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Volumn 110, Issue 6, 2016, Pages 1391-1399

Structural Influences: Cholesterol, Drug, and Proton Binding to Full-Length Influenza A M2 Protein

Author keywords

[No Author keywords available]

Indexed keywords

AMANTADINE; CHOLESTEROL; M2 PROTEIN, INFLUENZA A VIRUS; MATRIX PROTEIN; PROTON;

EID: 84964336621     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.11.3529     Document Type: Article
Times cited : (34)

References (61)
  • 1
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson, and J.M. Baldwin K.H. Downing Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy J. Mol. Biol. 213 1990 899 929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3
  • 2
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • R.R. Ketchem, W. Hu, and T.A. Cross High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR Science 261 1993 1457 1460
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 3
    • 84877773919 scopus 로고    scopus 로고
    • Influences of membrane mimetic environments on membrane protein structures
    • K.A. Dill, Annual Reviews Palo Alto, CA
    • H.X. Zhou, and T.A. Cross Influences of membrane mimetic environments on membrane protein structures K.A. Dill, Annual Review of Biophysics Vol 42 2013 Annual Reviews Palo Alto, CA 361 392
    • (2013) Annual Review of Biophysics , vol.42 VOL , pp. 361-392
    • Zhou, H.X.1    Cross, T.A.2
  • 4
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • M.F. Brown Modulation of rhodopsin function by properties of the membrane bilayer Chem. Phys. Lipids 73 1994 159 180
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 159-180
    • Brown, M.F.1
  • 5
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • C.B. Anfinsen Principles that govern the folding of protein chains Science 181 1973 223 230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 6
    • 0037027306 scopus 로고    scopus 로고
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR Biochemistry 41 2002 13170 13177
    • (2002) Biochemistry , vol.41 , pp. 13170-13177
    • Nishimura, K.1    Kim, S.2    Cross, T.A.3
  • 7
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus
    • J. Hu, and T. Asbury T.A. Cross Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus Biophys. J. 92 2007 4335 4343
    • (2007) Biophys. J. , vol.92 , pp. 4335-4343
    • Hu, J.1    Asbury, T.2    Cross, T.A.3
  • 8
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • J.R. Schnell, and J.J. Chou Structure and mechanism of the M2 proton channel of influenza A virus Nature 451 2008 591 595
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 9
    • 38749151911 scopus 로고    scopus 로고
    • Structural basis for the function and inhibition of an influenza virus proton channel
    • A.L. Stouffer, and R. Acharya W.F. DeGrado Structural basis for the function and inhibition of an influenza virus proton channel Nature 451 2008 596 599
    • (2008) Nature , vol.451 , pp. 596-599
    • Stouffer, A.L.1    Acharya, R.2    DeGrado, W.F.3
  • 10
    • 77958156306 scopus 로고    scopus 로고
    • Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer
    • M. Sharma, and M. Yi T.A. Cross Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer Science 330 2010 509 512
    • (2010) Science , vol.330 , pp. 509-512
    • Sharma, M.1    Yi, M.2    Cross, T.A.3
  • 11
    • 76249125649 scopus 로고    scopus 로고
    • Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers
    • S.D. Cady, and K. Schmidt-Rohr M. Hong Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers Nature 463 2010 689 692
    • (2010) Nature , vol.463 , pp. 689-692
    • Cady, S.D.1    Schmidt-Rohr, K.2    Hong, M.3
  • 12
    • 77956996035 scopus 로고    scopus 로고
    • Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus
    • R. Acharya, and V. Carnevale M.L. Klein Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus Proc. Natl. Acad. Sci. USA 107 2010 15075 15080
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15075-15080
    • Acharya, R.1    Carnevale, V.2    Klein, M.L.3
  • 13
    • 77957653235 scopus 로고    scopus 로고
    • Solution NMR structure of the V27A drug resistant mutant of influenza A M2 channel
    • R.M. Pielak, and J.J. Chou Solution NMR structure of the V27A drug resistant mutant of influenza A M2 channel Biochem. Biophys. Res. Commun. 401 2010 58 63
    • (2010) Biochem. Biophys. Res. Commun. , vol.401 , pp. 58-63
