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Volumn 100, Issue 12, 2011, Pages 3000-3007

Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: Insight from computer simulation of an amyloidogenic prion peptide

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Indexed keywords

MESOCRICETUS AURATUS;

EID: 79960306242     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.04.053     Document Type: Article
Times cited : (10)

References (54)
  • 1
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. 1991. Molecular biology of prion diseases. Science. 252:1515-1522. (Pubitemid 21917065)
    • (1991) Science , vol.252 , Issue.5012 , pp. 1515-1522
    • Prusiner, S.B.1
  • 2
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and priori diseases
    • Kelly, J. W. 1997. Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure. 5:595-600. (Pubitemid 27236259)
    • (1997) Structure , vol.5 , Issue.5 , pp. 595-600
    • Kelly, J.W.1
  • 3
    • 0025304678 scopus 로고
    • Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells
    • Borchelt, D. R., M. Scott, ..., S. B. Prusiner. 1990. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J. Cell Biol. 110:743-752.
    • (1990) J. Cell Biol. , vol.110 , pp. 743-752
    • Borchelt, D.R.1    Scott, M.2    Prusiner, S.B.3
  • 6
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • Caughey, B., and P. T. Lansbury. 2003. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:267-298. (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 7
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed, R., E. Head, ..., C. G. Glabe. 2003. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 300:486-489. (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 8
    • 43149083897 scopus 로고    scopus 로고
    • Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-β protein
    • DOI 10.1073/pnas.0708193105
    • Baumketner, A., M. G. Krone, and J. E. Shea. 2008. Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-beta protein. Proc. Natl. Acad. Sci. USA. 105:6027-6032. (Pubitemid 351758393)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.16 , pp. 6027-6032
    • Baumketner, A.1    Krone, M.G.2    Shea, J.-E.3
  • 9
    • 77953086457 scopus 로고    scopus 로고
    • Structural properties and dynamic behavior of nonfibrillar oligomers formed by PrP(106-126)
    • Walsh, P., P. Neudecker, and S. Sharpe. 2010. Structural properties and dynamic behavior of nonfibrillar oligomers formed by PrP(106-126). J. Am. Chem. Soc. 132:7684-7695.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7684-7695
    • Walsh, P.1    Neudecker, P.2    Sharpe, S.3
  • 10
    • 0028962532 scopus 로고
    • Prion protein gene variation among primates
    • Schätzl, H. M., M. Da Costa, ..., S. B. Prusiner. 1995. Prion protein gene variation among primates. J. Mol. Biol. 245:362-374.
    • (1995) J. Mol. Biol. , vol.245 , pp. 362-374
    • Schätzl, H.M.1    Da Costa, M.2    Prusiner, S.B.3
  • 11
    • 0028925377 scopus 로고
    • Prion protein peptides induce α-helix to β-sheet conformational transitions
    • Nguyen, J., M. A. Baldwin, ..., S. B. Prusiner. 1995. Prion protein peptides induce α-helix to β-sheet conformational transitions. Biochemistry. 34:4186-4192.
    • (1995) Biochemistry , vol.34 , pp. 4186-4192
    • Nguyen, J.1    Baldwin, M.A.2    Prusiner, S.B.3
  • 12
    • 0029294573 scopus 로고
    • Theoretical studies of sequence effects on the conformational properties of a fragment of the prion protein: Implications for scrapie formation
    • Kazmirski, S. L., D. O. V. Alonso, ..., V. Daggett. 1995. Theoretical studies of sequence effects on the conformational properties of a fragment of the prion protein: implications for scrapie formation. Chem. Biol. 2:305-315.
    • (1995) Chem. Biol. , vol.2 , pp. 305-315
    • Kazmirski, S.L.1    Alonso, D.O.V.2    Daggett, V.3
  • 14
    • 77954239509 scopus 로고    scopus 로고
    • The oligomerization properties of prion protein are restricted to the H2H3 domain
    • Chakroun, N., S. Prigent, ..., H. Rezaei. 2010. The oligomerization properties of prion protein are restricted to the H2H3 domain. FASEB J. 24:3222-3231.
