메뉴 건너뛰기




Volumn 411, Issue 3, 2011, Pages 700-712

Common structural traits across pathogenic mutants of the human prion protein and their implications for familial prion diseases

Author keywords

ADI; angular dispersion index; disease linked mutation; DLM; GD; globular domain; HB; HuPrP(E219K 129M); HuPrP(PP); hydrogen bond; MD; molecular dynamics; prion protein; PrP; RMSF; root mean square fluctuation; salt bridge; SB; wild type; WT

Indexed keywords

MUTANT PROTEIN; PRION PROTEIN;

EID: 79960904305     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.06.008     Document Type: Article
Times cited : (64)

References (116)
  • 1
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • DOI 10.1146/annurev.neuro.24.1.519
    • Collinge J. Prion diseases of humans and animals: their causes and molecular basis Annu. Rev. Neurosci. 24 2001 519 550 (Pubitemid 32695238)
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 519-550
    • Collinge, J.1
  • 3
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N., Borchelt D.R., Hsiao K., and Prusiner S.B. Scrapie prion protein contains a phosphatidylinositol glycolipid Cell 51 1987 229 240
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 4
    • 0026780714 scopus 로고
    • Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid
    • Stahl N., Baldwin M.A., Hecker R., Pan K.M., Burlingame A.L., and Prusiner S.B. Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid Biochemistry 31 1992 5043 5053
    • (1992) Biochemistry , vol.31 , pp. 5043-5053
    • Stahl, N.1    Baldwin, M.A.2    Hecker, R.3    Pan, K.M.4    Burlingame, A.L.5    Prusiner, S.B.6
  • 5
    • 0025237593 scopus 로고
    • Subcellular distribution and physicochemical properties of scrapie-associated precursor protein and relationship with scrapie agent
    • Safar J., Ceroni M., Piccardo P., Liberski P.P., Miyazaki M., Gajdusek D.C., and Gibbs C.J. Subcellular distribution and physicochemical properties of scrapie-associated precursor protein and relationship with scrapie agent Neurology 40 1990 503 508 (Pubitemid 20117539)
    • (1990) Neurology , vol.40 , Issue.3 , pp. 503-508
    • Safar, J.1    Ceroni, M.2    Piccardo, P.3    Liberski, P.P.4    Miyazaki, M.5    Gajdusek, D.C.6    Gibbs Jr., C.J.7
  • 6
    • 61849115784 scopus 로고    scopus 로고
    • Characterization of cell-surface prion protein relative to its recombinant analogue: Insights from molecular dynamics simulations of diglycosylated, membrane-bound human prion protein
    • DeMarco M.L., and Daggett V. Characterization of cell-surface prion protein relative to its recombinant analogue: insights from molecular dynamics simulations of diglycosylated, membrane-bound human prion protein J. Neurochem. 109 2009 60 73
    • (2009) J. Neurochem. , vol.109 , pp. 60-73
    • Demarco, M.L.1    Daggett, V.2
  • 7
    • 66949116095 scopus 로고    scopus 로고
    • Investigation of the effect of glycosylation on human prion protein by molecular dynamics
    • Zhong L., and Xie J. Investigation of the effect of glycosylation on human prion protein by molecular dynamics J. Biomol. Struct. Dyn. 26 2009 525 533
    • (2009) J. Biomol. Struct. Dyn. , vol.26 , pp. 525-533
    • Zhong, L.1    Xie, J.2
  • 9
    • 70349195971 scopus 로고    scopus 로고
    • The consequences of pathogenic mutations to the human prion protein
    • van der Kamp M.W., and Daggett V. The consequences of pathogenic mutations to the human prion protein Protein Eng. Des. Sel. 22 2009 461 468
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 461-468
    • Van Der Kamp, M.W.1    Daggett, V.2
  • 10
    • 78651246462 scopus 로고    scopus 로고
    • Genetic Creutzfeldt-Jakob disease and fatal familial insomnia: Insights into phenotypic variability and disease pathogenesis
    • Capellari S., Strammiello R., Saverioni D., Kretzschmar H., and Parchi P. Genetic Creutzfeldt-Jakob disease and fatal familial insomnia: insights into phenotypic variability and disease pathogenesis Acta Neuropathol. 121 2010 21 37
