Protein disulfide isomerases – a way to tackle malaria [PDF]
Trends in Parasitology, 2023 Protein disulfide isomerases (PDIs) ensure that specific substrate proteins are correctly folded. PDI activity plays an essential role in malaria transmission. Here we provide an overview of the role of PDIs in malaria-causing Plasmodium parasites and outline why PDI inhibition could be a novel way to treat malaria and prevent transmission.
Fiona Angrisano +2 more
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Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction [PDF]
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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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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Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A. [PDF]
PLoS ONE, 2017 Protein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms.
Benjamin Selles +4 more
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A protein disulfide isomerase coordinates redox homeostasis and ER calcium regulation for optimal lytic cycle progression in Toxoplasma gondii [PDF]
mBioThe endoplasmic reticulum (ER) maintains an oxidative environment that facilitates the formation of disulfide bonds, a critical process for proper protein folding. Protein disulfide isomerases (PDIs) are ER-resident enzymes that facilitate the formation,
Katherine E. Moen, Silvia N. J. Moreno
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Critical roles of protein disulfide isomerases in balancing proteostasis in the nervous system [PDF]
Journal of Biological Chemistry, 2022 Claudio Hetz +2 more
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Protein disulfide isomerase A6 (PDIA6) is essential for acrosome biogenesis and male fertility in mice [PDF]
Cell Communication and SignalingBackground The family of protein disulfide isomerases (PDIs) are thiol oxidoreductases located predominantly in the endoplasmic reticulum that catalyze thiol-disulfide exchange for normal protein folding.
Xiaofeng Yan +6 more
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Unveiling the thioredoxin fold: a systematic review and bioinformatic analysis of protein disulfide isomerase and Dsb family proteins [PDF]
Frontiers in BioinformaticsIntroductionProtein Disulfide Isomerases (PDIs) and bacterial Dsb proteins are key members of the thioredoxin-fold superfamily, essential for oxidative protein folding in eukaryotic and prokaryotic systems, respectively.
Daniel Cuevas Ortiz +8 more
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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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Atypical thioredoxin Patrx2 enhances alginate production in mucoid Pseudomonas aeruginosa [PDF]
Redox BiologyPseudomonas aeruginosa, an opportunistic human pathogen, is known for its ability to respond and adapt to its environment, employing intricate adaptation mechanisms that can lead to the formation of complex biofilms.
Marie M. Grandjean +7 more
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