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Statement of Retraction: Protein disulfide-isomerase A3 knockdown attenuates oxidized low-density lipoprotein-induced oxidative stress, inflammation and endothelial dysfunction in human umbilical vein endothelial cells by downregulating activating transcription factor 2. [PDF]
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Biochimica et Biophysica Acta (BBA) - Proteins and 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.
Bonney, Wilkinson, Hiram F, Gilbert
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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.
Bonney, Wilkinson, Hiram F, Gilbert
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A Gallium(III) Complex that Engages Protein Disulfide Isomerase A3 (PDIA3) as an Anticancer Target.
Angewandte Chemie, 2020Gallium(III)-based drugs have gained momentum in cancer therapy due to their iron-dependent anticancer activity. Judicious choice of ligands is critical for improved oral bioavailability, antitumor efficacy, and distinct mechanisms from simple GaIII ...
Hao-yan Yin +10 more
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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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Association and dissociation of protein disulfide isomerase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994Purified protein disulfide isomerase, homogeneous by SDS-PAGE, can be separated into two components by PAGE and by gel filtration. These two components, with the same amino-acid composition as well as N- and C-terminal sequences, are the tetramer and dimer of molecular weight 240 kDa and 120 kDa, respectively.
X C, Yu, C C, Wang, C L, Tsou
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Mammalian protein disulfide isomerases
1997Abstract PDI is readily purified from mammalian liver, or from other highly secretory tissues such as pancreas or placenta. [Here, in subsequent paragraphs where no specific citation is given see Freedman, Tuite (1994), Freedman etal., (1994, 1995), Freedman (1995) for pre-1994 references].
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Protein disulfide isomerase: the structure of oxidative folding
Trends in Biochemical Sciences, 2006Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond formation, a step in the oxidative folding pathway that takes place in specialized cellular compartments.
Gruber, Christian W +4 more
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