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β‐Amyloid aggregation and heterogeneous nucleation

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inferredcites →https://doi.org/10.1001/archneur.57.1.100openalex-snapshot

Plasma and Cerebrospinal Fluid Levels of Amyloid β Proteins 1-40 and 1-42 in Alzheimer Disease

inferredcites →https://doi.org/10.1001/archneurol.2008.596openalex-snapshot

Cerebrospinal Fluid β-Amyloid 42 and Tau Proteins as Biomarkers of Alzheimer-Type Pathologic Changes in the Brain

inferredcites →https://doi.org/10.1002/ana.1009openalex-snapshot

Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy

inferredcites →https://doi.org/10.1002/ana.410370414openalex-snapshot

Cerebrospinal fluid levels of amyloid β‐protein in alzheimer's disease: Inverse correlation with severity of dementia and effect of apolipoprotein e genotype

inferredcites →https://doi.org/10.1002/anie.201007265openalex-snapshot

Solid‐State NMR Spectroscopic Investigation of Aβ Protofibrils: Implication of a β‐Sheet Remodeling upon Maturation into Terminal Amyloid Fibrils

inferredcites →https://doi.org/10.1002/anie.201200965openalex-snapshot

An Asymmetric Dimer as the Basic Subunit in Alzheimer’s Disease Amyloid β Fibrils

inferredcites →https://doi.org/10.1002/anie.201501981openalex-snapshot

A Self‐Assembled Spherical Complex Displaying a Gangliosidic Glycan Cluster Capable of Interacting with Amyloidogenic Proteins

inferredcites →https://doi.org/10.1002/anie.201603178openalex-snapshot

GM1 Ganglioside Inhibits β‐Amyloid Oligomerization Induced by Sphingomyelin

inferredcites →https://doi.org/10.1002/cbic.200500057openalex-snapshot

Characterization of the ZnII Binding to the Peptide Amyloid‐β1–16 linked to Alzheimer's Disease

inferredcites →https://doi.org/10.1002/cbic.200600319openalex-snapshot

Amyloid‐Beta Peptide Forms Monomeric Complexes With CuII and ZnII Prior to Aggregation

inferredcites →https://doi.org/10.1002/cbic.200700784openalex-snapshot

Isomerization of the Asp7 Residue Results in Zinc‐Induced Oligomerization of Alzheimer’s Disease Amyloid β(1–16) Peptide

inferredcites →https://doi.org/10.1002/jcb.20978openalex-snapshot

Amyloid β oligomerization is induced by brain lipid rafts

inferredcites →https://doi.org/10.1002/pro.2544openalex-snapshot

Physical and structural basis for polymorphism in amyloid fibrils

inferredcites →https://doi.org/10.1002/pro.3396openalex-snapshot

Inhibition of amyloid beta fibril formation by monomeric human transthyretin

inferredcites →https://doi.org/10.1002/pro.3674openalex-snapshot

β‐Amyloid aggregation and heterogeneous nucleation

inferredcites →https://doi.org/10.1002/psc.626openalex-snapshot

Methionine regulates copper/hydrogen peroxide oxidation products of Aβ

inferredcites →https://doi.org/10.1002/rcm.2787openalex-snapshot

Quantitative analysis of amyloid β peptides in cerebrospinal fluid of Alzheimer's disease patients by immunoaffinity purification and stable isotope dilution liquid chromatography/negative electrospray ionization tandem mass spectrometry

inferredcites →https://doi.org/10.1006/exnr.2001.7814openalex-snapshot

Cerebrospinal Fluid Amyloid β1–42 Levels in the Mild Cognitive Impairment Stage of Alzheimer's Disease

inferredcites →https://doi.org/10.1006/jmbi.1998.2076openalex-snapshot

The 1.25 Å resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site

inferredcites →https://doi.org/10.1006/jmbi.1998.2299openalex-snapshot

Watching amyloid fibrils grow by time-lapse atomic force microscopy 1 1Edited by W. Baumeister

inferredcites →https://doi.org/10.1006/jmbi.1998.2348openalex-snapshot

Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer’s disease 1 1Edited by P. E. Wright

