메뉴 건너뛰기




Volumn 412, Issue 4, 2011, Pages 660-673

Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with v210i mutation

Author keywords

genetic Creutzfeldt Jakob disease; mutants; NMR structure determination; prions; transmissible spongiform encephalopathies

Indexed keywords

PRION PROTEIN; RECOMBINANT PROTEIN;

EID: 84860389727     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.067     Document Type: Article
Times cited : (53)

References (91)
  • 1
    • 33645290776 scopus 로고    scopus 로고
    • The prion protein and lipid rafts
    • Taylor D.R., and Hooper N.M. The prion protein and lipid rafts Mol. Membr. Biol. 23 2006 89 99
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 89-99
    • Taylor, D.R.1    Hooper, N.M.2
  • 4
    • 77952125527 scopus 로고    scopus 로고
    • Neurodevelopmental expression and localization of the cellular prion protein in the central nervous system of the mouse
    • Benvegnu S., Poggiolini I., and Legname G. Neurodevelopmental expression and localization of the cellular prion protein in the central nervous system of the mouse J. Comp. Neurol. 518 2010 1879 1891
    • (2010) J. Comp. Neurol. , vol.518 , pp. 1879-1891
    • Benvegnu, S.1    Poggiolini, I.2    Legname, G.3
  • 7
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler H., Fischer M., Lang Y., Bluethmann H., Lipp H.P., and DeArmond S.J. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein Nature 356 1992 577 582
    • (1992) Nature , vol.356 , pp. 577-582
    • Bueler, H.1    Fischer, M.2    Lang, Y.3    Bluethmann, H.4    Lipp, H.P.5    Dearmond, S.J.6
  • 8
    • 0345505687 scopus 로고    scopus 로고
    • Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival
    • DOI 10.1016/S1044-7431(02)00014-3
    • Chen S., Mange A., Dong L., Lehmann S., and Schachner M. Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival Mol. Cell. Neurosci. 22 2003 227 233 (Pubitemid 36379186)
    • (2003) Molecular and Cellular Neuroscience , vol.22 , Issue.2 , pp. 227-233
    • Chen, S.1    Mange, A.2    Dong, L.3    Lehmann, S.4    Schachner, M.5
  • 9
    • 28844477599 scopus 로고    scopus 로고
    • Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro
    • DOI 10.1111/j.1471-4159.2005.03469.x
    • Kanaani J., Prusiner S.B., Diacovo J., Baekkeskov S., and Legname G. Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro J. Neurochem. 95 2005 1373 1386 (Pubitemid 41779262)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.5 , pp. 1373-1386
    • Kanaani, J.1    Prusiner, S.B.2    Diacovo, J.3    Baekkeskov, S.4    Legname, G.5
  • 12
    • 0031456947 scopus 로고    scopus 로고
    • Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
    • Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., and Cohen F.E. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible Proc. Natl Acad. Sci. USA 94 1997 13452 13457
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13452-13457
    • Donne, D.G.1    Viles, J.H.2    Groth, D.3    Mehlhorn, I.4    James, T.L.5    Cohen, F.E.6
  • 13
    • 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
  • 19
    • 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., Perez 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    Perez, D.R.2    Hornemann, S.3    Wuthrich, K.4
  • 20
    • 77953808355 scopus 로고    scopus 로고
    • Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein
    • Perez D.R., Damberger F.F., and Wuthrich K. Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein J. Mol. Biol. 400 2010 121 128
    • (2010) J. Mol. Biol. , vol.400 , pp. 121-128
    • Perez, D.R.1    Damberger, F.F.2    Wuthrich, K.3
  • 21
    • 77957793037 scopus 로고    scopus 로고
    • Unique structural characteristics of the rabbit prion protein
    • Wen Y., Li J., Yao W., Xiong M., Hong J., and Peng Y. Unique structural characteristics of the rabbit prion protein J. Biol. Chem. 285 2010 31682 31693
    • (2010) J. Biol. Chem. , vol.285 , pp. 31682-31693
    • Wen, Y.1    Li, J.2    Yao, W.3    Xiong, M.4    Hong, J.5    Peng, Y.6
  • 24
    • 0034869693 scopus 로고    scopus 로고
    • Crystal structure of the human prion protein reveals a mechanism for oligomerization
    • DOI 10.1038/nsb0901-770
