. The stimuli responsible for inducing TF activation are largely undefined.
Altmann, Berid +13 more
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A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis [PDF]
, 2017 Background: Within the endoplasmic reticulum, thiol isomerase enzymes modulate the formation and rearrangement of disulphide bonds in newly folded proteins entering the secretory pathway to ensure correct protein folding.
Bicknell, A. B. +8 more
core +1 more source