Pore architecture and ion sites in acid-sensing ion channels and P2X receptors - Wikidata - awgldk - TriplyDB

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

http://www.wikidata.org/entity/Q27656772

about

Structure of the acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1 Molecular and functional properties of P2X receptors--recent progress and persisting challenges Crystal structure of the ATP-gated P2X(4) ion channel in the closed state Novel Insights into Acid-Sensing Ion Channels: Implications for Degenerative Diseases Insights into the channel gating of P2X receptors from structures, dynamics and small molecules ENaC regulation by proteases and shear stress Acid-sensing ion channels in pain and disease.Structure and activity of the acid-sensing ion channels Blood pressure and amiloride-sensitive sodium channels in vascular and renal cells Insights into the Molecular Mechanisms Underlying Mammalian P2X7 Receptor Functions and Contributions in Diseases, Revealed by Structural Modeling and Single Nucleotide Polymorphisms Structural plasticity and dynamic selectivity of acid-sensing ion channel–spider toxin complexes A stomatin dimer modulates the activity of acid-sensing ion channels Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase X-Ray Structure of Acid-Sensing Ion Channel 1–Snake Toxin Complex Reveals Open State of a Na+-Selective Channel Architecture of the mammalian mechanosensitive Piezo1 channel Epithelial sodium transport and its control by aldosterone: the story of our internal environment revisited A long isoform of the epithelial sodium channel alpha subunit forms a highly active channel Epithelial sodium channel (ENaC) family: Phylogeny, structure-function, tissue distribution, and associated inherited diseases ASIC and ENaC type sodium channels: conformational states and the structures of the ion selectivity filters Conserved charged residues at the surface and interface of epithelial sodium channel subunits--roles in cell surface expression and the sodium self-inhibition response Deoxyhypusine hydroxylase from Plasmodium vivax, the neglected human malaria parasite: molecular cloning, expression and specific inhibition by the 5-LOX inhibitor zileuton RNA-Seq Analysis of Human Trigeminal and Dorsal Root Ganglia with a Focus on Chemoreceptors Identification of P2X2/P2X4/P2X6 heterotrimeric receptors using atomic force microscopy (AFM) imaging Acid-sensing ion channels (ASICs) are differentially modulated by anions dependent on their subunit composition DEG/ENaC but not TRP channels are the major mechanoelectrical transduction channels in a C. elegans nociceptor Models of membrane-bound Alzheimer's Abeta peptide assemblies Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory.Expression and purification of the alpha subunit of the epithelial sodium channel, ENaC.Structures of membrane proteins.Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.How we feel: ion channel partnerships that detect mechanical inputs and give rise to touch and pain perception Physiological and pathological functions of acid-sensing ion channels in the central nervous system.The Concise Guide to PHARMACOLOGY 2013/14: ion channels A combined computational and functional approach identifies new residues involved in pH-dependent gating of ASIC1a.Constraint-based, homology model of the extracellular domain of the epithelial Na+ channel α subunit reveals a mechanism of channel activation by proteases.Acid-sensing ion channel (ASIC) 1a/2a heteromers have a flexible 2:1/1:2 stoichiometry Imaging P2X4 receptor subcellular distribution, trafficking, and regulation using P2X4-pHluorin P2X receptors: dawn of the post-structure era.Amiloride docking to acid-sensing ion channel-1 Tuning microbial hosts for membrane protein production.

P2860

Q24339479-F83CA353-BEEF-4F3A-82FF-13D6226269FB Q24617046-7DDAD299-5874-4BB5-8E6B-88B8D2AC61A6 Q24657193-59C51A0B-00B5-4038-B7BA-D7C3B9BFB881 Q26738902-9DC19B92-D4EE-49E3-B24B-C1E649907E96 Q26771359-C381953D-5852-40DD-ADD8-BE4E205D823C Q26825260-6B5EF2FB-BA4F-4351-BDE8-496EFA752226 Q26829975-18AA71B9-E7AC-4D00-9591-98C212C896DA Q26852449-529F3062-E472-42C0-AC41-F47C71571B61 Q27000436-64BDF7EF-4EE2-4CFB-A953-7AA0AB5F65D9 Q27500422-6E5ADE55-FD64-4CA4-979E-8BD2EA4F6A44 Q27670938-79695D53-2CFF-4FDD-9383-CB7110D6E3A3 Q27671013-A69CF7F7-B300-4957-88F2-24961E0CC937 Q27676276-AC049240-65F4-4B76-BB35-7ACDFD73C3A7 Q27681632-BC60AF51-F14C-4213-B02E-2585341BAD4B Q27702189-BB8BBC6B-08BC-4562-BE80-A2E9B4E3198B Q28083698-7B8796E5-4D67-411F-BC0D-8EC24D33CE1C Q28254111-49A723B0-AA10-456B-860A-5B061D4A5D41 Q28272095-8B9CF7C5-AD91-4EFB-9852-B727A29A1C61 Q28278216-539458B6-96D2-4A8F-AF88-D1E67C8CECB4 Q28308037-989BF7A3-267F-470B-B17F-AA5758639E49 Q28487727-E7FF3241-9186-4858-9E5C-9743C5B4DF07 Q28548290-9F2FB9A5-2A59-4F68-A2A6-B32BEC4F975D Q28573579-363EDFCF-AD40-40C2-B1E9-25CC0C6E0710 Q28710004-1F362A74-4401-40A0-8A4F-46ED6D5E58CE Q28740511-A2DC5C77-2992-4D00-B50E-AE2631C132B8 Q30155996-39E5563C-A074-4E2F-8D83-33F4465DCE3E Q30375519-2B616AD2-9996-4BBB-820B-BB4E35659EDF Q30379421-3D70450E-F6BB-4208-91B4-8581270309A0 Q30391943-5020A9EF-1210-49F2-BC87-1DF3E177B2D5 Q30417420-87B8814B-5FD1-41DC-97B5-4F4FD44C219A Q30454400-93E14F3B-D3F3-40A8-89FE-D5FE643BEE6A Q30458563-855C4022-5455-4A84-B78F-36BED17262ED Q30486735-D43545E4-11F0-4BF5-BD8F-754E45F59762 Q30494532-5B4209E2-3135-45E6-84C1-A17E2B8C74EE Q30497778-CBC8B59C-F298-4F8A-83C0-408BC62EF8F0 Q30580355-45B8B557-F9DD-4B7B-8CF0-9651491A3A79 Q30582093-BDDAB27E-2AFC-4C50-A14B-1584B879F4F7 Q33511146-DE562B1C-B990-4E5C-98E7-D3F0475EC6DF Q33521823-880C43C0-A504-45FE-B57B-1118C7EFFE9D Q33596003-D3C35A92-3D74-45DD-99C6-B31323583E46

