(Q57945089)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10507046%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

title

X-ray fiber diffraction of amyloid fibrils (English)

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31 October 2019

1

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31 October 2019

Margaret Sunde

series ordinal

3

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31 October 2019

author name string

P E Fraser

series ordinal

2

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31 October 2019

language of work or name

English

0 references

publication date

1 January 1999

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31 October 2019

published in

Methods in Enzymology

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31 October 2019

volume

309

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31 October 2019

page(s)

526-536

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X-ray diffraction studies on amyloid filaments

31 October 2019

cites work

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"Cross-beta" conformation in proteins.

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Cross- protein structures. I. Insulin fibrils

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Amyloid formation by salmon calcitonin

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X-ray diffraction of scrapie prion rods and PrP peptides

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

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Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide

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Infrared spectroscopy of human amyloid fibrils and immunoglobulin proteins

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Structure of Met30 variant of transthyretin and its amyloidogenic implications.

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Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern

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pH-dependent structural transitions of Alzheimer amyloid peptides

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Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

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X-ray diffraction analysis of scrapie prion: intermediate and folded structures in a peptide containing two putative alpha-helices

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Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments.

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Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of beta-amyloid protein precursor.

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Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions

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Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein

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Conformation and fibrillogenesis of Alzheimer A beta peptides with selected substitution of charged residues.

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Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

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X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin

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7 January 2021

The characterization of soluble amyloid prepared in water

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Isolation and characterization of the integral glycosaminoglycan constituents of human amyloid A and monoclonal light-chain amyloid fibrils.

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7 January 2021

Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease

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7 January 2021

Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro

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7 January 2021

EQUATORIAL X-RAY DIFFRACTION BY FIBROUS PROTEINS: SHORT-RANGE ORDER IN COLLAGEN, FEATHER KERATIN AND F-ACTIN

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7 January 2021

Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron Micrographs

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7 January 2021

Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10507046%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

1 reference