DOI: 10.1006/jmbi.1997.1348. Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen

Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen

10.1006/jmbi.1997.1348

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P. E., Pepys, M. B., & Blake, C. C. F. (1997). Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen. Journal of Molecular Biology, 273(3), 729â739.

Authors 6

Margaret Sunde (first)
Louise C Serpell (additional)
Mark Bartlam (additional)
Paul E Fraser (additional)
Mark B Pepys (additional)
Colin C.F Blake (additional)

References 67 Referenced 1,507

10.1038/224491a0 / Nature / The structure of rhombohedral 2 zinc insulin crystals by Adams (1969)
10.1016/0022-2836(67)90252-5 / J. Mol. Biol. / Structure of β-poly-l-alanine by Arnott (1967)
10.1016/0022-2836(92)90106-T / J. Mol. Biol. / Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer’s disease by Barrow (1992)
10.1073/pnas.82.12.4225 / Proc. Natl Acad. Sci USA / Three-dimensional structures β2-microglobulin by Becker (1985)
10.1016/S0969-2126(96)00104-9 / Structure / Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix by Blake (1996)
10.1016/0022-2836(78)90368-6 / J. Mol. Biol. / Structure of prealbumin by Blake (1978)
{'key': '10.1006/jmbi.1997.1348_BIB7', 'series-title': 'CIBA Symposium No. 199, The Nature and origin of Amyloid Fibrils', 'first-page': '6', 'article-title': 'A molecular model of the amyloid fibril', 'author': 'Blake', 'year': '1996'} / CIBA Symposium No. 199, The Nature and origin of Amyloid Fibrils / A molecular model of the amyloid fibril by Blake (1996)
10.1002/j.1460-2075.1988.tb03109.x / EMBO J. / The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases by Bode (1988)
10.3181/00379727-131-34110 / Proc. Soc. Expt. Biol. Med. / Characterization of the amyloid fibril as a cross-β Protein by Bonar (1967)
{'key': '10.1006/jmbi.1997.1348_BIB10', 'series-title': 'Amyloid and Amyloidosis 1993', 'first-page': '456', 'article-title': 'Three new amyloidogenic transthyretin gene mutations', 'author': 'Booth', 'year': '1994'} / Amyloid and Amyloidosis 1993 / Three new amyloidogenic transthyretin gene mutations by Booth (1994)
10.1038/385787a0 / Nature / Instability, unfolding and fibrillogenesis in amyloidogenic lysozyme variants by Booth (1997)
10.1016/S0022-2836(60)80024-1 / J. Mol. Biol. / The “cross-beta” structure in polypeptides of low molecular weight by Bradbury (1960)
10.1107/S0365110X59000883 / Acta Crystallog / X-ray scattering by bundles of cylinders by Burge (1959)
10.1016/S0022-2836(63)80001-7 / J. Mol. Biol. / Equatorial X-ray diffraction by fibrous proteins by Burge (1963)
10.1021/bi00763a008 / Biochemistry / Cross-β protein structures I. Insulin fibrils by Burke (1972)
{'key': '10.1006/jmbi.1997.1348_BIB16', 'article-title': 'The structure of horse plasma gelsolin to 2.5 Å', 'volume': '70', 'author': 'Burtnick', 'year': '1996', 'journal-title': 'Biophys. J.'} / Biophys. J. / The structure of horse plasma gelsolin to 2.5 Å by Burtnick (1996)
10.1016/0022-2836(73)90022-3 / J. Mol. Biol. / Conformations of twisted β-sheets in proteins by Chothia (1973)
{'key': '10.1006/jmbi.1997.1348_BIB18', 'first-page': '165', 'article-title': 'Electron microscopy of amyloid', 'volume': '3', 'author': 'Cohen', 'year': '1981'} / Electron microscopy of amyloid by Cohen (1981)
10.1021/bi00151a036 / Biochemistry / Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro by Colon (1992)
10.1073/pnas.90.13.5959 / Proc. Natl Acad. Sci. USA / A kinetic model for amyloid formation in the prion diseases by Come (1993)