P2860

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

http://www.wikidata.org/entity/Q27656772

description

2009 nî lūn-bûn

@nan

2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@ast

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@en

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@nl

type

label

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@ast

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@en

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@nl

prefLabel

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@ast

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@en

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@nl

P1433

Q27656772-96D030E2-0371-48A6-B860-5CC4D9010F8C

P1476

Q27656772-275F76C4-DFAC-4B6E-844E-557A3506E5BA

P2093

Q27656772-0813EBC0-5E75-4055-B823-295705EE6221

Q27656772-C8A449CE-51EB-4288-8210-E7B67569C4BC

P2860

Q27656772-04BF12F2-341A-4B7C-9087-55CEAAB577CC

Q27656772-05DC7D0F-264A-441C-BADB-A6160291A8EC

Q27656772-05E8E65D-A30E-4A3F-A4F2-8E21BD1E7CCE

Q27656772-0C4A97D0-F681-4841-83F8-BF01AB9AFE1C

Q27656772-1586690A-53DE-429C-A143-89AEEB064988

Q27656772-33F6EA21-3F08-430D-BE75-9F9B9C012ECD

Q27656772-36947ABE-3C0A-473B-A8CC-591837BF04CB

Q27656772-389AB65F-8D2C-4313-926F-A8445301FA67

Q27656772-4071C1D5-55C8-4430-8893-D49E8C3B94FC

Q27656772-46F4F9DE-2E57-4FC7-8EBD-E1AA675DAC5B

P2888

Q27656772-3B62F9F3-E716-4561-9444-1367F804B36E

P304

Q27656772-15762ECC-6C28-4335-9B93-D10277FD6225

P31

Q27656772-B26A061B-B7F5-4D0A-8EC7-E8F77E38222E

P3181

Q27656772-64D041C0-5642-499A-ABD8-2E4DD63C6EFB

P356

Q27656772-2A8903E6-095E-4DC7-863A-0C845C668BC6

P407

Q27656772-2B9612A4-AEFA-4592-97EB-C685176764D5

P433

Q27656772-2E1F5E9C-1C6C-4B12-9E68-D00C0266F0CA

P478

Q27656772-D55884DA-B213-4717-AB00-BE1770666703

P50

Q27656772-8F670C62-44DF-4844-9BD0-BE6CABC43A08

P577

Q27656772-2174D1CF-0655-40D2-A67D-6C3E85B33970

P5875

Q27656772-BEC8696F-0871-4D4D-B3E3-591D26C0171A

P6179

Q27656772-274ABF43-5E4D-428C-B864-C0F609655626

P698

Q27656772-07948ACA-AFE2-4B3C-8049-638E59264A6B

P932

Q27656772-90E56EA8-3167-4F70-931B-D20AB0BEE91F

P3181

P356

P1433

P1476

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

@en

P2093

Eric B Gonzales

http://www.w3.org/2001/XMLSchema#string

Toshimitsu Kawate

http://www.w3.org/2001/XMLSchema#string

P2860

Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution

Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes

A mutation causing pseudohypoaldosteronism type 1 identifies a conserved glycine that is involved in the gating of the epithelial sodium channel

A proton-gated cation channel involved in acid-sensing

P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels.

Permeability properties of ENaC selectivity filter mutants

Crystal structure of the ATP-gated P2X(4) ion channel in the closed state

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH

Coot: model-building tools for molecular graphics

P2888

P304

599-604

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

905038

http://www.w3.org/2001/XMLSchema#string

P356

10.1038/NATURE08218

http://www.w3.org/2001/XMLSchema#string

P407

P433

7255

http://www.w3.org/2001/XMLSchema#string

P478

460

http://www.w3.org/2001/XMLSchema#string

P50

P577

2009-07-30T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

26704306

http://www.w3.org/2001/XMLSchema#string

P6179

1008470922

http://www.w3.org/2001/XMLSchema#string

P698

19641589

http://www.w3.org/2001/XMLSchema#string

P932

2845979

http://www.w3.org/2001/XMLSchema#string