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Last Updated: 3 years ago

Possible Interaction: Adenosine Triphosphate and Alanine

Research Papers that Mention the Interaction

Mutation of the TRPM6 autophosphorylation site, Thr1851, into either an alanine or an aspartate, resulted in functional channels that could still be inhibited by ATP.
Journal of Biological Chemistry  •  2008  |  View Paper
During L-alanine infusion, ATP levels decreased in all groups (p<0.05); in CaWL, ATP levels were lower at all time-points between 0-90 min as compared to both CaWS and C (p<0.05).
Journal of hepatology  •  2000  |  View Paper
Recently, we identified six phosphorylation sites within the kinase homology domain of NPR-A and determined that the conversion of these residues to alanine abolished the ability of the receptor to be phosphorylated or to be activated by ANP and ATP.
Molecular biology of the cell  •  1999  |  View Paper
Disturbance to energy production in the S180 sarcoma (CB) by optical isomers of isoproterenol was assessed from altered adenine nucleotide levels at 1 h. The L-isomer almost halved the ATP level and lowered the energy charge significantly; the D-isomer was inactive.
Experientia  •  2005  |  View Paper
The rate of Na+-activated phosphorylation from ATP was reduced in Ile279 → Ala and Ile283 → Ala , and these mutants showed evidence similar to Glu329 → Gln of destabilization of the Na+-occluded state.
Journal of Biological Chemistry  •  2003  |  View Paper
RESULTS DeltaIsc and ATP levels were decreased after I/R. Intraluminal al nine al one or alanine/glucose mixture further reduced DeltaIsc and ATP co ntent.
Zhonghua yi xue za zhi  •  2002  |  View Paper
Mutation of Arg560 to Ala produces strong inhibition of ATPase activity and enzyme phosphorylation by ATP but has a much lower effect on enzyme phosphorylation by Pi.
Biochemistry  •  2002  |  View Paper
Mutation of R491 to Ala decreased k(cat) for ATP hydrolysis by 70-fold; however, dipeptide product was only formed in 5% of these turnovers.
Mutation of each of these residues to Ala increased the apparent K(m) for ATP by 20-100-fold while having only modest effects on k(cat) or the apparent K(m)'s for the other substrates.
Biochemistry  •  2002  |  View Paper
A mutation in the activation loop designed to relieve autoinhibition, Asp-1161 → Ala , substantially increases the ability of the unphosphorylated kinase to bind ATP.
The Journal of Biological Chemistry  •  2001  |  View Paper
We also demonstrate that swelling after exposure to a hypotonic solution or an isotonic solution containing alanine or glucose reduces inhibition of channel activity by ATP and that this finding cannot be simply attributed to dilution of intravesicular ATP.
American journal of physiology. Cell physiology  •  2000  |  View Paper
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