Crossref
journal-article
Elsevier BV
Journal of Molecular Biology (78)
References
38
Referenced
149
10.1073/pnas.95.23.13407
/ Proc. Natl Acad. Sci. USA / Propagating structure of Alzheimer’s β-amyloid (10-35) is parallel β-sheet with residues in exact register by Benzinger (1998)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-helix by Blake (1996)10.1093/infdis/161.3.467
/ J. Infect. Dis. / Resistance of scrapie infectivity to steam autoclaving after formaldehyde fixation and limited survival after ashing at 360 °C. Practical and theoretical implications by Brown (1990)10.1021/bi00245a003
/ Biochemistry / Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infra-red spectroscopy by Caughey (1991)10.1016/0022-2836(73)90022-3
/ J. Mol. Biol. / Conformations of twisted β-sheets in proteins by Chothia (1973){'key': '10.1006/jmbi.2000.3650_BIB6', 'first-page': '165', 'article-title': 'Electron microscopy of amyloid', 'volume': 'vol. 3', 'author': 'Cohen', 'year': '1982'}
/ Electron microscopy of amyloid by Cohen (1982)10.1006/jsbi.1996.0003
/ J. Strict. Biol. / MRC Image processing programs by Crowther (1996)10.1177/16.11.673
/ J. Histochem. Cytochem. / X-Ray diffraction studies on amyloid filaments by Eanes (1968)10.1016/S0006-3495(91)82154-3
/ Biophys. J. / pH dependent structural transitions of Alzheimers amyloid peptides by Fraser (1991)10.1021/bi00159a011
/ Biochemistry / Fibril formation by primate, rodent and Dutch-hemorrhagic analogues of Alzheimer amyloid β-protein by Fraser (1992)10.1006/jmbi.1994.1704
/ J. Mol. Biol. / Conformation and fibrillogenesis of Alzheimer Aβ peptides with selected substitution of charged residues by Fraser (1994)10.1016/0022-2836(68)90014-4
/ J. Mol. Biol. / “Cross β“ conformation in protein by Geddes (1968)10.1056/NEJM198006053022305
/ New England J. Med. / Amyloid deposits and amyloidosis. The beta-fibrilloses by Glenner (1980)10.1021/ja00017a068
/ J. Am. Chem. Soc. / Location of β-sheet-forming sequences in amyloid proteins by FTIR by Halverson (1991)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
/ Biophys. J. / Structure of β-crystallite assemblies by Alzheimer β amyloid protein analogues by Inouye (1993)10.1093/emboj/18.4.815
/ EMBO J. / Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing by Jimenez (1999)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.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/S0365110X58000517
/ Acta Crystallog. / Diffraction by helical structures by Klug (1958)10.1038/nsb1195-990
/ Nature 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)10.1126/science.2111584
/ Science / Mutation of the Alzheimers-disease gene in herediatary cerebral haemorrhage, Dutch type by Levy (1990)10.1016/S0006-3495(99)77442-4
/ Biophys. J. / An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments by Li (1999)10.1016/S0006-3495(98)77812-9
/ Biophys. J. / Structural analysis of Alzheimer’s β(1-40) amyloid by Malinchik (1998)10.1073/pnas.39.4.247
/ Proc. NAS Chem. / Two β-pleated sheet configurations of polypeptide chains involving both cis- and transamide groups by Pauling (1953)10.1016/0092-8674(83)90168-X
/ Cell / Scrapie prions aggregate to form amyloid-like birefringent rods by Prusiner (1983)10.1016/0896-6273(91)90052-2
/ Neuron / The molecular pathology of Alzheimer’s disease by Selkoe (1991)10.1083/jcb.33.3.679
/ J. Cell. Biol. / High resolution electron microscopic analysis of the amyloid fibril by Shirahama (1967)10.1006/jsbi.1998.4073
/ J. Struct. Biol. / XIMDISP by Smith (1999)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)10.1017/S0033583598003400
/ Quart. Rev. Biophys. / From the globular to the fibrous state by Sunde (1998)10.1006/jmbi.1997.1348
/ J. Mol. Biol. / Common core structure of amyloid fibrils by synchrotron X-ray diffraction by Sunde (1997)10.1074/jbc.271.15.8545
/ J. Biol. Chem. / Arrest of β-amyloid fibril formation by a pentapeptide ligand by Tjernberg (1996)10.1074/jbc.274.18.12619
/ J. Biol. Chem. / A molecular model of Alzheimer’s amyloid-β peptide fibril formation by Tjernberg (1999)10.1038/373037a0
/ Nature / Acetylcholine receptor channel imaged in the open state by Unwin (1995)10.1016/0006-291X(91)91706-I
/ Biochem. Biophys. Res. Commun. / Peptides homologous to the amyloid protein of Alzheimers disease containing glutamine for a glutamic acid substitution have accelerated amyloid fibril formation by Wisniewski (1991)10.1021/bi00139a028
/ Biochemistry / NMR studies of amyloid β-peptide by Zagorski (1992)10.1016/S1359-0278(98)00054-6
/ Folding Design / Residual structure in the Alzheimer’s disease peptide by Zhang (1998)
Dates
Type | When |
---|---|
Created | 22 years, 11 months ago (Sept. 18, 2002, 11:24 a.m.) |
Deposited | 6 years, 3 months ago (May 8, 2019, 6:25 p.m.) |
Indexed | 11 months, 2 weeks ago (Sept. 19, 2024, 10:49 a.m.) |
Issued | 25 years, 4 months ago (May 1, 2000) |
Published | 25 years, 4 months ago (May 1, 2000) |
Published Print | 25 years, 4 months ago (May 1, 2000) |
@article{Serpell_2000, title={Direct visualisation of the β-sheet structure of synthetic Alzheimer’s amyloid 1 1Edited by F. E. Cohen}, volume={299}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.2000.3650}, DOI={10.1006/jmbi.2000.3650}, number={1}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Serpell, Louise C and Smith, Judith M}, year={2000}, month=may, pages={225–231} }