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Volumn 5, Issue 2, 1996, Pages 310-319

Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain

Author keywords

dimer; E2 DNA binding domain; equilibrium unfolding; human papillomavirus

Indexed keywords

DNA BINDING PROTEIN; VIRUS DNA;

EID: 0030064186     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050215     Document Type: Article
Times cited : (93)

References (25)
  • 1
    • 0019456340 scopus 로고
    • Structure of the cro repressor from bacteriophage λ and its interaction with DNA
    • Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. 1981. Structure of the cro repressor from bacteriophage λ and its interaction with DNA. Nature 290:754-758.
    • (1981) Nature , vol.290 , pp. 754-758
    • Anderson, W.F.1    Ohlendorf, D.H.2    Takeda, Y.3    Matthews, B.W.4
  • 2
    • 0026552213 scopus 로고
    • Multiphasic denaturation of the λ repressor by urea and its implications for the repressor structure
    • Banik U, Saha R, Mandal NC, Bhattacharyya B, Roy S. 1992. Multiphasic denaturation of the λ repressor by urea and its implications for the repressor structure. Eur J Biochem 206:15-21.
    • (1992) Eur J Biochem , vol.206 , pp. 15-21
    • Banik, U.1    Saha, R.2    Mandal, N.C.3    Bhattacharyya, B.4    Roy, S.5
  • 3
    • 0026695145 scopus 로고
    • Mechanism of action of the papillomavirus E2 repressor: Repression in the absence of DNA binding
    • Barsoum J, Prakash SS, Han P, Androphy EJ. 1992. Mechanism of action of the papillomavirus E2 repressor: Repression in the absence of DNA binding. J Virol 66:3941-3945.
    • (1992) J Virol , vol.66 , pp. 3941-3945
    • Barsoum, J.1    Prakash, S.S.2    Han, P.3    Androphy, E.J.4
  • 4
    • 0024962376 scopus 로고
    • Equilibrium dissociation and unfolding of the Arc repressor dimer
    • Bowie JU, Sauer RT. 1989. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28:7139-7143.
    • (1989) Biochemistry , vol.28 , pp. 7139-7143
    • Bowie, J.U.1    Sauer, R.T.2
  • 5
    • 0025336625 scopus 로고
    • Structure of Arc repressor in solution: Evidence for a family of β-sheet DNA-binding proteins
    • Breg JN, van Opheusden JHL, Burgering MJM, Boelens R, Kaptein R. 1990. Structure of Arc repressor in solution: Evidence for a family of β-sheet DNA-binding proteins. Nature 346:586-589.
    • (1990) Nature , vol.346 , pp. 586-589
    • Breg, J.N.1    Van Opheusden, J.H.L.2    Burgering, M.J.M.3    Boelens, R.4    Kaptein, R.5
  • 6
    • 77956752195 scopus 로고
    • Thermodynamic analysis of multicomponent solutions
    • Casassa EF, Eisenberg H. 1964. Thermodynamic analysis of multicomponent solutions. Adv Protein Chem 19:287-395.
    • (1964) Adv Protein Chem , vol.19 , pp. 287-395
    • Casassa, E.F.1    Eisenberg, H.2
  • 7
    • 0026335812 scopus 로고
    • Structural analysis of the human papillomavirus type 16-E2 transactivator with antipeptide antibodies reveals a high mobility region linking the transactivation and the DNA-binding domain
    • Gauthier JM, Dillner J, Yaniv M. 1991. Structural analysis of the human papillomavirus type 16-E2 transactivator with antipeptide antibodies reveals a high mobility region linking the transactivation and the DNA-binding domain. Nucleic Acids Res 19:7073-7079.
    • (1991) Nucleic Acids Res , vol.19 , pp. 7073-7079
    • Gauthier, J.M.1    Dillner, J.2    Yaniv, M.3
  • 8
    • 0026813486 scopus 로고
    • Papillomaviruses and human oncogenesis
    • Gissmann L. 1992. Papillomaviruses and human oncogenesis. Curr Opin Genet Dev 2:97-102.
    • (1992) Curr Opin Genet Dev , vol.2 , pp. 97-102
    • Gissmann, L.1
  • 10
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • Greene RF, Pace CN. 1974. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J Biol Chem 249:5388-5393.
    • (1974) J Biol Chem , vol.249 , pp. 5388-5393
    • Greene, R.F.1    Pace, C.N.2
  • 11
    • 0027080868 scopus 로고
    • Domains in λ Cro repressor. A calorimetric study
