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Discover Supplement-Drug Interactions
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Last Updated: 3 years ago
Research Papers that Mention the Interaction
“Analysis of the activity of ADC in the presence of different amino determined that beta-alanine production from aspartate was diminished in the presence of cysteine.”
Mechanism of cysteine-dependent inactivation of aspartate/glutamate/cysteine sulfinic acid α-decarboxylases“The following observations indicate that cysteine may stimulate protein syntheis by increasing intracellular levels of aspartate : 1.”
Effect of nonprotein thiols on protein synthesis in isolated rat hepatocytes“This effect is suppressed by substituting the aspartates with cysteine , suggesting that protonation of these aspartates may contribute to the signaling pathway whereby external [H+] influences conformational changes in the channel's cytoplasmic domains (where deactivation takes place).”
“We infer the functional role of these aspartates by studying how substituting them with cysteine , one at a time, affects the channel function.”
“ Cysteine uptake was suppressed by extracellular glutamate and aspartate , substrates of EAATs, and not by substrates of cysteine transporters.”
“ Cysteine uptake was reduced by the EAAT substrates l‐glutamate and l‐aspartate and by synthetic EAAT inhibitors.”
“High K+ media (50 mM) containing cysteine (1 mM) evoked the net efflux of glutamate and aspartate by 1454% and 1019%, respectively.”
“Addition of glycine, arginine and cysteine to aspartate raised the hypocholesterolemic effect.”
“Competitive inhibition by various amino acids of l-aspartate or l-alanine in self-exchange reactions revealed that l-cysteine selectively inhibited l-aspartate self-exchange but only weakly inhibited l-alanine self-exchange.”
“The aspartate analogs l-cysteine sulfinic acid , l-cysteic acid, and d-cysteic acid competitively and strongly inhibited l-aspartate self-exchange compared with l-alanine self-exchange.”
Substrate Specificity of the Aspartate:Alanine Antiporter (AspT) of Tetragenococcus halophilus in Reconstituted Liposomes*“Prior work showed that L-cysteine sulfinic acid competitively inhibits this enzyme by interfering with L-aspartate binding.”
“In particular, 13 of the 26 modifications (6 cysteine pairs and 7 disulfides) significantly increase or decrease aspartate affinity, while 15 of the 26 modifications (5 cysteine pairs and 10 disulfides) destroy transmembrane kinase regulation.”
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