Results 161 to 170 of about 8,445 (200)

Glutaredoxin2 reduces age-associated B cell differentiation through maintaining redox homeostasis. [PDF]

Front Pharmacol
Jiang Y, Sun C, He Q, Liu S, Tian S, Zhang Y, Du Y, Li F, Zhang H.   +8 more
europepmc   +1 more source

Glutathione reductase underlies the stability of mutant p53 by antagonizing protein glutathionylation. [PDF]

Redox Biol
Wang L, Zhong S, Fan X, Xu Y, Wang M, Xu Y, Cai Y, Cao Z, Ye Z, Wen L, Wei P.   +10 more
europepmc   +1 more source

The core mechanism of hypertension-linked renal fibrosis: "RAAS-ROS-inflammation-fibrosis" axis. [PDF]

iScience
Wang Y, Chen J, Wang W, Yi X, Xing S, Lei X, Chen H, Xie X.   +7 more
europepmc   +1 more source

LCN2 promotes focal adhesion formation and invasion by stimulating c-Src activation.

J Cell Sci
Choudhary BS, Chaudhary N, Khan BK, Vijan A, Mandal D, Pilankar L, Gawand S, Uttankar P, Sharma M, Shivashankar A, Doloi R, Joshi N, Das M, Dalal SN.   +13 more
europepmc   +1 more source

Role of Glutathionylation in Infection and Inflammation [PDF]

Nutrients, 2019
Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by different cellular oxidoreductases, by which the redox state of the cell modulates protein function. So far, most studies on the identification of glutathionylated proteins
Paola Checconi, Dolores Limongi, Sara Baldelli   +2 more
exaly   +9 more sources

Protein Glutathionylation in Cardiovascular Diseases [PDF]

International Journal of Molecular Sciences, 2013
The perturbation of thiol-disulfide homeostasis is an important consequence of many diseases, with redox signals implicated in several physio-pathological processes. A prevalent form of cysteine modification is the reversible formation of protein mixed disulfides with glutathione (S-glutathionylation).
Anna Pastore, Fiorella Piemonte, Pastore Anna   +2 more
exaly   +4 more sources

Protein glutathionylation in health and disease

Biochimica Et Biophysica Acta - General Subjects, 2013
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 undergo different types of oxidation, one of which is glutathionylation, or the formation of mixed disulfides with glutathione (GSH).We will discuss how proteins can undergo ...
Pietro Ghezzi
exaly   +4 more sources

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Emerging chemistry and biology in protein glutathionylation

Current Opinion in Chemical Biology, 2022
Protein S-glutathionylation serves a regulatory role in proteins and modulates distinct biological processes implicated in health and diseases. Despite challenges in analyzing the dynamic and reversible nature of S-glutathionylation, recent chemical and biological methods have significantly advanced the field of S-glutathionylation, culminating in ...
Young-Hoon Ahn
exaly   +3 more sources