메뉴 건너뛰기




Volumn 93, Issue 2, 2011, Pages 254-259

Nanoscale topography of hepatitis B antigen particles by atomic force microscopy

Author keywords

Atomic force microscopy; Envelope; Hepatitis B virus; Structure; Vaccine

Indexed keywords

HEPATITIS B ANTIGEN;

EID: 78651298021     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.09.018     Document Type: Article
Times cited : (33)

References (23)
  • 1
    • 9644260511 scopus 로고    scopus 로고
    • Envelopment of the hepatitis B virus nucleocapsid
    • V. Bruss Envelopment of the hepatitis B virus nucleocapsid Virus Res. 106 2004 199 209
    • (2004) Virus Res. , vol.106 , pp. 199-209
    • Bruss, V.1
  • 2
    • 0026034960 scopus 로고
    • The role of envelope proteins in hepatitis B virus assembly
    • V. Bruss, and D. Ganem The role of envelope proteins in hepatitis B virus assembly Proc. Natl. Acad. Sci. U.S.A. 88 1991 1059 1063
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1059-1063
    • Bruss, V.1    Ganem, D.2
  • 4
    • 0002843412 scopus 로고
    • Model for the protein arrangement in HBsAg particles based on physical and chemical studies
    • E. Guerrero, F. Gavilanes, and D.L. Peterson Model for the protein arrangement in HBsAg particles based on physical and chemical studies A.J. Zuckerman, Viral Hepatitis and Liver Disease 1988 Alan R. Liss, Inc New York 606 613
    • (1988) Viral Hepatitis and Liver Disease , pp. 606-613
    • Guerrero, E.1    Gavilanes, F.2    Peterson, D.L.3
  • 5
    • 0026773810 scopus 로고
    • A topological model for hepatitis B surface antigen
    • H.J. Stirk, J.M. Thornton, and C.R. Howard A topological model for hepatitis B surface antigen Intervirology 33 1992 148 158
    • (1992) Intervirology , vol.33 , pp. 148-158
    • Stirk, H.J.1    Thornton, J.M.2    Howard, C.R.3
  • 8
    • 0025327583 scopus 로고
    • The antigenic structure of HBsAg: Study of the d/y subtype determinant by chemical modification and site directed mutagenesis
    • E. Guerrero, P.D. Swenson, P.S. Hu, and D.L. Peterson The antigenic structure of HBsAg: study of the d/y subtype determinant by chemical modification and site directed mutagenesis Mol. Immunol. 27 1990 435 441
    • (1990) Mol. Immunol. , vol.27 , pp. 435-441
    • Guerrero, E.1    Swenson, P.D.2    Hu, P.S.3    Peterson, D.L.4
  • 9
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • S.A. Wynne, R.A. Crowther, and A.G. Leslie The crystal structure of the human hepatitis B virus capsid Mol. Cell 3 1999 771 780
    • (1999) Mol. Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 11
    • 67349183743 scopus 로고    scopus 로고
    • Structure of hepatitis B surface antigen from subviral tubes determined by electron cryomicroscopy
    • J.M. Short, S. Chen, A.M. Roseman, P.J. Butler, and R.A. Crowther Structure of hepatitis B surface antigen from subviral tubes determined by electron cryomicroscopy J. Mol. Biol. 390 2009 135 141
    • (2009) J. Mol. Biol. , vol.390 , pp. 135-141
    • Short, J.M.1    Chen, S.2    Roseman, A.M.3    Butler, P.J.4    Crowther, R.A.5
  • 12
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • P. Penczek, M. Radermacher, and J. Frank Three-dimensional reconstruction of single particles embedded in ice Ultramicroscopy 40 1992 33 53
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 13
    • 0742272143 scopus 로고    scopus 로고
    • Recognition and separation of single particles with size variation by statistical analysis of their images
