about
Roscovitine binds to novel L-channel (CaV1.2) sites that separately affect activation and inactivationIdentification of CaV channel types expressed in muscle afferent neurons.Phospholemman modulates the gating of cardiac L-type calcium channels.Identification of specific sensory neuron populations for study of expressed ion channelsFunctional expression of α7-nicotinic acetylcholine receptors by muscle afferent neuronsVoltage control of Ca²⁺ permeation through N-type calcium (Ca(V)2.2) channels.Slowed N-type calcium channel (CaV2.2) deactivation by the cyclin-dependent kinase inhibitor roscovitine.Calcium channel blockers in the treatment of disease.Neurotransmitter modulation of neuronal calcium channels.Roscovitine inhibits CaV3.1 (T-type) channels by preferentially affecting closed-state inactivation.Limited efficacy of α-conopeptides, Vc1.1 and RgIA, to inhibit sensory neuron CaV currentDomain III regulates N-type (CaV2.2) calcium channel closing kineticsCloning, synthesis, and characterization of αO-conotoxin GeXIVA, a potent α9α10 nicotinic acetylcholine receptor antagonist.NaV1.8 channels are expressed in large, as well as small, diameter sensory afferent neurons.A single amino acid change in Ca(v)1.2 channels eliminates the permeation and gating differences between Ca(2+) and Ba(2+).EXPRESS: Voltage-dependent sodium (NaV) channels in group IV sensory afferents.Inhibition of α9α10 nicotinic acetylcholine receptors prevents chemotherapy-induced neuropathic pain.Open-state occupancy prevents gating charge relaxation of N-type (CaV2.2) calcium channels.The Timothy syndrome mutation of cardiac CaV1.2 (L-type) channels: multiple altered gating mechanisms and pharmacological restoration of inactivation.omega-conotoxin GVIA alters gating charge movement of N-type (CaV2.2) calcium channels.Roscovitine differentially affects CaV2 and Kv channels by binding to the open state.Site-specific effects of diselenide bridges on the oxidative folding of a cystine knot peptide, omega-selenoconotoxin GVIA.Single channel measurements demonstrate the voltage dependence of permeation through N-type and L-type CaV channels.Transmitter modulation of neuronal calcium channels.The separation of antagonist from agonist effects of trisubstituted purines on CaV2.2 (N-type) channels.The intravenous anesthetic propofol inhibits human L-type calcium channels by enhancing voltage-dependent inactivation.Iontophoresis of norepinephrine onto neurons of the pigeon's lateral geniculate nucleus: characterization of an inhibitory response.Reluctant gating of single N-type calcium channels during neurotransmitter-induced inhibition in bullfrog sympathetic neurons.Concentration dependence of neurotransmitter effects on calcium current kinetics in frog sympathetic neurones.