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Volumn 30, Issue 1, 2003, Pages 1-10

Overexpression, purification, and structural analysis of the hydrophobic E5 protein from human papillomavirus type 16

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; HUMAN PAPILLOMAVIRUS; HUMAN PAPILLOMAVIRUS TYPE 16; HUMAN PAPILLOMAVIRUS TYPES; PAPILLOMAVIRUS;

EID: 0038349054     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(03)00049-4     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 0030577120 scopus 로고    scopus 로고
    • Papillomavirus infections - A major cause of human cancers
    • H. zur Hausen, Papillomavirus infections - a major cause of human cancers, Biochim. Biophys. Acta 1288 (1996) F55-F78.
    • (1996) Biochim. Biophys. Acta , vol.1288
    • Zur Hausen, H.1
  • 2
    • 0034600355 scopus 로고    scopus 로고
    • Papillomaviruses causing cancer: Evasion from host-cell control in early events in carcinogenesis
    • H. zur Hausen, Papillomaviruses causing cancer: evasion from host-cell control in early events in carcinogenesis, J. Natl. Cancer Inst. 92 (2000) 690-698.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 690-698
    • Zur Hausen, H.1
  • 3
    • 0035956257 scopus 로고    scopus 로고
    • Mechanisms of cell transformation by papillomavirus E5 proteins
    • D. DiMaio, D. Mattoon, Mechanisms of cell transformation by papillomavirus E5 proteins, Oncogene 20 (2001) 7866-7873.
    • (2001) Oncogene , vol.20 , pp. 7866-7873
    • DiMaio, D.1    Mattoon, D.2
  • 5
    • 0024459020 scopus 로고
    • Heterogeneity of the human papillomavirus group
    • E.M. De Villiers, Heterogeneity of the human papillomavirus group, J. Virol. 63 (1989) 4898-4903.
    • (1989) J. Virol. , vol.63 , pp. 4898-4903
    • De Villiers, E.M.1
  • 7
    • 0023871067 scopus 로고
    • DNA sequence of the HPV-16 E5 ORF and the structural conservation of its encoded protein
    • V. Bubb, D.J. McCance, R. Schlegel, DNA sequence of the HPV-16 E5 ORF and the structural conservation of its encoded protein, Virology 163 (1988) 243-246.
    • (1988) Virology , vol.163 , pp. 243-246
    • Bubb, V.1    McCance, D.J.2    Schlegel, R.3
  • 8
    • 0027323269 scopus 로고
    • The human papillomavirus type 6 and 16 E5 proteins are membrane-associated proteins which associate with the 16-kilodalton pore-forming protein
    • M. Conrad, V.J. Bubb, R. Schlegel, The human papillomavirus type 6 and 16 E5 proteins are membrane-associated proteins which associate with the 16-kilodalton pore-forming protein, J. Virol. 67 (1993) 6170-6178.
    • (1993) J. Virol. , vol.67 , pp. 6170-6178
    • Conrad, M.1    Bubb, V.J.2    Schlegel, R.3
  • 9
    • 0029007034 scopus 로고
    • E5 oncoprotein retained in the endoplasmic reticulum/cis Golgi still induces PDGF receptor autophosphorylation but does not transform cells
    • J. Sparkowski, J. Anders, R. Schlegel, E5 oncoprotein retained in the endoplasmic reticulum/cis Golgi still induces PDGF receptor autophosphorylation but does not transform cells, EMBO J. 14 (1995) 3055-3063.
    • (1995) EMBO J. , vol.14 , pp. 3055-3063
    • Sparkowski, J.1    Anders, J.2    Schlegel, R.3
  • 10
    • 0018868889 scopus 로고
    • A quantitative in vitro focus assay for bovine papilloma virus
    • I. Dvoretzky, R. Shober, S.K. Chattopadhyay, D.R. Lowy, A quantitative in vitro focus assay for bovine papilloma virus, Virology 103 (1980) 369-375.
    • (1980) Virology , vol.103 , pp. 369-375
    • Dvoretzky, I.1    Shober, R.2    Chattopadhyay, S.K.3    Lowy, D.R.4
  • 11
    • 0022539283 scopus 로고
    • The E5 transforming gene of bovine papillomavirus encodes a small, hydrophobic polypeptide
    • R. Schlegel, M. Wade-Glass, M.S. Rabson, Y.C. Yang, The E5 transforming gene of bovine papillomavirus encodes a small, hydrophobic polypeptide, Science 233 (1986) 464-467.
    • (1986) Science , vol.233 , pp. 464-467
    • Schlegel, R.1    Wade-Glass, M.2    Rabson, M.S.3    Yang, Y.C.4
  • 12
    • 0032387826 scopus 로고    scopus 로고
    • Structural models of the bovine papillomavirus E5 protein
    • T. Surti, O. Klein, K. Aschheim, D. DiMaio, S.O. Smith, Structural models of the bovine papillomavirus E5 protein, Proteins 33 (1998) 601-612.
