메뉴 건너뛰기




Volumn 99, Issue 6, 2010, Pages 1764-1772

Structural Role of the Conserved Cysteines in the Dimerization of the Viral Transmembrane Oncoprotein E5

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE PAPILLOMAVIRUS TYPE 1;

EID: 77957366876     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.06.073     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0023100261 scopus 로고
    • Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
    • Yarden, Y., and J. Schlessinger. 1987. Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor. Biochemistry. 26:1443-1451.
    • (1987) Biochemistry. , vol.26 , pp. 1443-1451
    • Yarden, Y.1    Schlessinger, J.2
  • 2
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell. 61:203-212.
    • (1990) Cell. , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 3
    • 0023156382 scopus 로고
    • Self-phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation
    • Yarden, Y., and J. Schlessinger. 1987. Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation. Biochemistry. 26:1434-1442.
    • (1987) Biochemistry. , vol.26 , pp. 1434-1442
    • Yarden, Y.1    Schlessinger, J.2
  • 4
    • 0037429737 scopus 로고    scopus 로고
    • Epidermal growth factor receptor: Mechanisms of activation and signalling
    • Jorissen, R. N., F. Walker, A. W. Burgess. 2003. Epidermal growth factor receptor: mechanisms of activation and signalling. Exp. Cell Res. 284:31-53.
    • (2003) Exp. Cell Res. , vol.284 , pp. 31-53
    • Jorissen, R.N.1    Walker, F.2    Burgess, A.W.3
  • 5
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. 2000. Cell signaling by receptor tyrosine kinases. Cell.103:211-225.
    • (2000) Cell. , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 6
    • 0026069052 scopus 로고
    • Activation of the platelet-derived growth factor receptor by the bovine papillomavirus e5 transforming protein
    • Petti, L., L. A. Nilson, and D. DiMaio. 1991. Activation of the platelet- derived growth factor receptor by the bovine papillomavirus E5 transforming protein. EMBO J. 10:845-855.
    • (1991) EMBO J. , vol.10 , pp. 845-855
    • Petti, L.1    Nilson, L.A.2    Dimaio, D.3
  • 7
    • 0022539283 scopus 로고
    • The E5 transforming gene of bovine papillomavirus encodes a small, hydrophobic poly-peptide
    • Schlegel, R., M. Wade-Glass, Y. C. Yang. 1986. The E5 transforming gene of bovine papillomavirus encodes a small, hydrophobic poly-peptide. Science. 233:464-467.
    • (1986) Science. , vol.233 , pp. 464-467
    • Schlegel, R.1    Wade-Glass, M.2    Yang, Y.C.3
  • 8
    • 0032387826 scopus 로고    scopus 로고
    • Structural models of the bovine papillomavirus E5 protein
    • Surti, T., O. Klein, S. O. Smith. 1998. Structural models of the bovine papillomavirus E5 protein. Proteins. 33:601-612.
    • (1998) Proteins. , vol.33 , pp. 601-612
    • Surti, T.1    Klein, O.2    Smith, S.O.3
  • 9
    • 50149103930 scopus 로고    scopus 로고
    • In vitro dimerization of the bovine papillomavirus E5 protein transmembrane domain
    • Oates, J., M. Hicks, A. M. Dixon. 2008. In vitro dimerization of the bovine papillomavirus E5 protein transmembrane domain. Biochemistry. 47:8985-8992.
    • (2008) Biochemistry. , vol.47 , pp. 8985-8992
    • Oates, J.1    Hicks, M.2    Dixon, A.M.3
  • 10
    • 0023181357 scopus 로고
    • Human papillomavirus infections in women with and without abnormal cervical cytology
    • de Villiers, E. M., D. Wagner, H. zur Hausen. 1987. Human papillomavirus infections in women with and without abnormal cervical cytology. Lancet. 2:703-706.
    • (1987) Lancet. , vol.2 , pp. 703-706
    • De Villiers, E.M.1    Wagner, D.2    Zur Hausen, H.3
  • 11
    • 0023390931 scopus 로고
    • Genetic and biochemical definition of the bovine papillomavirus E5 transforming protein
    • Burkhardt, A., D. DiMaio, and R. Schlegel. 1987. Genetic and biochemical definition of the bovine papillomavirus E5 transforming protein. EMBO J. 6:2381-2385.
