Results 91 to 100 of about 43,163 (273)

Protein disulfide isomerase as an antithrombotic target [PDF]

Trends in Cardiovascular Medicine, 2013
Protein disulfide isomerase (PDI) is a ubiquitously expressed oxidoreductase required for proper protein folding. It is highly concentrated in the endoplasmic reticulum, but can also be released into the extracellular environment. Several in vivo thrombosis models have demonstrated that vascular PDI secreted by platelets and endothelial cells is ...
openaire   +2 more sources

ER proteostasis meets mitochondrial function: contact sites as hubs of communication and therapeutic targets

The FEBS Journal, EarlyView.
Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna, Alessandro Cherubini, Ersilia Varone, Serena Germani, Alice Marrazza, Ester Zito   +5 more
wiley   +1 more source

Review

, 2020
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R, Arai K, Baskakov IV, Creighton TE, Dittmer K, Du Vigneaud V, Janeček J, Metanis N, Musiol HJ, Muttenthaler M, Nygard B, O'Donnell ME, Welch M, Yang F   +13 more
core   +1 more source

Retarded PDI diffusion and a reductive shift in poise of the calcium depleted endoplasmic reticulum [PDF]

, 2015
Background: Endoplasmic reticulum (ER) lumenal protein thiol redox balance resists dramatic variation in unfolded protein load imposed by diverse physiological challenges including compromise in the key upstream oxidases.
AE Palmer, Alisa Zyryanova, Ana Crespillo-Casado, B Enyedi, C Wang, CH Kubisch, Clemens F Kaminski, D Givol, D Ron, David Ron, E Avezov, Eduardo Pinho Melo, Edward Avezov, EF Corbett, F Hatahet, H Harding, Heather P Harding, I Mehmeti, J Birk, J Birk, JD Blais, JH Frank, JR Lohman, K Araki, Kazuhiro Nagata, KT Chin, M Esfandiarei, M Hagiwara, M Lith van, MY Berezin, N Mesaeli, NJ Bulleid, OB Oka, R Ushioda, Romain Laine, Ryo Ushioda, S Tsunoda, SJ Ashcroft, SJ Wijeyesakere, T Anelli, T Higo, Tasuku Konno, Weiyue Chen, Y Li   +43 more
core   +2 more sources

Gaining extensive resistance against clubroot disease through the disruption of a susceptibility gene

Journal of Integrative Plant Biology, EarlyView.
This Commentary examines research by Wu et al. showing that β‐1,3‐glucan synthase‐like 5 (GSL5) functions as a key gene for susceptibility to clubroot in Brassica family members by suppressing immunity regulated by jasmonic acid. Inaction of GSL5 through genome editing provides broad‐spectrum resistance to clubroot.
Qibin Wu, Zhen Zeng, Daowen Wang, Zheng Qing Fu, Youxiong Que   +4 more
wiley   +1 more source

A substrate-driven allosteric switch that enhances PDI catalytic activity

Nature Communications, 2016
Protein Disulfide Isomerase (PDI) is a prothrombotic, multidomain enzyme with separate substrate binding and catalytic domains. Here, the authors identify a new class of compounds that target the PDI substrate binding site, inducing a conformational ...
Roelof H. Bekendam, Pavan K. Bendapudi, Lin Lin, Partha P. Nag, Jun Pu, Daniel R. Kennedy, Alexandra Feldenzer, Joyce Chiu, Kristina M. Cook, Bruce Furie, Mingdong Huang, Philip J. Hogg, Robert Flaumenhaft   +12 more
doaj   +1 more source

Reticulon1-C modulates protein disulphide isomerase function [PDF]

, 2013
Endoplasmic reticulum (ER) is the primary site for the synthesis and folding of secreted and membrane-bound proteins. Accumulation of unfolded and misfolded proteins in ER underlies a wide range of human neurodegenerative disorders.
Bernardoni, P, Ciriolo, M, Costanzi, A, Di Sano, F, Fazi, B, Filomeni, G, Montagna, C, Nardacci, R, Piacentini, M   +8 more
core   +1 more source

The Role of Oxidative Stress in Periodontitis

Journal of Periodontal Research, EarlyView.
Oxidative stress is involved in multiple chemical reactions that take place in different intracellular organelles: mitochondria, rough endoplasmic reticulum, peroxisomes, autophagy, and aging, and can be influenced by exogenous factors: nutrition, physical activity, psychological status, environmental conditions, microbiome, and drugs.
Pedro Bullon, Francesca Giampieri, Beatriz Bullon, Maurizio Battino   +3 more
wiley   +1 more source

Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast

Scientific Reports, 2023
Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide isomerase PDI and oxidoreductin Ero1. Their activity is tightly regulated and interconnected with the unfolded protein response (UPR).
Arianna Palma, Lukas A. Rettenbacher, Antti Moilanen, Mirva Saaranen, Christian Pacheco-Martinez, Brigitte Gasser, Lloyd Ruddock   +6 more
doaj   +1 more source

The protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection [PDF]

, 2015
The protein disulfide isomerase (PDI) is a ubiquitous and multifunction enzyme belonging to the thioredoxin (TRX) superfamily, which can reduce, oxidize, and catalyze dithiol-disulfide exchange reactions.
Biao Gu, Guiyan Huang, Meixiang Zhang, Qiang Zhang, Qinhu Wang, Weixing Shan, Yuling Meng   +6 more
core   +2 more sources