Results 171 to 180 of about 3,392,726 (209)
Structural characterization of OsPDIL2-3, a rice protein disulfide isomerase involved in prolamin accumulation. [PDF]
Biochem JFujimoto Z +6 more
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Pathogens and Disease, 2023 Leishmaniasis is a group of vector-borne diseases caused by intracellular protozoan parasites belonging to the genus Leishmania. Leishmania parasites can employ different and numerous sophisticated strategies, including modulating host proteins, cell ...
Majid Dousti +2 more
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Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 2004
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure.
L. Lopes +4 more
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During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure.
L. Lopes +4 more
+5 more sources
Protein disulfide isomerases in neurodegeneration: From disease mechanisms to biomedical applications [PDF]
FEBS Letters, 2012 Protein disulfide isomerases (PDIs) are a family of foldases and chaperones primarily located at the endoplasmic reticulum that catalyze the formation and isomerization of disulfide bonds thereby facilitating protein folding.
Claudio Hetz +2 more
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Comparative genomic study of protein disulfide isomerases from photosynthetic organisms [PDF]
Genomics, 2011 Protein disulfide isomerases (PDIs) are eukaryotic oxidoreductases essential for oxidative protein folding. Their diversity in photosynthetic organisms was assessed by analyzing 24 sequenced genomes belonging to algal, lycophyte, bryophyte and angiosperm
Nicolas Rouhier +2 more
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Protein disulfide isomerases exploit synergy between catalytic and specific binding domains [PDF]
EMBO Reports, 2002 Protein disulfide isomerases (PDIs) catalyse the formation of native disulfide bonds in protein folding pathways. The key steps involve disulfide formation and isomerization in compact folding intermediates.
Lloyd W Ruddock +2 more
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RSC Biomolecular Sciences, 2008 This review will focus on what is NOT known about protein disulfide-isomerases, rather than on what IS ...
Robert B Freedman
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Protein Disulfide Isomerase in Thrombosis
Seminars in Thrombosis and Hemostasis, 2015Protein disulfide isomerase (PDI) is a 57-kDa oxidoreductase that facilitates cysteine thiol reactions inside and outside the cell. It mediates reduction or oxidation of protein disulfide bonds, thiol/disulfide exchange reactions, and transfer of NO from one protein thiol to another. It also has chaperone properties.
Joyce, Chiu +3 more
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Protein Disulfide Isomerase in Alzheimer Disease
Antioxidants & Redox Signaling, 2000There is a great deal of evidence that places oxidative stress as a proximal event in the natural history of Alzheimer disease (AD). In addition to increased damage, there are compensatory increases in the levels of free sulfhydryls, glucose-6-phosphate dehydrogenase, and NAD(P)H:quinone oxidoreductase 1. To investigate redox homeostasis further in AD,
H T, Kim +9 more
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Overexpression of Protein Disulfide Isomerase in Aspergillus
Current Microbiology, 2000One of the major problems with the production of biotechnologically valuable proteins has been the purification of the product. For Escherichia coli and Saccharomyces cerevisiae, there are several techniques for the purification of intracellular proteins, but these are time consuming and often result in poor yields.
H, El-Adawi, N Q, Khanh, H, Gassen
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