메뉴 건너뛰기




Volumn 77, Issue 5, 1999, Pages 412-418

Alzheimer's and prion disease as disorders of protein conformation: Implications for the design of novel therapeutic approaches

Author keywords

Sheet breaker peptides; Alzheimer's disease; Protein conformation; Spongiform encephalopathies; Therapy

Indexed keywords

AMYLOID A PROTEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; PRION PROTEIN;

EID: 0033044804     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001090050371     Document Type: Review
Times cited : (79)

References (74)
  • 1
    • 0026468018 scopus 로고
    • Stability of a model β-sheet in water
    • 1. Tobias DJ, Sneddon SF, Brooks CL (1992) Stability of a model β-sheet in water. J Mol Biol 227:1244-1252
    • (1992) J Mol Biol , vol.227 , pp. 1244-1252
    • Tobias, D.J.1    Sneddon, S.F.2    Brooks, C.L.3
  • 2
    • 0030572683 scopus 로고    scopus 로고
    • For protein misassembly, it's the "I" decade
    • 2. Wetzel R (1996) For protein misassembly, it's the "I" decade. Cell 86:699-702
    • (1996) Cell , vol.86 , pp. 699-702
    • Wetzel, R.1
  • 3
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • 3. Thomas PJ, Qu B-H, Pedersen PL (1995) Defective protein folding as a basis of human disease. Trends Biochem Sci 20:456-459
    • (1995) Trends Biochem Sci , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.-H.2    Pedersen, P.L.3
  • 4
    • 0029011597 scopus 로고
    • Defective protein folding as a cause of disease
    • 4. Sifers RN (1995) Defective protein folding as a cause of disease. Nat Struct Biol 2:355-357
    • (1995) Nat Struct Biol , vol.2 , pp. 355-357
    • Sifers, R.N.1
  • 5
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • 5. Kelly JW (1996) Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 6:11-17
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 6
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • 6. Carrell RW, Lomas DA (1997) Conformational disease. Lancet 350:134-138
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 7
    • 0025911018 scopus 로고
    • Advances in Alzheimer's disease
    • 7. Katzman R, Saitoh T (1991) Advances in Alzheimer's disease. FASEB J 5:278-286
    • (1991) FASEB J , vol.5 , pp. 278-286
    • Katzman, R.1    Saitoh, T.2
  • 8
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • 8. Kang J, Lemaire HG, Unterbeck A, et al (1987) The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325:733-736
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 9
    • 2142777413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the neuritic plaque amyloid peptides
    • 9. Robakis NK, Ramakrishna N, Wolfe G, Wisniewski HM (1987) Molecular cloning and characterization of a cDNA encoding the neuritic plaque amyloid peptides. Proc Natl Acad Sci USA 84:4190-4194
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3    Wisniewski, H.M.4
  • 10
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • 10. Goldgaber D, Lerman MI, McBride OW, Saffiotti U, Gajdusek DC (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235:877-880
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 11
    • 0023109592 scopus 로고
    • Amyloid β-protein gene: CDNA, mRNA distribution and genetic linkage near the Alzheimer's locus
    • 11. Tanzi RE, Gusella JF, Watkins PC, et al (1987) Amyloid β-protein gene: cDNA, mRNA distribution and genetic linkage near the Alzheimer's locus Science 235:880-884
    • (1987) Science , vol.235 , pp. 880-884
    • Tanzi, R.E.1    Gusella, J.F.2    Watkins, P.C.3
  • 12
    • 0021956826 scopus 로고
    • Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome
    • 12. Wisniewski KE, Wisniewski HM, Wen GY (1985) Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome. Ann Neurol 17:278-282
    • (1985) Ann Neurol , vol.17 , pp. 278-282
    • Wisniewski, K.E.1    Wisniewski, H.M.2    Wen, G.Y.3
  • 13
    • 0025365306 scopus 로고
    • The prevalence of amyloid (A4) protein deposits within the cerebral and cerebellar cortex in Down's syndrome and Alzheimer's disease
    • 13. Mann DM, Jones D, Prinja D, Purkiss MS (1990) The prevalence of amyloid (A4) protein deposits within the cerebral and cerebellar cortex in Down's syndrome and Alzheimer's disease. Acta Neuropathol (Berl) 80:318-327
    • (1990) Acta Neuropathol (Berl) , vol.80 , pp. 318-327
    • Mann, D.M.1    Jones, D.2    Prinja, D.3    Purkiss, M.S.4
  • 14
    • 0026075602 scopus 로고
    • Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene
    • 14. Chartier-Harlin M-C, Crawford F, Houlden H, et al (1991) Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene. Nature 353:844-846
    • (1991) Nature , vol.353 , pp. 844-846
