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.

And they showed that so-called S-nitrosylation of amino acid cysteine 181 results in a 25 percent decrease in PDE5A activity, pinpointing how the enzyme's action is suppressed. "Knowing the ...

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 ...

S-Nitrosylation involves the transfer of a nitroso group to cysteine residues, resulting in the formation of S-nitrosothiols (SNO). This reversible post-translational modification dynamically ...

Next, the research team genetically engineered a version of CRTC1 that could no longer undergo S-nitrosylation, as the protein now lacked the sulfur-containing amino acid (called cysteine ...

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 ...

The isomerase becomes S-nitrosylated at any of four cysteine thiols present in two active site domains that lie at the N- and C-terminals of the protein. To find out if this modification has any ...

Next, the research team genetically engineered a version of CRTC1 that could no longer undergo S-nitrosylation, as the protein now lacked the sulfur-containing amino acid (called cysteine ...