Results 21 to 30 of about 83,411 (273)

A conserved protein disulfide isomerase enhances plant resistance against herbivores.

Plant Physiology, 2022
Herbivore-associated molecular patterns (HAMPs) enable plants to recognize herbivores and may help plants adjust their defense responses. Here, we report on herbivore-induced changes in a protein disulfide isomerase (PDI) widely distributed across ...
Jia-Rong Cui, Xiaoli Bing, Yi-Jing Tang, F. Liu, Lu-lu Ren, Jia-Yi Zhou, Huan-huan Liu, Mengxiao Wang, A. Hoffmann, X. Hong   +9 more
semanticscholar   +1 more source

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

British Journal of Pharmacology, 2021
Protein disulfide isomerase (PDI) is the prototypic member of the thiol isomerase family that catalyses disulfide bond rearrangement. Initially identified in the endoplasmic reticulum as folding catalysts, PDI and other members in its family have also ...
Xulin Xu, J. Chiu, Shuai Chen, C. Fang
semanticscholar   +1 more source

Two protein disulfide isomerase subgroups work synergistically in catalyzing oxidative protein folding.

Plant Physiology, 2021
Disulfide bonds play essential roles in the folding of secretory and plasma membrane proteins in the endoplasmic reticulum (ER). In eukaryotes, protein disulfide isomerase (PDI) is an enzyme catalyzing the disulfide bond formation and isomerization in ...
Fenggui Fan, Qiao Zhang, Yini Zhang, Guozhong Huang, Xuelian Liang, Chih‐chen Wang, Lei Wang, Dongping Lu   +7 more
semanticscholar   +1 more source

Disulfide bond engineering of AppA phytase for increased thermostability requires co-expression of protein disulfide isomerase in Pichia pastoris

Biotechnology for Biofuels, 2021
Background Phytases are widely used commercially as dietary supplements for swine and poultry to increase the digestibility of phytic acid. Enzyme development has focused on increasing thermostability to withstand the high temperatures during industrial ...
Laura Navone, T. Vogl, P. Luangthongkam, J. Blinco, C. Luna-Flores, Xiaojing Chen, Juhani von Hellens, S. Mahler, R. Speight   +8 more
semanticscholar   +1 more source

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.
Hirokazu Okudo, Tatsuya Moriyama, Makoto Kito, Ayako Yasunishi, Reiko Urade   +4 more
openaire   +3 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 interacts with a substrate protein at all stages along its folding pathway [PDF]

, 2014
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding).
A Jansens, A Land, A Pirneskoski, A. Katrine Wallis, Alistair G. Irvine, AR Karala, AR Karala, AY Denisov, B van den Berg, B van den Berg, B van den Berg, CB Anfinsen, Claudia A. Blindauer, CPM van Mierlo, CPM van Mierlo, CW Gruber, DP Goldenberg, E van Anken, F Hatahet, G Kozlov, G Wagner, HC Shin, HC Shin, J Riemer, JH Laity, JL Arolas, JS Weissman, JS Weissman, L Wang, LJ Byrne, Lloyd W. Ruddock, M Narayan, Mark J. Howard, Michelle L. Rowe, Narinder Sanghera, NJ Bulleid, NJ Darby, P Klappa, P Venetianer, RA Williamson, RB Freedman, RF Goldberger, Richard A. Williamson, RJ Ellis, Robert B. Freedman, S Masui, S Talluri, Salvador Ventura, TE Creighton, TE Creighton, TE Creighton, TE Creighton, VD Nguyen, VD Nguyen, WF Vranken   +54 more
core   +8 more sources

Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress

EMBO Journal, 2020
Accumulated unfolded proteins in the endoplasmic reticulum (ER) trigger the unfolded protein response (UPR) to increase ER protein folding capacity. ER proteostasis and UPR signaling need to be regulated in a precise and timely manner.
Jiaojiao Yu, Tao Li, Yu Liu, Xi Wang, Jianchao Zhang, Xi’e Wang, Guizhi Shi, J. Lou, Likun Wang, Chih‐chen Wang, Lei Wang   +10 more
semanticscholar   +1 more source

Interaction of Calreticulin with Protein Disulfide Isomerase [PDF]

Journal of Biological Chemistry, 1995
We report here that calreticulin interacts with protein disulfide isomerase (PDI). The PDI-calreticulin complex can be dissociated by Zn(2+)-iminodiacetate-substituted Sepharose-agarose chromatography, suggesting that these interactions may be Zn2+-dependent.
Marek Michalak, Shairaz Baksh, Kimberly Burns, Christi Andrin   +3 more
openaire   +3 more sources

Substrate recognition by the protein disulfide isomerases [PDF]

The FEBS Journal, 2007
Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.
Feras Hatahet, Lloyd W. Ruddock
openaire   +3 more sources