    • Chartier-Harlin, M.-C.1    Crawford, F.2    Houlden, H.3
  • 15
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N terminus of amyloid
    • 15. Mullan M, Crawford F, Axelman K, et al (1992) A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N terminus of amyloid. Nat Genet 1:345-347
    • (1992) Nat Genet , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 16
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
    • 16. Corder EH, Saunders AM, Strittmatter WJ, et al (1993) Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261:921-923
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1    Saunders, A.M.2    Strittmatter, W.J.3
  • 17
    • 0027407565 scopus 로고
    • Apolipoprotein E: High-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
    • 17. Strittmatter WJ, Saunders AM, Schmechel D, et al (1993) Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc Natl Acad Sci USA 90:1977-1981
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1977-1981
    • Strittmatter, W.J.1    Saunders, A.M.2    Schmechel, D.3
  • 18
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early onset familial Alzheimer's disease
    • 18. Sherrington R, Rogaev EI, Liang Y, et al (1995) Cloning of a gene bearing missense mutations in early onset familial Alzheimer's disease. Nature 375:754-760
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 19
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • 19. Levy-Lahad E, Wasco W, Poorkaj P, et al (1995) Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269:973-977
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 20
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • 20. Rogaev E, Sherrington R, Rogaeva EA, et al (1995) Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376:775-778
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.1    Sherrington, R.2    Rogaeva, E.A.3
  • 21
    • 0026745610 scopus 로고
    • Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production
    • 21. Citron M, Oltersdorf T, Haass C, et al (1992) Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production. Nature 360:672-674
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3
  • 22
    • 0028322017 scopus 로고
    • An increase percentage of long amyloid β protein secreted by familial amyloid β protein precursor (β PP717) mutants
    • 22. Suzuki N, Cheung TT, Cai TT, et al (1994) An increase percentage of long amyloid β protein secreted by familial amyloid β protein precursor (β PP717) mutants. Science 264: 1336-1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, T.T.3
  • 23
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments
    • 23. Ma J, Yee A, Brewer HB, Das S, Potter H (1994) Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372:92-94
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 24
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • 24. Wisniewski T, Castaño EM, Golabek A, Vogel T, Frangione B (1994) Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am J Pathol 145:1030-1035
    • (1994) Am J Pathol , vol.145 , pp. 1030-1035
    • Wisniewski, T.1    Castaño, E.M.2    Golabek, A.3    Vogel, T.4    Frangione, B.5
  • 25
    • 0028986408 scopus 로고
    • Fibrillogenesis in Alzheimer's disease of amyloid-β peptide and apolipoprotein E
    • 25. Castaño EM, Prelli F, Wisniewski T, et al (1995) Fibrillogenesis in Alzheimer's disease of amyloid-β peptide and apolipoprotein E. Biochem J 305:599-604
    • (1995) Biochem J , vol.305 , pp. 599-604
    • Castaño, E.M.1    Prelli, F.2    Wisniewski, T.3
  • 26
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
    • 26. Citron M, Westaway D, Xia WM, et al (1997) Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nat Med 3:67-72
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.M.3
  • 27
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's dis ease-linked presenilin 1 variants elevate Aβ 1-42/1-40 ratio in vitro and in vivo
    • 27. Borchelt DR, Thinakaran G, Eckman CB, et al (1996) Familial Alzheimer's dis ease-linked presenilin 1 variants elevate Aβ 1-42/1-40 ratio in vitro and in vivo. Neuron 17:1005-1013
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 28
    • 16044365171 scopus 로고    scopus 로고
    • The E280 a presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
    • 28. Lemere CA, Lopera F, Kosik KS, et al (1996) The E280 a presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology. Nat Med 2:1146-1150
    • (1996) Nat Med , vol.2 , pp. 1146-1150
    • Lemere, C.A.1    Lopera, F.2    Kosik, K.S.3
  • 29
    • 0030614569 scopus 로고    scopus 로고
    • Amyloid deposition in chromosome 1-linked Alzheimer's disease: The Volga German families