    • (2010) Acta Neuropathol. , vol.121 , pp. 21-37
    • Capellari, S.1    Strammiello, R.2    Saverioni, D.3    Kretzschmar, H.4    Parchi, P.5
  • 12
    • 0034721767 scopus 로고    scopus 로고
    • Solution structure of the E200K variant of human prion protein-implications for the mechanism of pathogenesis in familial prion diseases
    • Zhang Y.B., Swietnicki W., Zagorski M.G., Surewicz W.K., and Sonnichsen F.D. Solution structure of the E200K variant of human prion protein-implications for the mechanism of pathogenesis in familial prion diseases J. Biol. Chem. 275 2000 33650 33654
    • (2000) J. Biol. Chem. , vol.275 , pp. 33650-33654
    • Zhang, Y.B.1    Swietnicki, W.2    Zagorski, M.G.3    Surewicz, W.K.4    Sonnichsen, F.D.5
  • 13
    • 77955367206 scopus 로고    scopus 로고
    • NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features
    • Ilc G., Giachin G., Jaremko M., Jaremko L., Benetti F., and Plavec J. NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features PLoS ONE 5 2010 e11715
    • (2010) PLoS ONE , vol.5 , pp. 11715
    • Ilc, G.1    Giachin, G.2    Jaremko, M.3    Jaremko, L.4    Benetti, F.5    Plavec, J.6
  • 14
    • 75649120399 scopus 로고    scopus 로고
    • Conformational diversity in prion protein variants influences intermolecular β-sheet formation
    • Lee S., Antony L., Hartmann R., Knaus K.J., Surewicz K., and Yee V.C. Conformational diversity in prion protein variants influences intermolecular β-sheet formation EMBO J. 29 2009 251 262
    • (2009) EMBO J. , vol.29 , pp. 251-262
    • Lee, S.1    Antony, L.2    Hartmann, R.3    Knaus, K.J.4    Surewicz, K.5    Yee, V.C.6
  • 16
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T., Cramp W.A., Haig D.A., and Clarke M.C. Does the agent of scrapie replicate without nucleic acid? Nature 214 1967 764 766
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 17
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith J.S. Self-replication and scrapie Nature 215 1967 1043 1044
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 18
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl N., Baldwin M.A., Teplow D.B., Hood L., Gibson B.W., Burlingame A.L., and Prusiner S.B. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing Biochemistry 32 1993 1991 2002 (Pubitemid 23086050)
    • (1993) Biochemistry , vol.32 , Issue.8 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6    Prusiner, S.B.7
  • 22
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F., Wang X., Yuan C.G., and Ma J. Generating a prion with bacterially expressed recombinant prion protein Science 327 2010 1132 1135
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 24
    • 0022005315 scopus 로고
    • A cellular gene encodes scrapie PrP 27-30 protein
    • Oesch B., Westaway D., Wälchli M., McKinley M., Kent S., and Aebersold R. A cellular gene encodes scrapie PrP 27-30 protein Cell 40 1985 735 746 (Pubitemid 15240279)
    • (1985) Cell , vol.40 , Issue.4 , pp. 735-746
    • Oesch, B.1    Westaway, D.2    Walchli, M.3
  • 25
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan K.M., Baldwin M., Nguyen J., Gasset M., Serban A., and Groth D. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins Proc. Natl Acad. Sci. USA 90 1993 10962 10966
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5    Groth, D.6
  • 26
    • 67649204153 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils
    • Nazabal A., Hornemann S., Aguzzi A., and Zenobi R. Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils J. Mass Spectrom. 44 2009 965 977
    • (2009) J. Mass Spectrom. , vol.44 , pp. 965-977
    • Nazabal, A.1    Hornemann, S.2    Aguzzi, A.3    Zenobi, R.4
  • 29
    • 70349858126 scopus 로고    scopus 로고
    • Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils
    • Sim V., and Caughey B. Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils Neurobiol. Aging 30 2009 2031 2042
