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The use of Xenopus oocytes for the study of ion channels.
- N. Dascal
- Biology, MedicineCRC critical reviews in biochemistry
Oocytes of the African frog Xenopus laevis have been exploited for the study of numerous aspects of ion channel function and regulation, such as the properties of several endogenous voltage-dependent channels and the involvement of second messengers in mediation of neurotransmitter-evoked membrane responses.
cAMP-Dependent Regulation of Cardiac L-Type Ca2+ Channels Requires Membrane Targeting of PKA and Phosphorylation of Channel Subunits
The PKA-mediated regulation of L-type Ca2+ channels is critically dependent on a functional AKAP and phosphorylation of the alpha1C subunit at Ser1928, demonstrating that the events observed in the heterologous expression system reflect those occurring in the native system.
Signalling via the G protein-activated K+ channels.
- N. Dascal
- Chemistry, MedicineCellular signalling
- 1 December 1997
A review of the recent advances and the unresolved questions now on the agenda in GIRK studies concludes that these channels are important physiological tools to regulate excitability in heart and brain by neurotransmitters.
Atrial G protein-activated K+ channel: expression cloning and molecular properties.
- N. Dascal, W. Schreibmayer, +7 authors D. Trollinger
- Biology, MedicineProceedings of the National Academy of Sciences…
- 1 November 1993
The hypothesis that similar channels play a role in neuronal inhibition is supported by the cloning of a nearly identical channel (KGB1) from a rat brain cDNA library.
Movement of ‘gating charge’ is coupled to ligand binding in a G-protein-coupled receptor
- Y. Ben-Chaim, B. Chanda, N. Dascal, F. Bezanilla, I. Parnas, H. Parnas
- Chemistry, MedicineNature
- 2 November 2006
The data strongly indicate that GPCRs serve as sensors for both transmembrane potential and external chemical signals, and the gating charge–voltage relationship of m2R correlates well with the voltage dependence of the affinity of the receptor for acetylcholine.
The M2 Muscarinic G-protein-coupled Receptor Is Voltage-sensitive*
- Y. Ben-Chaim, O. Tour, N. Dascal, I. Parnas, H. Parnas
- Medicine, ChemistryJournal of Biological Chemistry
- 20 June 2003
The cumulative results suggest that m2R is, by itself, voltage-sensitive, and the voltage sensitivity does not reside in the ACh binding site, rather, it most likely resides in the receptor region that couples to the G-protein.
Calcium channel beta subunit heterogeneity: functional expression of cloned cDNA from heart, aorta and brain.
It is suggested that different types of calcium currents may depend on channel subunit composition, and that CaB2 is predominantly expressed in heart, aorta and brain, whereas CaB3 is most abundant in brain but also present in aortA, trachea, lung, heart and skeletal muscle.
Voltage clamping of Xenopus laevis oocytes utilizing agarose-cushion electrodes
Two-electrode voltage clamping of expressed ion channels in intact oocytes of the South African clawed frog Xenopus laevis has been refined to allow stable, low-resistance electrical access to the…
Gαi1 and Gαi3 Differentially Interact with, and Regulate, the G Protein-activated K+ Channel*
- T. Ivanina, Dalia Varon, +5 authors N. Dascal
- Biology, MedicineJournal of Biological Chemistry
- 12 February 2004
Differences in physical interactions of GIRK with GDP-bound Gα subunits, or Gαβγ heterotrimers, may dictate different extents of G αβγ anchoring, influence the efficiency of G IRK activation by Gβγ, and play a role in determining signaling specificity.
The roles of the subunits in the function of the calcium channel.
- D. Singer, M. Biel, I. Lotan, V. Flockerzi, F. Hofmann, N. Dascal
- Chemistry, MedicineScience
- 27 September 1991
Dihydropyridine-sensitive voltage-dependent L-type calcium channels are critical toexcitation-secretion and excitation-contraction coupling, and specific modulatory functions can be assigned to individual subunits, whereas in other cases the different subunits appear to act in concert to modulate the properties of the channel.