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Volumn , Issue 199, 1996, Pages 6-21

A molecular model of the amyloid fibril

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID;

EID: 0030344361     PISSN: 03005208     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (43)

References (16)
  • 1
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    • (1989) The Metabolic Basis of Inherited Disease , pp. 2439-2460
    • Benson, M.D.1    Wallace, M.R.2
  • 2
    • 0016140360 scopus 로고
    • Structure of human plasma prealbumin at 2.5 Å resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding
    • Blake C, Geisow M, Rerat B, Rerat C, Swan I 1974 Structure of human plasma prealbumin at 2.5 Å resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding. J Mol Biol 88:1-12
    • (1974) J Mol Biol , vol.88 , pp. 1-12
    • Blake, C.1    Geisow, M.2    Rerat, B.3    Rerat, C.4    Swan, I.5
  • 3
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • Blake CCF, Geisow MJ, Oatley SJ, Rerat B, Rerat C 1978 Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J Mol Biol 121:339-356
    • (1978) J Mol Biol , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 4
    • 0014578835 scopus 로고
    • Characterization of the amyloid fibril as a cross-β protein
    • Bonar L, Cohen A, Skinner M 1967 Characterization of the amyloid fibril as a cross-β protein. Proc Soc Exp Biol Med 131:1373-1375
    • (1967) Proc Soc Exp Biol Med , vol.131 , pp. 1373-1375
    • Bonar, L.1    Cohen, A.2    Skinner, M.3
  • 5
    • 0015914783 scopus 로고
    • Conformations of twisted-β sheets in proteins
    • Chothia C 1973 Conformations of twisted-β sheets in proteins. J Mol Biol 75:295-302
    • (1973) J Mol Biol , vol.75 , pp. 295-302
    • Chothia, C.1
  • 6
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W, Kelly JW 1992 Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31:8654-8660
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 7
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa P, Figueira A, Bravo F 1978 Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci USA 75:4499-4503
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4499-4503
    • Costa, P.1    Figueira, A.2    Bravo, F.3
  • 8
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes ED, Glenner GG 1968 X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 16:673
    • (1968) J Histochem Cytochem , vol.16 , pp. 673
    • Eanes, E.D.1    Glenner, G.G.2
  • 10
    • 0016238506 scopus 로고
    • The amino acid sequence of human plasma prealbumin
    • Kanda Y, Goodman D, Canfield R, Morgan F 1974 The amino acid sequence of human plasma prealbumin. J Biol Chem 249:6796-6805
    • (1974) J Biol Chem , vol.249 , pp. 6796-6805
    • Kanda, Y.1    Goodman, D.2    Canfield, R.3    Morgan, F.4
  • 11
    • 0000573263 scopus 로고
    • Configuration of polypeptide chains with favored orientation around single bonds: Two new pleated sheets
    • Pauling L, Corey R 1951 Configuration of polypeptide chains with favored orientation around single bonds: two new pleated sheets. Proc Natl Acad Sci USA 37:729-735
    • (1951) Proc Natl Acad Sci USA , vol.37 , pp. 729-735
    • Pauling, L.1    Corey, R.2
  • 12
    • 0027506498 scopus 로고
    • Human lysozyme gene mutations cause hereditary systemic amyloidosis
    • Pepys MB, Hawkins PN, Booth DR et al 1993 Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362:553-557
    • (1993) Nature , vol.362 , pp. 553-557
    • Pepys, M.B.1    Hawkins, P.N.2    Booth, D.R.3
  • 13
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • Saraiva MJM 1995 Transthyretin mutations in health and disease. Hum Mutat 5: 191-196
    • (1995) Hum Mutat , vol.5 , pp. 191-196
    • Saraiva, M.J.M.1
  • 14
    • 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 et al 1995 The 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.1    Sunde, M.2    Fraser, P.3
  • 15
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    • High resolution electron microscopic analysis of the amyloid fibril
    • Shirahama T, Cohen AS 1967 High resolution electron microscopic analysis of the amyloid fibril. J Cell Biol 33:679-708
    • (1967) J Cell Biol , vol.33 , pp. 679-708
    • Shirahama, T.1    Cohen, A.S.2
  • 16
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    • Amyloidosis
    • Sipe JD 1992 Amyloidosis. Ann Rev Biochem 61:947-975
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    • Sipe, J.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.