Protein disulfide isomerase-9 interacts with the lumenal region of the transmembrane endoplasmic reticulum stress sensor kinase, IRE1, to modulate the unfolded protein response in Arabidopsis. [PDF]
Front Plant SciCarrillo R +4 more
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Protein disulfide isomerase family member 4 promotes triple-negative breast cancer tumorigenesis and radiotherapy resistance through JNK pathway. [PDF]
Breast Cancer ResTao J +9 more
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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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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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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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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.
D A, Hillson, N, Lambert, R B, Freedman
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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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