Studies of structural changes in the M2 proton channel of influenza A virus by tryptophan fluorescence.
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NMR structures of polytopic integral membrane proteins.Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus.Conformational heterogeneity of the M2 proton channel and a structural model for channel activationProton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH JumpProton association constants of His 37 in the Influenza-A M218-60 dimer-of-dimers.Computational study of drug binding to the membrane-bound tetrameric M2 peptide bundle from influenza A virusThe lipophilic bullet hits the targets: medicinal chemistry of adamantane derivativesHistidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.A pH-dependent conformational ensemble mediates proton transport through the influenza A/M2 proteinThe interplay of functional tuning, drug resistance, and thermodynamic stability in the evolution of the M2 proton channel from the influenza A virus.Ab initio calculations and validation of the pH-dependent structures of the His37-Trp41 quartet, the heart of acid activation and proton conductance in the M2 protein of Influenza A virusTransmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.Identification of the functional core of the influenza A virus A/M2 proton-selective ion channelBinding hot spots and amantadine orientation in the influenza a virus M2 proton channelStructural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan.Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel.Fast Atomic Charge Calculation for Implementation into a Polarizable Force Field and Application to an Ion Channel Protein
P2860
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P2860
Studies of structural changes in the M2 proton channel of influenza A virus by tryptophan fluorescence.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Studies of structural changes ...... us by tryptophan fluorescence.
@en
Studies of structural changes ...... us by tryptophan fluorescence.
@nl
type
label
Studies of structural changes ...... us by tryptophan fluorescence.
@en
Studies of structural changes ...... us by tryptophan fluorescence.
@nl
prefLabel
Studies of structural changes ...... us by tryptophan fluorescence.
@en
Studies of structural changes ...... us by tryptophan fluorescence.
@nl
P2093
P1433
P1476
Studies of structural changes ...... us by tryptophan fluorescence.
@en
P2093
Alan J Hay
Peter E Czabotar
Stephen R Martin
P356
10.1016/J.VIRUSRES.2003.10.004
P577
2004-01-01T00:00:00Z