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Volumn 81, Issue 15, 2007, Pages 8352-8355

GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS PROTEIN;

EID: 34547100064     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00014-07     Document Type: Article
Times cited : (8)

References (13)
  • 1
    • 33749001207 scopus 로고    scopus 로고
    • A trimerizing GxxxG motif is uniquely inserted in the severe acute respiratory syndrome (SARS) coronavirus spike protein transmembrane domain
    • Arbely, E., Z. Granot, I. Kass, J. Orly, and I. T. Arkin. 2006. A trimerizing GxxxG motif is uniquely inserted in the severe acute respiratory syndrome (SARS) coronavirus spike protein transmembrane domain. Biochemistry 45:11349-11356.
    • (2006) Biochemistry , vol.45 , pp. 11349-11356
    • Arbely, E.1    Granot, Z.2    Kass, I.3    Orly, J.4    Arkin, I.T.5
  • 2
    • 31144434388 scopus 로고    scopus 로고
    • Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry
    • Broer, R., B. Boson, W. Spaan, F. L. Cosset, and J. Corver. 2006. Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry. J. Virol. 80:1302-1310.
    • (2006) J. Virol , vol.80 , pp. 1302-1310
    • Broer, R.1    Boson, B.2    Spaan, W.3    Cosset, F.L.4    Corver, J.5
  • 3
    • 0002437897 scopus 로고
    • The coronavirus surface glycoprotein
    • S. G. Siddell ed, Plenum Press, New York, NY
    • Cavanagh, D. 1995. The coronavirus surface glycoprotein, p. 73-113. In S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, NY.
    • (1995) The Coronaviridae , pp. 73-113
    • Cavanagh, D.1
  • 4
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley, D. Z., and J. Lenard. 1998. The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. USA 95:3425-3430.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 6
    • 4644323974 scopus 로고    scopus 로고
    • Cellular entry of the SARS coronavirus
    • Hofmann, H., and S. Pöhlmann. 2004. Cellular entry of the SARS coronavirus. Trends Microbiol. 12:466-472.
    • (2004) Trends Microbiol , vol.12 , pp. 466-472
    • Hofmann, H.1    Pöhlmann, S.2
  • 8
    • 0032827589 scopus 로고    scopus 로고
    • Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion
    • Luo, Z., A. M. Matthews, and S. R. Weiss. 1999. Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion. J. Virol. 73:8152-8159.
    • (1999) J. Virol , vol.73 , pp. 8152-8159
    • Luo, Z.1    Matthews, A.M.2    Weiss, S.R.3
  • 9
    • 0020339971 scopus 로고
    • Post-translational glycosylation of coronavirus glycoprotein E1: Inhibition by monensin
    • Niemann, H., B. Boschek, D. Evans, M. Rosing, T. Tamura, and H. D. Klenk. 1982. Post-translational glycosylation of coronavirus glycoprotein E1: inhibition by monensin. EMBO J. 1:1499-1504.
    • (1982) EMBO J , vol.1 , pp. 1499-1504
    • Niemann, H.1    Boschek, B.2    Evans, D.3    Rosing, M.4    Tamura, T.5    Klenk, H.D.6
  • 10
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ, W. P., and D. M. Engelman. 1999. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl. Acad. Sci. USA 96:863-868.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 11
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W. P., and D. M. Engelman. 2000. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296:911-919.
    • (2000) J. Mol. Biol , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 13
    • 4143118878 scopus 로고    scopus 로고
    • Oligomerization of the SARS-CoV S glycoprotein: Dimerization of the N-terminus and trimerization of the ectodomain
    • Xiao, X., Y. Feng, S. Chakraborti, and D. S. Dimitrov. 2004. Oligomerization of the SARS-CoV S glycoprotein: dimerization of the N-terminus and trimerization of the ectodomain. Biochem. Biophys. Res. Commun. 322:93-99.
    • (2004) Biochem. Biophys. Res. Commun , vol.322 , pp. 93-99
    • Xiao, X.1    Feng, Y.2    Chakraborti, S.3    Dimitrov, D.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.