| The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods. | The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods.
Barret DCA, Schertler GFX, Kaupp UB, Marino J. | 02/26/2022 |
| These results suggest that restraining the A' helix to the plasma membrane potentiates CNGA1 channel opening. | Regulation of CNGA1 Channel Gating by Interactions with the Membrane.
Aman TK, Gordon SE, Zagotta WN., Free PMC Article | 11/12/2016 |
| Conformation changes of CNGA1 associated with its gating function are reported. | Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy.
Maity S, Mazzolini M, Arcangeletti M, Valbuena A, Fabris P, Lazzarino M, Torre V., Free PMC Article | 05/7/2016 |
| Data show that when Pro365 is replaced with a threonine in cyclic nucleotide gated channel alpha 1 (CNGA1), cesium Cs+ permeation is nearly abolished. | A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels.
Napolitano LM, Bisha I, De March M, Marchesi A, Arcangeletti M, Demitri N, Mazzolini M, Rodriguez A, Magistrato A, Onesti S, Laio A, Torre V., Free PMC Article | 10/31/2015 |
| Stabilizing the C-helix of intact CNGA1 channels by metal binding to a pair of histidines promoted channel opening. | A secondary structural transition in the C-helix promotes gating of cyclic nucleotide-regulated ion channels.
Puljung MC, Zagotta WN., Free PMC Article | 07/13/2013 |
| A ring of threonines in the inner vestibule of the pore of CNGA1 channels constitutes a binding site for permeating ions | A ring of threonines in the inner vestibule of the pore of CNGA1 channels constitutes a binding site for permeating ions.
Marchesi A, Mazzolini M, Torre V., Free PMC Article | 06/22/2013 |
| Three CNGA1 subunits and a single CNGB1 subunit form the rod cyclic nucleotide-gated ion channels. | Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels.
Shuart NG, Haitin Y, Camp SS, Black KD, Zagotta WN., Free PMC Article | 11/19/2011 |
| Existence of a strong coupling between the upper portion of the S6 helix provides a simple molecular mechanism for CNGA1 gating. | The analysis of desensitizing CNGA1 channels reveals molecular interactions essential for normal gating.
Mazzolini M, Anselmi C, Torre V., Free PMC Article | 02/15/2010 |
| detailed analysis of conformational changes of the S6 domain and C-linker during gating of CNGA1 channels | Conformational rearrangements in the S6 domain and C-linker during gating in CNGA1 channels.
Nair AV, Nguyen CH, Mazzolini M. | 01/21/2010 |
| analyze in detail the molecular mechanisms underlying Cd2+ inhibition and longer cross-linkers in mutant CNGA1 channels | Movements of native C505 during channel gating in CNGA1 channels.
Nair AV, Anselmi C, Mazzolini M. | 01/21/2010 |
| Data suggest that the native rod cyclic nucleotide-gated (CNG) channel is a tetramer composed of three A1 and one B1 subunit. | Subunit stoichiometry of the CNG channel of rod photoreceptors.
Weitz D, Ficek N, Kremmer E, Bauer PJ, Kaupp UB. | 01/21/2010 |
| In CNGA1 channels, pore gating is involved in the rate-limiting reactions determining the activation time course in the sequence of events between cGMP binding and pore opening. | Gating of cyclic nucleotide-gated (CNGA1) channels by cGMP jumps and depolarizing voltage steps.
Nache V, Kusch J, Hagen V, Benndorf K., Free PMC Article | 01/21/2010 |
| These observations suggest that these effects are mediated by the formation of a disulfide bond (S-S) between F380C and the endogenous Cys-314 in the S5 segment. | Locking CNGA1 channels in the open and closed state.
Nair AV, Mazzolini M, Codega P, Giorgetti A, Torre V., Free PMC Article | 01/21/2010 |
| Structural models of the tetrameric cyclic nucleotide gated channel alpha 1 from bovine rod is presented. | Structural basis of gating of CNG channels.
Giorgetti A, Nair AV, Codega P, Torre V, Carloni P. | 01/21/2010 |
| The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry | The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry.
Zhong H, Molday LL, Molday RS, Yau KW., Free PMC Article | 01/21/2010 |
| Data show that the cyclic nucleotide-gated (CNG) channel contains three CNGA1 subunits and only one CNGB1 subunit. | Rod cyclic nucleotide-gated channels have a stoichiometry of three CNGA1 subunits and one CNGB1 subunit.
Zheng J, Trudeau MC, Zagotta WN. | 01/21/2010 |