    • (2009) Neurobiol. Aging , vol.30 , pp. 2031-2042
    • Sim, V.1    Caughey, B.2
  • 32
    • 69549129200 scopus 로고    scopus 로고
    • Human prion protein helices: Studying their stability by molecular dynamics simulations
    • Costantini S., and Facchiano A.M. Human prion protein helices: studying their stability by molecular dynamics simulations Protein Pept. Lett. 16 2009 1057 1062
    • (2009) Protein Pept. Lett. , vol.16 , pp. 1057-1062
    • Costantini, S.1    Facchiano, A.M.2
  • 33
    • 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
  • 34
    • 61749092017 scopus 로고    scopus 로고
    • Structural domains and main-chain flexibility in prion proteins
    • Blinov N., Berjanskii M., Wishart D.S., and Stepanova M. Structural domains and main-chain flexibility in prion proteins Biochemistry 48 2009 1488 1497
    • (2009) Biochemistry , vol.48 , pp. 1488-1497
    • Blinov, N.1    Berjanskii, M.2    Wishart, D.S.3    Stepanova, M.4
  • 35
    • 34548267542 scopus 로고    scopus 로고
    • Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species
    • DOI 10.1039/b700764g
    • Pappalardo M., Milardi D., Grasso D., and La Rosa C. Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species New J. Chem. 31 2007 901 905 (Pubitemid 47324752)
    • (2007) New Journal of Chemistry , vol.31 , Issue.6 , pp. 901-905
    • Pappalardo, M.1    Milardi, D.2    Grasso, D.3    La Rosa, C.4
  • 36
    • 4744351381 scopus 로고    scopus 로고
    • Slow Conformational Dynamics in the Hamster Prion Protein
    • DOI 10.1021/bi036123o
    • Kuwata K., Kamatari Y.O., Akasaka K., and James T.L. Slow conformational dynamics in the hamster prion protein Biochemistry 43 2004 4439 4446 (Pubitemid 38500572)
    • (2004) Biochemistry , vol.43 , Issue.15 , pp. 4439-4446
    • Kuwata, K.1    Kamatari, Y.O.2    Akasaka, K.3    James, T.L.4
  • 37
    • 0037108168 scopus 로고    scopus 로고
    • Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrPSc?
    • Kuwata K., Li H., Yamada H., Legname G., Prusiner S.B., Akasaka K., and James T.L. Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc? Biochemistry 41 2002 12277 12283
    • (2002) Biochemistry , vol.41 , pp. 12277-12283
    • Kuwata, K.1    Li, H.2    Yamada, H.3    Legname, G.4    Prusiner, S.B.5    Akasaka, K.6    James, T.L.7
  • 39
    • 77954238207 scopus 로고    scopus 로고
    • Prion fibrillization is mediated by a native structural element which comprises the helices H2 and H3
    • Adrover M., Pauwels K., Pringent S., De Chiara C., Xu Z., and Chapuis C. Prion fibrillization is mediated by a native structural element which comprises the helices H2 and H3 J. Biol. Chem. 285 2010 21004 21012
    • (2010) J. Biol. Chem. , vol.285 , pp. 21004-21012
    • Adrover, M.1    Pauwels, K.2    Pringent, S.3    De Chiara, C.4    Xu, Z.5    Chapuis, C.6
  • 40
    • 69249123818 scopus 로고    scopus 로고
    • Prion proteins with pathogenic and protective mutations show similar structure and dynamics
    • Bae S.H., Legname G., Serban A., Prusiner S.B., Wright P.E., and Dyson H.J. Prion proteins with pathogenic and protective mutations show similar structure and dynamics Biochemistry 48 2009 8120 8128
    • (2009) Biochemistry , vol.48 , pp. 8120-8128
    • Bae, S.H.1    Legname, G.2    Serban, A.3    Prusiner, S.B.4    Wright, P.E.5    Dyson, H.J.6
  • 41
    • 67650082630 scopus 로고    scopus 로고
    • The conversion of helix H2 to beta-sheet is accelerated in the monomer and dimer of the prion protein upon T183A mutation
    • Chebaro Y., and Derreumaux P. The conversion of helix H2 to beta-sheet is accelerated in the monomer and dimer of the prion protein upon T183A mutation J. Phys. Chem. B 113 2009 6942 6948
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6942-6948
    • Chebaro, Y.1    Derreumaux, P.2
  • 42
    • 78149436073 scopus 로고    scopus 로고
    • Diverse effects on the native beta-sheet of the human prion protein due to disease-associated mutations