    • (1998) Proteins , vol.33 , pp. 601-612
    • Surti, T.1    Klein, O.2    Aschheim, K.3    DiMaio, D.4    Smith, S.O.5
  • 13
    • 0031691070 scopus 로고    scopus 로고
    • Role of glutamine 17 of the bovine papillomavirus E5 protein in platelet-derived growth factor β receptor activation and cell transformation
    • O. Klein, G.W. Polack, T. Surti, D. Kegler-Ebo, S.O. Smith, D. DiMaio, Role of glutamine 17 of the bovine papillomavirus E5 protein in platelet-derived growth factor β receptor activation and cell transformation, J. Virol. 72 (1998) 8921-8932.
    • (1998) J. Virol. , vol.72 , pp. 8921-8932
    • Klein, O.1    Polack, G.W.2    Surti, T.3    Kegler-Ebo, D.4    Smith, S.O.5    DiMaio, D.6
  • 15
    • 0025138723 scopus 로고
    • The E5 oncoprotein of bovine papillomavirus binds to a 16kd cellular protein
    • D.J. Goldstein, R. Schlegel, The E5 oncoprotein of bovine papillomavirus binds to a 16kd cellular protein, EMBO J. 9 (1990) 137-145.
    • (1990) EMBO J. , vol.9 , pp. 137-145
    • Goldstein, D.J.1    Schlegel, R.2
  • 16
    • 0026586144 scopus 로고
    • The E5 gene from human papillomavirus type 16 is an oncogene which enhances growth factor-mediated signal transduction to the nucleus
    • P. Leechanachai, L. Banks, F. Moreau, G. Matlashewski, The E5 gene from human papillomavirus type 16 is an oncogene which enhances growth factor-mediated signal transduction to the nucleus, Oncogene 7 (1992) 19-25.
    • (1992) Oncogene , vol.7 , pp. 19-25
    • Leechanachai, P.1    Banks, L.2    Moreau, F.3    Matlashewski, G.4
  • 17
    • 0031818511 scopus 로고    scopus 로고
    • The human papillomavirus type 16 E5-protein modulates ligand-dependent activation of the EGF receptor family in the human epithelial cell line HaCaT
    • K. Crusius, E. Auvinen, B. Steuer, H. Gaissert, A. Alonso, The human papillomavirus type 16 E5-protein modulates ligand-dependent activation of the EGF receptor family in the human epithelial cell line HaCaT, Exp. Cell Res. 241 (1998) 76-83.
    • (1998) Exp. Cell Res. , vol.241 , pp. 76-83
    • Crusius, K.1    Auvinen, E.2    Steuer, B.3    Gaissert, H.4    Alonso, A.5
  • 18
    • 0029133598 scopus 로고
    • The HPV16 E5 protein: Expression, detection, and stable complex formation with transmembrane proteins in COS cells
    • E.S. Hwang, T. Nottoli, D. DiMaio, The HPV16 E5 protein: expression, detection, and stable complex formation with transmembrane proteins in COS cells, Virology 211 (1995) 227-233.
    • (1995) Virology , vol.211 , pp. 227-233
    • Hwang, E.S.1    Nottoli, T.2    DiMaio, D.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, J. Gordon, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 23
    • 0022342136 scopus 로고
    • Reconstitution of lymphocyte 5′-nucleotidase in lipid bilayers: Behaviour and interaction with concanavalin A
    • F.J. Sharom, I. Lorimer, M.P. Lamb, Reconstitution of lymphocyte 5′-nucleotidase in lipid bilayers: behaviour and interaction with concanavalin A, Can. J. Biochem. Cell Biol. 63 (1985) 1049-1057.
    • (1985) Can. J. Biochem. Cell Biol. , vol.63 , pp. 1049-1057
    • Sharom, F.J.1    Lorimer, I.2    Lamb, M.P.3
  • 24
    • 0030341893 scopus 로고    scopus 로고
    • Modulation of the cleavage of glycosylphosphatidylinositol-anchored proteins by specific bacterial phospholipases
    • F.J. Sharom, G.L. McNeil, J.R. Glover, S. Seier, Modulation of the cleavage of glycosylphosphatidylinositol-anchored proteins by specific bacterial phospholipases, Biochem. Cell Biol. 74 (1996) 701-713.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 701-713
    • Sharom, F.J.1    McNeil, G.L.2    Glover, J.R.3    Seier, S.4
  • 25
    • 0026620724 scopus 로고
    • Glycophorin A interacts with interleukin-2 and inhibits interleukin-2- dependent T-lymphocyte proliferation
    • J.W.K. Chu, F.J. Sharom, Glycophorin A interacts with interleukin-2 and inhibits interleukin-2- dependent T-lymphocyte proliferation, Cell Immunol. 145 (1992) 223-239.