    • (2010) FASEB J , vol.24 , pp. 3222-3231
    • Chakroun, N.1    Prigent, S.2    Rezaei, H.3
  • 15
    • 77957669973 scopus 로고    scopus 로고
    • The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form
    • Hosszu, L. L., M. H. Tattum, ..., A. R. Clarke. 2010. The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form. Biochemistry. 49:8729-8738.
    • (2010) Biochemistry , vol.49 , pp. 8729-8738
    • Hosszu, L.L.1    Tattum, M.H.2    Clarke, A.R.3
  • 17
    • 28844506608 scopus 로고    scopus 로고
    • Direct observation of protein folding, aggregation, and a prion-like conformational conversion
    • DOI 10.1074/jbc.M506372200
    • Ding, F., J. J. LaRocque, and N. V. Dokholyan. 2005. Direct observation of protein folding, aggregation, and a prion-like conformational conversion. J. Biol. Chem. 280:40235-40240. (Pubitemid 41779161)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40235-40240
    • Ding, F.1    LaRocque, J.J.2    Dokholyan, N.V.3
  • 18
    • 17844406143 scopus 로고    scopus 로고
    • Thermodynamic and kinetic characterization of a β-hairpin peptide in solution: An extended phase space sampling by molecular dynamics simulations in explicit water
    • DOI 10.1002/prot.20427
    • Daidone, I., A. Amadei, and A. Di Nola. 2005. Thermodynamic and kinetic characterization of a β-hairpin peptide in solution: an extended phase space sampling by molecular dynamics simulations in explicit water. Proteins. 59:510-518. (Pubitemid 40594294)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.3 , pp. 510-518
    • Daidone, I.1    Amadei, A.2    Di Nola, A.3
  • 20
    • 51649109850 scopus 로고    scopus 로고
    • Contrasting disease and nondisease protein aggregation by molecular simulation
    • Fawzi, N. L., E. H. Yap, ..., T. Head-Gordon. 2008. Contrasting disease and nondisease protein aggregation by molecular simulation. Acc. Chem. Res. 41:1037-1047.
    • (2008) Acc. Chem. Res. , vol.41 , pp. 1037-1047
    • Fawzi, N.L.1    Yap, E.H.2    Head-Gordon, T.3
  • 21
    • 72949120775 scopus 로고    scopus 로고
    • Diversity of kinetic pathways in amyloid fibril formation
    • Bellesia, G., and J. E. Shea. 2009. Diversity of kinetic pathways in amyloid fibril formation. J. Chem. Phys. 131:111102.
    • (2009) J. Chem. Phys. , vol.131 , pp. 111102
    • Bellesia, G.1    Shea, J.E.2
  • 22
    • 78349309658 scopus 로고    scopus 로고
    • Mechanism of fiber assembly: Treatment of Aβ peptide aggregation with a coarse-grained united-residue force field
    • Rojas, A., A. Liwo, ..., H. A. Scheraga. 2010. Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field. J. Mol. Biol. 404:537-552.
