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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.
Hiram F. Gilbert, Bonney Wilkinson
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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.
Hiram F. Gilbert, Bonney Wilkinson
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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.
Diego Butera +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,
Mark A. Smith +9 more
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[38] Protein disulfide-isomerase
1995Publisher Summary Protein disulfide-isomerase is an abundant protein within the lumen of the endoplasmic reticulum of secretory cells, and functions as a catalyst in the formation of native disulfide bonds in nascent secretory and cell surface proteins.
Hilary C. Hawkins +2 more
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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.
Chen-Lu Tsou +2 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.
Hala El-Adawi +2 more
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Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
1984Publisher Summary Protein disulfide-isomerase (PDI) catalyzes the formation of native proteins from the reduced denatured state. When incubated in the presence of a thiol compound, PDI catalyzes the regain of native ribonuclease structure from the scrambled ribonuclease, with concomitant return of activity toward RNA.
David A. Hillson +2 more
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Catalysis of Disulfide Isomerization in Thrombospondin 1 by Protein Disulfide Isomerase
Biochemistry, 1996Thrombospondin 1 is a multidomain glycoprotein from platelets and most cells that participates in diverse biological processes. The structure and some functional properties of thrombospondin 1 are regulated by disulfide interchange in the Ca(2+)-binding repeats and C-globular domain. The recent identification of the enzyme, protein disulfide isomerase,
Colin N. Chesterman +2 more
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Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase
Journal of Bioscience and Bioengineering, 2001Disulfide bond formation in the refolding of thermophilic fungal protein disulfide isomerase (PDI) was investigated. It was revealed that (i) a disulfide bond buried inside the molecule is preferentially formed and contributes to the thermal stability and the isomerizing power of PDI, and (ii) formation of disulfide bonds in active sites located on the
Kenrou Tokuhiro +6 more
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[4] Thermophilic fungal protein disulfide isomerase
1998Publisher Summary For the study the authors have isolated and characterized a thermostable protein disulfide isomerase (PDI) from a thermophilic fungus, Humicola insolens. The cDNA encoding the fungal PDI has been cloned and expressed in Bacillus brevis. PDIs from vertebrates and yeast are relatively heat labile.
Masana Hirai +5 more
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