    • Pielak, R.M.1    Chou, J.J.2
  • 14
    • 79551597049 scopus 로고    scopus 로고
    • Influence of solubilizing environments on membrane protein structures
    • T.A. Cross, and M. Sharma H.X. Zhou Influence of solubilizing environments on membrane protein structures Trends Biochem. Sci. 36 2011 117 125
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 117-125
    • Cross, T.A.1    Sharma, M.2    Zhou, H.X.3
  • 15
    • 84929359089 scopus 로고    scopus 로고
    • The influenza M2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conduction
    • S.Y. Liao, and Y. Yang M. Hong The influenza M2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conduction J. Am. Chem. Soc. 137 2015 6067 6077
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 6067-6077
    • Liao, S.Y.1    Yang, Y.2    Hong, M.3
  • 17
    • 38349105382 scopus 로고    scopus 로고
    • 41 participates in the gating mechanism of the M2 proton channel of influenza A virus
    • 41 participates in the gating mechanism of the M2 proton channel of influenza A virus J. Am. Chem. Soc. 130 2008 918 924
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 918-924
    • Witter, R.1    Nozirov, F.2    Fu, R.3
  • 18
    • 84948659347 scopus 로고    scopus 로고
    • Structure and mechanism of the influenza-A M218-60 dimer of dimers
    • L.B. Andreas, and M. Reese R.G. Griffin Structure and mechanism of the influenza-A M218-60 dimer of dimers J. Am. Chem. Soc. 137 2015 14877 14886
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 14877-14886
    • Andreas, L.B.1    Reese, M.2    Griffin, R.G.3
  • 19
    • 84892701827 scopus 로고    scopus 로고
    • Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
    • S.Y. Liao, K.J. Fritzsching, and M. Hong Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR Protein Sci. 22 2013 1623 1638
    • (2013) Protein Sci. , vol.22 , pp. 1623-1638
    • Liao, S.Y.1    Fritzsching, K.J.2    Hong, M.3
  • 20
    • 84946129251 scopus 로고    scopus 로고
    • Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain
    • B. Kwon, and D. Tietze M. Hong Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain Protein Sci. 24 2015 1087 1099
    • (2015) Protein Sci. , vol.24 , pp. 1087-1099
    • Kwon, B.1    Tietze, D.2    Hong, M.3
  • 21
    • 79959340086 scopus 로고    scopus 로고
    • Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method
    • R. Verardi, and L. Shi G. Veglia Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method Proc. Natl. Acad. Sci. USA 108 2011 9101 9106
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 9101-9106
    • Verardi, R.1    Shi, L.2    Veglia, G.3
  • 22
    • 84889565097 scopus 로고    scopus 로고
    • Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport
    • V.V. Vostrikov, and K.R. Mote G. Veglia Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport Structure 21 2013 2119 2130
    • (2013) Structure , vol.21 , pp. 2119-2130
    • Vostrikov, V.V.1    Mote, K.R.2    Veglia, G.3
  • 23
    • 84929129611 scopus 로고    scopus 로고
    • Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints
    • Y. Tian, and G.J. Lu S.J. Opella Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints J. Biomol. NMR 60 2014 67 71
    • (2014) J. Biomol. NMR , vol.60 , pp. 67-71
    • Tian, Y.1    Lu, G.J.2    Opella, S.J.3
  • 24
    • 84870290491 scopus 로고    scopus 로고
    • Structure of the chemokine receptor CXCR1 in phospholipid bilayers
    • S.H. Park, and B.B. Das S.J. Opella Structure of the chemokine receptor CXCR1 in phospholipid bilayers Nature 491 2012 779 783
    • (2012) Nature , vol.491 , pp. 779-783
    • Park, S.H.1    Das, B.B.2    Opella, S.J.3
  • 25
    • 84920969904 scopus 로고    scopus 로고
    • Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers
    • N. Das, and J. Dai T.A. Cross Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers Proc. Natl. Acad. Sci. USA 112 2015 E119 E126
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. E119-E126
    • Das, N.1    Dai, J.2    Cross, T.A.3
  • 26
    • 84884904937 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein
    • S. Wang, and R.A. Munro V. Ladizhansky Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein Nat. Methods 10 2013 1007 1012
    • (2013) Nat. Methods , vol.10 , pp. 1007-1012
    • Wang, S.1    Munro, R.A.2    Ladizhansky, V.3
  • 27
    • 84870847943 scopus 로고    scopus 로고
    • Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals
