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Volumn 1502, Issue 1, 2000, Pages 16-30

Alzheimer's amyloid fibrils: Structure and assembly

Author keywords

Alzheimer's disease; Amyloid; Beta sheet; Fibril; Structure

Indexed keywords

AMYLOID;

EID: 0034718157     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-4439(00)00029-6     Document Type: Review
Times cited : (872)

References (91)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron. 6:1991;487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 2
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation
    • Sunde M., Blake C. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. Q. Rev. Biophys. 31:1998;1-39.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.2
  • 3
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde M., Serpell L., Bartlam M., Fraser P., Pepys M., Blake C. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273:1997;729-739.
    • (1997) J. Mol. Biol. , vol.273 , pp. 729-739
    • Sunde, M.1    Serpell, L.2    Bartlam, M.3    Fraser, P.4    Pepys, M.5    Blake, C.6
  • 4
    • 0014098295 scopus 로고
    • High resolution electron microscopic analysis of the amyloid fibril
    • Shirahama T., Cohen A.S. High resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol. 33:1967;679-706.
    • (1967) J. Cell Biol. , vol.33 , pp. 679-706
    • Shirahama, T.1    Cohen, A.S.2
  • 5
    • 0000844417 scopus 로고
    • Electron microscopy of amyloid
    • in: I.R. Harris (Ed.), Academic Press, London
    • A.S. Cohen, T. Shirahama, M. Skinner, Electron microscopy of amyloid, in: I.R. Harris (Ed.), Electron Microscopy of Protein, 1982, Academic Press, London, pp. 165-205.
    • (1982) Electron Microscopy of Protein , pp. 165-205
    • Cohen, A.S.1    Shirahama, T.2    Skinner, M.3
  • 6
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes E.D., Glenner G.G. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16:1968;673-677.
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 8
    • 0025838381 scopus 로고
    • PH dependent structural transitions of Alzheimers amyloid peptides
    • Fraser P.E., Nguyen J.T., Surewicz W.K., Kirschner D.A. pH dependent structural transitions of Alzheimers amyloid peptides. Biophys. J. 60:1991;1190-1201.
    • (1991) Biophys. J. , vol.60 , pp. 1190-1201
    • Fraser, P.E.1    Nguyen, J.T.2    Surewicz, W.K.3    Kirschner, D.A.4
  • 10
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimers disease: Conformational studies of synthetic β-protein fragments
    • Halverson K., Fraser P., Kirschner D., Lansbury P. Molecular determinants of amyloid deposition in Alzheimers disease: Conformational studies of synthetic β-protein fragments. Biochemistry. 29:1990;2639-2644.
    • (1990) Biochemistry , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.2    Kirschner, D.3    Lansbury, P.4
  • 11
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βa4 peptides of Alzheimer's disease
    • Hilbich C., Kisters-Woike B., Reed J., Masters C., Beyreuther K. Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J. Mol. Biol. 218:1991;149-163.
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.4    Beyreuther, K.5
  • 13
    • 0028031486 scopus 로고
    • Structural determinants of the Alzheimer's amyloid beta-peptide
    • Soto C., Branes M., Alvarez J., Inestrosa N. Structural determinants of the Alzheimer's amyloid beta-peptide. J. Neurol. Chem. 63:1994;1191-1198.
    • (1994) J. Neurol. Chem. , vol.63 , pp. 1191-1198
    • Soto, C.1    Branes, M.2    Alvarez, J.3    Inestrosa, N.4
  • 14
    • 0023425365 scopus 로고
    • Synthetic peptide homologous to β-protein from Alzheimer's disease forms amyloid-like fibrils in vitro
    • Kirschner D., Inouye H., Duffy L., Sinclair A., Lind M., Selkoe D. Synthetic peptide homologous to β-protein from Alzheimer's disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA. 84:1987;6953-6957.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6953-6957
    • Kirschner, D.1    Inouye, H.2    Duffy, L.3    Sinclair, A.4    Lind, M.5    Selkoe, D.6
  • 15
    • 0025779179 scopus 로고
    • Solution structures of β-peptide and its constituent fragments relation to amyloid deposition
    • Barrow C.J., Zagorski M.G. Solution structures of β-peptide and its constituent fragments relation to amyloid deposition. Science. 253:1991;179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 16
    • 0026631361 scopus 로고
    • NMR studies of amyloid β-peptide: Proton assignments, secondary structure and mechanism of an α-helix-β-sheet conversion for a homologous, 28 residue, N-terminal fragment
    • Zagorski M., Barrow C. NMR studies of amyloid β-peptide: Proton assignments, secondary structure and mechanism of an α-helix-β-sheet conversion for a homologous, 28 residue, N-terminal fragment. Biochemistry. 31:1992;5621-5631.
