메뉴 건너뛰기




Volumn 97, Issue 1, 2009, Pages 303-311

Thermodynamics of β-sheet formation in polyglutamine

Author keywords

[No Author keywords available]

Indexed keywords

POLYGLUTAMINE;

EID: 68949127591     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.05.003     Document Type: Article
Times cited : (79)

References (35)
  • 1
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • Williams, A. J., and H. L. Paulson. 2008. Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci. 31:521-528.
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 2
    • 0029089172 scopus 로고
    • When more is less: Pathogenesis of glutamine repeat neurodegenerative diseases
    • Ross, C. A. 1995. When more is less: pathogenesis of glutamine repeat neurodegenerative diseases. Neuron. 15:493-496.
    • (1995) Neuron , vol.15 , pp. 493-496
    • Ross, C.A.1
  • 3
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A., and M. A. Poirier. 2004. Protein aggregation and neurodegenerative disease. Nat. Med. 10:S10-S17.
    • (2004) Nat. Med , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 4
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • Chen, S. M., V. Berthelier, J. B. Hamilton, B. O'Nuallain, and R. Wetzel. 2002. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry. 41:7391-7399.
    • (2002) Biochemistry , vol.41 , pp. 7391-7399
    • Chen, S.M.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 6
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • Sikorski, P., and E. Atkins. 2005. New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils. Biomacromolecules. 6:425-432.
    • (2005) Biomacromolecules , vol.6 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 7
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • Chen, S., V. Berthelier, W. Yang, and R. Wetzel. 2001. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J. Mol. Biol. 311:173-182.
    • (2001) J. Mol. Biol , vol.311 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 8
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • Masino, L., G. Kelly, K. Leonard, Y. Trottier, and A. Pastore. 2002. Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett. 513:267-272.
    • (2002) FEBS Lett , vol.513 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3    Trottier, Y.4    Pastore, A.5
  • 9
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions
    • Crick, S. L., M. Jayaraman, C. Frieden, R. Wetzel, and R. V. Pappu. 2006. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc. Natl. Acad. Sci. USA. 103:16764-16769.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3    Wetzel, R.4    Pappu, R.V.5
  • 10
    • 34548757409 scopus 로고    scopus 로고
    • Quantitative characterization of intrinsic disorder in polyglutamine: Insights from analysis based on polymer theories
    • Vitalis, A., X. Wang, and R. V. Pappu. 2007. Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories. Biophys. J. 93:1923-1937.
    • (2007) Biophys. J , vol.93 , pp. 1923-1937
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 11
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen, S. M., F. A. Ferrone, and R. Wetzel. 2002. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc. Natl. Acad. Sci. USA. 99:11884-11889.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11884-11889
    • Chen, S.M.1    Ferrone, F.A.2    Wetzel, R.3
  • 12
    • 54249132105 scopus 로고    scopus 로고
    • Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization
    • Vitalis, A., X. Wang, and R. V. Pappu. 2008. Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization. J. Mol. Biol. 384:279-297.
    • (2008) J. Mol. Biol , vol.384 , pp. 279-297
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 13
    • 64549131279 scopus 로고    scopus 로고
    • ABSINTH: A new continuum solvation model for simulations of polypeptides in aqueous solutions
    • Vitalis, A., and R. V. Pappu. 2009. ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions. J. Comput. Chem. 30:673-700.
    • (2009) J. Comput. Chem , vol.30 , pp. 673-700
    • Vitalis, A.1    Pappu, R.V.2
  • 14
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction
    • Bhattacharya, A. M., A. K. Thakur, and R. Wetzel. 2005. Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction. Proc. Natl. Acad. Sci. USA. 102:15400-15405.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15400-15405
    • Bhattacharya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 15
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for x-ray protein-structure refinement
    • Engh, R. A., and R. Huber. 1991. Accurate bond and angle parameters for x-ray protein-structure refinement. Acta Crystallogr. A. 47:392-400.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 16
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G. A., R. A. Friesner, J. Tirado-Rives, and W. L. Jorgensen. 2001. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B. 105:6474-6487.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 17
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still, W. C., A. Tempczyk, R. C. Hawley, and T. Hendrickson. 1990. Semianalytical treatment of solvation for molecular mechanics and dynamics. J. Am. Chem. Soc. 112:6127-6129.
    • (1990) J. Am. Chem. Soc , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 18
    • 1442330396 scopus 로고    scopus 로고
    • AGBNP: An analytic implicit solvent model suitable for molecular dynamics simulations and highresolution modeling
