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Volumn 44, Issue 48, 2005, Pages 15880-15888

Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CONFORMATIONS; DISEASES; GENES; MUTAGENESIS; PH EFFECTS;

EID: 28544443624     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051455+     Document Type: Article
Times cited : (77)

References (60)
  • 2
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge, J. (2001) Prion diseases of humans and animals: Their causes and molecular basis, Annu. Rev. Neurosci. 24, 519-550.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 3
    • 9444267651 scopus 로고    scopus 로고
    • The state of the prion
    • Weissmann, C. (2004) The state of the prion, Nat. Rev. Microbiol. 2, 861-871.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 861-871
    • Weissmann, C.1
  • 4
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: One century of evolving concepts
    • Aguzzi, A., and Polymenidou, M. (2004) Mammalian prion biology: One century of evolving concepts, Cell 116, 313-327.
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 5
    • 0035223716 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies and prion protein interconversions
    • Caughey, B., and Chesebro, B. (2001) Transmissible spongiform encephalopathies and prion protein interconversions, Adv. Virus Res. 56, 277-311.
    • (2001) Adv. Virus Res. , vol.56 , pp. 277-311
    • Caughey, B.1    Chesebro, B.2
  • 6
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • Caughey, B. (2001) Interactions between prion protein isoforms: The kiss of death? Trends Biochem. Sci. 26, 235-242.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 235-242
    • Caughey, B.1
  • 7
    • 0034943846 scopus 로고    scopus 로고
    • Prion protein diversity and disease in the transmissible spongiform encephalopathies
    • Priola, S. A. (2001) Prion protein diversity and disease in the transmissible spongiform encephalopathies, Adv. Protein Chem. 57, 1-27.
    • (2001) Adv. Protein Chem. , vol.57 , pp. 1-27
    • Priola, S.A.1
  • 8
    • 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. (1993) Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing, Biochemistry 32, 1991-2002.
    • (1993) Biochemistry , vol.32 , 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
  • 10
    • 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. (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy, Biochemistry 30, 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
  • 12
    • 0027363495 scopus 로고
    • Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity
    • Safar, J., Roller, P. P., Gajdusek, D. C., and Gibbs, C. J., Jr. (1993) Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity, Protein Sci. 2, 2206-2216.
    • (1993) Protein Sci. , vol.2 , pp. 2206-2216
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 13
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. (1982) Novel proteinaceous infectious particles cause scrapie, Science 216, 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 14
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla, J., Saa, P., Hetz, C., and Soto, C. (2005) In vitro generation of infectious scrapie prions, Cell 121, 195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 15
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka, M., Chien, P., Naber, N., Cooke, R., and Weissman, J. S. (2004) Conformational variations in an infectious protein determine prion strain differences, Nature 428, 323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 16
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King, C. Y., and Diaz-Avalos, R. (2004) Protein-only transmission of three yeast prion strains, Nature 428, 319-323.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 17
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien, P., Weissman, J. S., and DePace, A. H. (2004) Emerging principles of conformation-based prion inheritance, Annu. Rev. Biochem. 73, 617-656.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    Depace, A.H.3
  • 19
    • 0025865455 scopus 로고
    • Amino acid polymorphism in human prion protein and age at death in inherited prion disease
    • Baker, H. E., Poulter, M., Crow, T. J., Frith, C. D., Lofthouse, R., and Ridley, R. M. (1991) Amino acid polymorphism in human prion protein and age at death in inherited prion disease, Lancet 337, 1286.
    • (1991) Lancet , vol.337 , pp. 1286
    • Baker, H.E.1    Poulter, M.2    Crow, T.J.3    Frith, C.D.4    Lofthouse, R.5    Ridley, R.M.6
  • 20
    • 0025859996 scopus 로고
    • Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease
    • Collinge, J., Palmer, M. S., and Dryden, A. J. (1991) Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease, Lancet 337, 1441-1442.
    • (1991) Lancet , vol.337 , pp. 1441-1442
    • Collinge, J.1    Palmer, M.S.2    Dryden, A.J.3
  • 24
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W. K. (1999) Membrane environment alters the conformational structure of the recombinant human prion protein, J. Biol. Chem. 274, 36859-36865.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 25
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding
    • Zahn, R., von Schroetter, C., and Wuthrich, K. (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding, FEBS Lett. 417, 400-404.
    • (1997) FEBS Lett. , vol.417 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wuthrich, K.3
  • 26
    • 0037073678 scopus 로고    scopus 로고
    • Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form
    • Vanik, D. L., and Surewicz, W. K. (2002) Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form, J. Biol. Chem. 277, 49065-49070.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49065-49070
    • Vanik, D.L.1    Surewicz, W.K.2
  • 27
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • Naiki, H., Higuchi, K., Hosokawa, M., and Takeda, T. (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1, Anal. Biochem. 177, 244-249.
