Results 231 to 240 of about 43,163 (273)

Protein disulfide isomerase

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
  +5 more sources

Protein Disulfide Isomerase in Thrombosis

Seminars in Thrombosis and Hemostasis, 2015
Protein 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, Freda, Passam, Diego, Butera, Philip J, Hogg   +3 more
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Protein Disulfide Isomerase in Alzheimer Disease

Antioxidants & Redox Signaling, 2000
There 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, R L, Russell, A K, Raina, P L, Harris, S L, Siedlak, X, Zhu, R B, Petersen, S, Shimohama, M A, Smith, G, Perry   +9 more
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Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase

1984
Publisher 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.
D A, Hillson, N, Lambert, R B, Freedman
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Overexpression of Protein Disulfide Isomerase in Aspergillus

Current Microbiology, 2000
One 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, 1994
Purified 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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Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase

Journal of Bioscience and Bioengineering, 2001
Disulfide 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
T, Harada, E, Kurimoto, K, Tokuhiro, O, Asami, T, Sakai, D, Nohara, K, Kato   +6 more
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Catalysis of Disulfide Isomerization in Thrombospondin 1 by Protein Disulfide Isomerase

Biochemistry, 1996
Thrombospondin 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,
K A, Hotchkiss, C N, Chesterman, P J, Hogg   +2 more
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Mammalian protein disulfide isomerases

1997
Abstract 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, 2006
Cellular 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, Cemazar, Maga, Heras, Begona, Martin, Jennifer L, Craik, David J   +4 more
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