Recovery from slow inactivation in K+ channels is controlled by water molecules. - Wikidata - wikimedia - TriplyDB

Recovery from slow inactivation in K+ channels is controlled by water molecules.

Recovery from slow inactivation in K+ channels is controlled by water molecules.

http://www.wikidata.org/entity/Q37237569

about

Elucidation of Ligand-Dependent Modulation of Disorder-Order Transitions in the Oncoprotein MDM2 Structures of KcsA in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site P-loop conformation governed crizotinib resistance in G2032R-mutated ROS1 tyrosine kinase: clues from free energy landscape An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in (1) H-Detected Solid-State NMR Spectroscopy.Quantitative analysis of the water occupancy around the selectivity filter of a K+ channel in different gating modes.Synchrotron X-ray footprinting as a method to visualize water in proteins.Caution is required in interpretation of mutations in the voltage sensing domain of voltage gated channels as evidence for gating mechanisms Sodium channel slow inactivation as a therapeutic target for myotonia congenita Visualizing KcsA conformational changes upon ion binding by infrared spectroscopy and atomistic modeling.A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels.Simulating Current-Voltage Relationships for a Narrow Ion Channel Using the Weighted Ensemble Method.Modeling molecular kinetics with tICA and the kernel trick Mechanistic Insights into the Modulation of Voltage-Gated Ion Channels by Inhalational Anesthetics Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.CHARMM-GUI PDB manipulator for advanced modeling and simulations of proteins containing nonstandard residues.Reciprocal voltage sensor-to-pore coupling leads to potassium channel C-type inactivation.Multi-ion free energy landscapes underscore the microscopic mechanism of ion selectivity in the KcsA channel Hydrogen bonds as molecular timers for slow inactivation in voltage-gated potassium channels.Conduits of life's spark: a perspective on ion channel research since the birth of neuron.On the role of water density fluctuations in the inhibition of a proton channel Dynamics transitions at the outer vestibule of the KcsA potassium channel during gating.Lipid bilayer modules as determinants of K+ channel gating.A theoretical view of protein dynamics.Modeling ion channels: past, present, and future Computational Membrane Biophysics: From Ion Channels Interactions with Drugs to Cellular Function.Transmembrane allosteric energetics characterization for strong coupling between proton and potassium ion binding in the KcsA channel.Voltage-Gated Potassium Channels: A Structural Examination of Selectivity and Gating.Hysteresis in voltage-gated channels A relationship between three-dimensional surface hydration structures and force distribution measured by atomic force microscopy.Exploring the Dynamics of the TWIK-1 Channel.Probing the Effects of Gating on the Ion Occupancy of the K+ Channel Selectivity Filter Using Two-Dimensional Infrared Spectroscopy K+ congeners that do not compromise Na+ activation of the Na+,K+-ATPase: hydration of the ion binding cavity likely controls ion selectivity.Perspective: Markov models for long-timescale biomolecular dynamics.Size, separation, structural order, and mass density of molecules packing in water and ice.Atomic mutagenesis in ion channels with engineered stoichiometry Mechanism of activation at the selectivity filter of the KcsA K+ channel.Potassium channels in the heart: structure, function and regulation.Dynamic water patterns change the stability of the collapsed filter conformation of the KcsA K+ channel.The gating cycle of a K+ channel at atomic resolution.Incorporating Born solvation energy into the three-dimensional Poisson-Nernst-Planck model to study ion selectivity in KcsA K^{+} channels.

P2860

Q27318807-16176B5E-E830-4353-91FF-DE90B293A625 Q27684944-0899D83A-7F2B-4A9A-9C6A-9B415FB4FE84 Q28540825-AE18D20B-BF20-405B-AB55-A319460A6F75 Q30381228-6722D23C-0612-4295-8AA5-95A4833A0D76 Q30730679-210EDC53-409C-4E14-9FBE-CF3CC650FDB6 Q31125696-B15BB666-6F59-4029-A723-A360B28B0EF5 Q35016639-29BEE6BC-644F-44CE-9FE5-A0D5FF17C9F7 Q35044306-2A618AC2-D6AE-4C42-8670-0E0C7E4090F5 Q35595356-3492876B-4D7A-42A4-B9DD-2C8D2F8FA724 Q35846028-237A6578-9107-4264-A3BA-DED95269C1B1 Q36069614-0F658FAA-3007-4187-BE34-2B981CC4E49A Q36175542-3AA8C40E-AB4B-4EA1-83DE-9B8AE6635C08 Q36309696-7EF82D8D-51A8-4E9B-BC78-5B9F48FB067D Q36394444-3E16E387-D16F-44A6-804E-BED513A43F8B Q36539936-F52F50A9-D732-4828-85B9-0EAF8DB83DEE Q36985914-F6100DF3-B43B-44DC-9786-43C89DD93C0F Q37080887-CB35C1BA-ADC4-4ED6-AD99-268379C4CCA3 Q37365843-CDFF286E-010E-4268-B0F9-DA960097D925 Q37401733-320993F9-4A8C-4973-8EFC-DF7A862B0BCF Q37549833-3BB90558-1775-469D-ADF1-C308743895A7 Q37571365-AD27E425-675B-4F60-8F3A-6B2A9AA1F6AA Q37583526-E23491EB-5DB1-403B-BDE5-9FD72558B5B2 Q38202826-4ED2BCB0-9979-434C-8B4A-74346FB87650 Q38220791-9C3EF444-7C8B-4F28-938F-B7E398018764 Q38605343-9FE79593-4ECD-4FA6-A57E-9B2EB99F8D28 Q38646018-38EEFDBF-0ED0-4C29-BB66-77E38F5C9FD3 Q38824309-89D28978-CCBD-4AEA-9042-A41E723C9265 Q38968792-A5C907D4-E727-44CF-ACF6-CB760A3B9A34 Q39918236-6A3544BD-D582-45DD-AAE4-F818D96F7EBA Q40960166-F5626B4F-06E9-44CB-A89E-90128B1865EB Q41262323-1059AB52-753B-437A-92DA-4BFA76DD3A93 Q41657807-4CB3C06D-C369-45E2-98B9-5EF6DFE91EE0 Q41774653-4B4DA054-5F7F-45F3-8839-15E4CBC124E7 Q42233047-220C63A0-D937-4E08-A01B-FC2656FABD26 Q42375557-CF83153A-480C-4BE4-931B-155344BB9D9C Q44232952-9B25E393-FF72-43FD-A538-B23F7015C21A Q44505007-5E398BEB-48A3-4862-A119-AA2BCB20466D Q46269089-79B74B71-9232-4D5B-ACD7-1D3DF0267CE9 Q47374385-F00DA2BA-6024-48D6-AB9E-51D275654F09 Q47559899-B0ABA8A5-511B-4C65-A3A0-93ADFE78FA3E