inferredcites →https://doi.org/10.1006/jmbi.2001.4881openalex-snapshot

Cholesterol, a modulator of membrane-associated aβ-fibrillogenesis and neurotoxicity

inferredcites →https://doi.org/10.1007/978-3-319-57193-5_15openalex-snapshot

Traumatic Brain Injury as a Trigger of Neurodegeneration

inferredcites →https://doi.org/10.1007/s00775-004-0602-8openalex-snapshot

Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer?s A? peptides

inferredcites →https://doi.org/10.1007/s10719-008-9216-7openalex-snapshot

Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters

inferredcites →https://doi.org/10.1007/s10719-015-9579-5openalex-snapshot

GM1 ganglioside and Alzheimer’s disease

inferredcites →https://doi.org/10.1007/s10719-015-9587-5openalex-snapshot

Structural and dynamic views of GM1 ganglioside

inferredcites →https://doi.org/10.1016/0300-9084(94)90163-5openalex-snapshot

Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans

inferredcites →https://doi.org/10.1016/j.bbalip.2010.01.008openalex-snapshot

Aβ polymerization through interaction with membrane gangliosides

inferredcites →https://doi.org/10.1016/j.bbamem.2007.02.002openalex-snapshot

The redox chemistry of the Alzheimer's disease amyloid β peptide

inferredcites →https://doi.org/10.1016/j.bbamem.2017.05.012openalex-snapshot

Lipid membranes catalyse the fibril formation of the amyloid-β (1–42) peptide through lipid-fibril interactions that reinforce secondary pathways

inferredcites →https://doi.org/10.1016/j.bbamem.2018.04.012openalex-snapshot

Impact of membrane curvature on amyloid aggregation

inferredcites →https://doi.org/10.1016/j.bbapap.2008.10.016openalex-snapshot

Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature

inferredcites →https://doi.org/10.1016/j.bbrc.2012.02.129openalex-snapshot

Peptide–surfactant interactions: Consequences for the amyloid-beta structure

inferredcites →https://doi.org/10.1016/j.bbrc.2016.07.123openalex-snapshot

Amyloid-beta and tau pathology following repetitive mild traumatic brain injury

inferredcites →https://doi.org/10.1016/j.bpc.2009.05.008openalex-snapshot

Interaction of β-amyloid(1-40) peptide with pairs of metal ions: An electrospray ion trap mass spectrometric model study

inferredcites →https://doi.org/10.1016/j.bpj.2011.06.062openalex-snapshot

Effect of Zinc Binding on β-Amyloid Structure and Dynamics: Implications for Aβ Aggregation

inferredcites →https://doi.org/10.1016/j.bpj.2014.05.001openalex-snapshot

Amyloids of Alpha-Synuclein Affect the Structure and Dynamics of Supported Lipid Bilayers

inferredcites →https://doi.org/10.1016/j.bpj.2014.09.047openalex-snapshot

Fiber-Dependent and -Independent Toxicity of Islet Amyloid Polypeptide

inferredcites →https://doi.org/10.1016/j.colsurfb.2016.06.003openalex-snapshot

The rheological properties of beta amyloid Langmuir monolayers: Comparative studies with melittin peptide

inferredcites →https://doi.org/10.1016/j.febslet.2009.12.010openalex-snapshot

Sphingolipids and gangliosides of the nervous system in membrane function and dysfunction

inferredcites →https://doi.org/10.1016/j.febslet.2010.01.005openalex-snapshot

NMR characterization of the interactions between lyso‐GM1 aqueous micelles and amyloid β

inferredcites →https://doi.org/10.1016/j.jbiosc.2017.10.018openalex-snapshot

Effect of saturation in phospholipid/fatty acid monolayers on interaction with amyloid β peptide

inferredcites →https://doi.org/10.1016/j.jcis.2014.03.042openalex-snapshot

Adsorption of β-amyloid oligomers on octadecanethiol monolayers

inferredcites →https://doi.org/10.1016/j.jinorgbio.2007.06.001openalex-snapshot

An aluminum-based rat model for Alzheimer’s disease exhibits oxidative damage, inhibition of PP2A activity, hyperphosphorylated tau, and granulovacuolar degeneration

