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Last Updated: 2 months ago

Possible Interaction: Cysteine and Nitric Oxide

supplement:

Cysteine

Research Papers that Mention the Interaction

Significance S-nitrosylation, addition of an NO group to a cysteine thiol , can regulate protein activity.
Proceedings of the National Academy of Sciences  •  2016  |  View Paper
As NO can cause S-nitrosylation of active-site cysteines , we hypothesize that NO inhibits isopeptidase T activity through S-nitrosylation.
Journal of vascular surgery  •  2013  |  View Paper
The effect of L-cysteine on NO uptake was also concentration dependent.
Without preincubation with L-cysteine, NO uptake was significantly reduced.
Free radical biology & medicine  •  2010  |  View Paper
Under ambient air conditions, NO inhibits NMDAR activity by reacting with the NR2A subunit C399 along with two additional cysteine pairs if their disulfide bonds are reduced to free thiol groups [NR1(C744,C798); NR2(C87,C320)].
Neuron  •  2007  |  View Paper
One of the mechanisms by which NO exerts its effects is by posttranslational modification through S-nitrosylation of protein cysteines.
Circulation research  •  2007  |  View Paper
NO can react with cysteine thiol groups to form S-nitrosothiols and thus change protein function.
Cell Death and Differentiation  •  2007  |  View Paper
These results demonstrate for the first time that NO nitrosylates active site cysteines of complex IV, which is associated with persistent inhibition of complex IV.
American journal of physiology. Cell physiology  •  2005  |  View Paper
Incubation of these nitric oxide donor-nucleoside conjugates in the presence of 18 mM L-cysteine released a high percentage of *NO (21-48% at 1 h; 37-86% at 16 h).
Journal of medicinal chemistry  •  2004  |  View Paper
NO modifies proteins through nitrosylation of free cysteine residues , and such modifications are important in mediating NO's biologic activity.
Biochemistry  •  2001  |  View Paper
Indeed, due to its S-nitrosating activity in the presence of oxygen, NO can modify the activity of transcription factors containing zinc finger motifs or cysteines within the DNA-binding domain.
International immunopharmacology  •  2001  |  View Paper
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