Fibril formation by amyloid-beta proteins may involve beta-helical protofibrils (Q78007213)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10408337%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

title

Fibril formation by amyloid-beta proteins may involve beta-helical protofibrils (English)

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10 December 2019

1

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10 December 2019

author name string

D T Downing

series ordinal

2

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10 December 2019

publication date

1 June 1999

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Chemical Biology and Drug Design

10 December 2019

published in

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10 December 2019

volume

53

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10 December 2019

issue

6

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10 December 2019

page(s)

633-640

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Brain amyloid--a physicochemical perspective

10 December 2019

cites work

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Ultrastructural morphology of amyloid fibrils from neuritic and amyloid plaques

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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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High-resolution electron microscopic analysis of the amyloid fibril

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"Cross-beta" conformation in proteins.

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An investigation of the structure of silk fibroin

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An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.

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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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The nanometer-scale structure of amyloid-beta visualized by atomic force microscopy

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Observation of metastable Abeta amyloid protofibrils by atomic force microscopy

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Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein

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7 January 2021

Amyloid fibrils may be assembled from beta-helical protofibrils

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7 January 2021

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

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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

Circular dichroism of model peptides emulating the amphipathic alpha-helical regions of intermediate filaments

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7 January 2021

Calculation of protein conformation from circular dichroism

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7 January 2021

Molecular modeling indicates that homodimers form the basis for intermediate filament assembly from human and mouse epidermal keratins

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7 January 2021

Chemical cross-linking between lysine groups in vimentin oligomers is dependent on local peptide conformations

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7 January 2021

Molecular modeling of vimentin filament assembly

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7 January 2021

Beta-helical fibrils from a model peptide.

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7 January 2021

Stabilization of amphipathic alpha-helical and beta-helical conformations in synthetic peptides in the presence and absence of ionic interactions

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7 January 2021

Circular dichroism of the parallel beta helical proteins pectate lyase C and E

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7 January 2021

Amino-terminal Deletions Enhance Aggregation of β-Amyloid Peptides in Vitro

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7 January 2021

New domain motif: the structure of pectate lyase C, a secreted plant virulence factor

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7 January 2021

Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer

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7 January 2021

A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase

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7 January 2021

Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins

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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

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

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7 January 2021

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10408337%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

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