Results 21 to 30 of about 41,132 (234)

Disturbed flow regulates protein disulfide isomerase A1 expression via microRNA-204 [PDF]

Frontiers in Physiology
Redox processes can modulate vascular pathophysiology. The endoplasmic reticulum redox chaperone protein disulfide isomerase A1 (PDIA1) is overexpressed during vascular proliferative diseases, regulating thrombus formation, endoplasmic reticulum stress ...
Leonardo Y. Tanaka, Sandeep Kumar, Lucas F. Gutierre, Celso Magnun, Daniela Kajihara, Dong-Won Kang, Francisco R. M. Laurindo, Hanjoong Jo   +7 more
doaj   +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

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   +6 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.
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

Protein Disulfide-Isomerase A3 Is a Robust Prognostic Biomarker for Cancers and Predicts the Immunotherapy Response Effectively

Frontiers in Immunology, 2022
BackgroundProtein disulfide isomerase A3 (PDIA3) is a member of the protein disulfide isomerase (PDI) family that participates in protein folding through its protein disulfide isomerase function.
Zewei Tu, Zewei Tu, Zewei Tu, Zewei Tu, Qin Ouyang, Xiaoyan Long, Lei Wu, Lei Wu, Lei Wu, Lei Wu, Jingying Li, Xingen Zhu, Xingen Zhu, Xingen Zhu, Xingen Zhu, Kai Huang, Kai Huang, Kai Huang, Kai Huang   +18 more
doaj   +1 more source

Roles of Protein Disulfide Isomerase in Breast Cancer [PDF]

Cancers, 2022
Protein disulfide isomerase (PDI) is the endoplasmic reticulum (ER)’s most abundant and essential enzyme and serves as the primary catalyst for protein folding. Due to its apparent role in supporting the rapid proliferation of cancer cells, the selective blockade of PDI results in apoptosis through sustained activation of UPR pathways. The functions of
Suhui Yang, Chanel Jackson, Eduard Karapetyan, Pranabananda Dutta, Dulcie Kermah, Yong Wu, Yanyuan Wu, John Schloss, Jaydutt V. Vadgama   +8 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

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