10.3109/13506129509036922 / Amyloid: Int. J. Exp. Clin. Invest. / Structural studies on FAP fibrils by Damas (1995)
10.1177/16.11.673 / J. Histochem. Cytochem / X-ray diffraction studies on amyloid filaments by Eanes (1968)
10.1042/bj0920018 / Biochem. J. / X-ray diffraction and electron microscope observations on soluble derivatives of keratin by Filshie (1964)
10.1016/S0006-3495(91)82154-3 / Biophys. J. / pH dependent structural transitions of Alzheimer’s amyloid peptides by Fraser (1991)
10.1073/pnas.89.22.10940 / Proc. Natl Acad. Sci. USA / Predicted α-helical regions of the prion protein, when synthesized as peptides, form amyloid by Gasset (1992)
10.1073/pnas.90.1.1 / Proc. Natl Acad. Sci. USA / Perturbation of secondary structure of the scrapie prion protein under conditions that alter infectivity by Gasset (1993)
10.1016/0022-2836(68)90014-4 / J. Mol. Biol. / “Cross β“ conformation in protein by Geddes (1968)
10.1016/0925-4439(93)90160-3 / Biochim. Biophys. Acta / Amyloid formation by salmon calcitonin by Gilchrist (1993)
Glenner, G. G. (1080a). Amyloid deposits and amyloidosis. The beta-fibrilloses (part one). New Eng. J. Med.302, 1283–1292. (10.1056/NEJM198006053022305)
10.1056/NEJM198006123022403 / New Eng. J. Med. / Amyloid deposits and amyloidosis. The bea-fibrilloses (part two) by Glenner (1980)
10.1016/S0006-291X(84)80190-4 / Biochem. Biophys. Res. Commun. / Alzheimer’s disease by Glenner (1984)
10.1016/0006-291X(87)91008-4 / Biochem. Biophys. Res. Commun. / Ten to fourteen residue peptides of Alzheimer’s disease protein are sufficient for amyloid fibril formation and its characteristic X-ray diffraction pattern by Gorevic (1987)
10.1016/S0021-9258(18)53792-3 / J. Biol. Chem. / The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-Met variant to 1.7 Å resolution by Hamilton (1993)
10.1016/S0959-440X(97)80007-3 / Curr. Opin. Struct. Biol. / The prion folding problem by Harrison (1997)
10.1016/0022-2836(91)90881-6 / J. Mol. Biol. / Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer’s disease by Hilbich (1991)
10.1016/S0006-3495(93)81393-6 / Biopys. J. / Structure of β-crystallite assemblies by Alzheimer β-amyloid protein analogues by Inouye (1993)
10.1006/bbrc.1993.1514 / Biochem. Biophys. Res. Commun. / X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin by Jarvis (1993)
10.1016/S0959-440X(96)80089-3 / Curr. Opin. Struct. Biol. / Alternative conformations of amyloidogenic proteins govern their behaviour by Kelly (1996)
10.1016/S0969-2126(97)00215-3 / Structure / Amyloid fibril formation and protein misassembly by Kelly (1997)
10.1073/pnas.83.2.503 / Proc. Natl Acad. Sci. USA / X-ray diffraction from intraneuronal paired helical filaments and extra-neuronal amyloid fibres in Alzheimer’s disease indicates crossβ conformation by Kirschner (1986)
10.1073/pnas.84.19.6953 / Proc. Natl Acad. Sci. USA / Synthetic peptide homologous to β-protein from Alzheimer’s disease forms amyloid-like fibrils in vitro by Kirschner (1987)
10.1107/S0021889892008781 / J. Appl. Crystallog. / Computer processing and analysis of X-ray diffraction data by Lorenz (1993)
10.1021/bi00096a024 / Biochemistry / Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity by McCutchen (1993)
10.1021/bi00041a032 / Biochemistry / Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease by McCutchen (1995)
10.1042/bj2750067 / Biochem. J. / Isolation and characterisation of the integral glycosaminoglycan constitutents of human amyloid A and monoclonal light-chain amyloid fibrils by Nelson (1991)
10.1006/jmbi.1995.0507 / J. Mol. Biol. / X-ray diffraction from scrapie prion rod and PrP peptides by Nguyen (1995)