    • (1992) Biochemistry , vol.31 , pp. 5621-5631
    • Zagorski, M.1    Barrow, C.2
  • 18
    • 0028335794 scopus 로고
    • Solution structure of residues 1-28 of the amyloid β-peptide
    • Talafous J., Marcinowski K., Klopman G., Zagorski M. Solution structure of residues 1-28 of the amyloid β-peptide. Biochemistry. 33:1994;7788-7796.
    • (1994) Biochemistry , vol.33 , pp. 7788-7796
    • Talafous, J.1    Marcinowski, K.2    Klopman, G.3    Zagorski, M.4
  • 19
    • 0027953616 scopus 로고
    • Structure determination of extracellular fragments of amyloid proteins involved in Alzheimer's disease and Dutch-type hereditary cerebral haemorrhage with amyloidosis
    • Sorimachi K., Craik D. Structure determination of extracellular fragments of amyloid proteins involved in Alzheimer's disease and Dutch-type hereditary cerebral haemorrhage with amyloidosis. Eur. J. Biochem. 219:1994;237-251.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 237-251
    • Sorimachi, K.1    Craik, D.2
  • 20
    • 0030983767 scopus 로고    scopus 로고
    • The interaction of β-amyloid protein fragment (12-28) with lipid environments
    • Fletcher F., Keire D. The interaction of β-amyloid protein fragment (12-28) with lipid environments. Protein Sci. 6:1997;666-675.
    • (1997) Protein Sci. , vol.6 , pp. 666-675
    • Fletcher, F.1    Keire, D.2
  • 22
    • 0032530466 scopus 로고    scopus 로고
    • The influence of the central region containing residues 19-25 on the aggregation properties and secondary structure of Alzheimer's β-amyloid peptide
    • ElAgnaf O., Guthrie D., Walsh D., Irvine G. The influence of the central region containing residues 19-25 on the aggregation properties and secondary structure of Alzheimer's β-amyloid peptide. Eur. J. Biochem. 256:1998;560-569.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 560-569
    • Elagnaf, O.1    Guthrie, D.2    Walsh, D.3    Irvine, G.4
  • 23
    • 0030457933 scopus 로고    scopus 로고
    • Three-dimensional structures of the amyloid β peptide (25-35) in membrane-mimicking environment
    • Kohno T., Kobayashi K., Maeda T., Sato K., Takashima A. Three-dimensional structures of the amyloid β peptide (25-35) in membrane-mimicking environment. Biochemistry. 35:1996;16094-16104.
    • (1996) Biochemistry , vol.35 , pp. 16094-16104
    • Kohno, T.1    Kobayashi, K.2    Maeda, T.3    Sato, K.4    Takashima, A.5
  • 24
    • 0028179865 scopus 로고
    • Alzheimer β-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • Terzi E., Holzemann G., Seelig J. Alzheimer β-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes. Biochemistry. 33:1994;7434-7441.
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 27
    • 0029157531 scopus 로고
    • Solvent effects on self assemply of β-amyloid peptide
    • Shen C.-L., Murphy R.M. Solvent effects on self assemply of β-amyloid peptide. Biophys. J. 69:1995;640-651.
    • (1995) Biophys. J. , vol.69 , pp. 640-651
    • Shen, C.-L.1    Murphy, R.M.2
  • 28
    • 0027989805 scopus 로고
    • Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide
    • Shen C.-L., Fitzgerald M., Murphy R. Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide. Biophys. J. 67:1994;1238-1245.
    • (1994) Biophys. J. , vol.67 , pp. 1238-1245
    • Shen, C.-L.1    Fitzgerald, M.2    Murphy, R.3
  • 29
    • 0028980362 scopus 로고
    • The α-helical to β-sheet transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation
    • Soto C., Castano E., Frangione B., Inestrosa N. The α-helical to β-sheet transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J. Biol. Chem. 270:1995;3063-3067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.2    Frangione, B.3    Inestrosa, N.4
  • 30
    • 0026708694 scopus 로고
    • Kinetics of aggregation of synthetic β-amyloid peptide
    • Tomski S., Murphy R. Kinetics of aggregation of synthetic β-amyloid peptide. Arch. Biochem. Biophys. 294:1992;630-638.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 630-638
    • Tomski, S.1    Murphy, R.2
  • 31
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure amyloid β-peptide (1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • Coles M., Bicknell W., Watson A., Fairlie D., Craik D. Solution structure amyloid β-peptide (1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry. 37:1998;11064-11077.
