IndraLab

Statements


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"Moreover, BVES interacted with the 2-pore domain potassium channel TREK-1, and this was sensitive to cAMP stimulation."

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"This is supported by the finding that the interaction between POPDC1 and TREK1 undergoes an acute change upon an increase of cAMP concentration, as reported by a bimolecular FRET assay."

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"Based on the interaction of POPDC1 and TREK-1, a bi-molecular Forster-resonance energy transfer (FRET) sensor was constructed."

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"XREF_BIBR Recently, an investigation of ion channels and electrogenic proteins in Xenopus oocytes demonstrated that TREK-1 functionally interacts with BVES and POPDC1."

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"Disruption of the POPDC1-phosphodiesterase 4 complex—which prevents premature cAMP binding of POPDC1 under basal conditions—has been shown to prolong AP duration in rabbit isolated ventricular myocytes (possibly due to decreased interaction between POPDC1 and TREK1 and probably other ion channels [7])."

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"Indeed, our FRET analysis of Popdc1 and TREK-1 interaction support the concept of a rapid ligand mediated modulation of protein protein interactions [XREF_BIBR]."

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"This concept finds support from our analysis of the interaction of TREK-1 and Popdc1 in Xenopus oocytes."