Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix (Q57945110)

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19 October 2019

title

Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix (English)

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19 October 2019

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19 October 2019

C Blake

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19 October 2019

publication date

1 August 1996

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19 October 2019

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19 October 2019

volume

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19 October 2019

issue

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19 October 2019

page(s)

989-998

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19 October 2019

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https://api.crossref.org/works/10.1016%2FS0969-2126%2896%2900104-9

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X-ray diffraction studies on amyloid filaments

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Characterization of the Amyloid Fibril as a Cross- Protein

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X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation

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Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets

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"Cross-beta" conformation in proteins.

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https://api.crossref.org/works/10.1016%2FS0969-2126%2896%2900104-9

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Conformation of twisted β-pleated sheets in proteins

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https://api.crossref.org/works/10.1016%2FS0969-2126%2896%2900104-9

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High-resolution electron microscopic analysis of the amyloid fibril

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Morphology and antibody recognition of synthetic beta-amyloid peptides

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

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Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy

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Strjcture of human plasma prealbumin at 2-5 A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding

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Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A

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7 January 2021

Transthyretin amyloidosis

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Fibril in senile systemic amyloidosis is derived from normal transthyretin

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

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

1 reference

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Unusual structural features in the parallel beta-helix in pectate lyases

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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

1 reference

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A chemical approach to elucidate tin mechanism of transthyretin and β-protein amyloid fibril formation

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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7 January 2021

10.1016/S0969-2126(96)00104-9

Identifiers

DOI

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19 October 2019

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