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Discover Supplement-Drug Interactions

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Last Updated: 3 years ago

Possible Interaction: Cysteine and Tyrosine

supplement:

Cysteine

supplement:

Tyrosine

Research Papers that Mention the Interaction

Other substances found to inhibit the iodination of tyrosine by the thyroid particulate fraction are DPNH, TPNH, cysteine , epinephrine, norepinephrine, serotonin, ergothioneine, thiohistidine and dichlorophenol.
Biochimica et biophysica acta  •  1962  |  View Paper
The substitution of tyrosine with cysteine would affect the structure of the pore region, resulting in the loss of channel function.
Molecular medicine reports  •  2021  |  View Paper
We also describe a case of heterozygosity for both the substitution of tyrosine with cysteine at position 282 and the substitution of histidine to aspartic acid at position 63 (so-called "compound heterozygosity").
Annali italiani di medicina interna : organo ufficiale della Societa italiana di medicina interna  •  2000  |  View Paper
The tyrosine phosphorylation was also inhibited by exogenous glutathione or cysteine and could be enhanced by depletion of cellular glutathione by BSO.
Journal of cellular physiology  •  2000  |  View Paper
Dopa and/or tyrosine protects tyrosinase against inactivation by cysteine.
Acta dermato-venereologica  •  1984  |  View Paper
Cysteine inhibited it more efficiently than histidine, methionine, tryptophan, tyrosine or alanine under the conditions used.
Biochemical pharmacology  •  1991  |  View Paper
Due to the synergetic effect between Cys and the Au NPs, the characteristic Raman scattering intensities of the Tyr (or Phe) enantiomer with the same chirality of Cys are enantioselectively boosted by over four-fold compared with those of the counter enantiomer of Tyr (or Phe).
Journal of materials chemistry. B  •  2021  |  View Paper
We conclude that redox coupling between tyrosine and cysteine can act as a PCET control mechanism in proteins.
Chemical communications  •  2019  |  View Paper
Crystallography shows that when un-crosslinked, the cysteine thiol excludes tyrosine 159 from its native position, while kinetic analysis shows that the thioether bond impairs reactivity of the crosslinked form.
Biochemistry  •  2016  |  View Paper
Results indicated that only amino acids of tryptophan, cysteine and histidine are photoactive and possess potential interferences in analysis of Tyr.
Analytica chimica acta  •  2015  |  View Paper
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