    • H.E. White, H.R. Saibil, A. Ignatiou, and E.V. Orlova Recognition and separation of single particles with size variation by statistical analysis of their images J. Mol. Biol. 336 2004 453 460
    • (2004) J. Mol. Biol. , vol.336 , pp. 453-460
    • White, H.E.1    Saibil, H.R.2    Ignatiou, A.3    Orlova, E.V.4
  • 14
    • 47749100886 scopus 로고    scopus 로고
    • Atomic force microscopy investigation of vaccinia virus structure
    • Y. Kuznetsov, P.D. Gershon, and A. McPherson Atomic force microscopy investigation of vaccinia virus structure J. Virol. 82 2008 7551 7566
    • (2008) J. Virol. , vol.82 , pp. 7551-7566
    • Kuznetsov, Y.1    Gershon, P.D.2    McPherson, A.3
  • 15
    • 58849147969 scopus 로고    scopus 로고
    • Atomic force microscopy of biological membranes
    • P.L. Frederix, P.D. Bosshart, and A. Engel Atomic force microscopy of biological membranes Biophys. J. 96 2009 329 338
    • (2009) Biophys. J. , vol.96 , pp. 329-338
    • Frederix, P.L.1    Bosshart, P.D.2    Engel, A.3
  • 17
    • 77949378431 scopus 로고    scopus 로고
    • Atomic force microscopy: Probing the spatial organization, interactions and elasticity of microbial cell envelopes at molecular resolution
    • S. Scheuring, and Y.F. Dufrene Atomic force microscopy: probing the spatial organization, interactions and elasticity of microbial cell envelopes at molecular resolution Mol. Microbiol. 75 2010 1327 1336
    • (2010) Mol. Microbiol. , vol.75 , pp. 1327-1336
    • Scheuring, S.1    Dufrene, Y.F.2
  • 18
    • 16644381120 scopus 로고    scopus 로고
    • Unraveling the architecture of viruses by high-resolution atomic force microscopy
    • A.J. Malkin, M. Plomp, and A. McPherson Unraveling the architecture of viruses by high-resolution atomic force microscopy Methods Mol. Biol. 292 2005 85 108
    • (2005) Methods Mol. Biol. , vol.292 , pp. 85-108
    • Malkin, A.J.1    Plomp, M.2    McPherson, A.3
  • 19
    • 33747052259 scopus 로고    scopus 로고
    • Atomic force microscopy investigation of turnip yellow mosaic virus capsid disruption and RNA extrusion
    • Y.G. Kuznetsov, and A. McPherson Atomic force microscopy investigation of turnip yellow mosaic virus capsid disruption and RNA extrusion Virology 352 2006 329 337
    • (2006) Virology , vol.352 , pp. 329-337
    • Kuznetsov, Y.G.1    McPherson, A.2
  • 22
    • 33745235141 scopus 로고    scopus 로고
    • Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-A resolution
    • G.W. Min, H.B. Wang, T.T. Sun, and X.P. Kong Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-A resolution J. Cell. Biol. 173 2006 975 983
    • (2006) J. Cell. Biol. , vol.173 , pp. 975-983
    • Min, G.W.1    Wang, H.B.2    Sun, T.T.3    Kong, X.P.4
  • 23
    • 77954657585 scopus 로고    scopus 로고
    • Characterization of the lipid and protein organization in HBsAg viral particles by steady-state and time-resolved fluorescence spectroscopy
    • V.J. Greiner, C. Egele, S. Oncul, F. Ronzon, C. Manin, A. Klymchenko, and Y. Mely Characterization of the lipid and protein organization in HBsAg viral particles by steady-state and time-resolved fluorescence spectroscopy Biochimie 92 2010 994 1002
    • (2010) Biochimie , vol.92 , pp. 994-1002
    • Greiner, V.J.1    Egele, C.2    Oncul, S.3    Ronzon, F.4    Manin, C.5    Klymchenko, A.6    Mely, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.