inferredcites →https://doi.org/10.1016/j.jinorgbio.2009.07.023openalex-snapshot

Demonstration of aluminum in amyloid fibers in the cores of senile plaques in the brains of patients with Alzheimer’s disease

inferredcites →https://doi.org/10.1016/j.jmb.2003.11.046openalex-snapshot

Two Types of Alzheimer's β-Amyloid (1–40) Peptide Membrane Interactions: Aggregation Preventing Transmembrane Anchoring Versus Accelerated Surface Fibril Formation

inferredcites →https://doi.org/10.1016/j.jmb.2004.04.051openalex-snapshot

Rapid Self-assembly of α-Synuclein Observed by In Situ Atomic Force Microscopy

inferredcites →https://doi.org/10.1016/j.jmb.2011.11.006openalex-snapshot

Cholesterol Promotes the Interaction of Alzheimer β-Amyloid Monomer with Lipid Bilayer

inferredcites →https://doi.org/10.1016/j.jsb.2005.09.004openalex-snapshot

Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer’s disease

inferredcites →https://doi.org/10.1016/j.neurobiolaging.2014.12.004openalex-snapshot

Sustained high levels of neuroprotective, high molecular weight, phosphorylated tau in the longest-lived rodent

inferredcites →https://doi.org/10.1016/j.neuron.2015.03.017openalex-snapshot

Amyloid Polymorphism: Structural Basis and Neurobiological Relevance

inferredcites →https://doi.org/10.1016/j.neuroscience.2007.09.025openalex-snapshot

Amyloid plaques arise from zinc-enriched cortical layers in APP/PS1 transgenic mice and are paradoxically enlarged with dietary zinc deficiency

inferredcites →https://doi.org/10.1016/s0006-3495(02)75596-3openalex-snapshot

The Size of Lipid Rafts: An Atomic Force Microscopy Study of Ganglioside GM1 Domains in Sphingomyelin/DOPC/Cholesterol Membranes

inferredcites →https://doi.org/10.1016/s0006-3495(98)77788-4openalex-snapshot

Conformation of the Oligosaccharide Chain of GM1 Ganglioside in a Carbohydrate-Enriched Surface

inferredcites →https://doi.org/10.1016/s0021-9258(17)32694-7openalex-snapshot

Modulation of A beta adhesiveness and secretase site cleavage by zinc.

inferredcites →https://doi.org/10.1016/s0021-9258(19)61939-3openalex-snapshot

Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation.

inferredcites →https://doi.org/10.1016/s0021-9258(19)69159-3openalex-snapshot

The kinetics of the phospholipase A2-catalyzed hydrolysis of Egg phosphatidylcholine in unilamellar vesicles. Product inhibition and its relief by serum albumin.

inferredcites →https://doi.org/10.1016/s0021-9258(20)64322-8openalex-snapshot

Monolayers of long chain lecithins at the air/water interface and their hydrolysis by phospholipase A2

inferredcites →https://doi.org/10.1016/s0022-510x(98)00092-6openalex-snapshot

Copper, iron and zinc in Alzheimer's disease senile plaques

inferredcites →https://doi.org/10.1016/s0076-6879(99)09022-9openalex-snapshot

[20] Kinetic analysis of amyloid fibril formation

inferredcites →https://doi.org/10.1016/s0092-8674(03)00882-1openalex-snapshot

Lipid Rafts

inferredcites →https://doi.org/10.1016/s0166-2236(03)00067-5openalex-snapshot

The metallobiology of Alzheimer's disease

inferredcites →https://doi.org/10.1016/s0896-6273(01)00317-8openalex-snapshot

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

inferredcites →https://doi.org/10.1021/acs.analchem.7b04936openalex-snapshot

Direct Evidence of the Presence of Cross-Linked Aβ Dimers in the Brains of Alzheimer’s Disease Patients

inferredcites →https://doi.org/10.1021/acs.chemrev.8b00322openalex-snapshot

Membrane Lipid Nanodomains

inferredcites →https://doi.org/10.1021/acs.langmuir.7b02091openalex-snapshot

Size and Shape of Amyloid Fibrils Induced by Ganglioside Nanoclusters: Role of Sialyl Oligosaccharide in Fibril Formation