    • S.A. Shahid, and B. Bardiaux D. Linke Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals Nat. Methods 9 2012 1212 1217
    • (2012) Nat. Methods , vol.9 , pp. 1212-1217
    • Shahid, S.A.1    Bardiaux, B.2    Linke, D.3
  • 28
    • 77958162674 scopus 로고    scopus 로고
    • Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR
    • F. Hu, W. Luo, and M. Hong Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR Science 330 2010 505 508
    • (2010) Science , vol.330 , pp. 505-508
    • Hu, F.1    Luo, W.2    Hong, M.3
  • 29
    • 79960884898 scopus 로고    scopus 로고
    • Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein
    • S. Cady, T. Wang, and M. Hong Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein J. Am. Chem. Soc. 133 2011 11572 11579
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 11572-11579
    • Cady, S.1    Wang, T.2    Hong, M.3
  • 30
    • 13744254776 scopus 로고    scopus 로고
    • The influenza virus ion channel and maturation cofactor M2 is a cholesterol-binding protein
    • C. Schroeder, and H. Heider T.I. Lin The influenza virus ion channel and maturation cofactor M2 is a cholesterol-binding protein Eur. Biophys. J. 34 2005 52 66
    • (2005) Eur. Biophys. J. , vol.34 , pp. 52-66
    • Schroeder, C.1    Heider, H.2    Lin, T.I.3
  • 31
    • 77951437276 scopus 로고    scopus 로고
    • Influenza virus M2 ion channel protein is necessary for filamentous virion formation
    • J.S. Rossman, and X. Jing R.A. Lamb Influenza virus M2 ion channel protein is necessary for filamentous virion formation J. Virol. 84 2010 5078 5088
    • (2010) J. Virol. , vol.84 , pp. 5078-5088
    • Rossman, J.S.1    Jing, X.2    Lamb, R.A.3
  • 32
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • J.S. Rossman, and R.A. Lamb Influenza virus assembly and budding Virology 411 2011 229 236
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 33
    • 84883556425 scopus 로고    scopus 로고
    • How cholesterol interacts with membrane proteins: An exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
    • J. Fantini, and F.J. Barrantes How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains Front. Physiol. 4 2013 31
    • (2013) Front. Physiol. , vol.4 , pp. 31
    • Fantini, J.1    Barrantes, F.J.2
  • 34
    • 82955248059 scopus 로고    scopus 로고
    • Uncovering the intimate relationship between lipids, cholesterol and GPCR activation
    • J. Oates, and A. Watts Uncovering the intimate relationship between lipids, cholesterol and GPCR activation Curr. Opin. Struct. Biol. 21 2011 802 807
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 802-807
    • Oates, J.1    Watts, A.2
  • 35
    • 39749193522 scopus 로고    scopus 로고
    • Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy
    • N.J. Traaseth, R. Verardi, and G. Veglia Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy J. Am. Chem. Soc. 130 2008 2400 2401
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2400-2401
    • Traaseth, N.J.1    Verardi, R.2    Veglia, G.3
  • 36
    • 0000953276 scopus 로고    scopus 로고
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR Chem. Phys. Lett. 344 2001 631 637
    • (2001) Chem. Phys. Lett. , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 37
    • 0021532102 scopus 로고
    • Principles of operation of an evaporative light-scattering detector for liquid-chromatography
    • T.H. Mourey, and L.E. Oppenheimer Principles of operation of an evaporative light-scattering detector for liquid-chromatography Anal. Chem. 56 1984 2427 2434
    • (1984) Anal. Chem. , vol.56 , pp. 2427-2434
    • Mourey, T.H.1    Oppenheimer, L.E.2
  • 38
    • 84899452157 scopus 로고    scopus 로고
    • Detergent optimized membrane protein reconstitution in liposomes for solid state NMR
    • D.T. Murray, J. Griffin, and T.A. Cross Detergent optimized membrane protein reconstitution in liposomes for solid state NMR Biochemistry 53 2014 2454 2463
    • (2014) Biochemistry , vol.53 , pp. 2454-2463
    • Murray, D.T.1    Griffin, J.2    Cross, T.A.3
  • 39
    • 33947605702 scopus 로고    scopus 로고
    • Using low-E resonators to reduce RF heating in biological samples for static solid-state NMR up to 900 MHz
    • P.L. Gor'kov, and E.Y. Chekmenev W.W. Brey Using low-E resonators to reduce RF heating in biological samples for static solid-state NMR up to 900 MHz J. Magn. Reson. 185 2007 77 93
    • (2007) J. Magn. Reson. , vol.185 , pp. 77-93
    • Gor'kov, P.L.1    Chekmenev, E.Y.2    Brey, W.W.3
