The Role of S-Glutathionylation in Health and Disease: A Bird’s Eye View DOI Open Access
Luca Federici, Michele Masulli,

Vincenzo De Laurenzi

et al.

Nutrients, Journal Year: 2024, Volume and Issue: 16(16), P. 2753 - 2753

Published: Aug. 18, 2024

Protein glutathionylation is a reversible post-translational modification that involves the attachment of glutathione to cysteine residues. It plays role in regulation several cellular processes and protection against oxidative damage. Glutathionylation (GS-ylation) modulates protein function, inhibits or enhances enzymatic activity, maintains redox homeostasis, shields proteins from irreversible stress. Aberrant GS-ylation patterns are thus implicated various diseases, particularly those associated with stress inflammation, such as cardiovascular neurodegenerative disorders, cancer, many others. Research recent years has highlighted potential manipulate for therapeutic purposes strategies imply both its enhancement inhibition according different cases. Moreover, it become increasingly evident monitoring status selected offers diagnostic diseases. In this review, we try summarize research field focus on our current understanding molecular mechanisms related aberrant GS-ylation.

Language: Английский

S-nitrosylation and S-glutathionylation lying at the forefront of redox dichotomy or a visible synergism? DOI
Surupa Chakraborty, Ankita Choudhuri, Akansha Mishra

et al.

Biochemical and Biophysical Research Communications, Journal Year: 2025, Volume and Issue: unknown, P. 151734 - 151734

Published: March 1, 2025

Language: Английский

Citations

0
Glutathione Metabolism in Ferroptosis and Cancer Therapy DOI
Xiangfei Xue, Manyuan Wang,

Jiangtao Cui

et al.

Cancer Letters, Journal Year: 2025, Volume and Issue: unknown, P. 217697 - 217697

Published: April 1, 2025

Language: Английский

Citations

0
The Role of S-Glutathionylation in Health and Disease: A Bird’s Eye View DOI Open Access
Luca Federici, Michele Masulli,

Vincenzo De Laurenzi

et al.

Nutrients, Journal Year: 2024, Volume and Issue: 16(16), P. 2753 - 2753

Published: Aug. 18, 2024

Protein glutathionylation is a reversible post-translational modification that involves the attachment of glutathione to cysteine residues. It plays role in regulation several cellular processes and protection against oxidative damage. Glutathionylation (GS-ylation) modulates protein function, inhibits or enhances enzymatic activity, maintains redox homeostasis, shields proteins from irreversible stress. Aberrant GS-ylation patterns are thus implicated various diseases, particularly those associated with stress inflammation, such as cardiovascular neurodegenerative disorders, cancer, many others. Research recent years has highlighted potential manipulate for therapeutic purposes strategies imply both its enhancement inhibition according different cases. Moreover, it become increasingly evident monitoring status selected offers diagnostic diseases. In this review, we try summarize research field focus on our current understanding molecular mechanisms related aberrant GS-ylation.

Language: Английский

Citations

3