Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer’s disease progression

Imaging individual protein aggregates to follow aggregation and determine the role of aggregates in neurodegenerative disease

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Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

(2019) Suman De et al.   Nature Communications

CSF biomarkers of Alzheimer's disease concord with amyloid-β PET and predict clinical progression: A study of fully automated immunoassays in BioFINDER and ADNI cohorts

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NIA-AA Research Framework: Toward a biological definition of Alzheimer's disease

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Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils

(2018) Francesco Simone Ruggeri et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Picomolar concentrations of oligomeric alpha-synuclein sensitizes TLR4 to play an initiating role in Parkinson’s disease pathogenesis

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Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution

(2018) Christopher G. Taylor et al.   ANALYTICAL CHEMISTRY

Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells

(2018) Daniel R. Whiten et al.   CHEMBIOCHEM

TLR5 decoy receptor as a novel anti-amyloid therapeutic for Alzheimer’s disease

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Quantifying Co-Oligomer Formation by α-Synuclein

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The Gothenburg H70 Birth cohort study 2014–16: design, methods and study population

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Decoding the synaptic dysfunction of bioactive human AD brain soluble Aβ to inspire novel therapeutic avenues for Alzheimer’s disease

(2018) Shaomin Li et al.   Acta Neuropathologica Communications

The conformational epitope for a new Aβ42 protofibril-selective antibody partially overlaps with the peptide N-terminal region

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Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

(2017) Giuliana Fusco et al.   SCIENCE

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

(2017) Lothar Gremer et al.   SCIENCE

Inhibiting the Ca 2+ Influx Induced by Human CSF

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Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method

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Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures

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Neuroinflammation in Alzheimer's disease

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Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation

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Mild cognitive impairment and deficits in instrumental activities of daily living: a systematic review

(2015) Katrin Jekel et al.   Alzheimers Research & Therapy

A Sensitive A  Oligomer Assay Discriminates Alzheimer's and Aged Control Cerebrospinal Fluid

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Epitope structure and binding affinity of single chain llama anti-β-amyloid antibodies revealed by proteolytic excision affinity-mass spectrometry

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Amyloid-β(1–42) Protofibrils Formed in Modified Artificial Cerebrospinal Fluid Bind and Activate Microglia

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The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

(2012) Iryna Benilova et al.   NATURE NEUROSCIENCE

Respiratory Syncytial Virus Fusion Protein-Induced Toll-Like Receptor 4 (TLR4) Signaling Is Inhibited by the TLR4 Antagonists Rhodobacter sphaeroides Lipopolysaccharide and Eritoran (E5564) and Requires Direct Interaction with MD-2

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The presence of sodium dodecyl sulphate-stable Aβ dimers is strongly associated with Alzheimer-type dementia

(2010) Jessica M. Mc Donald et al.   BRAIN

A causative link between the structure of aberrant protein oligomers and their toxicity

(2010) Silvia Campioni et al.   Nature Chemical Biology

Cerebrospinal fluid and plasma biomarkers in Alzheimer disease

(2010) Kaj Blennow et al.   Nature Reviews Neurology

TAK-242 selectively suppresses Toll-like receptor 4-signaling mediated by the intracellular domain

(2008) Tomohiro Kawamoto et al.   EUROPEAN JOURNAL OF PHARMACOLOGY

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

(2008) Ganesh M Shankar et al.   NATURE MEDICINE

The TLR3 signaling complex forms by cooperative receptor dimerization

(2008) J. N. Leonard et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural Basis of Toll-Like Receptor 3 Signaling with Double-Stranded RNA

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