P2860

Recovery from slow inactivation in K+ channels is controlled by water molecules.

http://www.wikidata.org/entity/Q37237569

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 28 July 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Recovery from slow inactivation in K+ channels is controlled by water molecules.

@en

Recovery from slow inactivation in K+ channels is controlled by water molecules.

@nl

type

label

Recovery from slow inactivation in K+ channels is controlled by water molecules.

@en

Recovery from slow inactivation in K+ channels is controlled by water molecules.

@nl

prefLabel

Recovery from slow inactivation in K+ channels is controlled by water molecules.

@en

Recovery from slow inactivation in K+ channels is controlled by water molecules.

@nl

P1433

Q37237569-45B056A2-7066-4D53-A775-5A74CC7106BD

P1476

Q37237569-A29D0EC1-47F4-4A1C-B68D-67492A8423E2

P2093

Q37237569-511874DC-7C97-47DF-AD80-B145AB7E96B6

Q37237569-8961EB25-4C92-494E-A396-E418C9043F1F

Q37237569-F957780E-26BD-4F86-A9DB-1B9CEFDABE70

Q37237569-FF5C387D-FB8C-4436-BFC9-32E358BF104F

P2860

Q37237569-06CF9AE3-4151-4495-B528-7696EE6D0B20

Q37237569-0B39BE5F-D249-40A2-A233-7F11C4AD7E60

Q37237569-1536DCB2-2ADD-425E-AEF3-B41D64D12035

Q37237569-44CB4AD8-E64E-4E52-9F51-D4F05438AF58

Q37237569-48D9E812-450C-4F56-8CEB-E153168C34A2

Q37237569-4E37C885-EB2C-474E-9A1F-42CFB3454817

Q37237569-7627A37D-88F1-48FD-9301-0DE0BD00AF9E

Q37237569-7C173E1B-A4F7-455A-A411-2FCED299AB19

Q37237569-885484A0-7C4E-42CB-9C3D-CBA8F915DF3F

Q37237569-8C0CE57E-B388-43EF-9BC6-FAE6B95E0B8E

P2888

Q37237569-A1290FC6-1291-4520-B79B-0C7D35604A8D

P304

Q37237569-53173022-2023-4053-A2A3-1CBE12A8ED80

P31

Q37237569-2744D888-2F0D-4208-822E-A2739EB9DF11

P356

Q37237569-32940FE3-A9F2-4049-8531-FA76CBAC6395

P407

Q37237569-3B8DA76A-BA99-4AAD-9B31-5E68106D9541

P433

Q37237569-054AA86F-F59A-4297-8267-3B07C42B315A

P478

Q37237569-14BABB6A-5C2E-4ED5-880C-042E35DBFEF7

P50

Q37237569-2520BC71-F09D-4FE6-9EA4-DBFDCF68337A

P577

Q37237569-93C4EF4B-095D-4464-8572-063B5B1BD35A

P5875

Q37237569-C02555DA-393A-4536-900B-BD63E09840F8

P6179

Q37237569-ACC38E1E-9820-487A-BBE1-4C1AFB041E9F

P698

Q37237569-6D0496F6-670E-4FD0-ADAF-4BB938D4FB47

P932

Q37237569-84B53792-F24E-48EB-86DF-9A5FD2490E9A

P356

P1433

P1476

Recovery from slow inactivation in K+ channels is controlled by water molecules.

@en

P2093

Benoît Roux

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

Eduardo Perozo

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

Jared Ostmeyer

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

Sudha Chakrapani

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

Structural basis for the coupling between activation and inactivation gates in K(+) channels

Structural mechanism of C-type inactivation in K(+) channels

Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating

On the structural basis of modal gating behavior in K+ channels

All-atom empirical potential for molecular modeling and dynamics studies of proteins

Scalable molecular dynamics with NAMD

Temperature and pressure dependence of Shaker K+ channel N- and C-type inactivation.

Molecular determinants of gating at the potassium-channel selectivity filter.

A quantitative description of KcsA gating I: macroscopic currents

P2888

P304

121-124

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

P31

scholarly article

P356

10.1038/NATURE12395

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

P407

P433

7465

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

P478

501

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

P50

P577

2013-07-28T00:00:00Z

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

P5875

253334778

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

P6179

1045371290

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

P698

23892782

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

P932

3799803

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