    • (1989) Anal. Biochem. , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 28
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz, W. K., and Mantsch, H. H. (1988) New insight into protein secondary structure from resolution-enhanced infrared spectra, Biochim. Biophys. Acta 952, 115-130.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 29
    • 0037819879 scopus 로고    scopus 로고
    • Hierarchical assembly of β2-microglobulin amyloid in vitro revealed by atomic force microscopy
    • Kad, N. M., Myers, S. L., Smith, D. P., Smith, D. A., Radford, S. E., and Thomson, N. H. (2003) Hierarchical assembly of β2-microglobulin amyloid in vitro revealed by atomic force microscopy, J. Mol. Biol. 330, 785-797.
    • (2003) J. Mol. Biol. , vol.330 , pp. 785-797
    • Kad, N.M.1    Myers, S.L.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5    Thomson, N.H.6
  • 30
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 31
    • 0037160126 scopus 로고    scopus 로고
    • Kinetic intermediate in the folding of human prion protein
    • Apetri, A. C., and Surewicz, W. K. (2002) Kinetic intermediate in the folding of human prion protein, J. Biol. Chem. 277, 44589-44592.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44589-44592
    • Apetri, A.C.1    Surewicz, W.K.2
  • 32
    • 0032979289 scopus 로고    scopus 로고
    • Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates
    • Wildegger, G., Liemann, S., and Glockshuber, R. (1999) Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates, Nat. Struct. Biol. 6, 550-553.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 550-553
    • Wildegger, G.1    Liemann, S.2    Glockshuber, R.3
  • 33
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • Swietnicki, W., Morillas, M., Chen, S. G., Gambetti, P., and Surewicz, W. K. (2000) Aggregation and fibrillization of the recombinant human prion protein huPrP90-231, Biochemistry 39, 424-431.
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 34
    • 0035849540 scopus 로고    scopus 로고
    • On the mechanism of α-helix to β-sheet transition in the recombinant prion protein
    • Morillas, M., Vanik, D. L., and Surewicz, W. K. (2001) On the mechanism of α-helix to β-sheet transition in the recombinant prion protein, Biochemistry 40, 6982-6987.
    • (2001) Biochemistry , vol.40 , pp. 6982-6987
    • Morillas, M.1    Vanik, D.L.2    Surewicz, W.K.3
  • 37
    • 1542379868 scopus 로고    scopus 로고
    • Autocatalytic conversion of recombinant prion proteins displays a species barrier
    • Baskakov, I. V. (2004) Autocatalytic conversion of recombinant prion proteins displays a species barrier, J. Biol. Chem. 279, 7671-7677.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7671-7677
    • Baskakov, I.V.1
  • 38
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J. D., and Lansbury, P. T., Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins, Annu. Rev. Biochem. 66, 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 39
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., Mantsch, H. H., and Chapman, D. (1993) Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment, Biochemistry 32, 389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 40
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • Zandomeneghi, G., Krebs, M. R., McCammon, M. G., and Fandrich, M. (2004) FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils, Protein Sci. 13, 3314-3321.
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.2    McCammon, M.G.3    Fandrich, M.4
  • 41
    • 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. (1999) Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein, Biochemistry 38, 3258-3267.
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 42
    • 3142615402 scopus 로고    scopus 로고
    • The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC
    • Hosszu, L. L., Jackson, G. S., Trevitt, C. R., Jones, S., Batchelor, M., Bhelt, D., Prodromidou, K., Clarke, A. R., Waltho, J. P., and Collinge, J. (2004) The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC, J. Biol. Chem. 279, 28515-28521.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28515-28521
    • Hosszu, L.L.1    Jackson, G.S.2    Trevitt, C.R.3    Jones, S.4    Batchelor, M.5    Bhelt, D.6    Prodromidou, K.7    Clarke, A.R.8    Waltho, J.P.9    Collinge, J.10
  • 43
    • 0038266598 scopus 로고    scopus 로고
    • Atypical effect of salts on the thermodynamic stability of human prion protein
    • Apetri, A. C., and Surewicz, W. K. (2003) Atypical effect of salts on the thermodynamic stability of human prion protein, J. Biol. Chem. 278, 22187-22192.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22187-22192
    • Apetri, A.C.1    Surewicz, W.K.2
  • 44
    • 2342432162 scopus 로고    scopus 로고
    • The effect of disease-associated mutations on the folding pathway of human prion protein
    • Apetri, A. C., Surewicz, K., and Surewicz, W. K. (2004) The effect of disease-associated mutations on the folding pathway of human prion protein, J. Biol. Chem. 279, 18008-18014.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18008-18014
    • Apetri, A.C.1    Surewicz, K.2    Surewicz, W.K.3
  • 46
    • 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. (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein, J. Biol. Chem. 273, 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
  • 47
    • 23644449548 scopus 로고    scopus 로고
    • Influence of the N-terminal domain on the aggregation properties of the prion protein
    • Frankenfield, K. N., Powers, E. T., and Kelly, J. W. (2005) Influence of the N-terminal domain on the aggregation properties of the prion protein, Protein Sci. 14, 2154-2166.
