Results 81 to 90 of about 7,369 (220)

Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection

open access: yesRetrovirology, 2012
Background The role of disulfide bond remodeling in HIV-1 infection is well described, but the process still remains incompletely characterized. At present, the data have been predominantly obtained using established cell lines and/or CXCR4-tropic ...
Stantchev Tzanko S   +5 more
doaj   +1 more source

Protein disulfide isomerase as an antithrombotic target [PDF]

open access: yesTrends 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

Targeting protein–protein interactions with reversible covalent modalities: Non‐cysteine chemistries

open access: yesBritish Journal of Pharmacology, EarlyView.
Abstract Protein–protein interactions (PPIs) are central to diverse cellular functions, and represent a rapidly expanding class of therapeutic targets. Advancements in covalent drug design have enabled small‐molecule drugs to overcome challenges associated with engaging these targets, such as limited durations of action and difficult‐to‐drug (expansive,
Ruchira Basu, Steven Fletcher
wiley   +1 more source

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

open access: yesThe 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   +5 more
wiley   +1 more source

The dehydrogenase region of the NADPH oxidase component Nox2 acts as a protein disulfide isomerase (PDI) resembling PDIA3 with a role in the binding of the activator protein p67phox

open access: yesFrontiers in Chemistry, 2015
The superoxide (O2.-)-generating NADPH oxidase of phagocytes consists of a membrane component, cytochrome b558 (a heterodimer of Nox2 and p22phox), and four cytosolic components, p47phox, p67phox, p40phox, and Rac.
Edna eBechor   +7 more
doaj   +1 more source

Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion. [PDF]

open access: yes, 2017
Blood banks use pathogen inactivation (PI) technologies to increase the safety of platelet concentrates (PCs). The characteristics of PI-treated PCs slightly differ from those of untreated PCs, but the underlying reasons are not well understood.
Abonnenc, M.   +4 more
core   +1 more source

The competitive interplay of 12‐oxophytodienoic acid (OPDA), protein thiols, and glutathione

open access: yesThe FEBS Journal, EarlyView.
12‐Oxophytodienoic acid (OPDA) is a phytohormone involved in plant growth and stress defense. Due to its cyclopentenone moiety, OPDA can form Michael adducts with thiol‐containing compounds such as glutathione and cysteine residues of proteins, resulting in alterations of the cellular redox regulatory network.
Madita Knieper   +8 more
wiley   +1 more source

Protein disulfide isomerase MoPdi1 regulates fungal development, virulence, and endoplasmic reticulum homeostasis in Magnaporthe oryzae

open access: yesJournal of Integrative Agriculture
Rice blast, caused by Magnaporthe oryzae, is a fungal disease that causes devastating damage to rice production worldwide. During infection, pathogens secrete effector proteins that modulate plant immunity.
Yu Wang   +6 more
doaj   +1 more source

High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility [PDF]

open access: yes, 2013
ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxinfold domains homologous with the non-catalytic b and b domains of ...
A. Katrine Wallis   +52 more
core   +5 more sources

Biogenesis of TNF‐α‐insights into proteostasis and inflammation

open access: yesThe FEBS Journal, EarlyView.
TNF‐α biogenesis, trafficking, and signalling are tightly and reciprocally coupled to cellular proteostasis systems, including ER chaperones and endoplasmic reticulum‐associated degradation. This bidirectional crosstalk determines whether TNF‐α responses are adaptive or proteotoxic.
Bailasan Haidar   +3 more
wiley   +1 more source

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