Work

Acetylation of proximal cysteine-lysine pairs by alcohol metabolism

Year: 2024

Type: article

Abstract: ) each with a unique microenvironment. The motifs are composed of functionally relevant Cys-Ly altered within ALD, identifying potential therapeutic targets. Furthermore, these unique Cys-Lys redox signatures are translationally relevant as revealed by orthologous comparison with severe alcohol-associated hepatitis (SAH) explants, revealing numerous pathogenic thiol redox signals in these patients.

Source: Redox Biology

DOI: 10.1016/j.redox.2024.103462

Authors: Courtney D. McGinnis, Peter S. Harris, Brenton I.M. Graham, John O. Marentette, Cole R. Michel, Laura M. Saba, Richard Reisdorph, James R. Roede, Kristofer S. Fritz

Institution: University of Colorado Anschutz

Language: English

Topic: Redox biology and oxidative stress

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: gold

Estimated APC paid: $3,900

Funders: University of Colorado, Korea Sanhak Foundation, National Institutes of Health, National Institute on Alcohol Abuse and Alcoholism, National Cancer Institute, National Institute of Environmental Health Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences

Awards: Regulation of hepatic lysine N-acetylation by cysteine proximity due to alcohol toxicity, G2343708492, G3372847871, G3533842249, Fusion Lumos Orbitrap System for Quantitative Proteomics and Metabolomics Applications, G7382743091, G8071337789, G8575923797, University of Colorado Cancer Center Support Grant, G9001225491

OpenAlex ID: W4405315348

FWCI: 0.347

Cites: 56

Cited by: 3

Related to: 10