Results 111 to 120 of about 9,080 (229)

Manipulation of the Unfolded Protein Response by Intracellular Bacterial Pathogens: Mechanisms of ER Hijacking and Therapeutic Implications

The FASEB Journal, Volume 40, Issue 2, 31 January 2026.
This review illustrates how intracellular bacterial pathogens—such as Brucella, Mycobacterium tuberculosis, and Legionella—secrete effector proteins that specifically target the IRE1α, PERK, and ATF6 branches of the unfolded protein response (UPR) to hijack ER stress signaling.
Enhui Dai, Dongjie Sun, Yanxiao Zhao, Mengtao Zhang, Yifan Wu, Jiabo Ding   +5 more
wiley   +1 more source

Identifying Interaction Partners of Yeast Protein Disulfide Isomerases Using a Small Thiol-Reactive Cross-Linker: Implications for Secretory Pathway Proteostasis. [PDF]

Chem Res Toxicol, 2022
Freije BJ, Freije WM, Do TU, Adkins GE, Bruch A, Hurtig JE, Morano KA, Schaffrath R, West JD.   +8 more
europepmc   +1 more source

Interactions between cell surface protein disulphide isomerase and S-nitrosoglutathione during nitric oxide delivery [PDF]

, 2007
In this study, we investigated the role of protein disulphide isomerase (PDI) in rapid metabolism of S-nitrosoglutathione (GSNO) and S-nitrosoalbumin (albSNO) and in NO delivery from these compounds into cells.
Askew, Burgess, C.M. Shah, Chen, Cooper, Crane, Crane, de Belder, Essex, Essex, Freedman, Gordge, Gordge, H.S. Chowdrey, Hogg, Hogg, Hogg, I.C. Locke, Jordan, Lahav, Lipton, Liu, Liu, M.P. Gordge, Ogura, O’Neill, Park, Park, Pfeiffer, Ramachandran, Richardson, Root, S.E. Bell, Shah, Simon, Sogo, Stamler, Walsh, Yan, Zai, Zeng, Zhang, Zhang   +42 more
core   +1 more source

Protein disulfide isomerases (PDIs) negatively regulate ebolavirus structural glycoprotein expression in the endoplasmic reticulum (ER) via the autophagy-lysosomal pathway. [PDF]

Autophagy, 2022
Wang B, Zhang J, Liu X, Chai Q, Lu X, Yao X, Yang Z, Sun L, Johnson SF, Schwartz RC, Zheng YH.   +10 more
europepmc   +1 more source

Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1 [PDF]

, 2016
Yingbo Niu, Lihui Zhang, Jiaojiao Yu, Chih-chen Wang, Lei Wang   +4 more
openalex   +1 more source

The Secreted Protein Disulfide Isomerase Ag1 Lost by Ancestors of Poorly Regenerating Vertebrates Is Required for Xenopus laevis Tail Regeneration [PDF]

, 2021
A. S. Ivanova, Maria B. Tereshina, Karina R. Araslanova, N. Y. Martynova, Andrey G. Zaraisky   +4 more
openalex   +1 more source

Proteomic and Ubiquitinated Proteome Insights Into ER Stress Responses in Chinese Hamster Ovary Cells Under Mild Hypothermic Conditions

Biotechnology and Bioengineering, Volume 123, Issue 1, Page 5-25, January 2026.
Proteomic analysis of CHO cells under mild hypothermia (31°C) reveals ER stress responses, ubiquitination dynamics, and adaptive mechanisms. Magnetic immuno‐affinity enrichment and mass spectrometry highlight protein regulation differences in non‐producer versus producer cells, offering insights for optimising biopharmaceutical production of IgG1 and ...
David Ryan, Christiana‐Kondylo Sideri, Michael Henry, Selvaprakash Karuppuchamy, Esen Efeoglu, Paula Meleady   +5 more
wiley   +1 more source

24R,25(OH)2D3 regulates tumorigenesis in estrogen sensitive laryngeal cancer cells via membrane‐associated receptor complexes in ER+ and ER− cells

International Journal of Cancer, Volume 158, Issue 1, Page 202-217, 1 January 2026.
What's new? Estrogen receptors likely influence the development of laryngeal cancer and are of particular interest in regard to their relationship with the vitamin D metabolite 24R,25(OH)2D3. In this study the authors examined interactions between 24R,25(OH)2D3 and estrogen‐responsive laryngeal tumorigenesis.
Cydney D. Dennis, D. Joshua Cohen, Kusal Debnath, Nofrat Schwartz, Brock P. Lodato, Jonathan T. Dillon, Tillat Batool, Matthew S. Halquist, Preetam Ghosh, Zvi Schwartz, Barbara D. Boyan   +10 more
wiley   +1 more source

Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding

Protein Science, Volume 35, Issue 1, January 2026.
Abstract Disulphide bonds (Dsbs) are essential for the folding, stability, and function of many secreted and membrane‐associated proteins in bacteria. In Gram‐negative species, these bonds are introduced by the Dsb enzyme family, with DsbA acting as the primary thiol oxidase.
Stephanie Penning, Lachlan Mitchell, Yaoqin Hong, Taylor Cunliffe, Pramod Subedi, Geqing Wang, Lilian Hor, Makrina Totsika, Jason J. Paxman, Begoña Heras   +9 more
wiley   +1 more source

A guide to building the matrisome interactome: from computational predictions to experimental validation

The FEBS Journal, Volume 293, Issue 1, Page 42-70, January 2026.
This guide proposes a roadmap combining state‐of‐the‐art computational and experimental approaches (including biophysical, biochemical, and imaging techniques) to identify, characterize, and contextualize extracellular matrix (ECM) protein interactions.
Leanna Leverton, Amanpreet Kaur Bains, Ikram Isa, Sylvie Ricard‐Blum, Alexandra Naba   +4 more
wiley   +1 more source