Sentence examples for atp in binding to from inspiring English sources

Exact(1)

TKIs compete with ATP in binding to the ATP-binding pocket (catalytic domain of the kinase), which in turn inhibits EGFR transphosphorylation and downstream signaling.

Similar(59)

In contrast, ATP binding to the AMP-lid induces global domain closing, preventing further substrate binding to the ATP-lid site.

In fact, ATP binding to the ATPases by itself supports the rapid degradation of unfolded proteins.

In this view ATP binding to P2 purinergic receptors results in phospholipase C-mediated IP3 production, followed by calcium release from the ER.

Therefore, in E. coli ATP binding to MutL may stimulate the early steps in methyl-directed MMR repair and its hydrolysis is a transition to later steps.

Extracellular ATP binding to P2YR results in EGF family ligand release to bind EGFR and activate ERK response as monitored by ERK activity following ATP addition.

To this aim, we evaluated the F-actin binding/bundling activity under conditions of ATP binding to synapsin I in the presence of increasing concentrations of staurosporine ranging from to 1 to 20 µM.

Because the ATP-inhibited binding to F-actin in vitro could be mimicked by compromising myosin Va, a selective inactivation of ISG-associated myosin Va during maturation is conceivable (Kogel et al. 2010).

In combination with biochemical and mutational data, our structures recapture a mechanistic model of AMPK regulation by AMP and ATP, in which AMP binding to CBS-3 induces the interaction of AID-αRIM and γ-subunit and leads to AMPK activation by releasing AID inhibition of the kinase domain.

We also controlled the purity of the preparation by adding an excess of ATP to extracts, which prevented virtually all of the proteins otherwise recovered in the ATP-fraction from binding to microtubules (Figure S1).

This step prevented virtually all of the proteins otherwise recovered in the ATP-fraction from binding to microtubules (Figure S1), proving the veracity of the interaction.

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