    • (1998) Biochemistry , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, A.3    Fairlie, D.4    Craik, D.5
  • 32
    • 0032530953 scopus 로고    scopus 로고
    • Solution structure of methionine-oxidized amyloid β-peptide (1-40). Does oxidaton affect conformational switching?
    • Watson A., Fairlie D., Craik D. Solution structure of methionine-oxidized amyloid β-peptide (1-40). Does oxidaton affect conformational switching? Biochemistry. 37:1998;12700-12706.
    • (1998) Biochemistry , vol.37 , pp. 12700-12706
    • Watson, A.1    Fairlie, D.2    Craik, D.3
  • 34
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik S.B., Inouye H., Szumowski K., Kirschner D. Structural analysis of Alzheimer's β(1-40) amyloid: protofilament assembly of tubular fibrils. Biophys. J. 74:1998;537-545.
    • (1998) Biophys. J. , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.3    Kirschner, D.4
  • 35
    • 0033555275 scopus 로고    scopus 로고
    • Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease
    • Shao H., Jao S., Ma J., Zagorski M. Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease. J. Mol. Biol. 285:1999;755-773.
    • (1999) J. Mol. Biol. , vol.285 , pp. 755-773
    • Shao, H.1    Jao, S.2    Ma, J.3    Zagorski, M.4
  • 36
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood S., Maleeff B., Hart T., Wetzel R. Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ J. Mol. Biol. 256:1996;870-877.
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4
  • 37
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extra-neuronal amyloid fibres in Alzheimers disease indicates cross β conformation
    • Kirschner D., Abraham C., Selkoe D. X-ray diffraction from intraneuronal paired helical filaments and extra-neuronal amyloid fibres in Alzheimers disease indicates cross β conformation. Proc. Natl. Acad. Sci. USA. 83:1986;503-507.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 503-507
    • Kirschner, D.1    Abraham, C.2    Selkoe, D.3
  • 38
    • 0028172208 scopus 로고
    • The Alzheimer Aβ peptide develops protease resistance in associaction with its polymerization into fibrils
    • Norstedt C., Naslund J., Tjernberg L., Karlstrom A., Thyberg J., Terenius L. The Alzheimer Aβ peptide develops protease resistance in associaction with its polymerization into fibrils. J. Biol. Chem. 269:1994;30773-30776.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30773-30776
    • Norstedt, C.1    Naslund, J.2    Tjernberg, L.3    Karlstrom, A.4    Thyberg, J.5    Terenius, L.6
  • 39
    • 0031728016 scopus 로고    scopus 로고
    • Residual structure in the Alzheimer's disease peptide: Probing the origin of a central hydrophobic cluster
    • Zhang S., Casey N., Lee J. Residual structure in the Alzheimer's disease peptide: probing the origin of a central hydrophobic cluster. Folding Design. 3:1998;413-422.
    • (1998) Folding Design , vol.3 , pp. 413-422
    • Zhang, S.1    Casey, N.2    Lee, J.3
  • 41
    • 0026045862 scopus 로고
    • Peptides homologous to the amyloid protein of Alzheimers disease containing glutamine for a glutamic acid substitution have accelerated amyloid fibril formation
    • Wisniewski T., Ghiso J., Frangione B. Peptides homologous to the amyloid protein of Alzheimers disease containing glutamine for a glutamic acid substitution have accelerated amyloid fibril formation. Biochem. Biophys. Res. Coomun. 179:1991;1247-1254.