10.1016/S0006-3495(92)81698-3 / Biophys. J. / Conformational analysis of apolipoprotein A-1 and E-3 based on primary sequence and circular dichroism by Nolte (1992)
10.1073/pnas.90.23.10962 / Proc. Natl Acad. Sci. USA / Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins by Pan (1993)
10.1073/pnas.37.11.729 / Proc. Natl Acad. Sci. USA / Configuration of polypeptide chains with favoured orientation around single bonds by Pauling (1951)
{'key': '10.1006/jmbi.1997.1348_BIB50', 'series-title': 'The Oxford Textbook of Medicine', 'first-page': '1512', 'article-title': 'Amyloidosi', 'author': 'Pepys', 'year': '1996'} / The Oxford Textbook of Medicine / Amyloidosi by Pepys (1996)
10.1038/362553a0 / Nature / Human lysozyme gene mutations cause hereditary systemic amyloidosis by Pepys (1993)
10.1038/382180a0 / Nature / NMR structure of the mouse prion protein domain PrP(121–231) by Riek (1996)
10.1073/pnas.92.21.9490 / Proc. Natl Acad. Sci. USA / Tertiary structure of an amyloid immunoglobulin light chain protein by Schormann (1995)
10.1107/S0907444995013965 / Acta Crystallog. sect. D / Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin by Sebastião (1996)
10.1006/jmbi.1995.0604 / J. Mol. Biol. / The examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs by Serpell (1995)
10.1083/jcb.33.3.679 / J. Cell Biol / High resolution electron microscopic analysis of the amyloid fibril by Shirahama (1967)
10.4049/jimmunol.110.1.21 / J. Immunol. / Fibrillar assemblage of variable segments of immunoglobulin light chains by Shirahama (1973)
10.1074/jbc.270.7.3063 / J. Biol. Chem. / The α-helical to β-sheet transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation by Soto (1995)
10.1111/j.1432-1033.1995.293_1.x / Eur. J. Biochem. / Structure of amyloid A4(1-40)-peptide of Alzheimer’s disease by Sticht (1995)
10.1073/pnas.89.16.7389 / Proc. Natl Acad. Sci. USA / Apolipoprotein A-1 mutation Arg-60 causes autosomal dominant amyloidosis by Soutar (1992)
10.1073/pnas.90.20.9678 / Proc. Natl Acad. Sci. USA / Synthetic peptides homologous to prion protein residues 106–147 form amyloid-like fibrils in vitro by Tagliavini (1993)
10.1021/bi00191a006 / Biochemistry / Solution structure of residues 1–28 of the amyloid β-peptide by Talafous (1994)
10.1016/0272-6386(95)90647-9 / Am. J. Kidney Dis. / Treatment of amyloidosis by Tan (1995)
10.1002/j.1460-2075.1993.tb05707.x / EMBO J. / Structure of Met30 variant of transthyretin and its amyloidogenic variations by Terry (1993)
{'key': '10.1006/jmbi.1997.1348_BIB65', 'first-page': '409', 'article-title': 'X-Ray scattering and diffraction by wet gels of AA amyloid fibrils', 'volume': '3', 'author': 'Turnell', 'year': '1986', 'journal-title': 'Mol. Biol. Med.'} / Mol. Biol. Med. / X-Ray scattering and diffraction by wet gels of AA amyloid fibrils by Turnell (1986)
{'key': '10.1006/jmbi.1997.1348_BIB66', 'first-page': '387', 'article-title': 'Secondary structure preduction of human SAA1, presumptive identification of calcium and lipid binding sites', 'volume': '3', 'author': 'Turnell', 'year': '1986', 'journal-title': 'Mol. Biol. Med.'} / Mol. Biol. Med. / Secondary structure preduction of human SAA1, presumptive identification of calcium and lipid binding sites by Turnell (1986)
10.1073/pnas.75.11.5475 / Proc. Natl Acad. Sci. USA / Structural origins of diamagnetic anisotropy in proteins by Worcester (1978)

Dates

Type	When
Created	22 years, 10 months ago (Oct. 7, 2002, 12:30 p.m.)
Deposited	2 years, 5 months ago (April 4, 2023, 10:15 a.m.)
Indexed	1 day, 18 hours ago (Sept. 4, 2025, 9:33 a.m.)
