Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation. (Q41436984)

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1 March 2020

title

Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation (English)

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1

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Paula Desplats

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1 March 2020

Valentina L Kouznetsova

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object named as

Valentina L Kouznetsova

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Eliezer Masliah

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1 March 2020

author name string

Yuriy Sharikov

2

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1 March 2020

Jerry P Greenberg

4

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Wolfgang Wrasidlo

5

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Tania Gonzalez

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1 March 2020

Sarah E Michael

8

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Margarita Trejo-Morales

9

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Cassia R Overk

10

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language of work or name

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1 January 2014

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Journal of Alzheimer's Disease

1 March 2020

published in

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volume

39

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issue

3

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1 March 2020

page(s)

583-600

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Creative Commons Attribution-NonCommercial 4.0 International

1 March 2020

copyright license

start time

7 February 2014

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Energy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).

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Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox).

1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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Constant pressure and temperature molecular dynamics simulation of a fully hydrated liquid crystal phase dipalmitoylphosphatidylcholine bilayer

1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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Role of water in mediating the assembly of Alzheimer amyloid-beta Abeta16-22 protofilaments

11 June 2018

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11 June 2018

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11 June 2018

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11 June 2018

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11 June 2018

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19 August 2018

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19 August 2018

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19 August 2018

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Effects of the Arctic (E22-->G) mutation on amyloid beta-protein folding: discrete molecular dynamics study

19 August 2018

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The Alzheimer's beta amyloid (Abeta1-39) monomer in an implicit solvent.

19 August 2018

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Amyloid-beta(29-42) dimer formations studied by a multicanonical-multioverlap molecular dynamics simulation.

19 August 2018

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19 August 2018

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19 August 2018

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A strand-loop-strand structure is a possible intermediate in fibril elongation: long time simulations of amyloid-beta peptide (10-35).

19 August 2018

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19 August 2018

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Discrete molecular dynamics simulations of peptide aggregation

19 August 2018

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Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers

19 August 2018

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Distinct Dimerization for Various Alloforms of the Amyloid-Beta Protein: Aβ1–40, Aβ1–42, and Aβ1–40(D23N)

4 November 2018

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Monte Carlo Study of the Formation and Conformational Properties of Dimers of Aβ42 Variants

2 December 2018

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In Silico Assembly of Alzheimer's Aβ16-22Peptide into β-Sheets

2 December 2018

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Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra

2 December 2018

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12 December 2020

In SilicoStudy of Full-Length Amyloid β 1−42 Tri- and Penta-Oligomers in Solution

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Comparative Molecular Dynamics Study of Aβ Adsorption on the Self-Assembled Monolayers

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Alzheimer Aβ1−42Monomer Adsorbed on the Self-Assembled Monolayers

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Amyloid beta-peptide oligomerization in silico: dimer and trimer

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ADDLs & protofibrils--the missing links?

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Dynamics and fluidity of amyloid fibrils: a model of fibrous protein aggregates

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Identifiers

DOI

10.3233/JAD-131589

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24240640%20AND%20SRC:MED&resulttype=core&format=json

1 March 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24240640%20AND%20SRC:MED&resulttype=core&format=json

1 March 2020

1 reference