Results 21 to 30 of about 97,846 (317)

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

Emerging roles of protein disulfide isomerase in cancer

BMB Reports, 2017
The protein disulfide isomerase (PDI) family is a group of multifunctional endoplasmic reticulum (ER) enzymes that mediate the formation of disulfide bonds, catalyze the cysteine-based redox reactions and assist the quality control of client proteins ...
Eunyoug Lee, Do Hee Lee
openalex   +3 more sources

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

Thromb J
He C, Yang A, Zhang Y, Zhao Z, Lu Y, Zhang J, Wu Y.   +6 more
europepmc   +3 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   +11 more sources

The flexibility and dynamics of protein disulfide isomerase [PDF]

Proteins: Structure, Function, and Bioinformatics, 2016
We have studied the mobility of the multidomain folding catalyst, protein disulfide isomerase (PDI), by a coarse‐graining approach based on flexibility.
Rudolf A. Römer, Stephen A. Wells, J. Emilio Jimenez‐Roldan, Moitrayee Bhattacharyya, Saraswathi Vishweshwara, Robert B. Freedman   +5 more
openalex   +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

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.
Hatahet Feras, Ruddock Lloyd
openaire   +2 more sources

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.
S, Baksh, K, Burns, C, Andrin, M, Michalak   +3 more
openaire   +2 more sources

Inhibition of protein disulfide isomerase induces differentiation of acute myeloid leukemia cells

Haematologica, 2018
A cute myeloid leukemia is a malignant disease of immature myeloid cells. Despite significant therapeutic effects of differentiation-inducing agents in some acute myeloid leukemia subtypes, the disease remains incurable in a large fraction of patients ...
Justyna Chlebowska-Tuz, Olga Sokolowska, Pawel Gaj, Michal Lazniewski, Malgorzata Firczuk, Karolina Borowiec, Hanna Sas-Nowosielska, Malgorzata Bajor, Agata Malinowska, Angelika Muchowicz, Kavita Ramji, Piotr Stawinski, Mateusz Sobczak, Zofia Pilch, Anna Rodziewicz-Lurzynska, Malgorzata Zajac, Krzysztof Giannopoulos, Przemyslaw Juszczynski, Grzegorz W. Basak, Dariusz Plewczynski, Rafal Ploski, Jakub Golab, Dominika Nowis   +22 more
doaj   +1 more source