Results 11 to 20 of about 43,163 (273)

Compact conformations of human protein disulfide isomerase. [PDF]

PLoS ONE, 2014
Protein disulfide isomerase (PDI) composed of four thioredoxin-like domains a, b, b', and a', is a key enzyme catalyzing oxidative protein folding in the endoplasmic reticulum.
Shang Yang, Xi Wang, Lei Cui, Xiang Ding, Lili Niu, Fuquan Yang, Chao Wang, Chih-Chen Wang, Jizhong Lou   +8 more
doaj   +4 more sources

Protein Disulfide Isomerase and Host-Pathogen Interaction [PDF]

The Scientific World Journal, 2011
Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways ...
Beatriz S. Stolf, Ioannis Smyrnias, Lucia R. Lopes, Alcione Vendramin, Hiro Goto, Francisco R. M. Laurindo, Ajay M. Shah, Celio X. C. Santos   +7 more
doaj   +3 more sources

The human protein disulfide isomerase gene family [PDF]

Human Genomics, 2012
Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known ...
Galligan James J, Petersen Dennis R
doaj   +3 more sources

Protein disulfide isomerase mediates integrin‐dependent adhesion [PDF]

FEBS Letters, 2000
Cell adhesion is mediated by the integrin adhesion receptors. Receptor–ligand interaction involves conformational changes in the receptor, but the underlying mechanism remains unclear. Our earlier work implied a role for sulfhydryls in integrin response to ligand binding in the intact blood platelet.
Judith Lahav, N. Gofer-Dadosh, Jacob Luboshitz, Oded Hess, Mati Shaklai   +4 more
openalex   +4 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

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

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