DOI: 10.1016/s0969-2126(96)00104-9. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

10.1016/s0969-2126(96)00104-9

Crossref journal-article

Elsevier BV

Structure (78)

Bibliography

Blake, C., & Serpell, L. (1996). Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous Î²-sheet helix. Structure, 4(8), 989â998.

Authors 2

Colin Blake (first)
Louise Serpell (additional)

References 32 Referenced 331

{'key': '10.1016/S0969-2126(96)00104-9_BIB1', 'series-title': 'The metabolic basis of disease', 'first-page': '2439', 'article-title': 'Amyloidosis', 'author': 'Benson', 'year': '1989'} / The metabolic basis of disease / Amyloidosis by Benson (1989)
10.1111/j.1365-2559.1994.tb00001.x / Histopathology / Amyloidosis by Tan (1994)
{'key': '10.1016/S0969-2126(96)00104-9_BIB3', 'series-title': 'Electron microscopy of Proteins vol 3', 'first-page': '165', 'article-title': 'Electron microscopy of amyloid', 'author': 'Cohen', 'year': '1982'} / Electron microscopy of Proteins vol 3 / Electron microscopy of amyloid by Cohen (1982)
10.1177/16.11.673 / J. Histochem. Cytochem / X-ray diffraction studies on amyloid filaments by Eanes (1968)
10.3181/00379727-131-34110 / Proc. Soc. Exp. Biol. Med / Characterization of the amyloid fibril as a cross-β protein by Bonar (1967)
{'key': '10.1016/S0969-2126(96)00104-9_BIB6', '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)
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 alzheimers disease indicates cross-β conformation by Kirschner (1986)
10.1073/pnas.37.11.729 / Natl. Acad. Sci. USA / Configuration of polypeptide chains with favoured orientation around single bonds: two new pleated sheets. Proc by Pauling (1951)
10.1016/0022-2836(68)90014-4 / J. Mol. Biol / ‘Cross-β’ conformation in protein by Geddes (1968)
10.1016/0022-2836(73)90022-3 / J. Mol. Biol / Conformations of twisted β-sheets in proteins by Chothia (1973)
10.1083/jcb.33.3.679 / J. Cell. Biol / High resolution electron microscopic analysis of the amyloid fibril by Shirahama (1967)
10.1002/jnr.490280404 / J. Neurosci. Res / Morphology and antibody recognition of synthetic β-amyloid peptides by Fraser (1991)
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)
10.1073/pnas.75.9.4499 / Proc. Natl. Acad. Sci. USA / Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy by Costa (1978)
10.1016/S0021-9258(19)42128-5 / J. Biol. Chem / The amino acid sequence of human plasma prealbumin by Kanda (1974)
10.1016/0022-2836(74)90291-5 / J. Mol. Biol / Structure of human plasma prealbumin at 2.5 å resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding by Blake (1974)
10.1016/0022-2836(78)90368-6 / J. Mol. Biol / Structure of prealbumin: secondary, tertiary and quaternary interactions determined by fourier refinement at 1.8 å by Blake (1978)
10.3109/13506129609014354 / Amyloid-Int. J. Exp. Clin. Invest / Transthyretin amyloidosis by Benson (1996)
10.1073/pnas.87.7.2843 / Proc. Natl. Acad. Sci. USA / Fibril in senile systemic amyloidosis is derived from normal transthyretin by Westermark (1990)
R. Vidal, et al., T. Wisniewski, Meningocerebrovascular amyloidosis associated with a novel transthyretin (TTR) missense mutation at codon 18(TTR D18G), Am. J. Pathology in press.
C.J. Terry, Structural studies of plasma proteins of medical interest, PhD thesis, University of Oxford, UK.
10.1016/S0022-2836(63)80001-7 / J. Mol. Biol / Equatorial X-ray diffraction by fibrous proteins: short-range order in collagen, feather keratin and f-actin by Burge (1963)
10.1107/S0365110X59000883 / Acta Crystallogr / X-ray scattering by bundles of cylinders by Burge (1959)
10.1038/nsb1195-990 / Nat. Struct. Biol / Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide by Lansbury (1995)
10.1016/0969-2126(93)90013-7 / Structure / Unusual structural features in the parallel β-helix in pectate lyases by Yoder (1993)
10.1021/bi00151a036 / Biochemistry / Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro by Colon (1992)
{'key': '10.1016/S0969-2126(96)00104-9_BIB27', 'first-page': 'in press', 'article-title': 'The edge-strand hypothesis: prediction and test of a mutational hot-spot on the transthyretin molecule associated with FAP amyloidogenesis', 'author': 'Serpell', 'year': '1996', 'journal-title': 'Amyloid-Int. J. Exp. Clin. Invest'} / Amyloid-Int. J. Exp. Clin. Invest / The edge-strand hypothesis: prediction and test of a mutational hot-spot on the transthyretin molecule associated with FAP amyloidogenesis by Serpell (1996)
{'key': '10.1016/S0969-2126(96)00104-9_BIB28', 'series-title': 'Amyloid and Amyloidosis', 'first-page': '447', 'article-title': 'Frequency analysis and structural correlation of FAP mutations in transthyretin', 'author': 'Serpell', 'year': '1993'} / Amyloid and Amyloidosis / Frequency analysis and structural correlation of FAP mutations in transthyretin by Serpell (1993)
J.W. Kelly, P.T. Lansbury, A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation, Amyloid-Int. J. Exp. Clin. Invest 1 186-205. (10.3109/13506129409148451)
A. Brunger, XPLOR. Version 3.1: A system for X-ray crystallography and NMR, Yale University Press, New Haven and London.
10.1107/S0021889891004399 / J. Appl. Crystallogr / MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures by Kraulis (1991)
10.1107/S0021889892008781 / J. Appl. Crystallogr / Computer processing and analysis of X-ray diffraction data by Lorenz (1993)

Dates

Type	When
Created	21 years, 2 months ago (June 8, 2004, 2:49 p.m.)
Deposited	4 years, 2 months ago (June 22, 2021, 9:09 p.m.)
Indexed	3 months, 1 week ago (May 15, 2025, 1:28 p.m.)
Issued	29 years ago (Aug. 1, 1996)
Published	29 years ago (Aug. 1, 1996)
Published Print	29 years ago (Aug. 1, 1996)

Funders 0

None

BibTeX

@article{Blake_1996, title={Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix}, volume={4}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/s0969-2126(96)00104-9}, DOI={10.1016/s0969-2126(96)00104-9}, number={8}, journal={Structure}, publisher={Elsevier BV}, author={Blake, Colin and Serpell, Louise}, year={1996}, month=aug, pages={989–998} }

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  ],
  "URL": "http://dx.doi.org/10.1016/S0969-2126(96)00104-9",
  "relation": {},
  "ISSN": [
    "0969-2126"
  ],
  "subject": [],
  "container-title-short": "Structure",
  "published": {
    "date-parts": [
      [
        1996,
        8
      ]
    ]
  }
}