    • (1987) EMBO J. , vol.6 , pp. 2381-2385
    • Burkhardt, A.1    Dimaio, D.2    Schlegel, R.3
  • 12
    • 0028341252 scopus 로고
    • Specific interaction between the bovine papillomavirus E5 transforming protein and the β receptor for platelet-derived growth factor in stably transformed and acutely transfected cells
    • Petti, L., and D. DiMaio. 1994. Specific interaction between the bovine papillomavirus E5 transforming protein and the β receptor for platelet- derived growth factor in stably transformed and acutely transfected cells. J. Virol. 68:3582-3592.
    • (1994) J. Virol. , vol.68 , pp. 3582-3592
    • Petti, L.1    Dimaio, D.2
  • 13
    • 0024448561 scopus 로고
    • The bovine papillomavirus E5 transforming protein can stimulate the transforming activity of EGF and CSF-1 receptors
    • Martin, P., W. C. Vass, T. J. Velu. 1989. The bovine papillomavirus E5 transforming protein can stimulate the transforming activity of EGF and CSF-1 receptors. Cell. 59:21-32.
    • (1989) Cell. , vol.59 , pp. 21-32
    • Martin, P.1    Vass, W.C.2    Velu, T.J.3
  • 16
    • 0027052188 scopus 로고
    • The bpv-1 E5 protein, the 16 kDa membrane pore-forming protein and the pdgf receptor exist in a complex that is dependent on hydrophobic trans-membrane interactions
    • Goldstein, D. J., T. Andresson, .., R. Schlegel. 1992. The BPV-1 E5 protein, the 16 kDa membrane pore-forming protein and the PDGF receptor exist in a complex that is dependent on hydrophobic trans- membrane interactions. EMBO J. 11:4851-4859.
    • (1992) EMBO J. , vol.11 , pp. 4851-4859
    • Goldstein, D.J.1    Andresson, T.2    Schlegel, R.3
  • 17
    • 0023761323 scopus 로고
    • 44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids
    • Horwitz, B. H., A. L. Burkhardt, D. DiMaio. 1988. 44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids. Mol. Cell. Biol. 8:4071-4078.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4071-4078
    • Horwitz, B.H.1    Burkhardt, A.L.2    Dimaio, D.3
  • 18
    • 0024428921 scopus 로고
    • Mutational analysis of bovine papillomavirus type 1 E5 peptide domains involved in induction of cellular dna synthesis. J
    • Rawls, J. A., P. M. Loewenstein, and M. Green. 1989. Mutational analysis of bovine papillomavirus type 1 E5 peptide domains involved in induction of cellular DNA synthesis. J. Virol. 63:4962-4964.
    • (1989) Virol. , vol.63 , pp. 4962-4964
    • Rawls, J.A.1    Loewenstein, P.M.2    Green, M.3
  • 19
    • 0028338904 scopus 로고
    • Cellular transformation by a transmembrane peptide: Structural requirements for the bovine papillomavirus E5 oncoprotein
    • Meyer, A. N., Y. F. Xu, D. J. Donoghue. 1994. Cellular transformation by a transmembrane peptide: structural requirements for the bovine papillomavirus E5 oncoprotein. Proc. Natl. Acad. Sci. USA. 91:4634-4638.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 4634-4638
    • Meyer, A.N.1    Xu, Y.F.2    Donoghue, D.J.3
  • 20
    • 0024368259 scopus 로고
    • Genetic evidence that acute morphologic transformation, induction of cellular dna synthesis, and focus formation are mediated by a single activity of the bovine papillomavirus E5 protein
    • Settleman, J., A. Fazeli, D. DiMaio. 1989. Genetic evidence that acute morphologic transformation, induction of cellular DNA synthesis, and focus formation are mediated by a single activity of the bovine papillomavirus E5 protein. Mol. Cell. Biol. 9:5563-5572.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5563-5572
    • Settleman, J.1    Fazeli, A.2    Dimaio, D.3
  • 21
    • 0029125484 scopus 로고
    • Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous b receptor for platelet-derived growth factor in mouse C127 cells
    • Nilson, L. A., R. L. Gottlieb, D. DiMaio. 1995. Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous b receptor for platelet-derived growth factor in mouse C127 cells. J. Virol. 69:5869-5874.
