IndraLab

Statements

KCNQ1 binds IsK. 6 / 6
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"At the molecular level, I (Ks) channels are composed of KvLQT1 and IsK complexes."
11299204
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"In these systems, KvLQT1 and IsK complexes were totally insensitive to cAMP regulation."
11299204
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"In a variety of mammalian heterologous expression systems maintained at physiological temperature, we explored cAMP regulation of recombinant KvLQT1 and IsK complexes."
11299204
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"In contrast, coexpression of the neuronal A kinase anchoring protein (AKAP) 79, a fragment of a cardiac AKAP (mAKAP), or cardiac AKAP15/18 restored cAMP regulation of KvLQT1 and IsK complexes inasmuch as cAMP stimulation increased the I (Ks) amplitude, increased its deactivation time constant, and negatively shifted its activation curve."
11299204
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"KvLQT1, and IsK (minK) proteins associate to form the IKs cardiac potassium channel."
11152866
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"KvLQT1 and IsK (minK) proteins associate to form the Iks cardiac potassium current."
9561513