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Last Updated: 6 months ago

Possible Interaction: Nitric Oxide and Tyrosine

supplement:

Tyrosine

Research Papers that Mention the Interaction

Taken together, these observations suggest that NO modulates tyrosine phosphorylation in HER14 cells.
The Biochemical journal  •  1995  |  View Paper
NO promotes Akt-dependent phosphorylation of Cav-1 at tyrosine 14 , disrupting the Cav-1:Oct4 complex.
The Journal of Biological Chemistry  •  2018  |  View Paper
PA attenuated insulin-mediated insulin receptor substrate-1 (IRS-1) tyrosine phosphorylation, leading to decreased glucose uptake, and phosphorylation of eNOS, leading to a reduction in the production of NO.
Molecular medicine reports  •  2015  |  View Paper
We demonstrate further that NO may exert its inhibitory effects by influencing matrix metalloproteinase expression/activity and tyrosine phosphorylation of proteins in the sprouting tips of nascent capillaries.
American journal of physiology. Lung cellular and molecular physiology  •  2001  |  View Paper
Moreover, nitric oxide modulated tyrosine phosphorylation of sperm proteins.
Biology of reproduction  •  1999  |  View Paper
Peroxynitrite, but not nitric oxide , reacts with the phenolic ring of tyrosine to form the stable product 3-nitro-L-tyrosine.
Critical care medicine  •  1997  |  View Paper
We found that the NO coordination state, NO dissociation, and enzyme activation were significantly affected by the presence of a tyrosine in the distal heme pocket; however, the stability of the reduced porphyrin and the proteins affinity for oxygen were unaltered.
The Journal of Biological Chemistry  •  2010  |  View Paper
Increased nitric oxide (NO) results in increased nitration of proteins at tyrosine , which can cause protein dysfunction or alterations in signal transduction pathways.
Molecular and Cellular Biochemistry  •  2005  |  View Paper
Analysis of T cell lysates by immunoprecipitation with specific Abs and subsequent immunoblotting indicated marked reduction of tyrosine phosphorylation of Jak3 and STAT5 mediated by NO.
Journal of immunology  •  1998  |  View Paper
We hypothesized that NO or derivative reactive nitrogen species may generate adducts of tyrosine and/or cysteine residues, causing CYP2B6 down-regulation, and selected Tyr and Cys residues for mutation based on predicted solvent accessibility.
Molecular pharmacology  •  2020  |  View Paper
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