S-glutathionylation in protein redox regulation
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione
and low-pKa cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative …
and low-pKa cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative …
Molecular Mechanisms and Potential Clinical Significance of S-Glutathionylation
I Dalle–Donne, A Milzani, N Gagliano… - Antioxidants & redox …, 2008 - liebertpub.com
Protein S-glutathionylation, the reversible binding of glutathione to protein thiols (PSH), is
involved in protein redox regulation, storage of glutathione, and protection of PSH from …
involved in protein redox regulation, storage of glutathione, and protection of PSH from …
Markers of blood-brain barrier disruption increase early and persistently in COVID-19 patients with neurological manifestations
V Bonetto, L Pasetto, I Lisi, M Carbonara… - Frontiers in …, 2022 - frontiersin.org
Background Coronavirus disease 2019 (COVID-19) caused by SARS-CoV-2 infection is
associated with disorders affecting the peripheral and the central nervous system. A high …
associated with disorders affecting the peripheral and the central nervous system. A high …
Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function
Proteins, with their seemingly limitless functional diversity, are major players in the
maintenance of life. The ability of proteins to fulfill these various biological functions is …
maintenance of life. The ability of proteins to fulfill these various biological functions is …
Review regulation of protein function by glutathionylation
P Ghezzi - Free radical research, 2005 - Taylor & Francis
The main function of reduced glutathione (GSH) is to protect from oxidative stress as a
reactive oxygen scavenger. However, in the context of redox regulation, the ratio between …
reactive oxygen scavenger. However, in the context of redox regulation, the ratio between …
Protein glutathionylation in health and disease
P Ghezzi - Biochimica et Biophysica Acta (BBA)-General Subjects, 2013 - Elsevier
BACKGROUND: It is now recognized that protein cysteines exist not only as free thiols or
intramolecular disulfides, that help maintain the 3D structure of proteins, but can also …
intramolecular disulfides, that help maintain the 3D structure of proteins, but can also …
Cellular redox pathways as a therapeutic target in the treatment of cancer
AJ Montero, J Jassem - Drugs, 2011 - Springer
The vulnerability of some cancer cells to oxidative signals is a therapeutic target for the
rational design of new anticancer agents. In addition to their well characterized effects on …
rational design of new anticancer agents. In addition to their well characterized effects on …
Amyotrophic lateral sclerosis multiprotein biomarkers in peripheral blood mononuclear cells
Background Amyotrophic lateral sclerosis (ALS) is a fatal progressive motor neuron disease,
for which there are still no diagnostic/prognostic test and therapy. Specific molecular …
for which there are still no diagnostic/prognostic test and therapy. Specific molecular …
Redox-sensitive cyclophilin A elicits chemoresistance through realigning cellular oxidative status in colorectal cancer
Cancer cells utilize rapidly elevated cellular antioxidant programs to accommodate
chemotherapy-induced oxidative stress; however, the underlying mechanism remains …
chemotherapy-induced oxidative stress; however, the underlying mechanism remains …
[HTML][HTML] The mitochondrial permeability transition pore and cyclophilin D in cardioprotection
F Di Lisa, A Carpi, V Giorgio, P Bernardi - Biochimica et Biophysica Acta …, 2011 - Elsevier
Mitochondria play a central role in heart energy metabolism and Ca2+ homeostasis and are
involved in the pathogenesis of many forms of heart disease. The body of knowledge on …
involved in the pathogenesis of many forms of heart disease. The body of knowledge on …