inferredcites →https://doi.org/10.1021/acschemneuro.6b00109openalex-snapshot

Impact of Cu(II) Binding on Structures and Dynamics of Aβ42 Monomer and Dimer: Molecular Dynamics Study

inferredcites →https://doi.org/10.1021/acschemneuro.7b00121openalex-snapshot

Kinetic Analysis Reveals the Identity of Aβ-Metal Complex Responsible for the Initial Aggregation of Aβ in the Synapse

inferredcites →https://doi.org/10.1021/acschemneuro.8b00141openalex-snapshot

Stabilization and Characterization of Cytotoxic Aβ 40 Oligomers Isolated from an Aggregation Reaction in the Presence of Zinc Ions

inferredcites →https://doi.org/10.1021/ar050069hopenalex-snapshot

Kinetics and Thermodynamics of Amyloid Fibril Assembly

inferredcites →https://doi.org/10.1021/ar400293hopenalex-snapshot

Metal Ions and Intrinsically Disordered Proteins and Peptides: From Cu/Zn Amyloid-β to General Principles

inferredcites →https://doi.org/10.1021/ar500127zopenalex-snapshot

How Do Membranes Initiate Alzheimer’s Disease? Formation of Toxic Amyloid Fibrils by the Amyloid β-Protein on Ganglioside Clusters

inferredcites →https://doi.org/10.1021/bi015693qopenalex-snapshot

Aggregation of β 2 -Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

inferredcites →https://doi.org/10.1021/bi0255874openalex-snapshot

Interactions of Amyloid β-Protein with Various Gangliosides in Raft-Like Membranes: Importance of GM1 Ganglioside-Bound Form as an Endogenous Seed for Alzheimer Amyloid

inferredcites →https://doi.org/10.1021/bi0272151openalex-snapshot

Metal Binding and Oxidation of Amyloid-β within Isolated Senile Plaque Cores: Raman Microscopic Evidence

inferredcites →https://doi.org/10.1021/bi048846topenalex-snapshot

Rapid Assembly of Amyloid-β Peptide at a Liquid/Liquid Interface Produces Unstable β-Sheet Fibers

inferredcites →https://doi.org/10.1021/bi060323topenalex-snapshot

Secondary Structure and Interfacial Aggregation of Amyloid-β(1−40) on Sodium Dodecyl Sulfate Micelles

inferredcites →https://doi.org/10.1021/bi200771mopenalex-snapshot

Mechanism of Amyloid β-Protein Aggregation Mediated by GM1 Ganglioside Clusters

inferredcites →https://doi.org/10.1021/bi5008172openalex-snapshot

The Binding of Apolipoprotein E to Oligomers and Fibrils of Amyloid-β Alters the Kinetics of Amyloid Aggregation

inferredcites →https://doi.org/10.1021/bi7000032openalex-snapshot

Metal Ions Differentially Influence the Aggregation and Deposition of Alzheimer's β-Amyloid on a Solid Template

inferredcites →https://doi.org/10.1021/bi701112zopenalex-snapshot

Investigations of the Molecular Mechanism of Metal-Induced Aβ (1−40) Amyloidogenesis

inferredcites →https://doi.org/10.1021/bi800012eopenalex-snapshot

Influence of Multiple Metal Ions on β-Amyloid Aggregation and Dissociation on a Solid Surface

inferredcites →https://doi.org/10.1021/bi800993copenalex-snapshot

Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?

inferredcites →https://doi.org/10.1021/bi9012935openalex-snapshot

The Second Cu(II)-Binding Site in a Proton-Rich Environment Interferes with the Aggregation of Amyloid-β(1−40) into Amyloid Fibrils

inferredcites →https://doi.org/10.1021/bi972979fopenalex-snapshot

Solution Structure of Amyloid β-Peptide(1−40) in a Water−Micelle Environment. Is the Membrane-Spanning Domain Where We Think It Is?,

inferredcites →https://doi.org/10.1021/bi982345oopenalex-snapshot

Interactions of Amyloid β-Peptide (1−40) with Ganglioside-Containing Membranes

inferredcites →https://doi.org/10.1021/bi990205oopenalex-snapshot

Histidine-13 Is a Crucial Residue in the Zinc Ion-Induced Aggregation of the Aβ Peptide of Alzheimer's Disease

