Protein S-glutathionylation: a regulatory device from bacteria to humans.
By I. Dalle-Donne, R. Rossi, G. Colombo, D. Giustarini, A. Milzani. TIBS -Trends in Biochemical Sciences. Regular ed, 2009
636 citations recorded by the source corpus.
Subfields: Biochemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/02b14be6d8ddd818b749ca1cfd1bb7999de5f9cf
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In Biochemistry
In Molecular Biology
Citations in the corpus
- Herbal extracts and phytochemicals: plant secondary metabolites and the enhancement of human brain function. (2011, background): “Additionally, multiple aspects of cellular and redox signaling are conserved between the taxa (23,24), including similar gene expression in response to cellular stressors, which are regulated by common transcription factors (24).”
- Desiccation tolerant plants as model systems to study redox regulation of protein thiols (2010, background): “Together, thiol accessibility and reactivity confer specificity to protein S-glutathionylation (Dalle-Donne et al. 2007; Dalle-Donne et al. 2009; Paulsen and Carroll 2010).”
- GLUTATHIONE SYNTHESIS (2012, background): “GSH can be reversibly bound to the –SH of protein cysteinyl residues (Prot-SH) by a process called glutathionylation, generating glutathionylated proteins (Prot-SSG), which can either activate or inactivate the protein [18].”