Evidence for Two Concentration-Dependent Processes for β-Subunit Effects on α1B Calcium Channels
By C. Cantí, A. Davies, N. Berrow, Adrian J. Butcher, K. Page, A. Dolphin. 2001
111 citations recorded by the source corpus.
Subfields: Cardiology and Cardiovascular Medicine, Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/33697f938f28d8a2e7113fcb4df43d39644f3bf1
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In Molecular Biology
Citations in the corpus
- Structural basis of the α1–β subunit interaction of voltage-gated Ca2+ channels (2004, background): “The AID binds to a hydrophobic groove in the GK domain through extensive interactions, conferring extremely high affinity between α 1 and β-subunit”
- Ca2+ channel β-subunits: structural insights AID our understanding (2004, unknown): “In both these studies [13, 14 ] ,a n antisense oligonucleotide directed against b 3m RNA reduced the current amplitude resulting from a heterologously expressed CaVa1 subunit, and in one study [14] this antisense approach was also shown to reduce the amount of endogenous b3. Both studies indicate th”