    • Knaus K.J., Morillas M., Swietnicki W., Malone M., Surewicz W.K., and Yee V.C. Crystal structure of the human prion protein reveals a mechanism for oligomerization Nat. Struct. Biol. 8 2001 770 774 (Pubitemid 32803594)
    • (2001) Nature Structural Biology , vol.8 , Issue.9 , pp. 770-774
    • Knaus, K.J.1    Morillas, M.2    Swietnicki, W.3    Malone, M.4    Surewicz, W.K.5    Yee, V.C.6
  • 26
    • 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., Surewicz W.K., and Yee V.C. Conformational diversity in prion protein variants influences intermolecular β-sheet formation EMBO J. 29 2010 251 262
    • (2010) EMBO J. , vol.29 , pp. 251-262
    • Lee, S.1    Antony, L.2    Hartmann, R.3    Knaus, K.J.4    Surewicz, K.5    Surewicz, W.K.6    Yee, V.C.7
  • 28
    • 4544224048 scopus 로고    scopus 로고
    • Antiprion immunotherapy: To suppress or to stimulate?
    • DOI 10.1038/nri1437
    • Aguzzi A., and Sigurdson C.J. Antiprion immunotherapy: to suppress or to stimulate? Nat. Rev., Immunol. 4 2004 725 736 (Pubitemid 39223078)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.9 , pp. 725-736
    • Aguzzi, A.1    Sigurdson, C.J.2
  • 30
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey B.W., Dong A., Bhat K.S., Ernst D., Hayes S.F., and Caughey W.S. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy Biochemistry 30 1991 7672 7680
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 31
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-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 α-helices into β-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
  • 35
    • 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
  • 36
    • 70349858126 scopus 로고    scopus 로고
    • Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils
    • Sim V.L., 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.L.1    Caughey, B.2
  • 38
    • 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
  • 40
    • 77954238207 scopus 로고    scopus 로고
    • Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3
    • Adrover M., Pauwels K., Prigent S., de Chiara C., Xu Z., and Chapuis C. Prion fibrillization is mediated by a native structural element that comprises 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    Prigent, S.3    De Chiara, C.4    Xu, Z.5    Chapuis, C.6
  • 41
    • 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
  • 42
    • 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
  • 43
    • 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., Surewicz K., and Surewicz W.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
  • 44
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling G.C., Scott M., Mastrianni J., Gabizon R., Torchia M., and Cohen F.E. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein Cell 83 1995 79 90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6
  • 45
    • 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
  • 46
    • 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
  • 47
    • 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
  • 51
    • 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., 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.1    Swietnicki, W.2    Zagorski, M.G.3    Surewicz, W.K.4    Sonnichsen, F.D.5
  • 55
    • 0030587512 scopus 로고    scopus 로고
    • A Japanese case of Creutzfeldt-Jakob disease with a point mutation in the prion protein gene at codon 210
    • DOI 10.1016/0022-510X(96)00157-8
    • Furukawa H., Kitamoto T., Hashiguchi H., and Tateishi J. A Japanese case of Creutzfeldt-Jakob disease with a point mutation in the prion protein gene at codon 210 J. Neurol. Sci. 141 1996 120 122 (Pubitemid 26297742)
    • (1996) Journal of the Neurological Sciences , vol.141 , Issue.1-2 , pp. 120-122
    • Furukawa, H.1    Kitamoto, T.2    Hashiguchi, H.3    Tateishi, J.4
  • 56
    • 0030297073 scopus 로고    scopus 로고
    • Panencephalitic Creutzfeldt-Jakob disease in a Chinese family. Unusual presentation with PrP codon 210 mutation and identification by PCR-SSCP
    • Shyu W.C., Hsu Y.D., Kao M.C., and Tsao W.L. Panencephalitic Creutzfeldt-Jakob disease in a Chinese family. Unusual presentation with PrP codon 210 mutation and identification by PCR-SSCP J. Neurol. Sci. 143 1996 176 180
    • (1996) J. Neurol. Sci. , vol.143 , pp. 176-180