    • (1992) Cell Immunol. , vol.145 , pp. 223-239
    • Chu, J.W.K.1    Sharom, F.J.2
  • 26
    • 0037192130 scopus 로고    scopus 로고
    • PI-specific phospholipase C cleavage of a reconstituted GPI-anchored protein: Modulation by the lipid bilayer
    • M.T. Lehto, F.J. Sharom, PI-specific phospholipase C cleavage of a reconstituted GPI-anchored protein: modulation by the lipid bilayer, Biochemistry 41 (2002) 1398-1408.
    • (2002) Biochemistry , vol.41 , pp. 1398-1408
    • Lehto, M.T.1    Sharom, F.J.2
  • 27
    • 0037008103 scopus 로고    scopus 로고
    • Proximity of the protein moiety of a GPI-anchored protein to the membrane surface: A FRET study
    • M.T. Lehto, F.J. Sharom, Proximity of the protein moiety of a GPI-anchored protein to the membrane surface: a FRET study, Biochemistry 41 (2002) 8368-8376.
    • (2002) Biochemistry , vol.41 , pp. 8368-8376
    • Lehto, M.T.1    Sharom, F.J.2
  • 28
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • N.J. Greenfield, Methods to estimate the conformation of proteins and polypeptides from circular dichroism data, Anal. Biochem. 235 (1996) 1-10.
    • (1996) Anal. Biochem. , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 30
    • 0028037934 scopus 로고
    • Detection of E5 oncoprotein in human papillomavirus type 16-positive cervical scrapes using antibodies raised to synthetic peptides
    • B. Kell, R.J. Jewers, J. Cason, F. Pakarian, J.N. Kaye, J.M Best, Detection of E5 oncoprotein in human papillomavirus type 16-positive cervical scrapes using antibodies raised to synthetic peptides, J. Gen. Virol. 75 (1994) 2451-2456.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2451-2456
    • Kell, B.1    Jewers, R.J.2    Cason, J.3    Pakarian, F.4    Kaye, J.N.5    Best, J.M.6
  • 32
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane α-helix dimerization
    • K.G. Fleming, A.L. Ackerman, D.M. Engelman, The effect of point mutations on the free energy of transmembrane α-helix dimerization, J. Mol. Biol. 272 (1997) 266-275.
    • (1997) J. Mol. Biol. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 33
    • 0024505028 scopus 로고
    • A point mutation in the neu oncogene mimics ligand induction of receptor aggregation
    • D.B. Weiner, J. Liu, J.A Cohen, W.V. Williams, M.I. Greene, A point mutation in the neu oncogene mimics ligand induction of receptor aggregation, Nature 339 (1989) 230-231.
    • (1989) Nature , vol.339 , pp. 230-231
    • Weiner, D.B.1    Liu, J.2    Cohen, J.A.3    Williams, W.V.4    Greene, M.I.5
  • 34
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • K.R. MacKenzie, J.H. Prestegard, D.M. Engelman, A transmembrane helix dimer: structure and implications, Science 276 (1997) 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 35
    • 0024976405 scopus 로고
    • Neu receptor dimerization
    • M.J. Sternberg, W.J. Gullick, Neu receptor dimerization, Nature 339 (1989) 587.
    • (1989) Nature , vol.339 , pp. 587
    • Sternberg, M.J.1    Gullick, W.J.2
  • 36
    • 0023761323 scopus 로고
    • 44-Amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids
    • B.H. Horwitz, A.L. Burkhardt, R. Schlegel, D. DiMaio, 44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids, Mol. Cell Biol. 8 (1988) 4071-4078.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 4071-4078
    • Horwitz, B.H.1    Burkhardt, A.L.2    Schlegel, R.3    DiMaio, D.4
  • 37
    • 0026541315 scopus 로고
    • The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine
    • R. Kulke, B.H. Horwitz, T. Zibello, D. DiMaio, The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine, J. Virol. 66 (1992) 505-511.
    • (1992) J. Virol. , vol.66 , pp. 505-511
    • Kulke, R.1    Horwitz, B.H.2    Zibello, T.3    DiMaio, D.4
  • 38
    • 0029125484 scopus 로고
    • Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous β receptor for platelet-derived growth factor in mouse C127 cells
    • L.A. Nilson, R.L. Gottlieb, G.W. Polack, D. DiMaio, Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous β receptor for platelet-derived growth factor in mouse C127 cells, J. Virol. 69 (1995) 5869-5874.
    • (1995) J. Virol. , vol.69 , pp. 5869-5874
    • Nilson, L.A.1    Gottlieb, R.L.2    Polack, G.W.3    DiMaio, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.