Results 201 to 210 of about 41,132 (234)

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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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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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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Protein disulfide isomerase in thrombosis and vascular inflammation [PDF]

Journal of Thrombosis and Haemostasis, 2013
Protein disulfide isomerase (PDI) catalyzes disulfide bond oxidation, reduction and isomerization during protein synthesis in the endoplasmic reticulum (ER). In addition to its critical role in the ER, in vitro and in vivo studies with blocking antibodies and conditional knockout mice have demonstrated that cell surface PDI is required for thrombosis ...
Jaehyung Cho
exaly   +3 more sources

Bacitracin is not a specific inhibitor of protein disulfide isomerase

The FEBS Journal, 2010
To successfully dissect molecular pathways in vivo, there is often a need to use specific inhibitors. Bacitracin is very widely used as an inhibitor of protein disulfide isomerase (PDI) in vivo. However, the specificity of action of an inhibitor for a protein‐folding catalyst cannot be determined in vivo.
Karala Anna, Ruddock Lloyd
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Promotion of insulin aggregation by protein disulfide isomerase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007
We examined the aggregation of insulin as a result of reduction of disulfide bonds catalyzed by protein disulfide isomerase (PDI) using various techniques. We demonstrated the kinetic correlation between PDI-catalyzed insulin reduction and the aggregate formation, the relationship between aggregation and amyloid formation, and the structural ...
Ryosuke, Maeda, Kazuyoshi, Ado, Naohiro, Takeda, Yoshihiro, Taniguchi   +3 more
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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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Protein disulfide isomerase is both an enzyme and a chaperone

FASEB Journal, 1993
Protein disulfide isomerase (PDI) catalyzes the formation of native disulfides of peptide chains from either the reduced form or randomly joined disulfides. So that thiols situated at distant parts of the polypeptide chain can be joined together to form the native disulfides, the polypeptide chain has to be folded, at least to some
C C, Wang, C L, Tsou
exaly   +3 more sources

Purification and Characterization of Yeast Protein Disulfide Isomerase

The Journal of Biochemistry, 1990
Protein disulfide-isomerase (PDI), which reactivates inactive scrambled RNase, was purified from Saccharomyces cerevisiae. The enzyme was purified 1,850-fold to apparent homogeneity by five purification steps: 30-70% ammonium sulfate fractionation, DEAE Toyopearl-650S and Butyl Toyopearl-650S chromatographies, and differential Phenyl-5PW HPLC with or ...
T, Mizunaga, Y, Katakura, T, Miura, Y, Maruyama   +3 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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