    • Chen W., van der Kamp M.W., and Daggett V. Diverse effects on the native beta-sheet of the human prion protein due to disease-associated mutations Biochemistry 49 2010 9874 9881
    • (2010) Biochemistry , vol.49 , pp. 9874-9881
    • Chen, W.1    Van Der Kamp, M.W.2    Daggett, V.3
  • 43
    • 78349283012 scopus 로고    scopus 로고
    • Structural facets of disease-linked human prion protein mutants: A molecular dynamic study
    • Rossetti G., Giachin G., Legname G., and Carloni P. Structural facets of disease-linked human prion protein mutants: a molecular dynamic study Proteins: Struct., Funct., Bioinf. 78 2010 3270 3280
    • (2010) Proteins: Struct., Funct., Bioinf. , vol.78 , pp. 3270-3280
    • Rossetti, G.1    Giachin, G.2    Legname, G.3    Carloni, P.4
  • 44
    • 33744946784 scopus 로고    scopus 로고
    • Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations
    • DOI 10.1529/biophysj.105.075341
    • 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 (Pubitemid 43846109)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 3908-3918
    • Hirschberger, T.1    Stork, M.2    Schropp, B.3    Winklhofer, K.F.4    Tatzelt, J.5    Tavan, P.6
  • 46
    • 2442494894 scopus 로고    scopus 로고
    • Helix H1 of the prion protein is rather stable against environmental perturbations: Molecular dynamics of mutation and deletion variants of PrP(90-231)
    • DOI 10.1007/s00018-003-3455-3
    • Santini S., and Derreumaux P. Helix H1 of the prion protein is rather stable against environmental perturbations: molecular dynamics of mutation and deletion variants of PrP(90-231) Cell. Mol. Life Sci. 61 2004 951 960 (Pubitemid 38651010)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.7-8 , pp. 951-960
    • Santini, S.1    Derreumaux, P.2
  • 47
    • 2342432162 scopus 로고    scopus 로고
    • The Effect of Disease-associated Mutations on the Folding Pathway of Human Prion Protein
    • DOI 10.1074/jbc.M313581200
    • Apetri A.C., and Surewicz K. The effect of disease-associated mutations on the folding pathway of human prion protein J. Biol. Chem. 279 2004 18008 18014 (Pubitemid 38560570)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 18008-18014
    • Apetri, A.C.1    Surewicz, K.2    Surewicz, W.K.3
  • 48
    • 31544478521 scopus 로고    scopus 로고
    • Molecular dynamics study on the conformational transition of prion induced by the point mutation: F198S
    • DOI 10.1016/j.tsf.2005.07.008, PII S0040609005007522, Proceedings of the Sixth International Conference on Nano-Molecular Electronics (ICNME 2004)
    • Zhang Y., Dai L.R., Iwamoto M., and Ou-Yang Z.C. Molecular dynamics study on the conformational transition of prion induced by the point mutation: F198S Thin Solid Films 499 2006 224 228 (Pubitemid 43165571)
    • (2006) Thin Solid Films , vol.499 , Issue.1-2 , pp. 224-228
    • Zhang, Y.1    Dai, L.2    Iwamoto, M.3    Ou-Yang, Z.-C.4
  • 49
    • 36048995435 scopus 로고    scopus 로고
    • Contribution of a putative salt bridge and backbone dynamics in the structural instability of human prion protein upon R208H mutation
    • DOI 10.1016/j.bbrc.2007.10.011, PII S0006291X07021419
    • Bamdad K., and Naderi-Manesh H. Contribution of a putative salt bridge and backbone dynamics in the structural instability of human prion protein upon R208H mutation Biochem. Biophys. Res. Commun. 364 2007 719 724 (Pubitemid 350087864)
    • (2007) Biochemical and Biophysical Research Communications , vol.364 , Issue.4 , pp. 719-724
    • Bamdad, K.1    Naderi-Manesh, H.2
  • 50
    • 0041843693 scopus 로고    scopus 로고
    • Molecular dynamics simulation of dimeric and monomeric forms of human prion protein: Insight into dynamics and properties
    • Sekijima M., Motono C., Yamasaki S., Kaneko K., and Akiyama Y. Molecular dynamics simulation of dimeric and monomeric forms of human prion protein: insight into dynamics and properties Biophys. J. 85 2003 1176 1185 (Pubitemid 36909678)
