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A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.
scientific article published on 16 March 2012
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PMCID
3382451
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22860216%20AND%20SRC:MED&resulttype=core&format=json
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9 February 2020
title
A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity
(English)
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PMCID
3382451
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22860216%20AND%20SRC:MED&resulttype=core&format=json
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9 February 2020
main subject
protein folding
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author
Sharmistha Sinha
series ordinal
1
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Europe PubMed Central
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3382451
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9 February 2020
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Dahabada H J Lopes
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2
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Europe PubMed Central
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3382451
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9 February 2020
Gal Bitan
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3382451
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9 February 2020
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16 March 2012
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9 February 2020
published in
ACS Chemical Neuroscience
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3382451
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9 February 2020
volume
3
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9 February 2020
issue
6
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3382451
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9 February 2020
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473-481
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9 February 2020
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Comparison of three amyloid assembly inhibitors: the sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01
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Lysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid Proteins
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Amyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differences
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Structures and free-energy landscapes of the wild type and mutants of the Abeta(21-30) peptide are determined by an interplay between intrapeptide electrostatic and hydrophobic interactions
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Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus
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Role of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: a discrete molecular dynamics study
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Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13.
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Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
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6 June 2018
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6 June 2018
Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
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6 June 2018
A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR
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6 June 2018
Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
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6 June 2018
Amyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
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6 June 2018
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6 June 2018
Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
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6 June 2018
The Alzheimer's peptide a beta adopts a collapsed coil structure in water
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6 June 2018
Analyzing protein circular dichroism spectra for accurate secondary structures.
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6 June 2018
Inhibition of the electrostatic interaction between beta-amyloid peptide and membranes prevents beta-amyloid-induced toxicity
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6 June 2018
Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence
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6 June 2018
A self-consistent method for the analysis of protein secondary structure from circular dichroism.
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6 June 2018
Reversible random coil-beta-sheet transition of the Alzheimer beta-amyloid fragment (25-35).
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6 June 2018
Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type.
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6 June 2018
The conformations of the amyloid-beta (21-30) fragment can be described by three families in solution
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18 August 2018
Structure of the 21-30 fragment of amyloid beta-protein.
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18 August 2018
Structure and orientation of peptide inhibitors bound to beta-amyloid fibrils.
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18 August 2018
Conformational dynamics of amyloid beta-protein assembly probed using intrinsic fluorescence.
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18 August 2018
Neurotoxic protein oligomers--what you see is not always what you get.
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18 August 2018
Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
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18 August 2018
Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation.
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18 August 2018
Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization.
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18 August 2018
Interaction of amyloid beta-protein with anionic phospholipids: possible involvement of Lys28 and C-terminus aliphatic amino acids.
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18 August 2018
Abeta40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid
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3 November 2018
Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis
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12 December 2020
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Residual structure in the Alzheimer's disease peptide: probing the origin of a central hydrophobic cluster
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12 December 2020
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Surface structure of amyloid-beta fibrils contributes to cytotoxicity
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12 December 2020
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Identifiers
DOI
10.1021/CN3000247
1 reference
stated in
Europe PubMed Central
PMCID
3382451
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22860216%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 February 2020
PMCID
3382451
1 reference
stated in
Europe PubMed Central
PMCID
3382451
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22860216%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 February 2020
PubMed ID
22860216
1 reference
stated in
Europe PubMed Central
PMCID
3382451
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22860216%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 February 2020
ResearchGate publication ID
230617095
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