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Last Updated: 3 years ago

Possible Interaction: Adenosine Triphosphate and Polypeptides

Research Papers that Mention the Interaction

Here we show that the channel activity of the W1282X-CFTR polypeptide is exceptionally low in excised membrane patches at normally saturating doses of ATP and PKA (single channel open probability (PO) < 0.01).
PloS one  •  2016  |  View Paper
ATP binding allosterically accelerates polypeptide binding and release.
Structure  •  2015  |  View Paper
The chaperone functions of heat shock protein (Hsp)70 involve an allosteric control mechanism between the nucleotide-binding domain (NBD) and polypeptide substrate-binding domain (SBD): ATP binding and hydrolysis regulates the affinity for polypeptides , and polypeptide binding accelerates ATP hydrolysis.
Trends in biochemical sciences  •  2013  |  View Paper
In the course of signal transduction, complexes among these polypeptides form and dissociate, and undergo structural rearrangements that are coupled to their interactions with and catalysis of reactions by small molecules and ions, including guanine nucleotides, ATP , Ca(2+), Mg(2+), and lipids.
Vision Research  •  2008  |  View Paper
Complexes between the nascent polypeptide and at least hsp 73 appear to be sensitive to (disrupted by) ATP.
The Journal of biological chemistry  •  1994  |  View Paper
In the hsp70 reaction cycle, short segments of polypeptide bind rapidly and weakly to the ATP state, so triggering hydrolysis and consequent stabilization of the complex.
Current opinion in structural biology  •  1996  |  View Paper
Degradation of [35S]methionine-labeled polypeptides synthesized in isolated yeast mitochondria was activated by exogenously added ATP.
Journal of biochemistry  •  1994  |  View Paper
Second, radiolabeled ATP could be specially cross-linked to the p87 polypeptide.
Virology  •  1993  |  View Paper
257, 508-515] was similar to that of intact 21S dynein; the 135-kDa polypeptide was only slightly produced in the presence of ATP and Vi.
The digestion rate constant of the 135-kDa polypeptide from the beta chain in the presence of ATP and Vi was significantly decreased as compared with in the case of 21S dynein or that of the reconstituted 21S particle.
Journal of biochemistry  •  1990  |  View Paper
The binding of this polypeptide to microtubules was decreased in the presence of ATP.
The Journal of biological chemistry  •  1989  |  View Paper
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