Results 191 to 200 of about 41,132 (234)

Protein disulfide isomerase 1 is required for RodA assembling-based conidial hydrophobicity of Aspergillus fumigatus. [PDF]

Appl Environ Microbiol
Hu X, Zhou Y, Liu R, Wang J, Guo L, Huang X, Li J, Yan Y, Liu F, Li X, Tan X, Luo Y, Wang P, Zhou S.   +13 more
europepmc   +1 more source

Binding of Selected Ligands to Human Protein Disulfide Isomerase and Microsomal Triglyceride Transfer Protein Complex and the Associated Conformational Changes: A Computational Molecular Modelling Study. [PDF]

ChemistryOpen
Yang YX, Li P, Zhu BT.
europepmc   +1 more source

Integrated Transcriptome and Proteome Analysis Reveals the Regulatory Mechanism of Root Growth by Protein Disulfide Isomerase in Arabidopsis. [PDF]

Int J Mol Sci
Liu Y, Song P, Yan M, Luo J, Wang Y, Fan F.   +5 more
europepmc   +1 more source

Protein disulfide isomerase uses thrombin-antithrombin complex as a template to bind its target protein and alter the blood coagulation rates. [PDF]

Biosci Rep
Khan AB, Siddiqui U, Fatima S, Rehman AA, Jairajpuri MA.   +4 more
europepmc   +1 more source

Protein disulfide isomerase plays a crucial role in mediating chemically-induced, glutathione depletion-associated hepatocyte injury in vitro and in vivo. [PDF]

Cell Commun Signal
Zhu YY, Zhang Q, Jia YC, Hou MJ, Zhu BT.
europepmc   +1 more source

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]

Bioengineered
europepmc   +1 more source

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Protein disulfide isomerase

Biochimica Et Biophysica Acta - 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.
L. Lopes, M. Janiszewski, M. Pedro, A Carmo, F. Laurindo   +4 more
exaly   +7 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
openaire   +2 more sources