Results 271 to 280 of about 83,408 (297)

Protein disulfide isomerase family member 4 promotes triple-negative breast cancer tumorigenesis and radiotherapy resistance through JNK pathway. [PDF]

Breast Cancer Res
Tao J, Xue C, Cao M, Ye J, Sun Y, Chen H, Guan Y, Zhang W, Zhang W, Yao Y.   +9 more
europepmc   +1 more source

Long noncoding RNA protein-disulfide isomerase-associated 3 regulated high glucose-induced podocyte apoptosis in diabetic nephropathy through targeting miR-139-3p. [PDF]

World J Diabetes
He YX, Wang T, Li WX, Chen YX.
europepmc   +1 more source

Discovery of 5-Hydroxy-1,4-naphthoquinone (Juglone) Derivatives as Dual Effective Agents Targeting Platelet-Cancer Interplay through Protein Disulfide Isomerase Inhibition. [PDF]

J Med Chem
Juang YP, Tsai JY, Gu WL, Hsu HC, Lin CL, Wu CC, Liang PH.   +6 more
europepmc   +1 more source

Strong Protection by 4-Hydroxyestrone against Erastin-Induced Ferroptotic Cell Death in Estrogen Receptor-Negative Human Breast Cancer Cells: Evidence for Protein Disulfide Isomerase as a Mechanistic Target for Protection. [PDF]

Biochemistry
Wang H, Hou MJ, Liao L, Li P, Chen T, Wang P, Zhu BT.   +6 more
europepmc   +1 more source

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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.
Hiram F. Gilbert, Bonney Wilkinson
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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.
Diego Butera, Philip J. Hogg, Freda Passam, Joyce Chiu   +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,
Mark A. Smith, George Perry, Robert B. Petersen, Shun Shimohama, Arun K. Raina, Xiongwei Zhu, Robert L. Russell, Sandra L. Siedlak, Hyoun T. Kim, Peggy L.R. Harris   +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.
Chen-Lu Tsou, Xuan-chuan Yu, Chih-Chen Wang   +2 more
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[38] Protein disulfide-isomerase

1995
Publisher 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, Robert B. Freedman, Stephen H. McLaughlin   +2 more
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