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Volumn 287, Issue 48, 2012, Pages 40525-40534

The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation

Author keywords

[No Author keywords available]

Indexed keywords

CRYO-ELECTRON MICROSCOPY; DENGUE VIRUS; DIMERIC STRUCTURE; ENDOPLASMIC RETICULUM; EXOSOMES; FLUORESCENCE CORRELATION SPECTROSCOPY; INFECTIOUS PARTICLES; NEUTRAL PH; SURFACE PROTEINS;

EID: 84870014650     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.384446     Document Type: Article
Times cited : (44)

References (26)
  • 1
    • 34748873170 scopus 로고    scopus 로고
    • (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B., and Straus, S. E. eds), 5th Ed., Lippincott Williams & Wilkins, Baltimore
    • Lindenbach, B. D., Thiel, H. J., and Rice, C. M. (2007) in Fields Virology (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B., and Straus, S. E. eds), 5th Ed., pp. 1101-1152, Lippincott Williams & Wilkins, Baltimore
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 2
    • 0003487519 scopus 로고    scopus 로고
    • World Health Organization 2nd Ed., . World Health Organization, Geneva, Switzerland
    • World Health Organization (1997) Dengue Haemorrhagic Fever: Diagnosis, Treatment, Prevention and Control, 2nd Ed., pp. 12-23, World Health Organization, Geneva, Switzerland
    • (1997) Dengue Haemorrhagic Fever: Diagnosis, Treatment, Prevention and Control , pp. 12-23
  • 5
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C., and Harrison, S. C. (1995) The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375, 291-298
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 7
    • 4444338894 scopus 로고    scopus 로고
    • Conformational changes of the flavivirus E glycoprotein
    • DOI 10.1016/j.str.2004.06.019, PII S0969212604002722
    • Zhang, Y., Zhang, W., Ogata, S., Clements, D., Strauss, J. H., Baker, T. S., Kuhn, R. J., and Rossmann, M. G. (2004) Conformational changes of the flavivirus E glycoprotein. Structure 12, 1607-1618 (Pubitemid 39200514)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1607-1618
    • Zhang, Y.1    Zhang, W.2    Ogata, S.3    Clements, D.4    Strauss, J.H.5    Baker, T.S.6    Kuhn, R.J.7    Rossmann, M.G.8
  • 8
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • DOI 10.1038/sj.emboj.7600064
    • Bressanelli, S., Stiasny, K., Allison, S. L., Stura, E. A., Duquerroy, S., Lescar, J., Heinz, F. X., and Rey, F. A. (2004) Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J. 23, 728-738 (Pubitemid 38425440)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3    Stura, E.A.4    Duquerroy, S.5    Lescar, J.6    Heinz, F.X.7    Rey, F.A.8
  • 9
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • DOI 10.1038/nature02165
    • Modis, Y., Ogata, S., Clements, D., and Harrison, S. C. (2004) Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319 (Pubitemid 38133652)
    • (2004) Nature , vol.427 , Issue.6972 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 10
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: Structure and maturation
    • DOI 10.1126/science.1153263
    • Li, L., Lok, S. M., Yu, I. M., Zhang, Y., Kuhn, R. J., Chen, J., and Rossmann, M. G. (2008) The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 319, 1830-1834 (Pubitemid 351451591)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1830-1834
    • Li, L.1    Lok, S.-M.2    Yu, I.-M.3    Zhang, Y.4    Kuhn, R.J.5    Chen, J.6    Rossmann, M.G.7
  • 12
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • DOI 10.1126/science.1153264
    • Yu, I. M., Zhang, W., Holdaway, H. A., Li, L., Kostyuchenko, V. A., Chipman, P. R., Kuhn, R. J., Rossmann, M. G., and Chen, J. (2008) Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319, 1834-1837 (Pubitemid 351451592)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1834-1837
    • Yu, I.-M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5    Chipman, P.R.6    Kuhn, R.J.7    Rossmann, M.G.8    Chen, J.9
  • 13
    • 70450208515 scopus 로고    scopus 로고
    • Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion
    • Yu, I. M., Holdaway, H. A., Chipman, P. R., Kuhn, R. J., Rossmann, M. G., and Chen, J. (2009) Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J. Virol. 83, 12101-12107
