A conformation change in the extracellular domain that accompanies desensitization of acid-sensing ion channel (ASIC) 3.
about
Proton-binding sites of acid-sensing ion channel 1Structure and activity of the acid-sensing ion channelsPore architecture and ion sites in acid-sensing ion channels and P2X receptorsStructural plasticity and dynamic selectivity of acid-sensing ion channel–spider toxin complexesX-Ray Structure of Acid-Sensing Ion Channel 1–Snake Toxin Complex Reveals Open State of a Na+-Selective ChannelA combined computational and functional approach identifies new residues involved in pH-dependent gating of ASIC1a.Extracellular chloride modulates the desensitization kinetics of acid-sensing ion channel 1a (ASIC1a)Small molecule ion channel match making: a natural fit for new ASIC ligands.Insights into the mechanism of pore opening of acid-sensing ion channel 1a.Conformational changes in the lower palm domain of ASIC1a contribute to desensitization and RFamide modulation.Atomic level characterization of the nonproton ligand-sensing domain of ASIC3 channels.Nonproton ligand sensing domain is required for paradoxical stimulation of acid-sensing ion channel 3 (ASIC3) channels by amiloride.Subtype-specific modulation of acid-sensing ion channel (ASIC) function by 2-guanidine-4-methylquinazoline.Gating transitions in the palm domain of ASIC1a.Structural mechanisms underlying the function of epithelial sodium channel/acid-sensing ion channel.The Thumb Domain Mediates Acid-sensing Ion Channel Desensitization.Two residues in the extracellular domain convert a nonfunctional ASIC1 into a proton-activated channelProtonation controls ASIC1a activity via coordinated movements in multiple domains.Conformational changes associated with proton-dependent gating of ASIC1a.Structure, function, and pharmacology of acid-sensing ion channels (ASICs): focus on ASIC1a.Insight into DEG/ENaC channel gating from genetics and structure.Capturing Functional Motions of Membrane Channels and Transporters with Molecular Dynamics Simulation.Asp433 in the closing gate of ASIC1 determines stability of the open state without changing properties of the selectivity filter or Ca2+ block.The interaction between two extracellular linker regions controls sustained opening of acid-sensing ion channel 1.Toxin binding reveals two open state structures for one acid-sensing ion channelCandidate amino acids involved in H+ gating of acid-sensing ion channel 1a.Potent and long-lasting inhibition of human P2X2 receptors by copper.Intersubunit interactions between mutant DEG/ENaCs induce synthetic neurotoxicity.Naked mole-rat acid-sensing ion channel 3 forms nonfunctional homomers, but functional heteromers.Acid-sensing ion channels are tuned to follow high-frequency stimuli.Endogenous arginine-phenylalanine-amide-related peptides alter steady-state desensitization of ASIC1a.Identification of a unique Ca2+-binding site in rat acid-sensing ion channel 3.
P2860
Q21091061-95097497-94D9-4C8F-8A7F-12F4A8439F4CQ26852449-B5555972-A806-44D2-A952-650BC1738F1EQ27656772-04BF12F2-341A-4B7C-9087-55CEAAB577CCQ27670938-FB719409-F8C9-40F7-8AA2-5638F4ACABD0Q27681632-42F74FA3-8C77-483D-A66A-97B86B696F9BQ30494532-364905E2-0020-490F-82A4-A3B2CC2FFF38Q33885102-CF0CA8B5-E55D-48A8-91B8-AD374162335FQ34311126-2E5AF66F-3868-475B-B534-2E21A2C2A6DEQ34963583-C34364A5-5043-4805-BA78-070CEA04FFFBQ34972050-E2A9E873-310A-4A00-B38B-AD9FDE6963E7Q35107500-C8CF57F6-8858-4C9D-A0BA-7AB4673DDA8AQ35604972-37703622-0FC6-44E7-9CB6-0ED4B3CCBED3Q36332816-748FDA93-F5E1-42E9-9088-A3D5D20C4A34Q36635937-5D5AD397-8F45-4E1D-B187-22F7D74E0034Q36918605-84A33EA1-BED9-4EBF-8DF6-3FE419A569DAQ36987732-4854CBF2-8DCD-488B-963F-C828E7EDDD13Q37174464-C14B6683-2DF5-419A-A34B-EE92DBD6CB54Q37417918-CF928D12-42FB-41E7-93BD-03ED812FE65EQ37479384-F120C185-6226-47C8-AF83-688A49DBB249Q37850687-04CB5CD1-B0CA-4780-861D-16C191617F41Q38048561-841103DF-FC09-4831-B914-BB394B146B04Q40937985-2C92374D-151A-4EB8-920B-0B9BEF123601Q41953156-1C699401-3031-41C6-884F-CD687A424938Q42046997-DFE4BD6F-8F9D-4803-A40C-0BC44B9BE3D1Q42532329-9F1438DE-636B-4182-A5D7-6A3D18614DACQ42636301-D982B8AF-DEF0-4DB2-94A6-4E7712150DC8Q42768651-66B18057-E321-49A3-9CC2-B227B7C6CD05Q44576018-EE2C8C89-2F01-455E-A9D2-727341E988F1Q46241927-89810AC7-D829-4AC5-A59D-7373706FB842Q48062340-936EE517-BC41-45AC-9CC9-639FE7F13225Q50882707-3C135947-3808-4A3F-A4B3-C6BCA4816645Q55241951-FA9B537E-14E1-4B5B-9278-6193DABD95A8
P2860
A conformation change in the extracellular domain that accompanies desensitization of acid-sensing ion channel (ASIC) 3.
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
A conformation change in the e ...... -sensing ion channel (ASIC) 3.
@ast
A conformation change in the e ...... -sensing ion channel (ASIC) 3.
@en
type
label
A conformation change in the e ...... -sensing ion channel (ASIC) 3.
@ast
A conformation change in the e ...... -sensing ion channel (ASIC) 3.
@en
prefLabel
A conformation change in the e ...... -sensing ion channel (ASIC) 3.
@ast
A conformation change in the e ...... -sensing ion channel (ASIC) 3.
@en
P2093
P2860
P356
P1476
A conformation change in the e ...... -sensing ion channel (ASIC) 3.
@en
P2093
Edwin W McCleskey
John P Adelman
Josephine Marsh-Haffner
Kenneth A Cushman
P2860
P304
P356
10.1085/JGP.200709757
P577
2007-04-01T00:00:00Z