Issued	27 years, 11 months ago (Oct. 1, 1997)
Published	27 years, 11 months ago (Oct. 1, 1997)
Published Print	27 years, 11 months ago (Oct. 1, 1997)

Funders 0

None

BibTeX

@article{Sunde_1997, title={Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen}, volume={273}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.1997.1348}, DOI={10.1006/jmbi.1997.1348}, number={3}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Sunde, Margaret and Serpell, Louise C and Bartlam, Mark and Fraser, Paul E and Pepys, Mark B and Blake, Colin C.F}, year={1997}, month=oct, pages={729–739} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        9,
        4
      ]
    ],
    "date-time": "2025-09-04T13:33:12Z",
    "timestamp": 1756992792440
  },
  "reference-count": 67,
  "publisher": "Elsevier BV",
  "issue": "3",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            1997,
            10,
            1
          ]
        ],
        "date-time": "1997-10-01T00:00:00Z",
        "timestamp": 875664000000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://www.elsevier.com/tdm/userlicense/1.0/"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        1997,
        10
      ]
    ]
  },
  "DOI": "10.1006/jmbi.1997.1348",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2002,
        10,
        7
      ]
    ],
    "date-time": "2002-10-07T16:30:16Z",
    "timestamp": 1034008216000
  },
  "page": "729-739",
  "source": "Crossref",
  "is-referenced-by-count": 1507,
  "title": "Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen",
  "prefix": "10.1006",
  "volume": "273",
  "author": [
    {
      "given": "Margaret",
      "family": "Sunde",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Louise C",
      "family": "Serpell",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Mark",
      "family": "Bartlam",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Paul E",
      "family": "Fraser",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Mark B",
      "family": "Pepys",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Colin C.F",
      "family": "Blake",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "78",
  "reference": [
    {
      "key": "10.1006/jmbi.1997.1348_BIB1",
      "doi-asserted-by": "crossref",
      "first-page": "491",
      "DOI": "10.1038/224491a0",
      "article-title": "The structure of rhombohedral 2 zinc insulin crystals",
      "volume": "224",
      "author": "Adams",
      "year": "1969",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB2",
      "doi-asserted-by": "crossref",
      "first-page": "201",
      "DOI": "10.1016/0022-2836(67)90252-5",
      "article-title": "Structure of \u03b2-poly-l-alanine",
      "volume": "30",
      "author": "Arnott",
      "year": "1967",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB3",
      "doi-asserted-by": "crossref",
      "first-page": "1075",
      "DOI": "10.1016/0022-2836(92)90106-T",
      "article-title": "Solution conformations and aggregational properties of synthetic amyloid \u03b2-peptides of Alzheimer\u2019s disease",
      "volume": "225",
      "author": "Barrow",
      "year": "1992",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB4",
      "doi-asserted-by": "crossref",
      "first-page": "4225",
      "DOI": "10.1073/pnas.82.12.4225",
      "article-title": "Three-dimensional structures \u03b22-microglobulin",
      "volume": "82",
      "author": "Becker",
      "year": "1985",
      "journal-title": "Proc. Natl Acad. Sci USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB5",
      "doi-asserted-by": "crossref",
      "first-page": "989",
      "DOI": "10.1016/S0969-2126(96)00104-9",
      "article-title": "Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous \u03b2-sheet helix",
      "volume": "4",
      "author": "Blake",
      "year": "1996",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB6",
      "doi-asserted-by": "crossref",
      "first-page": "339",
      "DOI": "10.1016/0022-2836(78)90368-6",
      "article-title": "Structure of prealbumin",
      "volume": "121",
      "author": "Blake",
      "year": "1978",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB7",
      "series-title": "CIBA Symposium No. 199, The Nature and origin of Amyloid Fibrils",
      "first-page": "6",
      "article-title": "A molecular model of the amyloid fibril",
      "author": "Blake",
      "year": "1996"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB8",
      "doi-asserted-by": "crossref",
      "first-page": "2593",
      "DOI": "10.1002/j.1460-2075.1988.tb03109.x",
      "article-title": "The 2.0 \u00c5 X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases",
      "volume": "7",
      "author": "Bode",
      "year": "1988",
      "journal-title": "EMBO J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB9",
      "doi-asserted-by": "crossref",
      "first-page": "1373",
      "DOI": "10.3181/00379727-131-34110",
      "article-title": "Characterization of the amyloid fibril as a cross-\u03b2 Protein",
      "volume": "131",
      "author": "Bonar",
      "year": "1967",
      "journal-title": "Proc. Soc. Expt. Biol. Med."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB10",