    • Shyu, W.C.1    Hsu, Y.D.2    Kao, M.C.3    Tsao, W.L.4
  • 57
    • 0030902421 scopus 로고    scopus 로고
    • Identification of the prion protein allotypes which accumulate in the brain of sporadic and familial Creutzfeldt-Jakob disease patients
    • Silvestrini M.C., Cardone F., Maras B., Pucci P., Barra D., Brunori M., and Pocchiari M. Identification of the prion protein allotypes which accumulate in the brain of sporadic and familial Creutzfeldt-Jakob disease patients Nat. Med. 3 1997 521 525 (Pubitemid 27198649)
    • (1997) Nature Medicine , vol.3 , Issue.5 , pp. 521-525
    • Silvestrini, M.C.1    Cardone, F.2    Maras, B.3    Pucci, P.4    Barra, D.5    Brunori, M.6    Pocchiari, M.7
  • 58
    • 0032852215 scopus 로고    scopus 로고
    • Mutation at codon 210 (V210I) of the prion protein gene in a North African patient with Creutzfeldt-Jakob disease
    • DOI 10.1016/S0022-510X(99)00179-3, PII S0022510X99001793
    • Mouillet-Richard S., Teil C., Lenne M., Hugon S., Taleb O., and Laplanche J.L. Mutation at codon 210 (V210I) of the prion protein gene in a North African patient with Creutzfeldt-Jakob disease J. Neurol. Sci. 168 1999 141 144 (Pubitemid 29467433)
    • (1999) Journal of the Neurological Sciences , vol.168 , Issue.2 , pp. 141-144
    • Mouillet-Richard, S.1    Teil, C.2    Lenne, M.3    Hugon, S.4    Taleb, O.5    Laplanche, J.-L.6
  • 59
    • 0035654072 scopus 로고    scopus 로고
    • Familial Creutzfeldt-Jakob disease associated with a point mutation at codon 210 of the prion protein gene
    • Huang N., Marie S.K., Kok F., and Nitrini R. Familial Creutzfeldt-Jakob disease associated with a point mutation at codon 210 of the prion protein gene Arq. Neuro-Psiquiatr. 59 2001 932 935 (Pubitemid 33607521)
    • (2001) Arquivos de Neuro-Psiquiatria , vol.59 , Issue.4 , pp. 932-935
    • Huang, N.1    Marie, S.K.N.2    Kok, F.3    Nitrini, R.4
  • 62
    • 18144393080 scopus 로고    scopus 로고
    • High incidence of genetic human transmissible spongiform encephalopathies in Italy
    • DOI 10.1212/01.WNL.0000160118.26865.11
    • Ladogana A., Puopolo M., Poleggi A., Almonti S., Mellina V., Equestre M., and Pocchiari M. High incidence of genetic human transmissible spongiform encephalopathies in Italy Neurology 64 2005 1592 1597 (Pubitemid 40617697)
    • (2005) Neurology , vol.64 , Issue.9 , pp. 1592-1597
    • Ladogana, A.1    Puopolo, M.2    Poleggi, A.3    Almonti, S.4    Mellina, V.5    Equestre, M.6    Pocchiari, M.7
  • 65
    • 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
  • 66
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • 13C NMR chemical shifts can predict disulfide bond formation J. Biomol. NMR 18 2000 165 171
    • (2000) J. Biomol. NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 67
    • 77951666856 scopus 로고    scopus 로고
    • Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts
    • Shen Y., and Bax A. Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts J. Biomol. NMR 46 2010 199 204
    • (2010) J. Biomol. NMR , vol.46 , pp. 199-204
    • Shen, Y.1    Bax, A.2
  • 68
    • 77954758998 scopus 로고    scopus 로고
    • The unfolded state of the murine prion protein and properties of single-point mutants related to human prion diseases
    • Gerum C., Schlepckow K., and Schwalbe H. The unfolded state of the murine prion protein and properties of single-point mutants related to human prion diseases J. Mol. Biol. 401 2010 7 12
    • (2010) J. Mol. Biol. , vol.401 , pp. 7-12
    • Gerum, C.1    Schlepckow, K.2    Schwalbe, H.3
  • 69
    • 73249121817 scopus 로고    scopus 로고
    • Unfolded-state structure and dynamics influence the fibril formation of human prion protein
    • Gerum C., Silvers R., Wirmer-Bartoschek J., and Schwalbe H. Unfolded-state structure and dynamics influence the fibril formation of human prion protein Angew. Chem., Int. Ed. Engl. 48 2009 9452 9456
    • (2009) Angew. Chem., Int. Ed. Engl. , vol.48 , pp. 9452-9456
    • Gerum, C.1    Silvers, R.2    Wirmer-Bartoschek, J.3    Schwalbe, H.4
  • 70
    • 77953427821 scopus 로고    scopus 로고
    • Prion protein amyloid formation involves structural rearrangements in the C-terminal domain
    • Kumar J., Sreeramulu S., Schmidt T.L., Richter C., Vonck J., and Heckel A. Prion protein amyloid formation involves structural rearrangements in the C-terminal domain ChemBioChem 11 2010 1208 1213
