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Volumn 53, Issue 6, 1999, Pages 633-640

Fibril formation by amyloid-β proteins may involve β-helical protofibrils

Author keywords

helix; Alzheimer's disease; Amyloid ; Protofibrils

Indexed keywords

AMYLOID;

EID: 0032980443     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00057.x     Document Type: Article
Times cited : (24)

References (33)
  • 1
    • 0001193811 scopus 로고    scopus 로고
    • A reductionist view of Alzheimer's disease
    • 1. Lansbury, P.T. Jr (1996) A reductionist view of Alzheimer's disease. Acc. Chem. Res. 29, 317-321.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 317-321
    • Lansbury P.T., Jr.1
  • 2
    • 0029895147 scopus 로고    scopus 로고
    • Brain amyloid - A physicochemical perspective
    • 2. Maggio, J.E. & Mantyh, P.W. (1996) Brain amyloid - a physicochemical perspective. Brain Pathol. 6, 147-162.
    • (1996) Brain Pathol. , vol.6 , pp. 147-162
    • Maggio, J.E.1    Mantyh, P.W.2
  • 6
    • 0014098295 scopus 로고
    • High resolution electron microscopic analysis of the amyloid fibril
    • 6. Shirahama, T. & Cohen, A.S. (1967) High resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol. 33, 679-706.
    • (1967) J. Cell Biol. , vol.33 , pp. 679-706
    • Shirahama, T.1    Cohen, A.S.2
  • 8
    • 38349006853 scopus 로고
    • An investigation of the structure of silk fibroin
    • 8. Marsh, R.E., Corey, R.B. & Pauling, L. (1955) An investigation of the structure of silk fibroin. Biochim. Biophys. Acta 16, 1-34.
    • (1955) Biochim. Biophys. Acta , vol.16 , pp. 1-34
    • Marsh, R.E.1    Corey, R.B.2    Pauling, L.3
  • 9
    • 0026320119 scopus 로고
    • An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: Application of solid-state NMR to the determination of protein secondary structure
    • 9. Spenser, R.G.S., Halverson, K.J., Auger, M., McDermott, A.E., Griffin, R.G. & Lansbury, P.T. Jr (1991) An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Biochemistry 30, 10382-10387.
    • (1991) Biochemistry , vol.30 , pp. 10382-10387
    • Spenser, R.G.S.1    Halverson, K.J.2    Auger, M.3    McDermott, A.E.4    Griffin, R.G.5    Lansbury P.T., Jr.6
  • 12
    • 0030668710 scopus 로고    scopus 로고
    • Determination of peptide amide configuration in a model amyloid fibril by solid-state NMR
    • 12. Costa, P.R., Kocisko, D.A., Sun, B.Q., Lansbury, P.T. Jr & Griffin, R.G. (1997) Determination of peptide amide configuration in a model amyloid fibril by solid-state NMR. J. Am. Chem. Soc. 119, 10487-10493.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10487-10493
    • Costa, P.R.1    Kocisko, D.A.2    Sun, B.Q.3    Lansbury P.T., Jr.4    Griffin, R.G.5
  • 14
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • 14. Harper, J.D., Wong, S.S., Lieber, C.M. & Lansbury, P.T. Jr (1997) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury P.T., Jr.4
  • 15
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • 15. Harper, J.D., Lieber, C.M. & Lansbury, P.T. Jr (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem. Biol. 4, 951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury P.T., Jr.3
  • 16
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • 16. Lazo, N.D. & Downing, D.T. (1998) Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry 37, 1731-1735.
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 17
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments
    • 17. Halverson, K., Fraser, P.E., Kirschner, D.A. & Lansbury, P.T. Jr (1990) Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistiy 29, 2639-2644.
    • (1990) Biochemistiy , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.E.2    Kirschner, D.A.3    Lansbury P.T., Jr.4
  • 18
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation
    • 18. Kelly, J.W. & Lansbury, P.T. Jr (1994) A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation. Amyloid: Int. J. Exp. Clin. Invest. 1, 186-205.
    • (1994) Amyloid: Int. J. Exp. Clin. Invest. , vol.1 , pp. 186-205
    • Kelly, J.W.1    Lansbury P.T., Jr.2
  • 19
    • 0031019984 scopus 로고    scopus 로고
    • Circular dichroism of model peptides emulating the amphipathic α-helical regions of intermediate filaments
    • 19. Lazo, N.D. & Downing, D.T. (1997) Circular dichroism of model peptides emulating the amphipathic α-helical regions of intermediate filaments. Biochemistry 36, 2559-2565.
    • (1997) Biochemistry , vol.36 , pp. 2559-2565
    • Lazo, N.D.1    Downing, D.T.2
  • 20
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • 20. Yang, J.T., Wu, C.-S.C. & Martinez, H.M. (1986) Calculation of protein conformation from circular dichroism. Meth Enzymol. 130, 208-269.