    • (2003) Biophysical Journal , vol.85 , Issue.2 , pp. 1176-1185
    • Sekijima, M.1    Motono, C.2    Yamasaki, S.3    Kaneko, K.4    Akiyama, Y.5
  • 51
    • 0036606794 scopus 로고    scopus 로고
    • Conformational polymorphism of wild-type and mutant prion proteins: Energy landscape analysis
    • DOI 10.1002/prot.10095
    • Levy Y., and Becker O.M. Conformational polymorphism of wild-type and mutant prion proteins: energy landscape analysis Proteins 47 2002 458 468 (Pubitemid 34614725)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.4 , pp. 458-468
    • Levy, Y.1    Becker, O.M.2
  • 53
    • 28644432876 scopus 로고    scopus 로고
    • Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations
    • DOI 10.1002/prot.20755
    • Bujdoso R., Burke D.F., and Thackray A.M. Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations Proteins 61 2005 840 849 (Pubitemid 41753154)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.4 , pp. 840-849
    • Bujdoso, R.1    Burke, D.F.2    Thackray, A.M.3
  • 54
    • 0030600139 scopus 로고    scopus 로고
    • Molecular biology of transmissible spongiform encephalopathies
    • DOI 10.1016/0014-5793(96)00610-2
    • Weissmann C. Molecular biology of transmissible spongiform encephalopathies FEBS Lett. 389 1996 3 11 (Pubitemid 26227415)
    • (1996) FEBS Letters , vol.389 , Issue.1 , pp. 3-11
    • Weissmann, C.1
  • 56
    • 0028285923 scopus 로고
    • Identification of a PRNP gene mutation in Jakob's original Creutzfeldt-Jakob disease family [12]
    • Brown P., Cervenakova L., Boellaard J.W., Stavrou D., Goldfarb L.G., and Gajdusek D.C. Identification of a PRNP gene mutation in Jakob's original Creutzfeldt-Jakob disease family Lancet 344 1994 130 131 (Pubitemid 24214154)
    • (1994) Lancet , vol.344 , Issue.8915 , pp. 130-131
    • Brown, P.1    Cervenakova, L.2    Boellaard, J.W.3    Stavrou, D.4    Goldfarb, L.G.5    Gajdusek, D.C.6
  • 58
    • 1842644947 scopus 로고    scopus 로고
    • Inherited prion diseases
    • S.B. Prusiner, 2nd edit Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • Kong Q., Surewicz W.K., Petersen R.B., Zou W., Chen S.G., and Gambetti P. Inherited prion diseases S.B. Prusiner, Prion Biology and Diseases 2nd edit 2004 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 673 775
    • (2004) Prion Biology and Diseases , pp. 673-775
    • Kong, Q.1    Surewicz, W.K.2    Petersen, R.B.3    Zou, W.4    Chen, S.G.5    Gambetti, P.6
  • 59
    • 33749822624 scopus 로고    scopus 로고
    • The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro
    • Surewicz K., Jones E.M., and Apetri A.C. The emerging principles of mammalian prion propagation and transmissibility barriers: insight from studies in vitro Acc. Chem. Res. 39 2006 654 662
    • (2006) Acc. Chem. Res. , vol.39 , pp. 654-662
    • Surewicz, K.1    Jones, E.M.2    Apetri, A.C.3
  • 60
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki W., Petersen R.B., Gambetti P., and Surewicz W.K. Familial mutations and the thermodynamic stability of the recombinant human prion protein J. Biol. Chem. 273 1998 31048 31052
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 61
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann S., and Glockshuber R. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein Biochemistry 38 1999 3258 3267
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 62
    • 0033570204 scopus 로고    scopus 로고
    • Prion protein interconversions and the transmissible spongiform encephalopathies
    • Horiuchi M., and Caughey B. Prion protein interconversions and the transmissible spongiform encephalopathies Structure 7 1999 R231 240
    • (1999) Structure , vol.7 , pp. 231-240
    • Horiuchi, M.1    Caughey, B.2
  • 63
    • 78149417303 scopus 로고    scopus 로고
    • Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding
    • van der Kamp M.W., and Daggett V. Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding J. Mol. Biol. 404 2010 732 748