    • 29. Mann DMA, Iwatsubo T, Nochlin D, et al (1997) Amyloid deposition in chromosome 1-linked Alzheimer's disease: the Volga German families. Ann Neurol 41:52-57
    • (1997) Ann Neurol , vol.41 , pp. 52-57
    • Mann, D.M.A.1    Iwatsubo, T.2    Nochlin, D.3
  • 30
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
    • 30. Games D, Adams D, Alessandrini R, et al (1995) Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature 373:523-527
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 31
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • 31. Hsiao KK, Chapman P, Nilsen S, et al (1996) Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 274:99-102
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.K.1    Chapman, P.2    Nilsen, S.3
  • 33
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • 33. Pike CJ, Burdick D, Walencewicz AJ, Glabe CG, Cotman CW (1993) Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J Neurosci 13: 1676-1687
    • (1993) J Neurosci , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 34
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • 34. Lorenzo A, Yankner BA (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci USA 91:12243-12247
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 35
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • 35. Selkoe DJ (1994) Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Ann Rev Cell Biol 10:373-403
    • (1994) Ann Rev Cell Biol , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 36
    • 0024412495 scopus 로고
    • Molecular biology of Alzheimer's disease
    • 36. Muller-Hill B, Beyreuther K (1989) Molecular biology of Alzheimer's disease. Annu Rev Biochem 58:287-307
    • (1989) Annu Rev Biochem , vol.58 , pp. 287-307
    • Muller-Hill, B.1    Beyreuther, K.2
  • 37
    • 0026646604 scopus 로고
    • Amyloid beta-peptide is produced by cultured cells during normal metabolism
    • 37. Haass C, Schlossmacher MG, Hung AY, et al (1992) Amyloid beta-peptide is produced by cultured cells during normal metabolism. Nature 359:322-325
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1    Schlossmacher, M.G.2    Hung, A.Y.3
  • 38
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids
    • 38. Seubert P, Vigo-Pelfrey C, Esch F, et al (1992) Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids. Nature 359:325-327
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3
  • 39
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid beta protein by normal proteolytic processing
    • 39. Shoji M, Golde TE, Ghiso J, et al (1992) Production of the Alzheimer amyloid beta protein by normal proteolytic processing. Science 258:126-129
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1    Golde, T.E.2    Ghiso, J.3
  • 40
    • 0028031486 scopus 로고
    • Structural determinants of the Alzheimer's amyloid beta-peptide
    • 40. Soto C, Branes MC, Alvarez J, Inestrosa NC (1994) Structural determinants of the Alzheimer's amyloid beta-peptide. J Neurochem 63:1191-1198
    • (1994) J Neurochem , vol.63 , pp. 1191-1198
    • Soto, C.1    Branes, M.C.2    Alvarez, J.3    Inestrosa, N.C.4
  • 41
    • 0026619343 scopus 로고
    • Substitutions of hydrophobic amino acids reduce the amyloidogenieity of Alzheimer's disease βA4 peptides
    • 41. Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K (1992) Substitutions of hydrophobic amino acids reduce the amyloidogenieity of Alzheimer's disease βA4 peptides. J Mol Biol 228:460-473
    • (1992) J Mol Biol , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 42
    • 0013563990 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • 42. Jarrett JT, Berger EP, Lansbury PT Jr (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 31:12345-12352
    • (1993) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury P.T., Jr.3
  • 43
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • 43. Barrow CJ, Zagorski MG (1991) Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition. Science 253:179-182
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 44
    • 0026595567 scopus 로고
    • Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs
    • 44. Burdick D, Soreghan B, Kwon M, et al (1992) Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs. J Biol Chem 267:546-554
    • (1992) J Biol Chem , vol.267 , pp. 546-554
    • Burdick, D.1    Soreghan, B.2    Kwon, M.3
  • 45
    • 0026631361 scopus 로고
    • NMR studies of amyloid beta-peptides: Proton assignments, secondary structure, and mechanism of an alpha-helix-beta-sheet conversion for a homologous, 28-residue, N-terminal fragment