    • (1995) J. Virol. , vol.69 , pp. 5869-5874
    • Nilson, L.A.1    Gottlieb, R.L.2    Dimaio, D.3
  • 22
    • 0035963317 scopus 로고    scopus 로고
    • Identification of the trans- membrane dimer interface of the bovine papillomavirus E5 protein
    • Mattoon, D., K. Gupta, .., D. DiMaio. 2001. Identification of the trans- membrane dimer interface of the bovine papillomavirus E5 protein. Oncogene. 20:3824-3834.
    • (2001) Oncogene. , vol.20 , pp. 3824-3834
    • Mattoon, D.1    Gupta, K.2    Dimaio, D.3
  • 23
    • 70349279951 scopus 로고    scopus 로고
    • Artificial transmembrane oncoproteins smaller than the bovine papillomavirus E5 protein redefine sequence requirements for activation of the platelet- derived growth factor b receptor
    • Talbert-Slagle, K., S. Marlatt, D. Dimaio. 2009. Artificial transmembrane oncoproteins smaller than the bovine papillomavirus E5 protein redefine sequence requirements for activation of the platelet- derived growth factor b receptor. J. Virol. 83:9773-9785.
    • (2009) J. Virol. , vol.83 , pp. 9773-9785
    • Talbert-Slagle, K.1    Marlatt, S.2    Dimaio, D.3
  • 24
    • 0017873186 scopus 로고
    • Translation of the leader region of the Escherichia coli tryptophan operon
    • Miozzari, G. F., and C. Yanofsky. 1978. Translation of the leader region of the Escherichia coli tryptophan operon. J. Bacteriol. 133:1457-1466. (Pubitemid 8297007)
    • (1978) Journal of Bacteriology , vol.133 , Issue.3 , pp. 1457-1466
    • Miozzari, G.F.1    Yanofsky, C.2
  • 25
    • 34948880704 scopus 로고    scopus 로고
    • Structure analysis of the protein translocating channel tata in membranes using a multi-construct approach
    • Lange, C., S. D. Müller, A.S. Ulrich. 2007. Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach. Biochim. Biophys. Acta. 1768:2627-2634.
    • (2007) Biochim. Biophys. Acta. , vol.1768 , pp. 2627-2634
    • Lange, C.1    Müller, S.D.2    Ulrich, A.S.3
  • 26
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S. W., and J. Glockner. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:33-37.
    • (1981) Biochemistry. , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 27
    • 0025204703 scopus 로고
    • Estimation of protein secondary structure and error analysis from circular dichroism spectra
    • van Stokkum, I. H., H. J. Spoelder, F. C. Groen. 1990. Estimation of protein secondary structure and error analysis from circular dichroism spectra. Anal. Biochem. 191:110-118.
    • (1990) Anal. Biochem. , vol.191 , pp. 110-118
    • Van Stokkum, I.H.1    Spoelder, H.J.2    Groen, F.C.3
  • 28
    • 0034672325 scopus 로고    scopus 로고
    • Estimation ofprotein secondary structure from circular dichroism spectra: Comparison of contin, selcon, and cdsstr methods with an expanded reference set
    • Sreerama, N., and R. W. Woody. 2000. Estimation ofprotein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287:252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 29
    • 0036168995 scopus 로고    scopus 로고
    • Dichroweb: Aninteractive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley, A., L. Whitmore, and B. A. Wallace. 2002. DICHROWEB: aninteractive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics. 18:211-212.
    • (2002) Bioinformatics. , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 30
    • 3242877618 scopus 로고    scopus 로고
    • Dichroweb, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and B. A. Wallace. 2004. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32(Web Server issue):W668-W673.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.WEB SERVER ISSUE
    • Whitmore, L.1    Wallace, B.A.2
  • 31
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., F. Vajdos, T. Gray. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4:2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Gray, T.3
  • 32
    • 0001553959 scopus 로고
    • Evidence for an α II-type helical conformation for bacteriorhodopsin in the purple membrane
    • Gibson, N. J., and J. Y. Cassim. 1989. Evidence for an α II-type helical conformation for bacteriorhodopsin in the purple membrane. Biochemistry. 28:2134-2139.
    • (1989) Biochemistry. , vol.28 , pp. 2134-2139
    • Gibson, N.J.1    Cassim, J.Y.2
  • 33
    • 56049103780 scopus 로고    scopus 로고
    • Conformation and membrane orientation of amphiphilic helical peptides by oriented circular dichroism
    • Bürck, J., S. Roth, A. S. Ulrich. 2008. Conformation and membrane orientation of amphiphilic helical peptides by oriented circular dichroism. Biophys. J. 95:3872-3881.