inferredcites →https://doi.org/10.1021/bi990438fopenalex-snapshot

The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction

inferredcites →https://doi.org/10.1021/ic201233bopenalex-snapshot

Iron(II) Binding to Amyloid-β, the Alzheimer’s Peptide

inferredcites →https://doi.org/10.1021/ic4003059openalex-snapshot

Role of Metal Ions in the Self-assembly of the Alzheimer’s Amyloid-β Peptide

inferredcites →https://doi.org/10.1021/ja046032uopenalex-snapshot

NMR Reveals Anomalous Copper(II) Binding to the Amyloid Aβ Peptide of Alzheimer's Disease

inferredcites →https://doi.org/10.1021/ja054041copenalex-snapshot

Formation and Stabilization Model of the 42-mer Aβ Radical: Implications for the Long-Lasting Oxidative Stress in Alzheimer's Disease

inferredcites →https://doi.org/10.1021/ja305398fopenalex-snapshot

A Mobile Precursor Determines Amyloid-β Peptide Fibril Formation at Interfaces

inferredcites →https://doi.org/10.1021/ja3054095openalex-snapshot

Single Plasmonic Nanoparticle Tracking Studies of Solid Supported Bilayers with Ganglioside Lipids

inferredcites →https://doi.org/10.1021/ja3112093openalex-snapshot

The Backbone Dynamics of the Amyloid Precursor Protein Transmembrane Helix Provides a Rationale for the Sequential Cleavage Mechanism of γ-Secretase

inferredcites →https://doi.org/10.1021/ja311963fopenalex-snapshot

Polymorph-Specific Kinetics and Thermodynamics of β-Amyloid Fibril Growth

inferredcites →https://doi.org/10.1021/ja907518xopenalex-snapshot

Presentation of Membrane-Anchored Glycosphingolipids Determined from Molecular Dynamics Simulations and NMR Paramagnetic Relaxation Rate Enhancement

inferredcites →https://doi.org/10.1021/jp050716mopenalex-snapshot

Evidence of the Existence of Micelles in the Fibrillogenesis of β-Amyloid Peptide

inferredcites →https://doi.org/10.1021/jp103272vopenalex-snapshot

Quantification of the Binding Properties of Cu2+ to the Amyloid Beta Peptide: Coordination Spheres for Human and Rat Peptides and Implication on Cu2+-Induced Aggregation

inferredcites →https://doi.org/10.1021/jp207881kopenalex-snapshot

Formation of GM1 Ganglioside Clusters on the Lipid Membrane Containing Sphingomyeline and Cholesterol

inferredcites →https://doi.org/10.1021/jp4029062openalex-snapshot

Binding and Aggregation Mechanism of Amyloid β-Peptides onto the GM1 Ganglioside-Containing Lipid Membrane

inferredcites →https://doi.org/10.1023/a:1021361607611openalex-snapshot

Study of β-Amyloid Peptide (Aβ40) Insertion into Phospholipid Membranes Using Monolayer Technique

inferredcites →https://doi.org/10.1038/359325a0openalex-snapshot

Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids

inferredcites →https://doi.org/10.1038/nn0901-887openalex-snapshot

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

inferredcites →https://doi.org/10.1038/nrn3012openalex-snapshot

Linking lipids to Alzheimer's disease: cholesterol and beyond

inferredcites →https://doi.org/10.1038/s41557-018-0031-xopenalex-snapshot

Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes

inferredcites →https://doi.org/10.1038/s41598-018-19961-3openalex-snapshot

Critical aggregation concentration for the formation of early Amyloid-β (1–42) oligomers

inferredcites →https://doi.org/10.1038/s41598-018-23122-xopenalex-snapshot

Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer’s disease

inferredcites →https://doi.org/10.1038/s41598-019-43117-6openalex-snapshot

Conformational Change of Amyloid-β 40 in Association with Binding to GM1-Glycan Cluster

inferredcites →https://doi.org/10.1038/srep21734openalex-snapshot

Interplay of histidine residues of the Alzheimer’s disease Aβ peptide governs its Zn-induced oligomerization