    • 45. Zagorski MG, Barrow CJ (1992) NMR studies of amyloid beta-peptides: proton assignments, secondary structure, and mechanism of an alpha-helix-beta-sheet conversion for a homologous, 28-residue, N-terminal fragment. Biochemistry 31:5621-5631
    • (1992) Biochemistry , vol.31 , pp. 5621-5631
    • Zagorski, M.G.1    Barrow, C.J.2
  • 46
    • 0028980362 scopus 로고
    • The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation
    • 46. Soto C, Castaño EM, Frangione B, Inestrosa NC (1995) The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation. J Biol Chem 270:3063-3067
    • (1995) J Biol Chem , vol.270 , pp. 3063-3067
    • Soto, C.1    Castaño, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 47
    • 0028917968 scopus 로고
    • Two conformational states of amyloid beta-peptide: Implications for the pathogenesis of Alzheimer's disease
    • 47. Soto C, Frangione B (1995) Two conformational states of amyloid beta-peptide: implications for the pathogenesis of Alzheimer's disease. Neurosci Lett 186:115-118
    • (1995) Neurosci Lett , vol.186 , pp. 115-118
    • Soto, C.1    Frangione, B.2
  • 48
    • 0029916711 scopus 로고    scopus 로고
    • The conformation of Alzheimer's ß peptide determines the rate of amyloid formation and its resistance to proteolysis
    • 48. Soto C, Castaño EM (1996) The conformation of Alzheimer's ß peptide determines the rate of amyloid formation and its resistance to proteolysis. Biochem J 314:701-707
    • (1996) Biochem J , vol.314 , pp. 701-707
    • Soto, C.1    Castaño, E.M.2
  • 49
    • 0030707547 scopus 로고    scopus 로고
    • Alzheimer's amyloid-β aggregation is modulated by the interaction of multiple factors
    • 49. Soto C, Ghiso J, Frangione B (1997) Alzheimer's amyloid-β aggregation is modulated by the interaction of multiple factors. Alzheimers Res 3:215-222
    • (1997) Alzheimers Res , vol.3 , pp. 215-222
    • Soto, C.1    Ghiso, J.2    Frangione, B.3
  • 50
    • 0027365822 scopus 로고
    • Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in late-onset Alzheimer disease
    • 50. Schmechel DE, Saunders AM, Strittmatter WJ, et al (1993) Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in late-onset Alzheimer disease. Proc Natl Acad Sci USA 90:9649-9653
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9649-9653
    • Schmechel, D.E.1    Saunders, A.M.2    Strittmatter, W.J.3
  • 51
    • 0029866177 scopus 로고    scopus 로고
    • The interaction between Alzheimer β-peptide and apolipoprotein E is dependent on β-peptide conformation
    • 51. Golabek AA, Soto C, Vogel T, Wisniewski T (1996) The interaction between Alzheimer β-peptide and apolipoprotein E is dependent on β-peptide conformation. J Biol Chem 271: 10602-10606
    • (1996) J Biol Chem , vol.271 , pp. 10602-10606
    • Golabek, A.A.1    Soto, C.2    Vogel, T.3    Wisniewski, T.4
  • 52
    • 0029865644 scopus 로고    scopus 로고
    • Alzheimer's soluble β-amyloid is conformationally modified by apolipoproteins in vitro
    • 52. Soto C, Golabek AA, Wisniewski T, Castaño EM (1996) Alzheimer's soluble β-amyloid is conformationally modified by apolipoproteins in vitro. Neuroreport 7:721-725
    • (1996) Neuroreport , vol.7 , pp. 721-725
    • Soto, C.1    Golabek, A.A.2    Wisniewski, T.3    Castaño, E.M.4
  • 53
    • 0026542786 scopus 로고
    • Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • 53. Wisniewski T, Frangione B (1992) Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci Lett 135:235-238
    • (1992) Neurosci Lett , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 54
    • 0031278270 scopus 로고    scopus 로고
    • Lack of apolipoprotein E dramatically reduces amyloid beta-peptide deposition
    • 54. Bales KR, Verina T, Dodel RC, et al (1997) Lack of apolipoprotein E dramatically reduces amyloid beta-peptide deposition. Nat Gen 17:254-256
    • (1997) Nat Gen , vol.17 , pp. 254-256
    • Bales, K.R.1    Verina, T.2    Dodel, R.C.3
  • 56
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • 56. Prusiner SB (1991) Molecular biology of prion diseases. Science 252:1515-1522
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 57
    • 0015549846 scopus 로고
    • The clinical characteristics of trnsmissible Creutzfeldt-Jakob disease
    • 57. Roos R, Gajdusek DC, Gibbs CJ Jr (1973) The clinical characteristics of trnsmissible Creutzfeldt-Jakob disease. Brain 96:1-20
    • (1973) Brain , vol.96 , pp. 1-20
    • Roos, R.1    Gajdusek, D.C.2    Gibbs C.J., Jr.3
  • 58
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • 58. Bueler H, Aguzzi A, Sailer A, et al (1993) Mice devoid of PrP are resistant to scrapie. Cell 73:1339-1347
