Results 21 to 30 of about 7,315 (215)

Autodegradation of Protein Disulfide Isomerase [PDF]

Bioscience, Biotechnology, and Biochemistry, 1999
Protein disulfide isomerase (PDI) and its degradation products were found in HepG2, COS-1, and CHO-K1 cells. Whether or not the products were formed through autodegradation of PDI was examined, since PDI contains the CGHC motif, which is the active center of proteolytic activity in ER-60 protease.
R, Urade, A, Yasunishi, H, Okudo, T, Moriyama, M, Kito   +4 more
openaire   +2 more sources

PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

Molecules, 2020
Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the ...
Jiahui Fu, Jihui Gao, Zhongxin Liang, Dong Yang   +3 more
doaj   +1 more source

Protein disulfide isomerase in cardiovascular disease [PDF]

Experimental & Molecular Medicine, 2020
AbstractProtein disulfide isomerase (PDI) participates in the pathogenesis of numerous diseases. Increasing evidence indicates that intravascular cell-derived PDI plays an important role in the initiation and progression of cardiovascular diseases, including thrombosis and vascular inflammation.
Bei Xiong, Vishwanath Jha, Jeong-Ki Min, Jaehyung Cho   +3 more
openaire   +3 more sources

Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction

FEBS Open Bio, 2014
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
doaj   +1 more source

Influence of ellagitannins extracted by pomegranate fruit on disulfide isomerase PDIA3 activity [PDF]

, 2019
Pomegranate fruit is a functional food of high interest for human health due to its wide range of phytochemicals with antioxidant properties are implicated in the prevention of inflammation and cancer. Ellagitannins, such as punicalagin and ellagic acid,
Altieri, Fabio, Cairone, Francesco, Carradori, Simone, Cesa, Stefania, Chichiarelli, Silvia, Giamogante, Flavia, Locatelli, Marcello   +6 more
core   +1 more source

A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis [PDF]

, 2017
Background: Within the endoplasmic reticulum, thiol isomerase enzymes modulate the formation and rearrangement of disulphide bonds in newly folded proteins entering the secretory pathway to ensure correct protein folding.
Bicknell, A. B., Flora, G. D., Gibbins, J. M., Holbrook, L., Sahli, K., Sandhar, G. K., Sasikumar, P., Schenk, M. P., Stainer, A. R.   +8 more
core   +1 more source

Cloning, expression, purification and characterization of a DsbA-like protein from Wolbachia pipientis [PDF]

, 2008
Wolbachia pipientis are obligate endosymbionts that infect a wide range of insect and other arthropod species. They act as reproductive parasites by manipulating the host reproduction machinery to enhance their own transmission. This unusual phenotype is
Alun Jones, Bardwell, Begoña Heras, Collet, Debarbieux, Edeling, Ellermeier, Ellman, Floate, Gautier Robin, Gordon J. King, Goulding, Gruber, Heras, Hillson, Holmgren, Iñaki Iturbe-Ormaetxe, Jennifer L. Martin, Jeyaprakash, Kadokura, Kelley, Mareike Kurz, Martin, Martin, McCarthy, Messens, Nakamoto, Nathan Cowieson, O’Neill, O’Neill, Patrick Frei, Raina, Riegler, Rietsch, Rudi Glockshuber, Russell Jarrott, Sambrook, Scott L. O’Neill, Studier, Taylor, Taylor, Werren, Wu, Yu   +43 more
core   +1 more source

Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs

Redox Biology, 2023
Protein disulfide isomerases (PDIs) catalyze redox reactions that reduce, oxidize, or isomerize disulfide bonds and act as chaperones of proteins as they fold. The characteristic features of PDIs are the presence of one or more catalytic thioredoxin (TRX)
Natalia Zamorano Cuervo, Nathalie Grandvaux   +1 more
doaj   +1 more source

Structure of the non-catalytic domain of the protein disulfide isomerase-related protein (PDIR) reveals function in protein binding.

PLoS ONE, 2013
Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as
Roohi Vinaik, Guennadi Kozlov, Kalle Gehring   +2 more
doaj   +1 more source

Inhibition of thiol isomerase activity diminishes endothelial activation of plasminogen, but not of protein C [PDF]

, 2015
Highlights •A range of thiol isomerase enzymes were expressed by HMEC-1 endothelial cells. •Inhibition of thiol isomerases reduced plasminogen activation on HMEC-1 cells.
Gordge, M.P., Gordge, M.P., Kamaludin, N., Kamaludin, N., Shah, C.M., Shah, C.M., Smith, C.L., Smith, C.L.   +7 more
core   +1 more source