S-nitrosylation of critical cysteine thiols activates a subset of cation-permeable, transient receptor potential channel proteins (TRPs), which may represent a general mechanism for regulating ...

NMT5 could modify ACE2 at both of the cysteine residues (Cys261 and Cys498), which were susceptible to S-nitrosylation by S-nitrosocysteine (SNOC). ACE2 was successfully S-nitrosylated by SNOC.

Previous researches have reported that NO can mediate the S-nitrosylation modifications of cysteine residue, consequently affecting the activity and functions of protein. Researchers have verified ...

One of the key mechanisms by which NO exerts its effects is through protein S-nitrosylation. S-Nitrosylation involves the transfer of a nitroso group to cysteine residues, resulting in the formation ...

These two are likely available for S-nitrosylation via a reversible nucleophilic ... also performed site-directed mutagenesis of these cysteine residues in ACE2 to validate the results of biotin ...

A chemical process in the brain called S-nitrosylation - which can be activated by inflammations as well as a variety of airborne toxins - blocks brain cells from making new connections ...

Using in vitro reactions, Uehara and colleagues first found that PDI could be inactivated by NO donors such as S-nitrosocysteine (SNOC). The isomerase becomes S-nitrosylated at any of four cysteine ...

Molecular mechanism of vancomycin resistance mediated by NOS via S-nitrosylation modification. Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to ...