메뉴 건너뛰기




Volumn 364, Issue 4, 2007, Pages 719-724

Contribution of a putative salt bridge and backbone dynamics in the structural instability of human prion protein upon R208H mutation

Author keywords

Backbone dynamics; Conformational rearrangement; Molecular dynamics; Mutation; Prion protein; R208H; Salt bridge

Indexed keywords

PRION PROTEIN;

EID: 36048995435     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.011     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner S.B. Molecular biology of prion diseases. Science 252 (1991) 1515-1522
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 2
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 6
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., and Nicholls A. Classical electrostatics in biology and chemistry. Science 268 (1995) 1144-1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 8
    • 0038266598 scopus 로고    scopus 로고
    • Atypical effect of salts on the thermodynamic stability of human prion protein
    • Apetri A.C., and Surewicz W.K. Atypical effect of salts on the thermodynamic stability of human prion protein. J. Biol. Chem. 278 (2003) 22187-22192
    • (2003) J. Biol. Chem. , vol.278 , pp. 22187-22192
    • Apetri, A.C.1    Surewicz, W.K.2
  • 9
    • 0345493918 scopus 로고    scopus 로고
    • Molecular dynamics simulations of human prion protein: importance of correct treatment of electrostatic interactions
    • Zuegg J., and Gready J.E. Molecular dynamics simulations of human prion protein: importance of correct treatment of electrostatic interactions. Biochemistry 38 (1999) 13862-13876
    • (1999) Biochemistry , vol.38 , pp. 13862-13876
    • Zuegg, J.1    Gready, J.E.2
  • 10
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: protofibril formation of the prion protein
    • DeMarco M.L., and Daggett V. From conversion to aggregation: protofibril formation of the prion protein. Proc. Natl. Acad. Sci. USA 101 (2004) 2293-2298
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2293-2298
    • DeMarco, M.L.1    Daggett, V.2
  • 12
    • 0035425883 scopus 로고    scopus 로고
    • An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase
    • Schuler L.D., Daura X., and van Gunsteren W.F. An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase. J. Comp. Chem. 22 (2001) 1205-1218
    • (2001) J. Comp. Chem. , vol.22 , pp. 1205-1218
    • Schuler, L.D.1    Daura, X.2    van Gunsteren, W.F.3
  • 13
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 14
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • Calzolai L., and Zahn R. Influence of pH on NMR structure and stability of the human prion protein globular domain. J. Biol. Chem. 278 (2003) 35592-35596
    • (2003) J. Biol. Chem. , vol.278 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 15
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 16
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • Pullman B.D. (Ed), Reidel Publishing Company, Dordrecht
    • Berendsen H.J.C., Postma J.P.M., van Gunsteren W.F., and Hermans J. Interaction models for water in relation to protein hydration. In: Pullman B.D. (Ed). Intermolecular Forces (1981), Reidel Publishing Company, Dordrecht 331-342
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    van Gunsteren, W.F.3    Hermans, J.4
  • 18
    • 84986440341 scopus 로고
    • Settle: an analytical version of the shake and rattle algorithms for rigid water molecules
    • Miyamoto S., and Kollman P. Settle: an analytical version of the shake and rattle algorithms for rigid water molecules. J. Comp. Chem. 13 (1992) 952-962
    • (1992) J. Comp. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.2
  • 20
    • 33846823909 scopus 로고
    • Particle mesh ewald: an N log (N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh ewald: an N log (N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 22
    • 0034651867 scopus 로고    scopus 로고