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3
  • 59
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • 59. Stahl N, Baldwin MA, Teplow DB, et al (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
  • 60
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into β-sheets features in the formation of scrapie prion poteins
    • 60. Pan KM, Baldwin M, Njuyen J, et al (1993) Conversion of alpha-helices into β-sheets features in the formation of scrapie prion poteins. Proc Natl Acad Sci USA 90:10962-10966
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Njuyen, J.3
  • 61
    • 0029166464 scopus 로고
    • Prion protein isoforms, a convergence of biological and structural investigations
    • 61. Baldwin MA, Cohen FE, Prusiner SB (1995) Prion protein isoforms, a convergence of biological and structural investigations. J Biol Chem 270:19197-19200
    • (1995) J Biol Chem , vol.270 , pp. 19197-19200
    • Baldwin, M.A.1    Cohen, F.E.2    Prusiner, S.B.3
  • 62
    • 0028338441 scopus 로고
    • Structural clues to prion replication
    • 62. Cohen F E, Pan K M, Huang Z, et al (1994) Structural clues to prion replication. Science 264:530-531
    • (1994) Science , vol.264 , pp. 530-531
    • Cohen, F.E.1    Pan, K.M.2    Huang, Z.3
  • 63
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • 63. Telling GC, Scott M, Mastrianni J, et al (1995) Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:79-90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3
  • 64
    • 0025790313 scopus 로고
    • Evidence for biological and structural diversity among scrapie strains
    • 64. Kascsak RJ, Rubenstein R, Carp RI (1991) Evidence for biological and structural diversity among scrapie strains. Curr Top Microbiol Immunol 172:139-150
    • (1991) Curr Top Microbiol Immunol , vol.172 , pp. 139-150
    • Kascsak, R.J.1    Rubenstein, R.2    Carp, R.I.3
  • 65
    • 0027956109 scopus 로고
    • Cell-free formation of pro tease-resistant prion protein
    • 65. Kocisko DA, Come JH, Priola SA, et al (1994) Cell-free formation of pro tease-resistant prion protein. Nature 370:471-474
    • (1994) Nature , vol.370 , pp. 471-474
    • Kocisko, D.A.1    Come, J.H.2    Priola, S.A.3
  • 68
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • 68. Bessen RA, Marsh RF (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 68:7859-7868
    • (1994) J Virol , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 69
    • 12644272790 scopus 로고    scopus 로고
    • Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
    • 69. Telling GC, Parchi P, DeArmond SJ, Cortelli P, et al (1996) Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274:2079-2082
    • (1996) Science , vol.274 , pp. 2079-2082
    • Telling, G.C.1    Parchi, P.2    DeArmond, S.J.3    Cortelli, P.4
  • 70
    • 0031720905 scopus 로고    scopus 로고
    • sc molecules with different conformations
    • sc molecules with different conformations. Nat Med 4:1157-1165
    • (1998) Nat Med , vol.4 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3
  • 71
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in β-sheet conformation of abnormal prion protein
    • 71. Caughey B, Raymond GJ, Bessen RA (1998) Strain-dependent differences in β-sheet conformation 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
  • 72
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation
    • 72. Soto C, Kindy MS, Baumann M, Frangione B (1996) Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem Biophys Res Commun 226: 672-680
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3    Frangione, B.4
  • 73
    • 0031873102 scopus 로고    scopus 로고
    • β-sheet breaker peptides prevent Alzheimer's amyloid-β neurotoxicity in cell culture and inhibit fibrillogenesis in vitro and in a rat brain model of amyloidosis
    • 73. Soto C, Sigurdsson EM, Morelli L, et al (1998) β-sheet breaker peptides prevent Alzheimer's amyloid-β neurotoxicity in cell culture and inhibit fibrillogenesis in vitro and in a rat brain model of amyloidosis. Nat Med 4:822-826
    • (1998) Nat Med , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3
  • 74
    • 84986522918 scopus 로고
    • ICM: A new method for structure modeling and design: Application to docking and structure prediction from the distorted native conformation
    • 74. Abagyan RA, Totrov MM, Kuznetsov DA (1994) ICM: a new method for structure modeling and design: application to docking and structure prediction from the distorted native conformation. J Comp Chem 15:488-506
    • (1994) J Comp Chem , vol.15 , pp. 488-506
    • Abagyan, R.A.1    Totrov, M.M.2    Kuznetsov, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.