Results 31 to 40 of about 83,408 (297)

Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation [PDF]

, 2017
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and ...
Bulleid, Neil J., Pringle, Marie Anne, Robinson, Philip J., Woolhead, Cheryl A.   +3 more
core   +1 more source

A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding. [PDF]

PLoS ONE, 2014
Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI).
Li Zhu, Kai Yang, Xi'e Wang, Xi Wang, Chih-chen Wang   +4 more
doaj   +1 more source

The thiol-disulfide exchange activity of AtPDI1 is involved in the response to abiotic stresses

BMC Plant Biology, 2021
Background Arabidopsis protein disulfide isomerase 1 (AtPDI1) has been demonstrated to have disulfide isomerase activity and to be involved in the stress response.
Ying Lu, Li Yuan, Zhou Zhou, Mengyu Wang, Xiaoyun Wang, Shizhong Zhang, Qinghua Sun   +6 more
doaj   +1 more source

Oxidative protein folding in the mitochondrial intermembrane space [PDF]

, 2010
Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated ...
Anfinsen CB, Dionisia P. Sideris, Giorda R, Kamitani S, Kostas Tokatlidis   +4 more
core   +1 more source

Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans. [PDF]

, 2007
Protein disulfide isomerase (PDI) is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum.
Alan D. Winter, Antony P. Page, Barstead, Bulleid, Bulleid, Cox, Cox, Darby, Ellgaard, Eschenlauer, Friedman, Gething, Gillian McCormack, Goldberger, Johnstone, Kamath, Kelly, Kemmink, Kimble, Koivunen, Koivunen, Kramer, Kramer, Kulp, McMahon, Myllyharju, Myllyharju, Novelli, Novelli, Oliver, Page, Page, Page, Pirneskoski, Pirneskoski, Simmer, Soldà, Tian, Veijola, Vuori, Vuori, Wilkinson, Winter, Winter, Yang   +44 more
core   +1 more source

Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]

, 2014
Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Appenzeller-Herzog, Araki, Araki, Baker, Bulleid, Chambers, Colin Shepherd, Gross, Hatahet, Heldman, Inaba, Kim, Masui, Neil J. Bulleid, Nguyen, Nguyen, Ojore B. V. Oka, Sevier, Tavender, Tavender, Tu, Tu, Wang   +22 more
core   +1 more source

Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization. [PDF]

PLoS ONE, 2013
BACKGROUND: Tau protein is implicated in the pathogenesis of neurodegenerative disorders such as tauopathies including Alzheimer disease, and Tau fibrillization is thought to be related to neuronal toxicity. Physiological inhibitors of Tau fibrillization
Li-Rong Xu, Xiao-Ling Liu, Jie Chen, Yi Liang   +3 more
doaj   +1 more source

Targeting protein disulfide isomerase with the flavonoid isoquercetin to improve hypercoagulability in advanced cancer.

JCI Insight, 2019
BACKGROUND Protein disulfide isomerase (PDI) is a thiol isomerase secreted by vascular cells that is required for thrombus formation. Quercetin flavonoids inhibit PDI activity and block platelet accumulation and fibrin generation at the site of a ...
J. Zwicker, Benjamin L. Schlechter, Jack D. Stopa, H. Liebman, A. Aggarwal, M. Puligandla, Thomas Caughey, K. Bauer, N. Kuemmerle, E. Wong, T. Wun, M. Mclaughlin, M. Hidalgo, D. Neuberg, B. Furie, R. Flaumenhaft   +15 more
semanticscholar   +1 more source

Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]

, 2010
The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian, Chin, King-Tung, Ellgaard, Lars, Riemer, Jan, Ron, David, Spiess, Martin, Zito, Ester   +6 more
core   +3 more sources

Participation of the endoplasmic reticulum protein chaperone thio-oxidoreductase in gonadotropin-releasing hormone receptor expression at the plasma membrane

Brazilian Journal of Medical and Biological Research, 2009
Chaperone members of the protein disulfide isomerase family can catalyze the thiol-disulfide exchange reaction with pairs of cysteines. There are 14 protein disulfide isomerase family members, but the ability to catalyze a thiol disulfide exchange ...
W. Lucca-Junior, J.A. Janovick, P.M. Conn   +2 more
doaj   +1 more source