IndraLab

Statements


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"To support the notion that KCNQ1 and BACE1 physically interact, we performed co-immunoprecipitation and fluorescence recovery after photobleaching (FRAP) experiments in HEK293T cells."

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"The most direct explanation would be that the BACE1 molecule can physically associate with KCNQ1 channels in a β-subunit-like fashion as we have shown previously for KCNQ2/Q3 heteromers [26] ."

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"Additionally, BACE1 directly interacts with potassium voltage-gated channel subfamily Q member 1 channels, thereby modulating electrical activity in both healthy and diseased organs [ 77 ]."

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"The most parsimonious explanation for the electrophysiological changes introduced by BACE1 that is also supported by our co-immunoprecipitation experiments is to assume that BACE1 interacts with KCNQ1[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"If we elaborate on the above idea that BACE1 can physically interact with KCNQ1, we have to ask what will happen if KCNQ1 has now two binding partners, namely KCNE1 and BACE1, with one of them at leas[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"