    • (1991) Biochem. Biophys. Res. Coomun. , vol.179 , pp. 1247-1254
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 43
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury P. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. USA. 96:1999;3342-3344.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3342-3344
    • Lansbury, P.1
  • 45
    • 0030611858 scopus 로고    scopus 로고
    • Soluble amyloid Aβ-(1-40) exists as a stable dimer at low concentrations
    • Garzon-Rodriguez W., Sepulveda-Becerra M., Milton S., Glabe C. Soluble amyloid Aβ-(1-40) exists as a stable dimer at low concentrations. J. Biol. Chem. 272:1997;21037-21044.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21037-21044
    • Garzon-Rodriguez, W.1    Sepulveda-Becerra, M.2    Milton, S.3    Glabe, C.4
  • 46
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's β-amyoid peptide correlates with a distinct fiber morphology
    • Seilheimer B., Bohrmann B., Bondolfi L., Muller F., Stuber D., Dobeli H. The toxicity of the Alzheimer's β-amyoid peptide correlates with a distinct fiber morphology. J. Struct. Biol. 119:1997;59-71.
    • (1997) J. Struct. Biol. , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Muller, F.4    Stuber, D.5    Dobeli, H.6
  • 47
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation
    • Kowalewski T., Holtzman D. In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation. Proc. Natl. Acad. Sci. USA. 96:1999;3688-3693.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.2
  • 48
  • 49
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantification of rate constants
    • Lomakin A., Chung D., Benedek G., Kirschner D., Teplow D. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantification of rate constants. Proc. Natl. Acad. Sci. USA. 93:1996;1125-1129.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.2    Benedek, G.3    Kirschner, D.4    Teplow, D.5
  • 50
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper J., Wong S., Lieber C., Lansbury P. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 6:1997;119-125.
    • (1997) Chem. Biol. , vol.6 , pp. 119-125
    • Harper, J.1    Wong, S.2    Lieber, C.3    Lansbury, P.4
  • 52
    • 0031593854 scopus 로고    scopus 로고
    • Molecular modelling of the Aβ1-42 peptide from Alzheimer's disease
    • Chaney M.O., Webster S., Kuo Y., Roher A. Molecular modelling of the Aβ1-42 peptide from Alzheimer's disease. Protein Eng. 11:1998;761-767.
    • (1998) Protein Eng. , vol.11 , pp. 761-767
    • Chaney, M.O.1    Webster, S.2    Kuo, Y.3    Roher, A.4
  • 54
    • 0027411230 scopus 로고
    • Structure of β-crystallite assemblies by Alzheimer β amyloid protein analogues: Analysis by X-ray diffraction
    • Inouye H., Fraser P., Kirschner D. Structure of β-crystallite assemblies by Alzheimer β amyloid protein analogues: Analysis by X-ray diffraction. Biophys. J. 64:1993;502-519.
    • (1993) Biophys. J. , vol.64 , pp. 502-519
    • Inouye, H.1    Fraser, P.2    Kirschner, D.3
  • 55
    • 0028845988 scopus 로고
    • The examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs
    • Serpell L., Sunde M., Fraser P., Luther P.K., Morris E., Sandgren O., Lundgren E., Blake C. The examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254:1995;113-118.
    • (1995) J. Mol. Biol. , vol.254 , pp. 113-118
    • Serpell, L.1    Sunde, M.2    Fraser, P.3    Luther, P.K.4    Morris, E.5    Sandgren, O.6    Lundgren, E.7    Blake, C.8
  • 56
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-helix
    • Blake C., Serpell L. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-helix. Structure. 4:1996;989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 58
    • 0001402095 scopus 로고
    • Two β-pleated sheet configurations of polypeptide chains involving both cis- And trans- amide groups
    • Pauling L., Corey R. Two β-pleated sheet configurations of polypeptide chains involving both cis- and trans- amide groups. Proc. Natl. Acad. Sci. USA. 39:1953;247-252.
    • (1953) Proc. Natl. Acad. Sci. USA , vol.39 , pp. 247-252
    • Pauling, L.1    Corey, R.2
  • 59
    • 84977296697 scopus 로고
    • X-ray-scattering from a discrete helix with cumulative angular and translational disorders
    • Inouye H. X-ray-scattering from a discrete helix with cumulative angular and translational disorders. Acta Crystallogr. A. 50:1994;644-646.
    • (1994) Acta Crystallogr. A. , vol.50 , pp. 644-646
    • Inouye, H.1
  • 60
    • 0000680239 scopus 로고
    • An investigation of the structure of β-keratin
    • Fraser R., MacRae T. An investigation of the structure of β-keratin. J. Mol. Biol. 5:1962;457-466.