    • (2009) J. Virol. , vol.83 , pp. 12101-12107
    • Yu, I.M.1    Holdaway, H.A.2    Chipman, P.R.3    Kuhn, R.J.4    Rossmann, M.G.5    Chen, J.6
  • 14
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • Allison, S. L., Schalich, J., Stiasny, K., Mandl, C. W., Kunz, C., and Heinz, F. X. (1995) Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J. Virol. 69, 695-700
    • (1995) J. Virol. , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 15
    • 58149388463 scopus 로고    scopus 로고
    • Functional importance of dengue virus maturation: Infectious properties of immature virions
    • Zybert, I. A., van der Ende-Metselaar, H., Wilschut, J., and Smit, J. M. (2008) Functional importance of dengue virus maturation: infectious properties of immature virions. J. Gen. Virol. 89, 3047-3051
    • (2008) J. Gen. Virol. , vol.89 , pp. 3047-3051
    • Zybert, I.A.1    Van Der Ende-Metselaar, H.2    Wilschut, J.3    Smit, J.M.4
  • 16
    • 55549118226 scopus 로고    scopus 로고
    • Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides
    • Chan, R., Uchil, P. D., Jin, J., Shui, G., Ott, D. E., Mothes, W., and Wenk, M. R. (2008) Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides. J. Virol. 82, 11228 -11238
    • (2008) J. Virol. , vol.82 , pp. 11228-11238
    • Chan, R.1    Uchil, P.D.2    Jin, J.3    Shui, G.4    Ott, D.E.5    Mothes, W.6    Wenk, M.R.7
  • 17
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and Dyer, W. J. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37, 911-917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 18
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M. A., Chacón, P., Merelo, J. J., and Morán, F. (1993) Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6, 383-390 (Pubitemid 23197398)
    • (1993) Protein Engineering , vol.6 , Issue.4 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 19
    • 33947368167 scopus 로고    scopus 로고
    • O ATPase from Aedes albopictus
    • DOI 10.1016/j.pep.2007.01.009, PII S104659280700023X
    • Hunke, C., Chen, W. J., Schäfer, H. J., and Grüber, G. (2007) Cloning, purification, and nucleotide-binding traits of the catalytic subunit A of the V1VO ATPase from Aedes albopictus. Protein Expr. Purif. 53, 378-383 (Pubitemid 46453215)
    • (2007) Protein Expression and Purification , vol.53 , Issue.2 , pp. 378-383
    • Hunke, C.1    Chen, W.-J.2    Schafer, H.-J.3    Gruber, G.4
  • 20
    • 30744453243 scopus 로고    scopus 로고
    • Versatile interactions of the antimicrobial peptide novispirin with detergents and lipids
    • DOI 10.1021/bi051876r
    • Wimmer, R., Andersen, K. K., Vad, B., Davidsen, M., Mølgaard, S., Nesgaard, L. W., Kristensen, H. H., and Otzen, D. E. (2006) Versatile interactions of the antimicrobial peptide novispirin with detergents and lipids. Biochemistry 45, 481-497 (Pubitemid 43100414)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 481-497
    • Wimmer, R.1    Andersen, K.K.2    Vad, B.3    Davidsen, M.4    Molgaard, S.5    Nesgaard, L.W.6    Kristensen, H.H.7    Otzen, D.E.8
  • 21
  • 22
    • 0016156587 scopus 로고
    • Studies on the lipid composition of the rat liver endoplasmic reticulum after induction with phenobarbitone and 20-methylcholanthrene
    • Davison, S. C., and Wills, E. D. (1974) Studies on the lipid composition of the rat liver endoplasmic reticulum after induction with phenobarbitone and 20-methylcholanthrene. Biochem. J. 140, 461-468
    • (1974) Biochem. J. , vol.140 , pp. 461-468
    • Davison, S.C.1    Wills, E.D.2
  • 24
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • DOI 10.1093/nar/gkh381
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-667 (Pubitemid 38997419)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 25
    • 33749266195 scopus 로고    scopus 로고
    • The Role of Histidine Residues in Low-pH-Mediated Viral Membrane Fusion
    • DOI 10.1016/j.str.2006.07.011, PII S096921260600356X
    • Kampmann, T., Mueller, D. S., Mark, A. E., Young, P. R., and Kobe, B. (2006) The role of histidine residues in low-pH-mediated viral membrane fusion. Structure 14, 1481-1487 (Pubitemid 44486813)
    • (2006) Structure , vol.14 , Issue.10 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.