  • 40
    • 62149088575 scopus 로고    scopus 로고
    • A low-E magic angle spinning probe for biological solid state NMR at 750 MHz
    • S.A. McNeill, and P.L. Gor'kov J.R. Long A low-E magic angle spinning probe for biological solid state NMR at 750 MHz J. Magn. Reson. 197 2009 135 144
    • (2009) J. Magn. Reson. , vol.197 , pp. 135-144
    • McNeill, S.A.1    Gor'kov, P.L.2    Long, J.R.3
  • 41
    • 84893969715 scopus 로고    scopus 로고
    • A LC3-interacting motif in the influenza A virus M2 protein is required to subvert autophagy and maintain virion stability
    • R. Beale, and H. Wise F. Randow A LC3-interacting motif in the influenza A virus M2 protein is required to subvert autophagy and maintain virion stability Cell Host Microbe 15 2014 239 247
    • (2014) Cell Host Microbe , vol.15 , pp. 239-247
    • Beale, R.1    Wise, H.2    Randow, F.3
  • 42
    • 33646494326 scopus 로고    scopus 로고
    • Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity
    • J. Hu, and R. Fu T.A. Cross Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity Proc. Natl. Acad. Sci. USA 103 2006 6865 6870
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6865-6870
    • Hu, J.1    Fu, R.2    Cross, T.A.3
  • 43
    • 84876721844 scopus 로고    scopus 로고
    • Dynamic nuclear polarization study of inhibitor binding to the M2(18-60) proton transporter from influenza A
    • L.B. Andreas, and A.B. Barnes R.G. Griffin Dynamic nuclear polarization study of inhibitor binding to the M2(18-60) proton transporter from influenza A Biochemistry 52 2013 2774 2782
    • (2013) Biochemistry , vol.52 , pp. 2774-2782
    • Andreas, L.B.1    Barnes, A.B.2    Griffin, R.G.3
  • 44
    • 84949218464 scopus 로고    scopus 로고
    • + channel reveals tetrameric structural heterogeneity and functional mechanism structure
    • + channel reveals tetrameric structural heterogeneity and functional mechanism structure Structure 23 2015 2300 2308
    • (2015) Structure , vol.23 , pp. 2300-2308
    • Miao, Y.M.1    Fu, R.2    Cross, T.A.3
  • 45
    • 84861917718 scopus 로고    scopus 로고
    • Magic angle spinning and oriented sample solid-state NMR structural restraints combine for influenza A M2 protein functional insights
    • T.V. Can, and M. Sharma T.A. Cross Magic angle spinning and oriented sample solid-state NMR structural restraints combine for influenza A M2 protein functional insights J. Am. Chem. Soc. 134 2012 9022 9025
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 9022-9025
    • Can, T.V.1    Sharma, M.2    Cross, T.A.3
  • 46
    • 78649796981 scopus 로고    scopus 로고
    • Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness
    • F. Hu, and W. Luo M. Hong Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness Biochim. Biophys. Acta 1808 2011 415 423
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 415-423
    • Hu, F.1    Luo, W.2    Hong, M.3
  • 47
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • C. Tian, and P.F. Gao T.A. Cross Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers Protein Sci. 12 2003 2597 2605
    • (2003) Protein Sci. , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, P.F.2    Cross, T.A.3
  • 48
    • 52249123874 scopus 로고    scopus 로고
    • PH-induced conformational change of the influenza M2 protein C-terminal domain
    • P.A. Nguyen, and C.S. Soto K.P. Howard pH-induced conformational change of the influenza M2 protein C-terminal domain Biochemistry 47 2008 9934 9936
    • (2008) Biochemistry , vol.47 , pp. 9934-9936
    • Nguyen, P.A.1    Soto, C.S.2    Howard, K.P.3
  • 49
    • 84873050159 scopus 로고    scopus 로고
    • Detection of drug-induced conformational change of a transmembrane protein in lipid bilayers using site-directed spin labeling
    • J.L. Thomaston, and P.A. Nguyen K.P. Howard Detection of drug-induced conformational change of a transmembrane protein in lipid bilayers using site-directed spin labeling Protein Sci. 22 2013 65 73
    • (2013) Protein Sci. , vol.22 , pp. 65-73
    • Thomaston, J.L.1    Nguyen, P.A.2    Howard, K.P.3
  • 50
    • 36849047240 scopus 로고    scopus 로고
    • Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel
    • C. Li, and H. Qin T.A. Cross Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel Biochim. Biophys. Acta 1768 2007 3162 3170
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3162-3170
    • Li, C.1    Qin, H.2    Cross, T.A.3
  • 51
    • 0032946243 scopus 로고    scopus 로고