    • (2010) J. Mol. Biol. , vol.404 , pp. 732-748
    • Van Der Kamp, M.W.1    Daggett, V.2
  • 65
    • 77649237972 scopus 로고    scopus 로고
    • Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants
    • Zhang J. Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants J. Theor. Biol. 264 2010 119 122
    • (2010) J. Theor. Biol. , vol.264 , pp. 119-122
    • Zhang, J.1
  • 66
    • 16344380603 scopus 로고    scopus 로고
    • One gene, two diseases and three conformations: Molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures
    • DOI 10.1002/prot.20401
    • Shamsir M.S., and Dalby A.R. One gene, two diseases and three conformations: molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures Proteins 59 2005 275 290 (Pubitemid 40471566)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.2 , pp. 275-290
    • Shamsir, M.S.1    Dalby, A.R.2
  • 67
    • 77950175319 scopus 로고    scopus 로고
    • Structure of the prion protein and its gene: An analysis using bioinformatics and computer simulation
    • Sakudo A., Xue G., Kawashita N., Ano Y., Takagi T., and Shintani H. Structure of the prion protein and its gene: an analysis using bioinformatics and computer simulation Curr. Protein Pept. Sci. 11 2010 166 179
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 166-179
    • Sakudo, A.1    Xue, G.2    Kawashita, N.3    Ano, Y.4    Takagi, T.5    Shintani, H.6
  • 68
    • 79955729783 scopus 로고    scopus 로고
    • Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target
    • Meli M., Gasset M., and Colombo G. Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target PLoS ONE 6 2011 e19093
    • (2011) PLoS ONE , vol.6 , pp. 19093
    • Meli, M.1    Gasset, M.2    Colombo, G.3
  • 70
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang J., Cieplak P., and Kollman P.A. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21 2000 1049 1074
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 71
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 75
    • 67349152665 scopus 로고    scopus 로고
    • Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta 2-alpha 2 loop is modulated by long-range sequence effects
    • Christen B., Hornemann S., Damberger F.F., and Wuthrich K. Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta 2-alpha 2 loop is modulated by long-range sequence effects J. Mol. Biol. 389 2009 833 845
    • (2009) J. Mol. Biol. , vol.389 , pp. 833-845
    • Christen, B.1    Hornemann, S.2    Damberger, F.F.3    Wuthrich, K.4
  • 76
    • 52949137870 scopus 로고    scopus 로고
    • NMR structure of the bank vole prion protein at 20 °c contains a structured loop of residues 165-171
    • Christen B., Pérez D.R., Hornemann S., and Wuthrich K. NMR structure of the bank vole prion protein at 20 °C contains a structured loop of residues 165-171 J. Mol. Biol. 383 2008 306 312
    • (2008) J. Mol. Biol. , vol.383 , pp. 306-312
    • Christen, B.1    Pérez, D.R.2    Hornemann, S.3    Wuthrich, K.4
  • 79
    • 0029937271 scopus 로고    scopus 로고
    • NMR structure of the mouse prion protein domain PrP(121-231)
    • DOI 10.1038/382180a0
    • Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R., and Wuthrich K. NMR structure of the mouse prion protein domain PrP(121-321) Nature 382 1996 180 182 (Pubitemid 26242887)
    • (1996) Nature , vol.382 , Issue.6587 , pp. 180-182
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Billeter, M.4    Glockshuber, R.5    Wuthrich, K.6
  • 80
    • 0036708438 scopus 로고    scopus 로고
    • C to form β sheet using NMR structures and sequence alignments
    • Dima R., and Thirumalai D. Exploring the propensities of helices in PrPc to form beta sheet using NMR structures and sequence alignments Biophys. J. 83 2002 1268 1280 (Pubitemid 34977702)
    • (2002) Biophysical Journal , vol.83 , Issue.3 , pp. 1268-1280
    • Dima, R.I.1    Thirumalai, D.2
  • 83
    • 0029351694 scopus 로고
    • Protein motifs. 7. The four-helix bundle: What determines a fold?