inferredcites →https://doi.org/10.1039/c0mb00334dopenalex-snapshot

Zinc-induced dimerization of the amyloid-β metal-binding domain 1–16 is mediated by residues 11–14

inferredcites →https://doi.org/10.1039/c0mt00073fopenalex-snapshot

Interactions of Zn(ii) and Cu(ii) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity

inferredcites →https://doi.org/10.1039/c4mb00332bopenalex-snapshot

Phosphorylation of Ser8 promotes zinc-induced dimerization of the amyloid-β metal-binding domain

inferredcites →https://doi.org/10.1039/c5cp02366aopenalex-snapshot

Raman spectroscopy for detecting supported planar lipid bilayers composed of ganglioside-GM1/sphingomyelin/cholesterol in the presence of amyloid-β

inferredcites →https://doi.org/10.1039/c8cc02204fopenalex-snapshot

Secondary nucleation in amyloid formation

inferredcites →https://doi.org/10.1039/c8cp02685hopenalex-snapshot

Dynamic micellar oligomers of amyloid beta peptides play a crucial role in their aggregation mechanisms

inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03815.xopenalex-snapshot

β‐Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH

inferredcites →https://doi.org/10.1046/j.1471-4159.1998.70020736.xopenalex-snapshot

Heparin Oligosaccharides that Pass the Blood‐Brain Barrier Inhibit β‐Amyloid Precursor Protein Secretion and Heparin Binding to β‐Amyloid Peptide

inferredcites →https://doi.org/10.1046/j.1471-4159.2000.0751219.xopenalex-snapshot

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides

inferredcites →https://doi.org/10.1063/1.3682986openalex-snapshot

Kinetic pathways to peptide aggregation on surfaces: The effects of β-sheet propensity and surface attraction

inferredcites →https://doi.org/10.1073/pnas.012584899openalex-snapshot

Structure determination of micelle-like intermediates in amyloid β-protein fibril assembly by using small angle neutron scattering

inferredcites →https://doi.org/10.1073/pnas.0710301105openalex-snapshot

Structural basis of GM1 ganglioside recognition by simian virus 40

inferredcites →https://doi.org/10.1073/pnas.0711664105openalex-snapshot

Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly

inferredcites →https://doi.org/10.1073/pnas.0806270105openalex-snapshot

Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils

inferredcites →https://doi.org/10.1073/pnas.1102356108openalex-snapshot

Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity

inferredcites →https://doi.org/10.1073/pnas.1421961112openalex-snapshot

Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation

inferredcites →https://doi.org/10.1073/pnas.1605104113openalex-snapshot

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

inferredcites →https://doi.org/10.1073/pnas.78.5.2732openalex-snapshot

Binding of amphiphilic peptides to phospholipid/cholesterol unilamellar vesicles: a model for protein--cholesterol interaction.

inferredcites →https://doi.org/10.1073/pnas.90.17.8098openalex-snapshot

Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer disease.

inferredcites →https://doi.org/10.1073/pnas.93.3.1125openalex-snapshot

On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants.

inferredcites →https://doi.org/10.1073/pnas.95.23.13407openalex-snapshot

Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register

inferredcites →https://doi.org/10.1074/jbc.271.3.1613openalex-snapshot

Regulation of Amyloid Protein Precursor (APP) Binding to Collagen and Mapping of the Binding Sites on APP and Collagen Type I

inferredcites →https://doi.org/10.1074/jbc.273.21.12817openalex-snapshot

Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

inferredcites →https://doi.org/10.1074/jbc.273.40.25527openalex-snapshot

Enzyme Catalytic Power Minireview Series

inferredcites →https://doi.org/10.1074/jbc.c000165200openalex-snapshot

Evidence that the β-Amyloid Plaques of Alzheimer's Disease Represent the Redox-silencing and Entombment of Aβ by Zinc

inferredcites →https://doi.org/10.1074/jbc.c200338200openalex-snapshot

Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Aβ-(1–42) Peptide of Alzheimer's Disease

inferredcites →https://doi.org/10.1074/jbc.m100175200openalex-snapshot

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

inferredcites →https://doi.org/10.1074/jbc.m100252200openalex-snapshot

Cholesterol-dependent Formation of GM1 Ganglioside-bound Amyloid β-Protein, an Endogenous Seed for Alzheimer Amyloid