    • Cholesterol orientation and dynamics in dimyristoylphosphatidylcholine bilayers: A solid state deuterium NMR analysis
    • M.P. Marsan, and I. Muller A. Milon Cholesterol orientation and dynamics in dimyristoylphosphatidylcholine bilayers: a solid state deuterium NMR analysis Biophys. J. 76 1999 351 359
    • (1999) Biophys. J. , vol.76 , pp. 351-359
    • Marsan, M.P.1    Muller, I.2    Milon, A.3
  • 52
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • H. Li, and V. Papadopoulos Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern Endocrinology 139 1998 4991 4997
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 53
    • 44649172481 scopus 로고    scopus 로고
    • A specific cholesterol binding site is established by the 2.8 Å structure of the human β2-adrenergic receptor
    • M.A. Hanson, and V. Cherezov R.C. Stevens A specific cholesterol binding site is established by the 2.8 Å structure of the human β2-adrenergic receptor Structure 16 2008 897 905
    • (2008) Structure , vol.16 , pp. 897-905
    • Hanson, M.A.1    Cherezov, V.2    Stevens, R.C.3
  • 54
    • 78650919372 scopus 로고    scopus 로고
    • Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein coupled receptors
    • M. Jafurulla, S. Tiwari, and A. Chattopadhyay Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein coupled receptors Biochem. Biophys. Res. Commun. 404 2011 569 573
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 569-573
    • Jafurulla, M.1    Tiwari, S.2    Chattopadhyay, A.3
  • 55
    • 77955664320 scopus 로고    scopus 로고
    • The cholesterol recognition/interaction amino acid consensus motif of the influenza A virus M2 protein is not required for virus replication but contributes to virulence
    • S.M. Stewart, and W.H. Wu A. Pekosz The cholesterol recognition/interaction amino acid consensus motif of the influenza A virus M2 protein is not required for virus replication but contributes to virulence Virology 405 2010 530 538
    • (2010) Virology , vol.405 , pp. 530-538
    • Stewart, S.M.1    Wu, W.H.2    Pekosz, A.3
  • 56
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • J.S. Rossman, and X. Jing R.A. Lamb Influenza virus M2 protein mediates ESCRT-independent membrane scission Cell 142 2010 902 913
    • (2010) Cell , vol.142 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Lamb, R.A.3
  • 57
    • 79960269727 scopus 로고    scopus 로고
    • Intrinsic membrane association of the cytoplasmic tail of influenza virus M2 protein and lateral membrane sorting regulated by cholesterol binding and palmitoylation
    • B. Thaa, and I. Levental M. Veit Intrinsic membrane association of the cytoplasmic tail of influenza virus M2 protein and lateral membrane sorting regulated by cholesterol binding and palmitoylation Biochem. J. 437 2011 389 397
    • (2011) Biochem. J. , vol.437 , pp. 389-397
    • Thaa, B.1    Levental, I.2    Veit, M.3
  • 58
    • 84884469272 scopus 로고    scopus 로고
    • Influenza virus A M2 protein generates negative Gaussian membrane curvature necessary for budding and scission
    • N.W. Schmidt, and A. Mishra G.C.L. Wong Influenza virus A M2 protein generates negative Gaussian membrane curvature necessary for budding and scission J. Am. Chem. Soc. 135 2013 13710 13719
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 13710-13719
    • Schmidt, N.W.1    Mishra, A.2    Wong, G.C.L.3
  • 59
    • 84883309308 scopus 로고    scopus 로고
    • The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particles
    • K.L. Roberts, and G.P. Leser R.A. Lamb The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particles J. Virol. 87 2013 9973 9982
    • (2013) J. Virol. , vol.87 , pp. 9973-9982
    • Roberts, K.L.1    Leser, G.P.2    Lamb, R.A.3
  • 60
    • 53749092893 scopus 로고    scopus 로고
    • The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding
    • B.J. Chen, and G.P. Leser R.A. Lamb The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding J. Virol. 82 2008 10059 10070
    • (2008) J. Virol. , vol.82 , pp. 10059-10070
    • Chen, B.J.1    Leser, G.P.2    Lamb, R.A.3
  • 61
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor
    • V. Cherezov, and D.M. Rosenbaum R.C. Stevens High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor Science 318 2007 1258 1265
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1    Rosenbaum, D.M.2    Stevens, R.C.3


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