    • Kamtekar S., and Hecht M.H. Protein motifs. 7. The four-helix bundle: what determines a fold? FASEB J. 9 1995 1013 1022
    • (1995) FASEB J. , vol.9 , pp. 1013-1022
    • Kamtekar, S.1    Hecht, M.H.2
  • 84
    • 33748191666 scopus 로고    scopus 로고
    • Fundamental processes of protein folding: Measuring the energetic balance between helix formation and hydrophobic interactions
    • DOI 10.1110/ps.062297006
    • Xian W., Connolly P.J., Oslin M., Hausrath A.C., and Osterhout J.J. Fundamental processes of protein folding: measuring the energetic balance between helix formation and hydrophobic interactions Protein Sci. 15 2006 2062 2070 (Pubitemid 44316009)
    • (2006) Protein Science , vol.15 , Issue.9 , pp. 2062-2070
    • Xian, W.1    Connolly, P.J.2    Oslin, M.3    Hausrath, A.C.4    Osterhout, J.J.5
  • 86
    • 48249132090 scopus 로고    scopus 로고
    • Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and voles
    • Agrimi U., Nonno R., Dell'Omo G., Di Bari M.A., Conte M., and Chiappini B. Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and voles PLoS Pathog. 4 2008 e1000113
    • (2008) PLoS Pathog. , vol.4 , pp. 1000113
    • Agrimi, U.1    Nonno, R.2    Dell'Omo, G.3    Di Bari, M.A.4    Conte, M.5    Chiappini, B.6
  • 88
    • 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., Liu H., Ulyanov N.B., Farr-Jones S., Zhang H., and Donne D.G. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform Proc. Natl Acad. Sci. USA 94 1997 10086 10091
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10086-10091
    • James, T.L.1    Liu, H.2    Ulyanov, N.B.3    Farr-Jones, S.4    Zhang, H.5    Donne, D.G.6
  • 91
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Kaneko K., Zulianello L., Scott M., Cooper C.M., Wallace A.C., and James T.L. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation Proc. Natl Acad. Sci. USA 94 1997 10069 10074
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10069-10074
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3    Cooper, C.M.4    Wallace, A.C.5    James, T.L.6
  • 93
    • 78649507705 scopus 로고    scopus 로고
    • Parallel synthesis, evaluation, and preliminary structure-activity relationship of 2,5-diamino-1,4-benzoquinones as a novel class of bivalent anti-prion compound
    • Bongarzone S., Tran H.N.A., Cavalli A., Roberti M., Carloni P., Legname G., and Bolognesi M.L. Parallel synthesis, evaluation, and preliminary structure-activity relationship of 2,5-diamino-1,4-benzoquinones as a novel class of bivalent anti-prion compound J. Med. Chem. 53 2010 8197 8201
    • (2010) J. Med. Chem. , vol.53 , pp. 8197-8201
    • Bongarzone, S.1    Tran, H.N.A.2    Cavalli, A.3    Roberti, M.4    Carloni, P.5    Legname, G.6    Bolognesi, M.L.7
  • 94
    • 79751525877 scopus 로고    scopus 로고
    • High hydrophobic amino acid exposure is responsible of the neurotoxic effects induced by E200K or D202N disease-related mutations of the human prion protein
    • Corsaro A., Thellung S., Bucciarelli T., Scotti L., Chiovitti K., and Villa V. High hydrophobic amino acid exposure is responsible of the neurotoxic effects induced by E200K or D202N disease-related mutations of the human prion protein Int. J. Biochem. Cell Biol. 43 2010 372 382
    • (2010) Int. J. Biochem. Cell Biol. , vol.43 , pp. 372-382
    • Corsaro, A.1    Thellung, S.2    Bucciarelli, T.3    Scotti, L.4    Chiovitti, K.5    Villa, V.6
  • 97
    • 1242339661 scopus 로고    scopus 로고
    • The C-terminal Globular Domain of the Prion Protein Is Necessary and Sufficient for Import into the Endoplasmic Reticulum
    • DOI 10.1074/jbc.M309570200