inferredcites →https://doi.org/10.1074/jbc.m102879200openalex-snapshot

Secreted Forms of the Amyloid-β Precursor Protein Are Ligands for the Class A Scavenger Receptor

inferredcites →https://doi.org/10.1074/jbc.m112.344036openalex-snapshot

Zn2+-Aβ40 Complexes Form Metastable Quasi-spherical Oligomers That Are Cytotoxic to Cultured Hippocampal Neurons

inferredcites →https://doi.org/10.1074/jbc.m116.764092openalex-snapshot

Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β

inferredcites →https://doi.org/10.1074/jbc.m117.795617openalex-snapshot

Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T

inferredcites →https://doi.org/10.1074/jbc.m206428200openalex-snapshot

Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid

inferredcites →https://doi.org/10.1074/jbc.m313572200openalex-snapshot

Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease

inferredcites →https://doi.org/10.1074/jbc.m410553200openalex-snapshot

Amyloid-β Protofibrils Differ from Amyloid-β Aggregates Induced in Dilute Hexafluoroisopropanol in Stability and Morphology

inferredcites →https://doi.org/10.1074/jbc.m413340200openalex-snapshot

CLAC Binds to Amyloid β Peptides through the Positively Charged Amino Acid Cluster within the Collagenous Domain 1 and Inhibits Formation of Amyloid Fibrils

inferredcites →https://doi.org/10.1074/jbc.m504454200openalex-snapshot

Structural Changes of Region 1-16 of the Alzheimer Disease Amyloid β-Peptide upon Zinc Binding and in Vitro Aging

inferredcites →https://doi.org/10.1074/jbc.m504484200openalex-snapshot

Lipids as Modulators of Proteolytic Activity of BACE

inferredcites →https://doi.org/10.1074/jbc.m702146200openalex-snapshot

Site-specific Effects of Peptide Lipidation on β-Amyloid Aggregation and Cytotoxicity

inferredcites →https://doi.org/10.1074/jbc.m802912200openalex-snapshot

Independent Generation of Aβ42 and Aβ38 Peptide Species by γ-Secretase

inferredcites →https://doi.org/10.1074/jbc.ra118.002787openalex-snapshot

Amyloid-β fibrils assembled on ganglioside-enriched membranes contain both parallel β-sheets and turns

inferredcites →https://doi.org/10.1089/neu.2017.5558openalex-snapshot

A Systematic Review of Positron Emission Tomography of Tau, Amyloid Beta, and Neuroinflammation in Chronic Traumatic Encephalopathy: The Evidence To Date

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Gangliosides as components of lipid membrane domains

inferredcites →https://doi.org/10.1097/jom.0000000000000063openalex-snapshot

Is the Aluminum Hypothesis Dead?

inferredcites →https://doi.org/10.1101/cshperspect.a024083openalex-snapshot

Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance

inferredcites →https://doi.org/10.1110/ps.052048706openalex-snapshot

Structure and topology of the non‐amyloid‐β component fragment of human α‐synuclein bound to micelles: Implications for the aggregation process

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pH‐Dependent Binding of Synthetic β‐Amyloid Peptides to Glycosaminoglycans

inferredcites →https://doi.org/10.1111/j.1471-4159.2004.02459.xopenalex-snapshot

Environment‐ and mutation‐dependent aggregation behavior of Alzheimer amyloid β‐protein

inferredcites →https://doi.org/10.1111/j.1471-4159.2004.02849.xopenalex-snapshot

Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent‐resistant membrane domains

inferredcites →https://doi.org/10.1111/j.1471-4159.2009.06269.xopenalex-snapshot

Zn(II)‐ and Cu(II)‐induced non‐fibrillar aggregates of amyloid‐β (1–42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators

inferredcites →https://doi.org/10.1111/j.1471-4159.2010.06997.xopenalex-snapshot

Ganglioside‐mediated aggregation of amyloid β‐proteins (Aβ): comparison between Aβ‐(1–42) and Aβ‐(1–40)

inferredcites →https://doi.org/10.1111/j.1742-4658.2006.05563.xopenalex-snapshot

High‐resolution NMR studies of the zinc‐binding site of the Alzheimer's amyloid β‐peptide

inferredcites →https://doi.org/10.1111/j.1742-4658.2011.08228.xopenalex-snapshot

Membrane and surface interactions of Alzheimer’s Aβ peptide – insights into the mechanism of cytotoxicity

inferredcites →https://doi.org/10.1111/j.1750-3639.1996.tb00799.xopenalex-snapshot

