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Volumn 47, Issue 38, 2008, Pages 9934-9936

pH-induced conformational change of the influenza M2 protein C-terminal domain

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; CHEMOTHERAPY; DRUG DELIVERY; DRUG DOSAGE; ELECTRON RESONANCE; LABELING; LIFE CYCLE; MONOMERS; PARAMAGNETIC RESONANCE; PORT TERMINALS; QUANTUM THEORY;

EID: 52249123874     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801315m     Document Type: Article
Times cited : (62)

References (13)
  • 1
    • 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, 13170-13177.
    • (2002) Biochemistry , vol.41 , pp. 13170-13177
    • Nishimura, K.1    Kim, S.2    Zhang, L.3    Cross, T.A.4
  • 3
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • Schnell, J. R., and Chou, J. J. (2008) Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451, 591-595.
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 4
    • 0032736043 scopus 로고    scopus 로고
    • Effect of cytoplasmic tail truncations on the activity of the M2 ion channel of influenza A virus
    • Tobler, K., Kelly, M. L., Pinto, L. H., and Lamb, R. A. (1999) Effect of cytoplasmic tail truncations on the activity of the M2 ion channel of influenza A virus. J. Virol 73, 9695-9701.
    • (1999) J. Virol , vol.73 , pp. 9695-9701
    • Tobler, K.1    Kelly, M.L.2    Pinto, L.H.3    Lamb, R.A.4
  • 5
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly
    • Kochendoerfer, G. G., Salom, D., Lear, J. D., Wilk-Orescan, R., Kent, S. B., and DeGrado, W. F. (1999) Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly. Biochemistry 38, 11905-11913.
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.5    DeGrado, W.F.6
  • 6
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian, C., Gao, P. F., Pinto, L. H., Lamb, R. A., and Cross, T. A. (2003) Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers. Protein Sci. 12, 2597-2605.
    • (2003) Protein Sci , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, P.F.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 7
    • 33646932780 scopus 로고    scopus 로고
    • The M2 Proton Channels of Influenza A and B Viruses
    • Pinto, L. H., and Lamb, R. A. (2006) The M2 Proton Channels of Influenza A and B Viruses. J. Biol. Chem. 281, 8997-9000.
    • (2006) J. Biol. Chem , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 8
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • Fanucci, G. E., and Cafiso, D. S. (2006) Recent advances and applications of site-directed spin labeling. Curr. Opin. Struct. Biol. 16, 644-653.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 9
    • 0028346566 scopus 로고
    • A Collision Gradient-Method to Determine the Immersion Depth of Nitroxides in Lipid Bilayers
    • Altenbach, C., Greenhalgh, D., Khorana, H. G., and Hubbell, W. L. (1994) A Collision Gradient-Method to Determine the Immersion Depth of Nitroxides in Lipid Bilayers. Proc. Natl. Acad. Sci. U.S.A. 91, 1667-1671.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.2    Khorana, H.G.3    Hubbell, W.L.4
  • 11
    • 35448961949 scopus 로고    scopus 로고
    • Methods and applications of site-directed spin labeling EPR spectroscopy
    • Elsevier Academic Press: San Diego, pp
    • Klug, C. S., and Feix, J. B. (2008) Methods and applications of site-directed spin labeling EPR spectroscopy. In Biophysical Tools for Biologists: Vol 1. In Vitro Techniques, Elsevier Academic Press: San Diego, pp 617-658.
    • (2008) Biophysical Tools for Biologists: Vol 1. In Vitro Techniques , pp. 617-658
    • Klug, C.S.1    Feix, J.B.2
  • 12
    • 0000672379 scopus 로고    scopus 로고
    • Determination of Protein Folds and Conformational Dynamics Using Spin-Labeling EPR Spectroscopy
    • Berliner, L, Eaton, S, and Eaton, G, Eds, pp, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Mchaourab, H. S., and Perozo, E. (2000) Determination of Protein Folds and Conformational Dynamics Using Spin-Labeling EPR Spectroscopy. In Distance Measurements in Biological Systems by EPR (Berliner, L., Eaton, S., and Eaton, G., Eds.) pp 185-247, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2000) Distance Measurements in Biological Systems by EPR , pp. 185-247
    • Mchaourab, H.S.1    Perozo, E.2
  • 13
    • 0033073762 scopus 로고    scopus 로고
    • The influenza virus M2 ion channel protein: Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking
    • Bauer, C. M., Pinto, L. H., Cross, T. A., and Lamb, R. A. (1999) The influenza virus M2 ion channel protein: Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking. Virology 254, 196-209.
    • (1999) Virology , vol.254 , pp. 196-209
    • Bauer, C.M.1    Pinto, L.H.2    Cross, T.A.3    Lamb, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.