    • Heske J., Heller U., Winklhofer K.F., and Tatzelt J. The C-terminal globular domain of the prion protein is necessary and sufficient for import into the endoplasmic reticulum J. Biol. Chem. 279 2004 5435 5443 (Pubitemid 38220567)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5435-5443
    • Heske, J.1    Heller, U.2    Winklhofer, K.F.3    Tatzelt, J.4
  • 98
    • 67650915066 scopus 로고    scopus 로고
    • Selective processing and metabolism of disease-causing mutant prion proteins
    • Ashok A., and Hegde R.S. Selective processing and metabolism of disease-causing mutant prion proteins PLoS Pathog. 5 2009 e1000479
    • (2009) PLoS Pathog. , vol.5 , pp. 1000479
    • Ashok, A.1    Hegde, R.S.2
  • 99
    • 0037306746 scopus 로고    scopus 로고
    • Aggresome formation by mutant prion proteins: The unfolding role of proteasomes in familial prion disorders
    • Mishra R.S., Bose S., Gu Y., Li R., and Singh N. Aggresome formation by mutant prion proteins: the unfolding role of proteasomes in familial prion disorders J. Alzheimers Dis. 5 2003 15 23 (Pubitemid 36422847)
    • (2003) Journal of Alzheimer's Disease , vol.5 , Issue.1 , pp. 15-23
    • Mishra, R.S.1    Bose, S.2    Gu, Y.3    Li, R.4    Singh, N.5
  • 103
    • 70349490056 scopus 로고    scopus 로고
    • Regulating the conformation of prion protein through ligand binding
    • Yamamoto N., and Kuwata K. Regulating the conformation of prion protein through ligand binding J. Phys. Chem. B 113 2009 12853 12856
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12853-12856
    • Yamamoto, N.1    Kuwata, K.2
  • 104
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • DOI 10.1074/jbc.M303005200
    • 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 (Pubitemid 37102332)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 105
    • 77957317648 scopus 로고    scopus 로고
    • Constant-pH molecular dynamics simulations reveal a beta-rich form of the human prion protein
    • Campos S.R.R., Machuqueiro M., and Baptista A.M. Constant-pH molecular dynamics simulations reveal a beta-rich form of the human prion protein J. Phys. Chem. B 114 2010 12692 12700
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12692-12700
    • Campos, S.R.R.1    MacHuqueiro, M.2    Baptista, A.M.3
  • 106
    • 0344796204 scopus 로고
    • Ion-water interaction potentials derived from free energy perturbation simulations
    • Åqvist J. Ion-water interaction potentials derived from free energy perturbation simulations J. Phys. Chem. 94 1990 8021 8024
    • (1990) J. Phys. Chem. , vol.94 , pp. 8021-8024
    • Åqvist, J.1
  • 108
    • 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
  • 109
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B., Kutzner C., van der Spoel D., and Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 110
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • Nose S., and Klein M. Constant pressure molecular dynamics for molecular systems Mol. Phys. 50 1983 1055 1076
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.2
  • 111
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant pressure and/or temperature
    • Andersen H. Molecular dynamics simulations at constant pressure and/or temperature J. Chem. Phys. 72 1980 2384 2393
    • (1980) J. Chem. Phys. , vol.72 , pp. 2384-2393
    • Andersen, H.1
  • 112
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • DOI 10.1063/1.328693
    • Parrinello M., and Rahman A. Polymorphic transitions in single crystals: a new molecular dynamics method J. Appl. Phys. 52 1981 7182 7190 (Pubitemid 12456820)
    • (1981) Journal of Applied Physics , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.