BACKGROUND: Glutathione-dependent catalysis is a metabolic adaptation to chemical
challenges encountered by all life forms. In the course of evolution, nature optimized …

Abstract Thioredoxins (Trxs), glutaredoxins (Grxs), and peroxiredoxins (Prxs) have been
characterized as electron donors, guards of the intracellular redox state, and “antioxidants” …

A very fast empirical method is presented for structure‐based protein pKa prediction and
rationalization. The desolvation effects and intra‐protein interactions, which cause variations …

Staphylococcus aureus is a deadly human bacterial pathogen that causes a wide variety of
clinical manifestations. Invasive S. aureus infections in hospitals and the community are one …

Over the last decade fundamentally new features have been revealed for the participation of
glutathione and glutathione-dependent enzymes (glutathione transferase and glutaredoxin) …

Thioredoxin —a fold for all reasons: Structure Skip to Main Content Advertisement Structure
This journal offers authors two options (open access or subscription) to publish research …

Thioredoxins are ubiquitous antioxidant enzymes that play important roles in many health-
related cellular processes. As such, the fundamental knowledge of how these enzymes work …

Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the
reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH …

Significance: Over the past several years, oxidative post-translational modifications of
protein cysteines have been recognized for their critical roles in physiology and …

PROTEINS that contain disulphide bonds are often slow to fold in vitro because the
oxidation and correct pairing of the cysteine residues is rate limiting1, 2. The folding of such …