      "series-title": "Amyloid and Amyloidosis 1993",
      "first-page": "456",
      "article-title": "Three new amyloidogenic transthyretin gene mutations",
      "author": "Booth",
      "year": "1994"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB11",
      "doi-asserted-by": "crossref",
      "first-page": "787",
      "DOI": "10.1038/385787a0",
      "article-title": "Instability, unfolding and fibrillogenesis in amyloidogenic lysozyme variants",
      "volume": "385",
      "author": "Booth",
      "year": "1997",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB12",
      "doi-asserted-by": "crossref",
      "first-page": "276",
      "DOI": "10.1016/S0022-2836(60)80024-1",
      "article-title": "The \u201ccross-beta\u201d structure in polypeptides of low molecular weight",
      "volume": "2",
      "author": "Bradbury",
      "year": "1960",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB13",
      "doi-asserted-by": "crossref",
      "first-page": "285",
      "DOI": "10.1107/S0365110X59000883",
      "article-title": "X-ray scattering by bundles of cylinders",
      "volume": "12",
      "author": "Burge",
      "year": "1959",
      "journal-title": "Acta Crystallog"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB14",
      "doi-asserted-by": "crossref",
      "first-page": "213",
      "DOI": "10.1016/S0022-2836(63)80001-7",
      "article-title": "Equatorial X-ray diffraction by fibrous proteins",
      "volume": "7",
      "author": "Burge",
      "year": "1963",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB15",
      "doi-asserted-by": "crossref",
      "first-page": "2435",
      "DOI": "10.1021/bi00763a008",
      "article-title": "Cross-\u03b2 protein structures I. Insulin fibrils",
      "volume": "11",
      "author": "Burke",
      "year": "1972",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB16",
      "article-title": "The structure of horse plasma gelsolin to 2.5 \u00c5",
      "volume": "70",
      "author": "Burtnick",
      "year": "1996",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB17",
      "doi-asserted-by": "crossref",
      "first-page": "295",
      "DOI": "10.1016/0022-2836(73)90022-3",
      "article-title": "Conformations of twisted \u03b2-sheets in proteins",
      "volume": "75",
      "author": "Chothia",
      "year": "1973",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB18",
      "first-page": "165",
      "article-title": "Electron microscopy of amyloid",
      "volume": "3",
      "author": "Cohen",
      "year": "1981"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB19",
      "doi-asserted-by": "crossref",
      "first-page": "8654",
      "DOI": "10.1021/bi00151a036",
      "article-title": "Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro",
      "volume": "31",
      "author": "Colon",
      "year": "1992",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB20",
      "doi-asserted-by": "crossref",
      "first-page": "5959",
      "DOI": "10.1073/pnas.90.13.5959",
      "article-title": "A kinetic model for amyloid formation in the prion diseases",
      "volume": "90",
      "author": "Come",
      "year": "1993",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB21",
      "doi-asserted-by": "crossref",
      "DOI": "10.3109/13506129509036922",
      "article-title": "Structural studies on FAP fibrils",
      "volume": "2",
      "author": "Damas",
      "year": "1995",
      "journal-title": "Amyloid: Int. J. Exp. Clin. Invest."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB22",
      "doi-asserted-by": "crossref",
      "first-page": "673",
      "DOI": "10.1177/16.11.673",
      "article-title": "X-ray diffraction studies on amyloid filaments",
      "volume": "16",
      "author": "Eanes",
      "year": "1968",
      "journal-title": "J. Histochem. Cytochem"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB23",
      "doi-asserted-by": "crossref",
      "first-page": "19",
      "DOI": "10.1042/bj0920018",
      "article-title": "X-ray diffraction and electron microscope observations on soluble derivatives of keratin",
      "volume": "92",
      "author": "Filshie",
      "year": "1964",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB24",
      "doi-asserted-by": "crossref",
      "first-page": "1190",
      "DOI": "10.1016/S0006-3495(91)82154-3",
      "article-title": "pH dependent structural transitions of Alzheimer\u2019s amyloid peptides",
      "volume": "60",
      "author": "Fraser",
      "year": "1991",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB25",
      "doi-asserted-by": "crossref",
      "first-page": "10940",
      "DOI": "10.1073/pnas.89.22.10940",
      "article-title": "Predicted \u03b1-helical regions of the prion protein, when synthesized as peptides, form amyloid",
      "volume": "89",
      "author": "Gasset",
      "year": "1992",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB26",
      "doi-asserted-by": "crossref",
      "first-page": "1",
      "DOI": "10.1073/pnas.90.1.1",
      "article-title": "Perturbation of secondary structure of the scrapie prion protein under conditions that alter infectivity",