    • Molecular dynamics of the mouse and Syrian hamster PrP: implications for activity
    • Parchment O.G., and Essex J.W. Molecular dynamics of the mouse and Syrian hamster PrP: implications for activity. Proteins: Struct. Funct. Genet. 38 (2000) 327-340
    • (2000) Proteins: Struct. Funct. Genet. , vol.38 , pp. 327-340
    • Parchment, O.G.1    Essex, J.W.2
  • 23
    • 0035199471 scopus 로고    scopus 로고
    • Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations
    • Gsponer J., Ferrara P., and Caflisch A. Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations. J. Mol. Graph. Model. 20 (2001) 169-182
    • (2001) J. Mol. Graph. Model. , vol.20 , pp. 169-182
    • Gsponer, J.1    Ferrara, P.2    Caflisch, A.3
  • 24
    • 0034933285 scopus 로고    scopus 로고
    • Simulations and computational analyses of prion protein conformations
    • Alonso D.O., and Daggett V. Simulations and computational analyses of prion protein conformations. Adv. Protein Chem. 57 (2001) 107-137
    • (2001) Adv. Protein Chem. , vol.57 , pp. 107-137
    • Alonso, D.O.1    Daggett, V.2
  • 25
    • 7444240183 scopus 로고    scopus 로고
    • Probing the instabilities in the dynamics of helical fragments from mouse PrPc
    • Dima R.I., and Thirumalai D. Probing the instabilities in the dynamics of helical fragments from mouse PrPc. Proc. Natl. Acad. Sci. USA 101 (2004) 15335-15340
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15335-15340
    • Dima, R.I.1    Thirumalai, D.2
  • 26
    • 0004479272 scopus 로고    scopus 로고
    • Derivation of class II force fields: V. Quantum force field for amides, peptides, and related compounds
    • Maple J.R., Hwang M.J., Jalkanen K.J., Stockfisch T.P., and Hagler A.T. Derivation of class II force fields: V. Quantum force field for amides, peptides, and related compounds. J. Comp. Chem. 19 (1998) 430-458
    • (1998) J. Comp. Chem. , vol.19 , pp. 430-458
    • Maple, J.R.1    Hwang, M.J.2    Jalkanen, K.J.3    Stockfisch, T.P.4    Hagler, A.T.5
  • 27
    • 0038576230 scopus 로고    scopus 로고
    • The role of Helix 1 aspartates and salt bridges in the stability and conversion of prion protein
    • Speare J.O., Rush III T.S., Bloom M.E., and Caughey B. The role of Helix 1 aspartates and salt bridges in the stability and conversion of prion protein. J. Biol. Chem. 278 (2003) 12522-12529
    • (2003) J. Biol. Chem. , vol.278 , pp. 12522-12529
    • Speare, J.O.1    Rush III, T.S.2    Bloom, M.E.3    Caughey, B.4
  • 28
    • 34250215683 scopus 로고    scopus 로고
    • A comparative molecular dynamics study on thermostability of human and chicken prion proteins
    • Ji H.F., and Zhang H.Y. A comparative molecular dynamics study on thermostability of human and chicken prion proteins. Biochem. Biophys. Res. Commun. 359 (2007) 790-794
    • (2007) Biochem. Biophys. Res. Commun. , vol.359 , pp. 790-794
    • Ji, H.F.1    Zhang, H.Y.2
  • 29
    • 33744946784 scopus 로고    scopus 로고
    • Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations
    • Hirschberger T., Stork M., Schropp B., Winklhofer K.F., Tatzelt J., and Tavan P. Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations. Biophys. J. 90 (2006) 3908-3918
    • (2006) Biophys. J. , vol.90 , pp. 3908-3918
    • Hirschberger, T.1    Stork, M.2    Schropp, B.3    Winklhofer, K.F.4    Tatzelt, J.5    Tavan, P.6
  • 30
    • 0036305609 scopus 로고    scopus 로고
    • Effects of the N2144S mutation on backbone dynamics of a TB-cbEGF domain pair from human fibrillin-1
    • Yuan X., Werner J.M., Lack J., Knott V., Handford P.A., Campbell I.D., and Downing K. Effects of the N2144S mutation on backbone dynamics of a TB-cbEGF domain pair from human fibrillin-1. J. Mol. Biol. 316 (2002) 113-125
    • (2002) J. Mol. Biol. , vol.316 , pp. 113-125
    • Yuan, X.1    Werner, J.M.2    Lack, J.3    Knott, V.4    Handford, P.A.5    Campbell, I.D.6    Downing, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.