A quantitative description of KcsA gating I: macroscopic currents
about
Structural basis for the coupling between activation and inactivation gates in K(+) channelsStructural mechanism of C-type inactivation in K(+) channelsCrystal structure of full-length KcsA in its closed conformationMechanism of potassium-channel selectivity revealed by Na+ and Li+ binding sites within the KcsA poreOn the structural basis of modal gating behavior in K+ channelsMechanism for selectivity-inactivation coupling in KcsA potassium channelsUsing protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K+ channelsDesign and characterization of a constitutively open KcsA.A quantitative description of KcsA gating II: single-channel currentsConformational changes in the selectivity filter of the open-state KcsA channel: an energy minimization studyFunctional reconstitution of a voltage-gated potassium channel in giant unilamellar vesicles.Structural basis underlying the dual gate properties of KcsAConformational dynamics at the inner gate of KcsA during activationAn electrostatic interaction between TEA and an introduced pore aromatic drives spring-in-the-door inactivation in Shaker potassium channels.Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentrationRegulation of ion channel function by the host lipid bilayer examined by a stopped-flow spectrofluorometric assay.Molecular and electrophysiological characterization of a novel cation channel of Trypanosoma cruzi.Importance of lipid-pore loop interface for potassium channel structure and function.Molecular mechanism of pH sensing in KcsA potassium channels.A multipoint hydrogen-bond network underlying KcsA C-type inactivation.Thermodynamic coupling between activation and inactivation gating in potassium channels revealed by free energy molecular dynamics simulations.A chimeric prokaryotic pentameric ligand-gated channel reveals distinct pathways of activation.Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.Functional equilibrium of the KcsA structure revealed by NMR.Individual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation.Ion channels in microbes.Fluorescence detection of the movement of single KcsA subunits reveals cooperativity.KirBac1.1: it's an inward rectifying potassium channel.Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.Semisynthetic K+ channels show that the constricted conformation of the selectivity filter is not the C-type inactivated state.The analysis of desensitizing CNGA1 channels reveals molecular interactions essential for normal gatingRecovery from slow inactivation in K+ channels is controlled by water molecules.Biochemical and structural analysis of the hyperpolarization-activated K(+) channel MVPCrystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel.Modes of glutamate receptor gating.Transmembrane allosteric energetics characterization for strong coupling between proton and potassium ion binding in the KcsA channel.Kir4.1 K+ channels are regulated by external cations.Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA.Inactivation of the KcsA potassium channel explored with heterotetramers
P2860
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P2860
A quantitative description of KcsA gating I: macroscopic currents
description
2007 nî lūn-bûn
@nan
2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
A quantitative description of KcsA gating I: macroscopic currents
@ast
A quantitative description of KcsA gating I: macroscopic currents
@en
type
label
A quantitative description of KcsA gating I: macroscopic currents
@ast
A quantitative description of KcsA gating I: macroscopic currents
@en
prefLabel
A quantitative description of KcsA gating I: macroscopic currents
@ast
A quantitative description of KcsA gating I: macroscopic currents
@en
P2860
P356
P1476
A quantitative description of KcsA gating I: macroscopic currents
@en
P2093
Eduardo Perozo
Julio F Cordero-Morales
P2860
P304
P356
10.1085/JGP.200709843
P577
2007-10-15T00:00:00Z