    • (2005) Protein Sci. , vol.14 , pp. 2154-2166
    • Frankenfield, K.N.1    Powers, E.T.2    Kelly, J.W.3
  • 48
    • 15244347485 scopus 로고    scopus 로고
    • Rapid formation of amyloid from α-monomeric recombinant human PrP in vitro
    • Tahiri-Alaoui, A., and James, W. (2005) Rapid formation of amyloid from α-monomeric recombinant human PrP in vitro, Protein Sci. 14, 942-947.
    • (2005) Protein Sci. , vol.14 , pp. 942-947
    • Tahiri-Alaoui, A.1    James, W.2
  • 50
    • 0345493918 scopus 로고    scopus 로고
    • Molecular dynamics simulations of human prion protein: Importance of correct treatment of electrostatic interactions
    • Zuegg, J., and Gready, J. E. (1999) Molecular dynamics simulations of human prion protein: Importance of correct treatment of electrostatic interactions, Biochemistry 38, 13862-13876.
    • (1999) Biochemistry , vol.38 , pp. 13862-13876
    • Zuegg, J.1    Gready, J.E.2
  • 51
    • 21244436720 scopus 로고    scopus 로고
    • Misfolding pathways of the prion protein probed by molecular dynamics simulations
    • Barducci, A., Chelli, R., Procacci, P., and Schettino, V. (2005) Misfolding pathways of the prion protein probed by molecular dynamics simulations, Biophys. J. 88, 1334-1343.
    • (2005) Biophys. J. , vol.88 , pp. 1334-1343
    • Barducci, A.1    Chelli, R.2    Procacci, P.3    Schettino, V.4
  • 52
    • 0035853093 scopus 로고    scopus 로고
    • Mapping the early steps in the pH-induced conformational conversion of the prion protein
    • Alonso, D. O., DeArmond, S. J., Cohen, F. E., and Daggett, V. (2001) Mapping the early steps in the pH-induced conformational conversion of the prion protein, Proc. Natl. Acad. Sci. U.S.A. 98, 2985-2989.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2985-2989
    • Alonso, D.O.1    Dearmond, S.J.2    Cohen, F.E.3    Daggett, V.4
  • 54
    • 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. (2000) Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases, J. Biol. Chem. 275, 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
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • Calzolai, L., and Zahn, R. (2003) Influence of pH on NMR structure and stability of the human prion protein globular domain, J. Biol. Chem. 278, 35592-35596.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 56
    • 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
    • Shamsir, M. S., and Dalby, A. R. (2005) One gene, two diseases, and three conformations: Molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures, Proteins 59, 275-290.
    • (2005) Proteins , vol.59 , pp. 275-290
    • Shamsir, M.S.1    Dalby, A.R.2
  • 57
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in β-sheet conformations of abnormal prion protein
    • Caughey, B., Raymond, G. J., and Bessen, R. A. (1998) Strain-dependent differences in β-sheet conformations of abnormal prion protein, J. Biol. Chem. 273, 32230-32235.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 58
    • 17544366508 scopus 로고    scopus 로고
    • Effect of the D178N mutation and the codon 129 polymorphism on the metabolism of the prion protein
    • Petersen, R. B., Parchi, P., Richardson, S. L., Urig, C. B., and Gambetti, P. (1996) Effect of the D178N mutation and the codon 129 polymorphism on the metabolism of the prion protein, J. Biol. Chem. 271, 12661-12668.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12661-12668
    • Petersen, R.B.1    Parchi, P.2    Richardson, S.L.3    Urig, C.B.4    Gambetti, P.5
  • 59
    • 3843131903 scopus 로고    scopus 로고
    • Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant: Implications for disease susceptibility to Creutzfeldt-Jakob disease
    • Tahiri-Alaoui, A., Gill, A. C., Disterer, P., and James, W. (2004) Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant: Implications for disease susceptibility to Creutzfeldt-Jakob disease, J. Biol. Chem. 279, 31390-31397.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31390-31397
    • Tahiri-Alaoui, A.1    Gill, A.C.2    Disterer, P.3    James, W.4
  • 60
    • 18144416596 scopus 로고    scopus 로고
    • The presence of valine at residue 129 in human prion protein accelerates amyloid formation
    • Baskakov, I., Disterer, P., Breydo, L., Shaw, M., Gill, A., James, W., and Tahiri-Alaoui, A. (2005) The presence of valine at residue 129 in human prion protein accelerates amyloid formation, FEBS Lett. 579, 2589-2596.
    • (2005) FEBS Lett. , vol.579 , pp. 2589-2596
    • Baskakov, I.1    Disterer, P.2    Breydo, L.3    Shaw, M.4    Gill, A.5    James, W.6    Tahiri-Alaoui, A.7


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