Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease

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Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease is …
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scholarly articleQ13442814
review articleQ7318358

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P6179Dimensions Publication ID1045749261
P356DOI10.1007/S00018-014-1634-Z
P3181OpenCitations bibliographic resource ID3064396
P932PMC publication ID4143600
P698PubMed publication ID24803005
P5875ResearchGate publication ID262108602

P50authorKris PauwelsQ41875108
P2093author name stringK Broersen
E Hubin
N A J van Nuland
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Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons.Q46733868
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A causative link between the structure of aberrant protein oligomers and their toxicity.Q39750915
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Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlatedQ42546560
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Transformation of amyloid β(1-40) oligomers into fibrils is characterized by a major change in secondary structureQ44808414
Simulations of monomeric amyloid β-peptide (1-40) with varying solution conditions and oxidation state of Met35: implications for aggregationQ44992656
Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacementQ45086533
Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death.Q45249955
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Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling.Q45941938
Methylene blue inhibits amyloid Abeta oligomerization by promoting fibrillization.Q45975923
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Alzheimer's disease and amyloid beta-peptide deposition in the brain: a matter of 'aging'?Q34021735
Interaction of intracellular beta amyloid peptide with chaperone proteinsQ34035607
Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation.Q34043216
Racemization: its biological significance on neuropathogenesis of Alzheimer's diseaseQ34058929
The recombinant amyloid-beta peptide Abeta1-42 aggregates faster and is more neurotoxic than synthetic Abeta1-42.Q34089265
Neuronutrition and Alzheimer's diseaseQ34099466
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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanismQ34346440
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The aluminium-amyloid cascade hypothesis and Alzheimer's diseaseQ34394038
Structural disorder throws new light on moonlightingQ34438504
Common core structure of amyloid fibrils by synchrotron X-ray diffraction.Q34444888
The role of apolipoprotein E in Alzheimer's diseaseQ34603092
Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 speciesQ34624507
Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degenerationQ34804911
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Converging concepts of protein folding in vitro and in vivoQ34984598
Advanced glycation end products contribute to amyloidosis in Alzheimer diseaseQ35285651
Misfolded proteins in Alzheimer's disease and type II diabetes.Q35535599
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Structural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer diseaseQ35774046
Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicityQ36098093
Two-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formationQ36238193
Molecular plasticity regulates oligomerization and cytotoxicity of the multipeptide-length amyloid-β peptide poolQ36347659
Side-chain dynamics reveals transient association of Aβ(1-40) monomers with amyloid fibers.Q36502645
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Hydrogen/deuterium exchange mass spectrometry--a window into amyloid structureQ36596594
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Paired beta-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopyQ36677152
Environmental novelty activates β2-adrenergic signaling to prevent the impairment of hippocampal LTP by Aβ oligomers.Q36682401
Characterization of beta-amyloid peptide from human cerebrospinal fluidQ36754599
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Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain TissueQ27679935
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Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchangeQ28394786
Aβ peptide fibrillar architectures controlled by conformational constraints of the monomerQ28744420
A specific amyloid-beta protein assembly in the brain impairs memoryQ28854597
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesisQ29547501
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3D structure of Alzheimer's amyloid-beta(1-42) fibrilsQ29617475
Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrilsQ29617476
Amyloid deposition as the central event in the aetiology of Alzheimer's diseaseQ29619450
The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetryQ30156940
Annular protofibrils are a structurally and functionally distinct type of amyloid oligomerQ30157440
Structural polymorphism of Alzheimer Abeta and other amyloid fibrilsQ30319061
Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Q30427825
Interprotofilament interactions between Alzheimer's Abeta1-42 peptides in amyloid fibrils revealed by cryoEMQ30438461
Structural classification of toxic amyloid oligomersQ30484255
Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaquesQ30486499
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).Q30666112
Hydrogen exchange-mass spectrometry analysis of beta-amyloid peptide structureQ30731017
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanismQ30873586
Highly conserved and disease-specific patterns of carboxyterminally truncated Abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation.Q31078434
Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's diseaseQ31939978
Solution state characterization of amyloid beta-derived diffusible ligandsQ33266914
Alzheimer's disease: clinical trials and drug developmentQ33349401
Metals, membranes, and amyloid-β oligomers: key pieces in the Alzheimer's disease puzzle?Q33353753
Inflammation, microglia, and Alzheimer's diseaseQ33664099
Rational design of a structural framework with potential use to develop chemical reagents that target and modulate multiple facets of Alzheimer's diseaseQ33894829
Nucleated conformational conversion and the replication of conformational information by a prion determinantQ33915141
Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.Q33946695
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue18
P407language of work or nameEnglishQ1860
P921main subjectAlzheimer's diseaseQ11081
peptideQ172847
membrane proteinQ423042
P304page(s)3507-3521
P577publication date2014-09-01
P1433published inCellular and Molecular Life SciencesQ5058352
P1476titleTransient dynamics of Aβ contribute to toxicity in Alzheimer's disease
P478volume71

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