Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols [PDF]
AntioxidantsThiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie +3 more
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Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development [PDF]
Thrombosis JournalVascular thiol isomerases (VTIs) encompass proteins such as protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERp5), ERp46, ERp57, ERp72, thioredoxin-related transmembrane protein 1 (TMX1), and TMX4, and play pivotal functions in ...
Longguang Jiang +3 more
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Thiol isomerase ERp18 enhances platelet activation and arterial thrombosis [PDF]
Research and Practice in Thrombosis and HaemostasisBackground: Thiol isomerases regulate the thiol-disulfide exchange of functional proteins in cells. Using genetically modified mouse models and inhibitors, we and others demonstrated that 7 thiol isomerases (ERp57, protein diisulfide isomerase, ERp72 ...
Chao He +11 more
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Integration of metabolic and evolutionary processes to construct efficient xylose-utilizing strain of Zymomonas mobilis for lignocellulosic ethanol production [PDF]
Synthetic and Systems BiotechnologyXylose is a major component of lignocellulose, and it is crucial to enable microorganisms the capability of efficient xylose utilization for economical lignocellulosic biochemical production.
Jiyun Lou +7 more
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Non-Canonical, Strongly Selective Protein Disulfide Isomerases as Anticancer Therapeutic Targets [PDF]
BiomoleculesProtein Disulfide Isomerases (PDIs) are emerging targets in anticancer therapy, with several PDI inhibitors demonstrating anticancer efficacy in preclinical models.
Mary E. Law +9 more
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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 ...
James Dotimas +2 more
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Structural and Biochemical Characterization of the Human Cyclophilin Family of Peptidyl-Prolyl Isomerases [PDF]
PLoS Biology, 2010 Peptidyl-prolyl isomerases catalyze the conversion between cis and trans isomers of proline. The cyclophilin family of peptidyl-prolyl isomerases is well known for being the target of the immunosuppressive drug cyclosporin, used to combat organ ...
Tara L Davis +2 more
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Transmembrane thiol isomerase TMX1 counterbalances the effect of ERp46 to inhibit platelet activation and integrin αIIbβ3 function [PDF]
Research and Practice in Thrombosis and HaemostasisBackground: Previous studies have shown that thiol isomerases such as ERp46 positively regulate platelet function by reducing integrin αIIbβ3 disulfides, and the transmembrane thiol isomerase TMX1 negatively regulates integrin αIIbβ3 activation. However,
Zhenzhen Zhao +7 more
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Catalyzing Protein Folding by Chaperones [PDF]
BiologyProtein folding is a fundamental process essential for cellular growth and health, yet it is also susceptible to errors that can result in misfolding and disease.
Zijue Huang, Scott Horowitz
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Isoenzymatic variability in wild potatoes [PDF]
Pesquisa Agropecuária Brasileira, 2001 Two species of wild potato Solanum commersonii, subspecies commersonii and malmeanum, and S. chacoense, subspecies muelleri occur in southern Brazil.
Beatriz Helena Gomes Rocha +3 more
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