Thiol-disulfide exchange reactions are highly reversible, displaying nucleophilic substitutions mechanism (S(N)2 type). For aliphatic, low molecular thiols, these reactions are slow, but can attain million times faster ...

BACKGROUND: Human sperm nuclear decondensation in vivo involves protamine disulfide bond reduction by glutathione (GSH) and protamine/histone exchange, presumably with heparan sulfate (HS) as the protamine acceptor. The ...

Thimet oligopeptidase (EC 3.4.24.15; EP24.15) is a thiol-rich metallopeptidase ubiquitously distributed in mammalian tissues and involved in oligopeptide metabolism both within and outside cells. Fifteen Cys residues are ...

Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly due to the presence of low-molecular-weight thiols and cysteine residues in proteins involved in catalysis and regulation. ...

A straightforward, novel strategy based on the in situ functionalization of polymers prepared by nitroxide-mediated polymerization (NMP), for the use as an extension toward block copolymers and post-polymerization ...

Reversibility of dithioacetal bond formation is reported under acidic mild conditions. Its utility for dynamic combinatorial chemistry was explored by combining it with orthogonal disulfide exchange. In such a setup, thiols ...

La infectividad de rotavirus es reducida por moléculas que alteran el intercambio tiol-disulfuro y por anticuerpos contra PDI. El objetivo fue evaluar la interacción y asociación funcional entre PDI y TLPs de Rotavirus ...

Organic hydroperoxides are oxidants generated during bacterial-host interactions. Here, we demonstrate that the peroxidase OhrA and its negative regulator OhrR comprise a major pathway for sensing and detoxifying organic ...

The stroma of higher plant chloroplasts contains two thioredoxins (Trx) with different specificity for the reduction of protein disulfide bonds. Based upon electrostatic features of domains that participate in the ...