    • (2010) J. Mol. Biol. , vol.404 , pp. 537-552
    • Rojas, A.1    Liwo, A.2    Scheraga, H.A.3
  • 24
    • 0030967895 scopus 로고    scopus 로고
    • Solution structure of a 142- residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
    • James, T. L., H. Liu, ..., F. E. Cohen. 1997. Solution structure of a 142- residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA. 94:10086-10091.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10086-10091
    • James, T.L.1    Liu, H.2    Cohen, F.E.3
  • 25
    • 0031707767 scopus 로고    scopus 로고
    • Polypeptide chain folding in the hydrophobic core of hamster scrapie prion: Analysis by X-ray diffraction
    • DOI 10.1006/jsbi.1998.3998
    • Inouye, H., and D. A. Kirschner. 1998. Polypeptide chain folding in the hydrophobic core of hamster scrapie prion: analysis by x-ray diffraction. J. Struct. Biol. 122:247-255. (Pubitemid 28411205)
    • (1998) Journal of Structural Biology , vol.122 , Issue.1-2 , pp. 247-255
    • Inouye, H.1    Kirschner, D.A.2
  • 26
    • 0034653970 scopus 로고    scopus 로고
    • 117>Val mutation
    • DOI 10.1042/0264-6021:3460785
    • Brown, D. R. 2000. Altered toxicity of the prion protein peptide PrP106-126 carrying the Ala(117)->Val mutation. Biochem. J. 346:785-791. (Pubitemid 30171041)
    • (2000) Biochemical Journal , vol.346 , Issue.3 , pp. 785-791
    • Brown, D.R.1
  • 27
    • 15444367176 scopus 로고    scopus 로고
    • Correlations among morphology, β-sheet stability, and molecular structure in prion peptide aggregates
    • DOI 10.1021/bi047445a
    • Petty, S. A., T. Adalsteinsson, and S. M. Decatur. 2005. Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates. Biochemistry. 44:4720-4726. (Pubitemid 40396750)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4720-4726
    • Petty, S.A.1    Adalsteinsson, T.2    Decatur, S.M.3
  • 30
    • 84946449441 scopus 로고
    • A comparison of constant energy, constant temperature, and constant pressure ensembles in molecular dynamics simulations of atomic liquids
    • Brown, D., and J. H. R. Clarke. 1984. A comparison of constant energy, constant temperature, and constant pressure ensembles in molecular dynamics simulations of atomic liquids. Mol. Phys. 51:1243-1252.
    • (1984) Mol. Phys. , vol.51 , pp. 1243-1252
    • Brown, D.1    Clarke, J.H.R.2
  • 32
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 34
    • 34548273698 scopus 로고    scopus 로고
    • Folding Time Predictions from All-atom Replica Exchange Simulations
    • DOI 10.1016/j.jmb.2007.07.010, PII S0022283607009242
    • Yang, S., J. N. Onuchic, ..., H. Levine. 2007. Folding time predictions from all-atom replica exchange simulations. J. Mol. Biol. 372:756-763. (Pubitemid 47321796)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 756-763
    • Yang, S.1    Onuchic, J.N.2    Garcia, A.E.3    Levine, H.4
  • 38
    • 33745027667 scopus 로고    scopus 로고
    • Folding and aggregation kinetics of a β-hairpin
    • Muñoz, V., R. Ghirlando, ..., W. A. Eaton. 2006. Folding and aggregation kinetics of a β-hairpin. Biochemistry. 45:7023-7035.
    • (2006) Biochemistry , vol.45 , pp. 7023-7035
    • Muñoz, V.1    Ghirlando, R.2    Eaton, W.A.3
  • 39
    • 77952324067 scopus 로고    scopus 로고
    • Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: A replica exchange molecular dynamics study in explicit solvent
    • De Simone, A., and P. Derreumaux. 2010. Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent. J. Chem. Phys. 132:165103.
    • (2010) J. Chem. Phys. , vol.132 , pp. 165103
    • De Simone, A.1    Derreumaux, P.2
  • 40
    • 0242490659 scopus 로고    scopus 로고
    • The Organization and Assembly of a β-Sheet Formed by a Prion Peptide in Solution: An Isotope-Edited FTIR Study
    • DOI 10.1021/ja036725v
    • Silva, R. A., W. Barber-Armstrong, and S. M. Decatur. 2003. The organization and assembly of a β-sheet formed by a prion peptide in solution: an isotope-edited FTIR study. J. Am. Chem. Soc. 125:13674-13675. (Pubitemid 37386037)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.45 , pp. 13674-13675
    • Gangani, R.A.1    Silva, D.2    Barber-Armstrong, W.3    Decatur, S.M.4
  • 41
    • 42649108674 scopus 로고    scopus 로고
    • Steric zipper of the amyloid fibrils formed by residues 109-122 of the Syrian hamster prion protein
    • Lee, S. W., Y. Mou, ..., J. C. Chan. 2008. Steric zipper of the amyloid fibrils formed by residues 109-122 of the Syrian hamster prion protein. J. Mol. Biol. 378:1142-1154.