    • (2008) Biophys. J. , vol.95 , pp. 3872-3881
    • Bürck, J.1    Roth, S.2    Ulrich, A.S.3
  • 34
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • Wu, Y., H. W. Huang, and G. A. Olah. 1990. Method of oriented circular dichroism. Biophys. J. 57:797-806.
    • (1990) Biophys. J. , vol.57 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3
  • 35
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F. Y., M. T. Lee, and H. W. Huang. 2002. Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin. Biophys. J. 82:908-914.
    • (2002) Biophys. J. , vol.82 , pp. 908-914
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 36
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., C. S. Wu, and H. M. Martinez. 1986. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130: 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 38
    • 0027275516 scopus 로고
    • Comparison of antiparallel and parallel two-stranded a-helical coiled-coils. Design, synthesis, and characterization
    • Monera, O. D., N. E. Zhou, .., R. S. Hodges. 1993. Comparison of antiparallel and parallel two-stranded a-helical coiled-coils. Design, synthesis, and characterization. J. Biol. Chem. 268:19218-19227.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19218-19227
    • Monera, O.D.1    Zhou, N.E.2    Hodges, R.S.3
  • 39
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao, D., and B. A. Wallace. 1984. Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry. 23:2667-2673.
    • (1984) Biochemistry. , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 40
    • 0023248806 scopus 로고
    • Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes
    • Vogel, H. 1987. Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes. Biochemistry. 26:4562-4572.
    • (1987) Biochemistry. , vol.26 , pp. 4562-4572
    • Vogel, H.1
  • 41
    • 0034738609 scopus 로고    scopus 로고
    • Oriented circular dichroism of a class a amphipathic helix in aligned phospholipid multilayers
    • Clayton, A. H., and W. H. Sawyer. 2000. Oriented circular dichroism of a class A amphipathic helix in aligned phospholipid multilayers. Biochim. Biophys. Acta. 1467:124-130.
    • (2000) Biochim. Biophys. Acta. , vol.1467 , pp. 124-130
    • Clayton, A.H.1    Sawyer, W.H.2
  • 42
    • 0031826040 scopus 로고    scopus 로고
    • Sosui: Classification and secondary structure prediction system for membrane proteins
    • Hirokawa, T., S. Boon-Chieng, and S. Mitaku. 1998. SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics. 14:378-379.
    • (1998) Bioinformatics. , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 43
    • 0035910270 scopus 로고    scopus 로고
    • Predicting trans-membrane protein topology with a hidden markov model: Application to complete genomes
    • Krogh, A., B. Larsson, E. L. Sonnhammer. 2001. Predicting trans-membrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Sonnhammer, E.L.3
  • 44
    • 0037379159 scopus 로고    scopus 로고
    • Analyses of circular dichroism spectra of membrane proteins
    • Wallace, B. A., J. G. Lees, R. W. Janes. 2003. Analyses of circular dichroism spectra of membrane proteins. Protein Sci. 12:875-884.
    • (2003) Protein Sci. , vol.12 , pp. 875-884
    • Wallace, B.A.1    Lees, J.G.2    Janes, R.W.3
  • 45
    • 33644533148 scopus 로고    scopus 로고
    • Random coils, β-sheet ribbons, and α-helical fibers: One peptide adopting three different secondary structures at will
    • Pagel, K., S. C. Wagner, B. Koksch. 2006. Random coils, β-sheet ribbons, and α-helical fibers: one peptide adopting three different secondary structures at will. J. Am. Chem. Soc. 128:2196-2197.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2196-2197
    • Pagel, K.1    Wagner, S.C.2    Koksch, B.3
  • 46
    • 0035194257 scopus 로고    scopus 로고
    • De novo design of fibrils made of short a-helical coiled coil peptides
    • Potekhin, S. A., T. N. Melnik, A. V. Kajava. 2001. De novo design of fibrils made of short a-helical coiled coil peptides. Chem. Biol. 8:1025-1032.
    • (2001) Chem. Biol. , vol.8 , pp. 1025-1032
    • Potekhin, S.A.1    Melnik, T.N.2    Kajava, A.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.