Brain Parenchymal and Microvascular Amyloid in Alzheimer's Disease

inferredcites →https://doi.org/10.1111/joim.12732openalex-snapshot

Amyloid fibril polymorphism: a challenge for molecular imaging and therapy

inferredcites →https://doi.org/10.1126/sciadv.1601576openalex-snapshot

Interplay between protein glycosylation pathways in Alzheimer’s disease

inferredcites →https://doi.org/10.1126/science.1105850openalex-snapshot

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

inferredcites →https://doi.org/10.1126/science.1219988openalex-snapshot

The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol

inferredcites →https://doi.org/10.1126/science.2111584openalex-snapshot

Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type

inferredcites →https://doi.org/10.1126/science.8073293openalex-snapshot

Rapid induction of Alzheimer A beta amyloid formation by zinc

inferredcites →https://doi.org/10.1126/science.aao2825openalex-snapshot

Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

inferredcites →https://doi.org/10.1146/annurev.bi.34.070165.000405openalex-snapshot

Mechanism of Action of Proteolytic Enzymes

inferredcites →https://doi.org/10.1146/annurev.bioeng.4.092801.094202openalex-snapshot

Peptide Aggregation in Neurodegenerative Disease

inferredcites →https://doi.org/10.1146/annurev.biophys.32.110601.141803openalex-snapshot

Model Systems, Lipid Rafts, and Cell Membranes

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Alzheimer's Disease: Genes, Proteins, and Therapy

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Intracellular Distribution of a Biotin-labeled Ganglioside, GM1, by Immunoelectron Microscopy After Endocytosis in Fibroblasts

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Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae.

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Apolipoprotein E and Alzheimer's disease: the influence of apolipoprotein E on amyloid-β and other amyloidogenic proteins

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Lipid rafts: bringing order to chaos

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Redox‐Active Metals, Oxidative Stress, and Alzheimer's Disease Pathology

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Early onset familial Alzheimer’s disease

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Interaction of amyloid precursor protein with contactins and NgCAM in the retinotectal system

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Membrane Lipid Co-Aggregation with α-Synuclein Fibrils

inferredcites →https://doi.org/10.1371/journal.pone.0081926openalex-snapshot

Analysis of the Overall Structure of the Multi-Domain Amyloid Precursor Protein (APP)

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Aluminium exposure induces Alzheimer's disease-like histopathological alterations in mouse brain.

inferredcites →https://doi.org/10.1523/jneurosci.0297-04.2004openalex-snapshot

Neuronal Zinc Exchange with the Blood Vessel Wall Promotes Cerebral Amyloid Angiopathy in an Animal Model of Alzheimer's Disease

inferredcites →https://doi.org/10.1523/jneurosci.0861-04.2004openalex-snapshot

A Seed for Alzheimer Amyloid in the Brain

inferredcites →https://doi.org/10.1523/jneurosci.14-04-02117.1994openalex-snapshot

A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth

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Dynamics and Cleavability at the α-Cleavage Site of APP(684-726) in Different Lipid Environments

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Brain Burdens of Aluminum, Iron, and Copper and their Relationships with Amyloid-β Pathology in 60 Human Brains

inferredcites →https://doi.org/10.3389/fnagi.2018.00226openalex-snapshot

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β-Amyloid Fibrils Activate the C1 Complex of Complement Under Physiological Conditions: Evidence for a Binding Site for Aβ on the C1q Globular Regions

inferredcites →https://doi.org/10.4061/2011/925073openalex-snapshot

Spectroscopic Characterization of Intermolecular Interaction of Amyloid β Promoted on GM1 Micelles

inferredcites →https://doi.org/10.5402/2012/506160openalex-snapshot

Ganglioside Biochemistry

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Parallel in-register contact propensity predicts the Amyloidogenicity of ADan and ABri in familial dementias

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