Voltage is a partial activator of rat thermosensitive TRP channels.
about
Transient receptor potential (TRP) channels as drug targets for diseases of the digestive systemSpecies-specific temperature sensitivity of TRPA1Modulation of thermoreceptor TRPM8 by cooling compoundsTRPV1 structures in distinct conformations reveal activation mechanismsOptical control of TRPV1 channelsInorganic polyphosphate modulates TRPM8 channelsEndocannabinoid dynamics gate spike-timing dependent depression and potentiationHypersensitivity Induced by Activation of Spinal Cord PAR2 Receptors Is Partially Mediated by TRPV1 ReceptorsGeneral anesthetics activate a nociceptive ion channel to enhance pain and inflammationExploring functional roles of TRPV1 intracellular domains with unstructured peptide-insertion screeningEngineering vanilloid-sensitivity into the rat TRPV2 channelActivity-dependent targeting of TRPV1 with a pore-permeating capsaicin analogA linkage analysis toolkit for studying allosteric networks in ion channels.Interaction with phosphoinositides confers adaptation onto the TRPV1 pain receptor.Sex differences in mouse Transient Receptor Potential Cation Channel, Subfamily M, Member 8 expressing trigeminal ganglion neurons.Thermosensitive TRP channel pore turret is part of the temperature activation pathway.High temperature sensitivity is intrinsic to voltage-gated potassium channels.Hill coefficients of a polymodal Monod-Wyman-Changeux model for ion channel gating.Structure-functional intimacies of transient receptor potential channels.A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domainKinetic and energetic analysis of thermally activated TRPV1 channelsTRPA1 is a polyunsaturated fatty acid sensor in mammalsVoltage- and cold-dependent gating of single TRPM8 ion channels.Voltage- and temperature-dependent activation of TRPV3 channels is potentiated by receptor-mediated PI(4,5)P2 hydrolysis.Temperature and voltage coupling to channel opening in transient receptor potential melastatin 8 (TRPM8).Scraping through the ice: uncovering the role of TRPM8 in cold transductionModular thermal sensors in temperature-gated transient receptor potential (TRP) channelsTrafficking of Na+/Ca2+ exchanger to the site of persistent inflammation in nociceptive afferentsSelective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations.Intracellular proton-mediated activation of TRPV3 channels accounts for the exfoliation effect of α-hydroxyl acids on keratinocytes.An external sodium ion binding site controls allosteric gating in TRPV1 channelsA yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gatingPermeation and block of TRPV1 channels by the cationic lidocaine derivative QX-314Use Dependence of Heat Sensitivity of Vanilloid Receptor TRPV2.The role of allosteric coupling on thermal activation of thermo-TRP channels.Lack of potentiating effect of increasing temperature on responses to chemical activators in vagal sensory neurons isolated from TRPV1-null mice.Understanding the role of voltage gating of polymodal TRP channels.The pharmacological challenge to tame the transient receptor potential vanilloid-1 (TRPV1) nocisensorTwo amino acid residues determine 2-APB sensitivity of the ion channels TRPV3 and TRPV4Mechanisms of eosinophil major basic protein-induced hyperexcitability of vagal pulmonary chemosensitive neurons
P2860
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P2860
Voltage is a partial activator of rat thermosensitive TRP channels.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Voltage is a partial activator of rat thermosensitive TRP channels.
@en
type
label
Voltage is a partial activator of rat thermosensitive TRP channels.
@en
prefLabel
Voltage is a partial activator of rat thermosensitive TRP channels.
@en
P2860
P1476
Voltage is a partial activator of rat thermosensitive TRP channels.
@en
P2093
Gerard P Ahern
José A Matta
P2860
P304
P356
10.1113/JPHYSIOL.2007.144287
P407
P577
2007-10-11T00:00:00Z