    • (1962) J. Mol. Biol. , vol.5 , pp. 457-466
    • Fraser, R.1    MacRae, T.2
  • 61
    • 0000831917 scopus 로고
    • Brain transglutaminase - In vitro crosslinking of human neurofilament proteins into insoluble polymers
    • Selkoe D.J., Abraham C., Ihara Y. Brain transglutaminase - in vitro crosslinking of human neurofilament proteins into insoluble polymers. Proc. Natl. Acad. Sci. USA. 79:1982;6070-6074.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6070-6074
    • Selkoe, D.J.1    Abraham, C.2    Ihara, Y.3
  • 62
    • 0028144630 scopus 로고
    • Identification of glutamine and lysine residues in Alzheimer amyloid β-A4 peptide responsible for transglutaminase-catalyzed homopolymerization and cross-linking to alpha(2)M receptor
    • Rasmussen L., Sorensen E., Petersen T., Gliemann J., Jensen P. Identification of glutamine and lysine residues in Alzheimer amyloid β-A4 peptide responsible for transglutaminase-catalyzed homopolymerization and cross-linking to alpha(2)M receptor. FEBS Lett. 338:1994;161-166.
    • (1994) FEBS Lett. , vol.338 , pp. 161-166
    • Rasmussen, L.1    Sorensen, E.2    Petersen, T.3    Gliemann, J.4    Jensen, P.5
  • 63
    • 0028177277 scopus 로고
    • Cross-linking of β-amyloid protein precursor catalyzed by tissue transglutaminase
    • Ho G., Gregory E., Smirmova I., Zoubine M., Festoff B. Cross-linking of β-amyloid protein precursor catalyzed by tissue transglutaminase. FEBS Lett. 349:1994;151-154.
    • (1994) FEBS Lett. , vol.349 , pp. 151-154
    • Ho, G.1    Gregory, E.2    Smirmova, I.3    Zoubine, M.4    Festoff, B.5
  • 64
    • 0028298620 scopus 로고
    • Transglutaminase facilitates the formation of polymers of the β-amyloid peptide
    • Dudek S., Johnson G. Transglutaminase facilitates the formation of polymers of the β-amyloid peptide. Brain Res. 651:1994;129-133.
    • (1994) Brain Res. , vol.651 , pp. 129-133
    • Dudek, S.1    Johnson, G.2
  • 65
    • 0027289153 scopus 로고
    • Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer β/A4 amyloid protein by transglutaminase
    • Ikura K., Takahata K., Sasaki R. Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer β/A4 amyloid protein by transglutaminase. FEBS Lett. 349:1993;109-111.
    • (1993) FEBS Lett. , vol.349 , pp. 109-111
    • Ikura, K.1    Takahata, K.2    Sasaki, R.3
  • 67
    • 0027918655 scopus 로고
    • Unusual structural features in the parallel β-helix in pectate lyases
    • Yoder M., Lietzke S., Jurnak F. Unusual structural features in the parallel β-helix in pectate lyases. Structure. 1:1993;241-251.
    • (1993) Structure , vol.1 , pp. 241-251
    • Yoder, M.1    Lietzke, S.2    Jurnak, F.3
  • 68
    • 0027329090 scopus 로고
    • New domain motif - The structure of pectate lyase-C, a secreted plant virulence factor
    • Yoder M., Keen N., Jurnak F. New domain motif - the structure of pectate lyase-C, a secreted plant virulence factor. Science. 260:1993;1503-1506.
    • (1993) Science , vol.260 , pp. 1503-1506
    • Yoder, M.1    Keen, N.2    Jurnak, F.3
  • 69
    • 0029257535 scopus 로고
    • Protein motifs. 3. The parallel β-helix and other coiled folds
    • Yoder M., Jurnak F. Protein motifs. 3. The parallel β-helix and other coiled folds. FASEB J. 9:1995;335-342.
    • (1995) FASEB J. , vol.9 , pp. 335-342
    • Yoder, M.1    Jurnak, F.2
  • 70
    • 0029081224 scopus 로고
    • Circular dichroism of the parallel β-helical proteins pectate lyase-C and lyase-E
    • Sieber V., Jurnak F., Moe G. Circular dichroism of the parallel β-helical proteins pectate lyase-C and lyase-E. Proteins Struct. Funct. Genet. 23:1995;32-37.