    • (2010) ChemBioChem , vol.11 , pp. 1208-1213
    • Kumar, J.1    Sreeramulu, S.2    Schmidt, T.L.3    Richter, C.4    Vonck, J.5    Heckel, A.6
  • 71
    • 40549105157 scopus 로고    scopus 로고
    • Intracellular accumulation of a mild-denatured monomer of the human PrP fragment 90-231, as possible mechanism of its neurotoxic effects
    • Chiovitti K., Corsaro A., Thellung S., Villa V., Paludi D., and D'Arrigo C. Intracellular accumulation of a mild-denatured monomer of the human PrP fragment 90-231, as possible mechanism of its neurotoxic effects J. Neurochem. 103 2007 2597 2609
    • (2007) J. Neurochem. , vol.103 , pp. 2597-2609
    • Chiovitti, K.1    Corsaro, A.2    Thellung, S.3    Villa, V.4    Paludi, D.5    D'Arrigo, C.6
  • 72
    • 79959967767 scopus 로고    scopus 로고
    • Human PrP90-231-induced cell death is associated with intracellular accumulation of insoluble and protease-resistant macroaggregates and lysosomal dysfunction
    • Thellung S., Corsaro A., Villa V., Simi A., Vella S., Pagano A., and Florio T. Human PrP90-231-induced cell death is associated with intracellular accumulation of insoluble and protease-resistant macroaggregates and lysosomal dysfunction Cell Death Dis. 2 2011 e138
    • (2011) Cell Death Dis. , vol.2 , pp. 138
    • Thellung, S.1    Corsaro, A.2    Villa, V.3    Simi, A.4    Vella, S.5    Pagano, A.6    Florio, T.7
  • 73
    • 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 2011 372 382
    • (2011) 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
  • 74
    • 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
  • 75
    • 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 78 2010 3270 3280
    • (2010) Proteins , vol.78 , pp. 3270-3280
    • Rossetti, G.1    Giachin, G.2    Legname, G.3    Carloni, P.4
  • 77
    • 67349152665 scopus 로고    scopus 로고
    • Prion protein NMR structure from Tammar Wallaby (Macropus eugenii) shows that the β2-α2 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 β2-α2 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
  • 80
    • 84860405204 scopus 로고    scopus 로고
    • Insights into the mechanism of prion strain mutation from chronic wasting disease
    • Y.O. Chernoff, Landes Bioscience Montreal, QC Canada
    • Telling G.C. Insights into the mechanism of prion strain mutation from chronic wasting disease Y.O. Chernoff, Prion 2011 vol. 5 2011 Landes Bioscience Montreal, QC Canada 2
    • (2011) Prion 2011 , vol.5 , pp. 2
    • Telling, G.C.1
  • 82
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures Protein Expression Purif. 41 2005 207 234
    • (2005) Protein Expression Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 83
    • 0035095521 scopus 로고    scopus 로고
    • Large-scale purification of a stable form of recombinant tobacco etch virus protease
    • Lucast L.J., Batey R.T., and Doudna J.A. Large-scale purification of a stable form of recombinant tobacco etch virus protease BioTechniques 30 2001 544 546
    • (2001) BioTechniques , vol.30 , pp. 544-546
    • Lucast, L.J.1    Batey, R.T.2    Doudna, J.A.3
  • 87
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • DOI 10.1006/jmbi.1997.1284
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298 (Pubitemid 27460230)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 88
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227 (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 89
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA-A self-parameterizing force field
    • Krieger E., Koraimann G., and Vriend G. Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field Proteins: Struct., Funct., Genet. 47 2002 477 486
    • (2002) Proteins: Struct., Funct., Genet. , vol.47 , pp. 477-486
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 91
    • 0025398721 scopus 로고
    • WHAT IF. A molecular modeling and drug design program
    • DOI 10.1016/0263-7855(90)80070-V
    • Vriend G. WHAT IF: a molecular modelling and drug design program J. Mol. Graphics 9 1990 52 56 (Pubitemid 20717037)
    • (1990) Journal of Molecular Graphics , vol.8 , Issue.1 , pp. 52-56
    • Vriend, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.