      "volume": "90",
      "author": "Gasset",
      "year": "1993",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB27",
      "doi-asserted-by": "crossref",
      "first-page": "343",
      "DOI": "10.1016/0022-2836(68)90014-4",
      "article-title": "\u201cCross \u03b2\u201c conformation in protein",
      "volume": "32",
      "author": "Geddes",
      "year": "1968",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB28",
      "doi-asserted-by": "crossref",
      "first-page": "111",
      "DOI": "10.1016/0925-4439(93)90160-3",
      "article-title": "Amyloid formation by salmon calcitonin",
      "author": "Gilchrist",
      "year": "1993",
      "journal-title": "Biochim. Biophys. Acta"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB29",
      "doi-asserted-by": "crossref",
      "unstructured": "Glenner, G. G. (1080a). Amyloid deposits and amyloidosis. The beta-fibrilloses (part one). New Eng. J. Med.302, 1283\u20131292.",
      "DOI": "10.1056/NEJM198006053022305"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB30",
      "doi-asserted-by": "crossref",
      "first-page": "1333",
      "DOI": "10.1056/NEJM198006123022403",
      "article-title": "Amyloid deposits and amyloidosis. The bea-fibrilloses (part two)",
      "volume": "302",
      "author": "Glenner",
      "year": "1980",
      "journal-title": "New Eng. J. Med."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB31",
      "doi-asserted-by": "crossref",
      "first-page": "885",
      "DOI": "10.1016/S0006-291X(84)80190-4",
      "article-title": "Alzheimer\u2019s disease",
      "volume": "120",
      "author": "Glenner",
      "year": "1984",
      "journal-title": "Biochem. Biophys. Res. Commun."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB32",
      "doi-asserted-by": "crossref",
      "first-page": "854",
      "DOI": "10.1016/0006-291X(87)91008-4",
      "article-title": "Ten to fourteen residue peptides of Alzheimer\u2019s disease protein are sufficient for amyloid fibril formation and its characteristic X-ray diffraction pattern",
      "volume": "147",
      "author": "Gorevic",
      "year": "1987",
      "journal-title": "Biochem. Biophys. Res. Commun."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB33",
      "doi-asserted-by": "crossref",
      "first-page": "2416",
      "DOI": "10.1016/S0021-9258(18)53792-3",
      "article-title": "The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-Met variant to 1.7 \u00c5 resolution",
      "volume": "268",
      "author": "Hamilton",
      "year": "1993",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB34",
      "doi-asserted-by": "crossref",
      "first-page": "53",
      "DOI": "10.1016/S0959-440X(97)80007-3",
      "article-title": "The prion folding problem",
      "volume": "7",
      "author": "Harrison",
      "year": "1997",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB35",
      "doi-asserted-by": "crossref",
      "first-page": "149",
      "DOI": "10.1016/0022-2836(91)90881-6",
      "article-title": "Aggregation and secondary structure of synthetic amyloid \u03b2A4 peptides of Alzheimer\u2019s disease",
      "volume": "218",
      "author": "Hilbich",
      "year": "1991",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB36",
      "doi-asserted-by": "crossref",
      "first-page": "502",
      "DOI": "10.1016/S0006-3495(93)81393-6",
      "article-title": "Structure of \u03b2-crystallite assemblies by Alzheimer \u03b2-amyloid protein analogues",
      "volume": "64",
      "author": "Inouye",
      "year": "1993",
      "journal-title": "Biopys. J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB37",
      "doi-asserted-by": "crossref",
      "first-page": "991",
      "DOI": "10.1006/bbrc.1993.1514",
      "article-title": "X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin",
      "volume": "192",
      "author": "Jarvis",
      "year": "1993",
      "journal-title": "Biochem. Biophys. Res. Commun."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB38",
      "doi-asserted-by": "crossref",
      "first-page": "11",
      "DOI": "10.1016/S0959-440X(96)80089-3",
      "article-title": "Alternative conformations of amyloidogenic proteins govern their behaviour",
      "volume": "6",
      "author": "Kelly",
      "year": "1996",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB39",
      "doi-asserted-by": "crossref",
      "first-page": "595",
      "DOI": "10.1016/S0969-2126(97)00215-3",
      "article-title": "Amyloid fibril formation and protein misassembly",
      "volume": "5",
      "author": "Kelly",
      "year": "1997",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB40",
      "doi-asserted-by": "crossref",
      "first-page": "503",
      "DOI": "10.1073/pnas.83.2.503",
      "article-title": "X-ray diffraction from intraneuronal paired helical filaments and extra-neuronal amyloid fibres in Alzheimer\u2019s disease indicates cross\u03b2 conformation",
      "volume": "83",
      "author": "Kirschner",
      "year": "1986",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB41",
      "doi-asserted-by": "crossref",
      "first-page": "6953",
