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0030881872
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A Functionally Defined Model for the M2 Proton Channel of Influenza A Virus Suggests a Mechanism for Its Ion Selectivity
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Pinto, L. H.; Dieckmann, G. R.; Gandhi, C. S.; Papworth, C. G.; Braman, J.; Shaughnessy, M. A.; Lear, J. D.; Lamb, R. A.; DeGrado, W. F. A Functionally Defined Model for the M2 Proton Channel of Influenza A Virus Suggests a Mechanism for Its Ion Selectivity Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 11301-11306
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Pinto, L.H.1
Dieckmann, G.R.2
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Papworth, C.G.4
Braman, J.5
Shaughnessy, M.A.6
Lear, J.D.7
Lamb, R.A.8
Degrado, W.F.9
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2
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0034708477
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2 Ion Channel of Influenza a Virus
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2 Ion Channel of Influenza a Virus J. Biol. Chem. 2000, 275, 8592-8599
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Mould, J.A.1
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Lamb, R.A.6
Pinto, L.H.7
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3
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59049103481
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Molecular Dynamics Calculations Suggest a Conduction Mechanism for the M2 Proton Channel from Influenza A Virus
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Khurana, E.; Peraro, M. D.; Devane, R.; Vemparala, S.; Degrado, W. F.; Klein, M. L. Molecular Dynamics Calculations Suggest a Conduction Mechanism for the M2 Proton Channel from Influenza A Virus Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 1069-1074
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Khurana, E.1
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Klein, M.L.6
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69549104773
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Conformational Heterogeneity of the M2 Proton Channel and a Structural Model for Channel Activation
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Yi, M.; Cross, T. A.; Zhou, H.-X. Conformational Heterogeneity of the M2 Proton Channel and a Structural Model for Channel Activation Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 13311-13316
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Yi, M.1
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Histidines, Heart of the Hydrogen Ion Channel from Influenza A Virus: Toward an Understanding of Conductance and Proton Selectivity
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Hu, J.; Fu, R.; Nishimura, K.; Zhang, L.; Zhou, H.-X.; Busath, D. D.; Vijayvergiya, V.; Cross, T. A. Histidines, Heart of the Hydrogen Ion Channel from Influenza A Virus: Toward an Understanding of Conductance and Proton Selectivity Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 6865-6870
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Hu, J.1
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Cross, T.A.8
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77954270096
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The M2 protein functions as a tetramer; hence the His37 tetrad provides four protonation sites. The channel becomes activated when viral exterior pH is lowed to ∼6. At this pH, two protons are always bound to the His37 tetrad (ref 7); it is the binding of the third proton that leads to channel conductance. Hence what we model here is the binding/unbinding of a proton to/from a doubly protonated His37 tetrad. That the doubly protonated His37 tetrad has two equivalent protonation sites serves to double the binding and unbinding rate constants. Here we model the two protonation sites together as an absorbing disk.
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The M2 protein functions as a tetramer; hence the His37 tetrad provides four protonation sites. The channel becomes activated when viral exterior pH is lowed to ∼6. At this pH, two protons are always bound to the His37 tetrad (ref 7); it is the binding of the third proton that leads to channel conductance. Hence what we model here is the binding/unbinding of a proton to/from a doubly protonated His37 tetrad. That the doubly protonated His37 tetrad has two equivalent protonation sites serves to double the binding and unbinding rate constants. Here we model the two protonation sites together as an absorbing disk.
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9
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0039789834
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Elementary Steps in Enzyme Reactions (as Studied by Relaxation Spectrometry)
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Diffusion-Controlled Bimolecular Reaction Rates. the Effect of Rotational Diffusion and Orientation Constraints
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Conformation Gating as a Mechanism for Enzyme Specificity
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Zhou, H.-X.1
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Effect of Rotation on Diffusion-Controlled Rate of Ligand-Protein Association
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A Rate Process with an Entropy Barrier
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0037440103
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Differences in Conductance of M2 Proton Channels of Two Influenza Viruses at Low and High pH
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Chizhmakov, I. V.; Ogden, D. C.; Geraghty, F. M.; Hayhurst, A.; Skinner, A.; Betakova, T.; Hay, A. J. Differences in Conductance of M2 Proton Channels of Two Influenza Viruses at Low and High pH J. Physiol. 2003, 546, 427-438
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Hay, A.J.7
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0035085645
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Definitive Assignment of Proton Selectivity and Attoampere Unitary Current to the M2 Ion Channel Protein of Influenza A Virus
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Proton Transport through Influenza A Virus M2 Protein Reconstituted in Vesicles
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Moffat, J. C.; Vijayvergiya, V.; Gao, P. F.; Cross, T. A.; Woodbury, D. J.; Busath, D. D. Proton Transport through Influenza A Virus M2 Protein Reconstituted in Vesicles Biophys. J. 2008, 94, 434-445
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49149107480
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A Secondary Gate as a Mechanism for Inhibition of the M2 Proton Channel by Amantadine
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The Gate of the Influenza Virus M2 Proton Channel Is Formed by a Single Tryptophan Residue
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i -, occurs on the millisecond time scale.
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Solid-State NMR Characterization of Conformational Plasticity within the Transmembrane Domain of the Influenza A M2 Proton Channel
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Functional Studies and Modeling of Pore-Lining Residue Mutants of the Influenza a Virus M2 Ion Channel
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Balannik, V.; Carnevale, V.; Fiorin, G.; Levine, B. G.; Lamb, R. A.; Klein, M. L.; DeGrado, W. F.; Pinto, L. H. Functional Studies and Modeling of Pore-Lining Residue Mutants of the Influenza a Virus M2 Ion Channel Biochemistry 2010, 49, 696-708
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