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 32-37
    • Sieber, V.1    Jurnak, F.2    Moe, G.3
  • 71
    • 0028095571 scopus 로고
    • Crystal-structure of P22 tailspike protein - interdigitated subunits in a thermostable trimer
    • Steinbacher S., Seckley R., Miller D., Steipe B., Huber R., Reinemer P. Crystal-structure of P22 tailspike protein - interdigitated subunits in a thermostable trimer. Science. 265:1994;383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckley, R.2    Miller, D.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 72
    • 0028844306 scopus 로고
    • A left-handed parallel β-helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz C., Roderick S. A left-handed parallel β-helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science. 270:1995;997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.1    Roderick, S.2
  • 73
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • Lazo N., Downing D. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry. 37:1998;1731-1735.
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.1    Downing, D.2
  • 75
    • 0029839357 scopus 로고    scopus 로고
    • In situ characterization of β-amyloid in Alzheimer's disease tissue by synchrotron Fourier transform infrared microspectroscopy
    • Choo L., Wetzel D., Halliday W., Jackson M., LeVine S., Mantsch H. In situ characterization of β-amyloid in Alzheimer's disease tissue by synchrotron Fourier transform infrared microspectroscopy. Biophys. J. 71:1996;1672-1679.
    • (1996) Biophys. J. , vol.71 , pp. 1672-1679
    • Choo, L.1    Wetzel, D.2    Halliday, W.3    Jackson, M.4    Levine, S.5    Mantsch, H.6
  • 76
    • 0024387388 scopus 로고
    • Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses
    • Snow A., Wight T. Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses. Neurobiol. Aging. 10:1989;481-497.
    • (1989) Neurobiol. Aging , vol.10 , pp. 481-497
    • Snow, A.1    Wight, T.2
  • 79
    • 0028410543 scopus 로고
    • The apolipoprotein E connection
    • Utermann G. The apolipoprotein E connection. Curr. Biol. 4:1994;362-365.
    • (1994) Curr. Biol. , vol.4 , pp. 362-365
    • Utermann, G.1
  • 80
    • 0023838532 scopus 로고
    • Immunochemical identification of the serine protease inhibitor α-1 antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • Abraham C., Selkoe D., Potter H. Immunochemical identification of the serine protease inhibitor α-1 antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell. 52:1988;487-501.
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.1    Selkoe, D.2    Potter, H.3
  • 81
    • 0029610011 scopus 로고
    • The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases
    • McGeer P.L., McGeer E.G. The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases. Brain Res. Rev. 21:1995;195-218.
    • (1995) Brain Res. Rev. , vol.21 , pp. 195-218
    • McGeer, P.L.1    McGeer, E.G.2
  • 82
    • 0026673537 scopus 로고
    • Effects of sulphate ions on Alzheimer β/A4 peptide assemblies for amyloid fibril-proteoglycan interactions
    • Fraser P., Nguyen J., Chin D., Kirschner D. Effects of sulphate ions on Alzheimer β/A4 peptide assemblies for amyloid fibril-proteoglycan interactions. J. Neurochem. 59:1992;1531-1540.
    • (1992) J. Neurochem. , vol.59 , pp. 1531-1540
    • Fraser, P.1    Nguyen, J.2    Chin, D.3    Kirschner, D.4
  • 84
    • 0028988187 scopus 로고
    • 2+-dependent binding of human serum amyloid P component to Alzheimer's β-amyloid peptide
    • 2+-dependent binding of human serum amyloid P component to Alzheimer's β-amyloid peptide. J. Biol. Chem. 270:1995;10392-10394.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10392-10394
    • Hamazaki, H.1
  • 87
    • 0029010736 scopus 로고
    • Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer's disease and systemic amyloidosis
    • Tennent G., Lovat L., Pepys M. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer's disease and systemic amyloidosis. Proc. Natl. Acad. Sci. USA. 92:1995;4299-4303.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4299-4303
    • Tennent, G.1    Lovat, L.2    Pepys, M.3
  • 89
    • 0025265675 scopus 로고
    • α-1 Antichymotypsin is associated solely with amyloid deposition containing the β-protein. Amyloid and cell localization of α-1 antichymotrypsin
    • Abraham C., Shirahama T., Potter H. α-1 Antichymotypsin is associated solely with amyloid deposition containing the β-protein. Amyloid and cell localization of α-1 antichymotrypsin. Neurobiol. Aging. 11:1990;123-129.
    • (1990) Neurobiol. Aging , vol.11 , pp. 123-129
    • Abraham, C.1    Shirahama, T.2    Potter, H.3
  • 91
    • 0028173205 scopus 로고
    • Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • Ma J., Yee A., Brewer B., Das S., Potter H. Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments. Nature. 372:1994;92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, B.3    Das, S.4    Potter, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.