      "DOI": "10.1073/pnas.84.19.6953",
      "article-title": "Synthetic peptide homologous to \u03b2-protein from Alzheimer\u2019s disease forms amyloid-like fibrils in vitro",
      "volume": "84",
      "author": "Kirschner",
      "year": "1987",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB42",
      "doi-asserted-by": "crossref",
      "first-page": "82",
      "DOI": "10.1107/S0021889892008781",
      "article-title": "Computer processing and analysis of X-ray diffraction data",
      "volume": "26",
      "author": "Lorenz",
      "year": "1993",
      "journal-title": "J. Appl. Crystallog."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB43",
      "doi-asserted-by": "crossref",
      "first-page": "12119",
      "DOI": "10.1021/bi00096a024",
      "article-title": "Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity",
      "volume": "32",
      "author": "McCutchen",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB44",
      "doi-asserted-by": "crossref",
      "first-page": "13527",
      "DOI": "10.1021/bi00041a032",
      "article-title": "Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease",
      "volume": "34",
      "author": "McCutchen",
      "year": "1995",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB45",
      "doi-asserted-by": "crossref",
      "first-page": "67",
      "DOI": "10.1042/bj2750067",
      "article-title": "Isolation and characterisation of the integral glycosaminoglycan constitutents of human amyloid A and monoclonal light-chain amyloid fibrils",
      "volume": "275",
      "author": "Nelson",
      "year": "1991",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB46",
      "doi-asserted-by": "crossref",
      "first-page": "412",
      "DOI": "10.1006/jmbi.1995.0507",
      "article-title": "X-ray diffraction from scrapie prion rod and PrP peptides",
      "volume": "252",
      "author": "Nguyen",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB47",
      "doi-asserted-by": "crossref",
      "first-page": "1221",
      "DOI": "10.1016/S0006-3495(92)81698-3",
      "article-title": "Conformational analysis of apolipoprotein A-1 and E-3 based on primary sequence and circular dichroism",
      "volume": "63",
      "author": "Nolte",
      "year": "1992",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB48",
      "doi-asserted-by": "crossref",
      "first-page": "10962",
      "DOI": "10.1073/pnas.90.23.10962",
      "article-title": "Conversion of \u03b1-helices into \u03b2-sheets features in the formation of the scrapie prion proteins",
      "volume": "90",
      "author": "Pan",
      "year": "1993",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB49",
      "doi-asserted-by": "crossref",
      "first-page": "729",
      "DOI": "10.1073/pnas.37.11.729",
      "article-title": "Configuration of polypeptide chains with favoured orientation around single bonds",
      "volume": "37",
      "author": "Pauling",
      "year": "1951",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB50",
      "series-title": "The Oxford Textbook of Medicine",
      "first-page": "1512",
      "article-title": "Amyloidosi",
      "author": "Pepys",
      "year": "1996"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB51",
      "doi-asserted-by": "crossref",
      "first-page": "553",
      "DOI": "10.1038/362553a0",
      "article-title": "Human lysozyme gene mutations cause hereditary systemic amyloidosis",
      "volume": "362",
      "author": "Pepys",
      "year": "1993",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB52",
      "doi-asserted-by": "crossref",
      "first-page": "180",
      "DOI": "10.1038/382180a0",
      "article-title": "NMR structure of the mouse prion protein domain PrP(121\u2013231)",
      "volume": "382",
      "author": "Riek",
      "year": "1996",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB53",
      "doi-asserted-by": "crossref",
      "first-page": "9490",
      "DOI": "10.1073/pnas.92.21.9490",
      "article-title": "Tertiary structure of an amyloid immunoglobulin light chain protein",
      "volume": "92",
      "author": "Schormann",
      "year": "1995",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB54",
      "doi-asserted-by": "crossref",
      "first-page": "566",
      "DOI": "10.1107/S0907444995013965",
      "article-title": "Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin",
      "volume": "52",
      "author": "Sebasti\u00e3o",
      "year": "1996",
      "journal-title": "Acta Crystallog. sect. D"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB55",
      "doi-asserted-by": "crossref",
      "first-page": "113",
      "DOI": "10.1006/jmbi.1995.0604",
      "article-title": "The examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs",
      "volume": "254",
      "author": "Serpell",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB56",
      "doi-asserted-by": "crossref",
      "first-page": "679",
      "DOI": "10.1083/jcb.33.3.679",
      "article-title": "High resolution electron microscopic analysis of the amyloid fibril",
      "volume": "33",
      "author": "Shirahama",
      "year": "1967",