    • Gallicchio, E., and R. M. Levy. 2004. AGBNP: an analytic implicit solvent model suitable for molecular dynamics simulations and highresolution modeling. J. Comput. Chem. 25:479-499.
    • (2004) J. Comput. Chem , vol.25 , pp. 479-499
    • Gallicchio, E.1    Levy, R.M.2
  • 19
    • 0842333152 scopus 로고    scopus 로고
    • Implicit solvation based on generalized Born theory in different dielectric environments
    • Feig, M., W. Im, and C. L. Brooks. 2004. Implicit solvation based on generalized Born theory in different dielectric environments. J. Chem. Phys. 120:903-911.
    • (2004) J. Chem. Phys , vol.120 , pp. 903-911
    • Feig, M.1    Im, W.2    Brooks, C.L.3
  • 20
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis, T., and M. Karplus. 1999. Effective energy function for proteins in solution. Proteins Struct. Funct. Genet. 35:133-152.
    • (1999) Proteins Struct. Funct. Genet , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 21
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar, S., J. M. Rosenberg, D. Bouzida, R. H. Swendsen, and P. A. Kollman. 1992. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J. Comput. Chem. 13:1011-1021.
    • (1992) J. Comput. Chem , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 22
    • 0029633155 scopus 로고
    • Calculation of the potential of mean force using computer simulations
    • Roux, B. 1995. Calculation of the potential of mean force using computer simulations. Comput. Phys. Commun. 91:275-282.
    • (1995) Comput. Phys. Commun , vol.91 , pp. 275-282
    • Roux, B.1
  • 23
    • 0027092678 scopus 로고
    • Selection of a representative set of structures from the Brookhaven Protein Data Bank
    • Hobohm, U., M. Scharf, R. Schneider, and S. Sander. 1992. Selection of a representative set of structures from the Brookhaven Protein Data Bank. Protein Sci. 1:409-417.
    • (1992) Protein Sci , vol.1 , pp. 409-417
    • Hobohm, U.1    Scharf, M.2    Schneider, R.3    Sander, S.4
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0034294024 scopus 로고    scopus 로고
    • Multidimensional replicaexchange method for free-energy calculations
    • Sugita, Y., A. Kitao, and Y. Okamoto. 2000. Multidimensional replicaexchange method for free-energy calculations. J. Chem. Phys. 113:6042-6051.
    • (2000) J. Chem. Phys , vol.113 , pp. 6042-6051
    • Sugita, Y.1    Kitao, A.2    Okamoto, Y.3
  • 26
    • 0001510938 scopus 로고
    • Minimum energy compact structures of random sequences of heteropolymers
    • Camacho, C. J., and D. Thirumalai. 1993. Minimum energy compact structures of random sequences of heteropolymers. Phys. Rev. Lett. 71:2505-2508.
    • (1993) Phys. Rev. Lett , vol.71 , pp. 2505-2508
    • Camacho, C.J.1    Thirumalai, D.2
  • 27
    • 0042402021 scopus 로고
    • Off-lattice Monte Carlo simulation of dilute and concentrated polymer solutions under theta conditions
    • Milchev, A., W. Paul, and K. Binder. 1993. Off-lattice Monte Carlo simulation of dilute and concentrated polymer solutions under theta conditions. J. Chem. Phys. 99:4786-4798.
    • (1993) J. Chem. Phys , vol.99 , pp. 4786-4798
    • Milchev, A.1    Paul, W.2    Binder, K.3
  • 28
    • 33845652619 scopus 로고    scopus 로고
    • Effects of chain length on the aggregation of model polyglutamine peptides: Molecular dynamics simulations
    • Marchut, A. J., and C. K. Hall. 2007. Effects of chain length on the aggregation of model polyglutamine peptides: molecular dynamics simulations. Proteins Struct. Funct. Bioinform. 66:96-109.
    • (2007) Proteins Struct. Funct. Bioinform , vol.66 , pp. 96-109
    • Marchut, A.J.1    Hall, C.K.2
  • 29
    • 34548510580 scopus 로고    scopus 로고
    • The length dependence of the polyQ-mediated protein aggregation
    • Barton, S., R. Jacak, S. D. Khare, F. Ding, and N. V. Dokholyan. 2007. The length dependence of the polyQ-mediated protein aggregation. J. Biol. Chem. 282:25487-25492.
    • (2007) J. Biol. Chem , vol.282 , pp. 25487-25492
    • Barton, S.1    Jacak, R.2    Khare, S.D.3    Ding, F.4    Dokholyan, N.V.5
  • 30
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • Lee, C. C., R. H. Walters, and R. M. Murphy. 2007. Reconsidering the mechanism of polyglutamine peptide aggregation. Biochemistry. 46:12810-12820.
    • (2007) Biochemistry , vol.46 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 31
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan, R., and S. L. Lindquist. 2005. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature. 435:765-772.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 32
    • 0042337433 scopus 로고    scopus 로고
    • Liquid-solid transition in nuclei of protein crystals
    • Lomakin, A., N. Asherie, and G. B. Benedek. 2003. Liquid-solid transition in nuclei of protein crystals. Proc. Natl. Acad. Sci. USA. 100:10254-10257.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10254-10257
    • Lomakin, A.1    Asherie, N.2    Benedek, G.B.3
  • 33
    • 36749056299 scopus 로고    scopus 로고
    • A polymer physics perspective on driving forces and mechanisms for protein aggregation
    • Pappu, R. V., X. Wang, A. Vitalis, and S. L. Crick. 2008. A polymer physics perspective on driving forces and mechanisms for protein aggregation. Arch. Biochem. Biophys. 469:132-141.
    • (2008) Arch. Biochem. Biophys , vol.469 , pp. 132-141
    • Pappu, R.V.1    Wang, X.2    Vitalis, A.3    Crick, S.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.