A new era of cysteine proteomics–Technological advances in thiol biology

N Burger, ET Chouchani - Current Opinion in Chemical Biology, 2024 - Elsevier
Cysteines are amenable to a diverse set of modifications that exhibit critical regulatory
functions over the proteome and thereby control a wide range of cellular processes …

[HTML][HTML] Redox regulation of proteostasis

LD Duong, JD West, KA Morano - Journal of Biological Chemistry, 2024 - Elsevier
Oxidants produced through endogenous metabolism or encountered in the environment
react directly with reactive sites in biological macromolecules. Many proteins, in particular …

Protein phosphatase PP2Cα S-glutathionylation regulates cell migration

DSK Kukulage, KTG Samarasinghe, NNJM Don… - Journal of Biological …, 2024 - jbc.org
Redox signaling is a fundamental mechanism that controls all major biological processes
partly via protein cysteine oxidations, including S-glutathionylation. Despite over 2000 …

Functions of p120-catenin in physiology and diseases

X Jin, T Lin, Y Wang, X Li, Y Yang - Frontiers in Molecular …, 2024 - frontiersin.org
p120-catenin (p120) plays a vital role in regulating cell-cell adhesion at adherens junctions,
interacting with the juxtamembrane domain (JMD) core region of E-cadherin and regulates …

Tag, you're it: G-ICAT identifies p120-cysteine glutathionylation triggering E-cadherin destabilization

KT Fridianto, Y Aye - Cell Chemical Biology, 2023 - cell.com
Current methods have limited ability in directly quantifying the extent of glutathionylation on
specific protein-cysteines. In this issue of Cell Chemical Biology, Ahn et al. 1 report G-ICAT …

Dehydroglutathione to induce non-reducible glutathionylation for functional analysis

D Oppong, R Padmavathi, DSK Kukulage… - 2025 - chemrxiv.org
Protein cysteine is susceptible to diverse oxidations, including disulfide, S-sulfenylation, S-
nitrosylation, and S-glutathionylation, that regulate many biological processes in physiology …