Results 21 to 30 of about 86,419 (320)

A novel role for protein disulfide isomerase ERp18 in venous thrombosis [PDF]

Thromb J
Chao He, Aizhen Yang, Yuxin Zhang, Zhenzhen Zhao, Yi Lü, Jingyu Zhang, Yi Wu   +6 more
openalex   +2 more sources

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, Meng-Ke 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

Protein disulfide isomerase‐A1 regulates intraplatelet reactive oxygen species–thromboxane A2‐dependent pathway in human platelets

Journal of Thrombosis and Haemostasis, 2021
Platelet‐derived protein disulfide isomerase 1 (PDIA1) regulates thrombus formation, but its role in the regulation of platelet function is not fully understood.
K. Przyborowski, Anna Kurpińska, Dagmara Wojkowska, Patrycja Kaczara, Joanna Suraj‐Prażmowska, K. Karolczak, A. Malinowska, A. Pełesz, A. Kij, I. Kalvins, C. Watała, S. Chłopicki   +11 more
semanticscholar   +1 more source

Novel Protein Disulfide Isomerase Inhibitor with Anticancer Activity in Multiple Myeloma [PDF]

Cancer Research, 2016
Sergei Vatolin, James G. Phillips, Babal K. Jha, Shravya Govindgari, Jennifer J. Hu, Dale Grabowski, Yvonne Parker, Daniel J. Lindner, Fei Zhong, Clark Distelhorst, Mitchell R. Smith, Claudiu Cotta, Yan Xu, Sujatha Chilakala, Rebecca R. Kuang, Samantha Tall, Frederic J. Reu   +16 more
openalex   +2 more sources

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

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

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

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