      "journal-title": "J. Cell Biol"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB57",
      "doi-asserted-by": "crossref",
      "first-page": "21",
      "DOI": "10.4049/jimmunol.110.1.21",
      "article-title": "Fibrillar assemblage of variable segments of immunoglobulin light chains",
      "volume": "110",
      "author": "Shirahama",
      "year": "1973",
      "journal-title": "J. Immunol."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB58",
      "doi-asserted-by": "crossref",
      "first-page": "3063",
      "DOI": "10.1074/jbc.270.7.3063",
      "article-title": "The \u03b1-helical to \u03b2-sheet transition in the amino-terminal fragment of the amyloid \u03b2-peptide modulates amyloid formation",
      "volume": "270",
      "author": "Soto",
      "year": "1995",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB59",
      "doi-asserted-by": "crossref",
      "first-page": "293",
      "DOI": "10.1111/j.1432-1033.1995.293_1.x",
      "article-title": "Structure of amyloid A4(1-40)-peptide of Alzheimer\u2019s disease",
      "volume": "233",
      "author": "Sticht",
      "year": "1995",
      "journal-title": "Eur. J. Biochem."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB60",
      "doi-asserted-by": "crossref",
      "first-page": "7389",
      "DOI": "10.1073/pnas.89.16.7389",
      "article-title": "Apolipoprotein A-1 mutation Arg-60 causes autosomal dominant amyloidosis",
      "volume": "89",
      "author": "Soutar",
      "year": "1992",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB61",
      "doi-asserted-by": "crossref",
      "first-page": "9678",
      "DOI": "10.1073/pnas.90.20.9678",
      "article-title": "Synthetic peptides homologous to prion protein residues 106\u2013147 form amyloid-like fibrils in vitro",
      "volume": "90",
      "author": "Tagliavini",
      "year": "1993",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB62",
      "doi-asserted-by": "crossref",
      "first-page": "7788",
      "DOI": "10.1021/bi00191a006",
      "article-title": "Solution structure of residues 1\u201328 of the amyloid \u03b2-peptide",
      "volume": "33",
      "author": "Talafous",
      "year": "1994",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB63",
      "doi-asserted-by": "crossref",
      "first-page": "267",
      "DOI": "10.1016/0272-6386(95)90647-9",
      "article-title": "Treatment of amyloidosis",
      "volume": "26",
      "author": "Tan",
      "year": "1995",
      "journal-title": "Am. J. Kidney Dis."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB64",
      "doi-asserted-by": "crossref",
      "first-page": "735",
      "DOI": "10.1002/j.1460-2075.1993.tb05707.x",
      "article-title": "Structure of Met30 variant of transthyretin and its amyloidogenic variations",
      "volume": "12",
      "author": "Terry",
      "year": "1993",
      "journal-title": "EMBO J."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB65",
      "first-page": "409",
      "article-title": "X-Ray scattering and diffraction by wet gels of AA amyloid fibrils",
      "volume": "3",
      "author": "Turnell",
      "year": "1986",
      "journal-title": "Mol. Biol. Med."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB66",
      "first-page": "387",
      "article-title": "Secondary structure preduction of human SAA1, presumptive identification of calcium and lipid binding sites",
      "volume": "3",
      "author": "Turnell",
      "year": "1986",
      "journal-title": "Mol. Biol. Med."
    },
    {
      "key": "10.1006/jmbi.1997.1348_BIB67",
      "doi-asserted-by": "crossref",
      "first-page": "5475",
      "DOI": "10.1073/pnas.75.11.5475",
      "article-title": "Structural origins of diamagnetic anisotropy in proteins",
      "volume": "75",
      "author": "Worcester",
      "year": "1978",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    }
  ],
  "container-title": "Journal of Molecular Biology",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.elsevier.com/content/article/PII:S0022283697913486?httpAccept=text/xml",
      "content-type": "text/xml",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://api.elsevier.com/content/article/PII:S0022283697913486?httpAccept=text/plain",
      "content-type": "text/plain",
      "content-version": "vor",
      "intended-application": "text-mining"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        4,
        4
      ]
    ],
    "date-time": "2023-04-04T14:15:22Z",
    "timestamp": 1680617722000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://linkinghub.elsevier.com/retrieve/pii/S0022283697913486"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1997,
        10
      ]
    ]
  },
  "references-count": 67,
  "journal-issue": {
    "issue": "3",
    "published-print": {
      "date-parts": [
        [
          1997,
          10
        ]
      ]
    }
  },
  "alternative-id": [
    "S0022283697913486"
  ],
  "URL": "http://dx.doi.org/10.1006/jmbi.1997.1348",
  "relation": {},
  "ISSN": [
    "0022-2836"
  ],
  "subject": [],
  "container-title-short": "Journal of Molecular Biology",
  "published": {
    "date-parts": [
      [
        1997,
        10
      ]
    ]
  }
}