    • (2008) J. Mol. Biol. , vol.378 , pp. 1142-1154
    • Lee, S.W.1    Mou, Y.2    Chan, J.C.3
  • 42
    • 35748943830 scopus 로고    scopus 로고
    • Pathways and Intermediates of Amyloid Fibril Formation
    • DOI 10.1016/j.jmb.2007.09.090, PII S0022283607013022
    • Pellarin, R., E. Guarnera, and A. Caflisch. 2007. Pathways and intermediates of amyloid fibril formation. J. Mol. Biol. 374:917-924. (Pubitemid 350052098)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.4 , pp. 917-924
    • Pellarin, R.1    Guarnera, E.2    Caflisch, A.3
  • 43
    • 66749092410 scopus 로고    scopus 로고
    • Structures and thermodynamics of Alzheimer's amyloid-β Abeta(16-35) monomer and dimer by replica exchange molecular dynamics simulations: Implication for full-length Abeta fibrillation
    • Chebaro, Y., N. Mousseau, and P. Derreumaux. 2009. Structures and thermodynamics of Alzheimer's amyloid-β Abeta(16-35) monomer and dimer by replica exchange molecular dynamics simulations: implication for full-length Abeta fibrillation. J. Phys. Chem. B. 113:7668- 7675.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7668-7675
    • Chebaro, Y.1    Mousseau, N.2    Derreumaux, P.3
  • 44
    • 77950219248 scopus 로고    scopus 로고
    • Elucidation of amyloid β-protein oligomerization mechanisms: Discrete molecular dynamics study
    • Urbanc, B., M. Betnel, ..., D. B. Teplow. 2010. Elucidation of amyloid β-protein oligomerization mechanisms: discrete molecular dynamics study. J. Am. Chem. Soc. 132:4266-4280.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4266-4280
    • Urbanc, B.1    Betnel, M.2    Teplow, D.B.3
  • 46
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • Dobson, C. M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332. (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 47
    • 0242300624 scopus 로고    scopus 로고
    • Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease
    • DOI 10.1126/science.1087348
    • Aguzzi, A., and C. Haass. 2003. Games played by rogue proteins in prion disorders and Alzheimer's disease. Science. 302:814-818. (Pubitemid 37339613)
    • (2003) Science , vol.302 , Issue.5646 , pp. 814-818
    • Aguzzi, A.1    Haass, C.2
  • 48
    • 0347480547 scopus 로고    scopus 로고
    • Infrared Study of the Stability and Folding Kinetics of a 15-Residue β-Hairpin
    • DOI 10.1021/ja037053b
    • Xu, Y., R. Oyola, and F. Gai. 2003. Infrared study of the stability and folding kinetics of a 15-residue β-hairpin. J. Am. Chem. Soc. 125:15388-15394. (Pubitemid 37532180)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.50 , pp. 15388-15394
    • Xu, Y.1    Oyola, R.2    Gai, F.3
  • 49
    • 33845403686 scopus 로고    scopus 로고
    • Nanosecond folding dynamics of a three-stranded β-sheet
    • DOI 10.1021/ja064865+
    • Xu, Y., P. Purkayastha, and F. Gai. 2006. Nanosecond folding dynamics of a three-stranded beta-sheet. J. Am. Chem. Soc. 128:15836-15842. (Pubitemid 44894125)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.49 , pp. 15836-15842
    • Xu, Y.1    Purkayastha, P.2    Gai, F.3
  • 51
    • 0036500833 scopus 로고    scopus 로고
    • Making a network of hydrophobic clusters
    • Baldwin, R. L. 2002. Making a network of hydrophobic clusters. Science. 295:1657-1658.
    • (2002) Science , vol.295 , pp. 1657-1658
    • Baldwin, R.L.1
  • 52
    • 0344551137 scopus 로고    scopus 로고
    • The Role of the Unfolded State in Hairpin Stability
    • Lei, H., and P. E. Smith. 2003. The role of the unfolded state in hairpin stability. Biophys. J. 85:3513-3520. (Pubitemid 37490267)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3513-3520
    • Lei, H.1    Smith, P.E.2


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