α-Neurexins Together with α2δ-1 Auxiliary Subunits Regulate Ca2+ Influx through Cav2.1 Channels.Calcium current modulation in frog sympathetic neurones: multiple neurotransmitters and G proteinsLHRH and GTP-gamma-S modify calcium current activation in bullfrog sympathetic neuronsIntracellular ATP and GTP are both required to preserve modulation of N-type calcium channel current by norepinephrineEffects of temperature on calcium current of bullfrog sympathetic neuronsReevaluation of Ca2+ channel types and their modulation in bullfrog sympathetic neuronsIdentification of the single channels that underlie the N-type and L-type calcium currents in bullfrog sympathetic neuronsEffect of high Ba(2+) on norepinephrine-induced inhibition of N-type calcium current in bullfrog sympathetic neuronsRapid and reversible block of N-type calcium channels (CaV 2.2) by omega-conotoxin GVIA in the absence of divalent cationsCa2+ enhances U-type inactivation of N-type (CaV2.2) calcium current in rat sympathetic neuronsInterference between two modulators of N-type (CaV2.2) calcium channel gating demonstrates that omega-conotoxin GVIA disrupts open state gating
P50
Q33581333-A18DED1C-AA56-4CCB-AF1C-48134A77F6CBQ33702443-C312428D-17F9-40A3-9E29-C61DBFDE4FE9Q33767704-93ED6311-77CC-4E89-AC17-07EA052473C7Q33943292-36A6213A-C793-4C58-922D-ADFBD019C5B1Q34063192-806B0FB8-9BD1-4758-BB50-DC4819A871FAQ34088855-3D1F1784-EEC8-4364-89AB-68CD54D5663BQ34351071-E3D6BD41-9C61-4626-8EB4-D8C66575801BQ35679969-8DF8DB74-CFB2-407C-B365-952102554707Q35682291-9F56A62A-AECD-4539-9DD8-BE744C6C68E0Q35688524-5DF9EBC9-DB08-4613-99AF-5E36492EDDADQ35735112-0CB60AC5-1934-481F-84F0-F035E04D4A9EQ35902607-79810EFC-562D-4D11-A3FE-18BB96C0A96BQ35910100-AD6D01EE-C58B-4F94-A573-827B8EDD0E0AQ36659677-51E8770A-14F2-44B3-A7DC-CD39351BB884Q36991694-91D5F722-17FF-4228-AE45-A067BE85249FQ37115257-A5A42B94-EBF2-497B-B9C5-FF686DB4F890Q37695948-8B3F3A86-6DF4-46E1-BB6B-5499CD1A8C84Q39780330-8BF05654-B635-4B90-AC0C-665CFC537D4AQ39905970-1127EFD8-457D-46ED-A8A5-A5E2ECB0BE2AQ39923695-E8C3FAF5-9F78-47E0-8DDC-BEC3A4452F2AQ40204622-F80F59D0-9A17-40C0-951D-157612EE2C7EQ40462382-EB18ED31-0780-482B-A9E9-D8DACEBE36F9Q41288694-C9F999E7-BA3F-4A03-BAE8-9FE7880CF61CQ41323193-84FF0468-BD8B-4F1A-BF4C-194A2BF83BE7Q46790405-CECC3397-9BBD-4ED1-BCE0-D60F5346C6B9Q48351056-3AD18983-BAC6-4DB0-B551-4EE15E68BFD2Q48968104-EA7545DA-0E95-403C-906A-FD2AA37B57D5Q53913583-77BFA03B-EF88-4E9B-9B0A-35F3F4F23C1AQ54020967-62E24742-C2C6-467C-A999-ABC8138AE234Q64915258-CF023A9B-AD44-4980-B61B-4ECB5B3A95D1Q67521784-FD23F446-246A-4D6F-89FA-3541D3D4159FQ68467691-A5E17CAA-F5CC-4C6C-BBE1-40762364A685Q70469959-7E77F85D-333C-481B-A344-1FE43CB99330Q70507067-B4346EBE-9D1F-413E-83F4-5AA24818D1F2Q72088998-0825C503-8EBD-41F7-8E6E-2D8EB2DAAAC2Q73201888-4E7331A0-0B3B-4676-9681-56C6846E2425Q73434902-EE34DD1D-22F0-43C3-AFB5-F0E5C75153D2Q78397283-EF97E379-AE44-4E87-B430-BE020EF3448BQ83946698-859A430A-74FF-4ADE-BBFF-1DD572D119C6Q84227844-C5D0D355-9FB9-45D3-9CF0-20AB7AE1AFBF
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Keith S Elmslie
@ast
Keith S Elmslie
@en
Keith S Elmslie
@es
Keith S Elmslie
@nl
type
label
Keith S Elmslie
@ast
Keith S Elmslie
@en
Keith S Elmslie
@es
Keith S Elmslie
@nl
prefLabel
Keith S Elmslie
@ast
Keith S Elmslie
@en
Keith S Elmslie
@es
Keith S Elmslie
@nl
P106
P31
P496
0000-0002-2988-4482