    • (1986) Meth Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3
  • 21
    • 0028864109 scopus 로고
    • Molecular modeling indicates that homodimers form the basis for intermediate filament assembly from human and mouse epidermal keratins
    • 21. Downing, D.T. (1995) Molecular modeling indicates that homodimers form the basis for intermediate filament assembly from human and mouse epidermal keratins. Proteins: Struct. Func. Genet. 23, 204-217.
    • (1995) Proteins: Struct. Func. Genet. , vol.23 , pp. 204-217
    • Downing, D.T.1
  • 22
    • 0029902083 scopus 로고    scopus 로고
    • Chemical cross-linking between lysine groups in vimentin oligomers is dependent on local peptide conformations
    • 22. Downing, D.T. (1996) Chemical cross-linking between lysine groups in vimentin oligomers is dependent on local peptide conformations. Proteins: Struct. Func. Genet. 25, 215-224.
    • (1996) Proteins: Struct. Func. Genet. , vol.25 , pp. 215-224
    • Downing, D.T.1
  • 23
    • 0030443369 scopus 로고    scopus 로고
    • Molecular modeling of vimentin filament assembly
    • 23. Downing, D.T. (1996) Molecular modeling of vimentin filament assembly. Proteins: Struct. Func. Genet. 26, 472-478.
    • (1996) Proteins: Struct. Func. Genet. , vol.26 , pp. 472-478
    • Downing, D.T.1
  • 24
    • 0031587922 scopus 로고    scopus 로고
    • β-helical protofibrils from a model peptide
    • 24. Lazo, N.D. & Downing, D.T. (1997) β-helical protofibrils from a model peptide. Biochem. Biophys. Res. Commun. 235, 675-679.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 675-679
    • Lazo, N.D.1    Downing, D.T.2
  • 25
    • 0031907944 scopus 로고    scopus 로고
    • Stabilization of amphipathic α-helical and β-helical conformations in synthetic peptides in the presence and absence of ionic interactions
    • 25. Lazo, N.D. & Downing, D.T. (1998) Stabilization of amphipathic α-helical and β-helical conformations in synthetic peptides in the presence and absence of ionic interactions. J. Peptide Res. 51, 85-89.
    • (1998) J. Peptide Res. , vol.51 , pp. 85-89
    • Lazo, N.D.1    Downing, D.T.2
  • 26
    • 0029081224 scopus 로고
    • Circular dichroism of the parallel β-helical proteins pectate lyase C and E
    • 26. Sieber, V., Jumak, F. & Moe, G.R. (1995) Circular dichroism of the parallel β-helical proteins pectate lyase C and E. Proteins: Struct. Func. Genet. 23, 32-37.
    • (1995) Proteins: Struct. Func. Genet. , vol.23 , pp. 32-37
    • Sieber, V.1    Jumak, F.2    Moe, G.R.3
  • 27
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro
    • 27. Pike, C.J., Overman, M.J. & Cotman, C.W. (1995) Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro. J. Biol. Chem. 270, 23895-23898.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 28
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase c, a secreted plant virulence factor
    • 28. Yoder, M.D., Keen, N.T. & Jurnak, F. (1993) New domain motif: the structure of pectate lyase c, a secreted plant virulence factor. Science 260, 1503-1507.
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 29
    • 0028095571 scopus 로고
    • Crystal structure of p22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • 29. Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R. & Reinemer, P. (1994) Crystal structure of p22 tailspike protein: interdigitated subunits in a thermostable trimer. Science 265, 383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 30
    • 0028844306 scopus 로고
    • A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • 30. Raetz, C.R.H. & Roderick, S.L. (1995) A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270, 997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, S.L.2
  • 31
    • 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
    • 31. Harper, J.D. & 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 P.T., Jr.2
  • 32
    • 0028845988 scopus 로고
    • Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs
    • 32. Serpell, L.C., Sunde, M., Fraser, P.E., Luther, P.K., Morris, E.P. Sangren, O., Lundgren, E. & Blake, C.C.F. (1995) Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254, 113-118.
    • (1995) J. Mol. Biol. , vol.254 , pp. 113-118
    • Serpell, L.C.1    Sunde, M.2    Fraser, P.E.3    Luther, P.K.4    Morris, E.P.5    Sangren, O.6    Lundgren, E.7    Blake, C.C.F.8
  • 33
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyoid fibril is a continuous β-sheet helix
    • 33. Blake, C. & Serpell, L. (1996) Synchrotron X-ray studies suggest that the core of the transthyretin amyoid fibril is a continuous β-sheet helix. Structure 4, 989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.