    • Griko YV, Rogov VV, Privalov PL 1992. Domains in λ Cro repressor. A calorimetric study. Biochemistry 31:12701-12705.
    • (1992) Biochemistry , vol.31 , pp. 12701-12705
    • Griko, Y.V.1    Rogov, V.V.2    Privalov, P.L.3
  • 13
    • 0025995844 scopus 로고
    • A structural taxonomy of DNA-binding domains
    • Harrison SC. 1991. A structural taxonomy of DNA-binding domains. Nature 553:715-719.
    • (1991) Nature , vol.553 , pp. 715-719
    • Harrison, S.C.1
  • 14
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 Ȧ of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • Hegde RS, Grossman SR, Laimins LA, Sigler PB. 1992. Crystal structure at 1.7 Ȧ of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target. Nature 359:505-512.
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 15
    • 0002908628 scopus 로고
    • Papillomavirinae and their replication
    • Fields BN, Knipe DM, eds. New York: Raven Press, Ltd.
    • Howley PM. 1990. Papillomavirinae and their replication. In: Fields BN, Knipe DM, eds. Virology 2nd ed. New York: Raven Press, Ltd. pp 1625-1676.
    • (1990) Virology 2nd Ed. , pp. 1625-1676
    • Howley, P.M.1
  • 16
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson WCJ. 1988. Secondary structure of proteins through circular dichroism spectroscopy. Annu Rev Biophys Biophys Chem 17:145-166.
    • (1988) Annu Rev Biophys Biophys Chem , vol.17 , pp. 145-166
    • Johnson, W.C.J.1
  • 17
    • 0015823664 scopus 로고
    • The determination of the partial specific volume of proteins by the mechanical oscillator technique
    • Kratky O, Leopold H, Stabinger H. 1973. The determination of the partial specific volume of proteins by the mechanical oscillator technique. Methods Enzymol 27:98-108.
    • (1973) Methods Enzymol , vol.27 , pp. 98-108
    • Kratky, O.1    Leopold, H.2    Stabinger, H.3
  • 18
    • 0025953354 scopus 로고
    • The papillomavirus E2 regulatory proteins
    • McBride AA, Romanczuk H, Howley PM. 1991. The papillomavirus E2 regulatory proteins. J Biol Chem 266:18411-18414.
    • (1991) J Biol Chem , vol.266 , pp. 18411-18414
    • McBride, A.A.1    Romanczuk, H.2    Howley, P.M.3
  • 19
    • 0028606077 scopus 로고
    • Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
    • Neet KE, Timm DE. 1994. Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation. Protein Sci 3:2167-2174.
    • (1994) Protein Sci , vol.3 , pp. 2167-2174
    • Neet, K.E.1    Timm, D.E.2
  • 20
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-279.
    • (1986) Methods Enzymol , vol.131 , pp. 266-279
    • Pace, C.N.1
  • 21
    • 0028904072 scopus 로고
    • Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2)
    • Ruiz-Sanz J, Prat Gay Gd, Otzen DE, Fersht AR. 1995. Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2). Biochemistry 34:1695-1701.
    • (1995) Biochemistry , vol.34 , pp. 1695-1701
    • Ruiz-Sanz, J.1    Prat Gay, Gd.2    Otzen, D.E.3    Fersht, A.R.4
  • 22
    • 0028589386 scopus 로고
    • Kinetic and equilibrium binding studies of the human papillomavirus type-16 transcription regulatory protein E2 interacting with core enhancer elements
    • Sanders CM, Maitland NJ. 1994. Kinetic and equilibrium binding studies of the human papillomavirus type-16 transcription regulatory protein E2 interacting with core enhancer elements. Nucleic Acids Res 22:4890-4897.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4890-4897
    • Sanders, C.M.1    Maitland, N.J.2
  • 24
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. 1968. Protein denaturation. Adv Prot Chem 23:121-282.
    • (1968) Adv Prot Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 25
    • 0001351894 scopus 로고
    • Rapid attainment of sedimentation equilibrium
    • van Holde KE, Baldwin RL. 1958. Rapid attainment of sedimentation equilibrium. J Phys Chem 62:734-743.
    • (1958) J Phys Chem , vol.62 , pp. 734-743
    • Van Holde, K.E.1    Baldwin, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.