A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence.
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Flexibility and Solvation of Amyloid-β Hydrophobic CoreFast Motions of Key Methyl Groups in Amyloid-β Fibrils.Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation.Structural and optical properties of short peptides: nanotubes-to-nanofibers phase transformation.Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease.Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.Label-free imaging of amyloids using their intrinsic linear and nonlinear optical properties.Photoluminescent Peptide-Based Nanostructures as FRET Donor for Fluorophore Dye.Bioinspired fluorescent dipeptide nanoparticles for targeted cancer cell imaging and real-time monitoring of drug release.Advanced imaging of tau pathology in Alzheimer Disease: New perspectives from super resolution microscopy and label-free nanoscopy.Anti-amyloid compounds inhibit α-synuclein aggregation induced by protein misfolding cyclic amplification (PMCA)Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.In vitro aggregation assays for the characterization of α-synuclein prion-like properties.Near UV-Visible electronic absorption originating from charged amino acids in a monomeric protein.In situ studies of protein aggregation kinetics with multiparametric and superresolution imaging.Effect of the surface chemistry of insulin fibrils on the aggregation rate.Self-assembling peptide semiconductors.Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence.Photoluminescence of Diphenylalanine Peptide Nano/Microstructures: From Mechanisms to Applications.A computational study on how structure influences the optical properties in model crystal structures of amyloid fibrils.Structural Characterization of PEGylated Hexaphenylalanine Nanostructures Exhibiting Green Photoluminescence Emission.Amyloid-hydroxyapatite bone biomimetic composites.Controlling molecular self-assembly: from amyloid oligomerization and therapy to novel biomaterials and technological applications in nanomedicine.Near infrared fluorescent peptide nanoparticles for enhancing esophageal cancer therapeutic efficacy.The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behaviorDifferent Structural Conformers of Monomeric α-Synuclein Identified after Lyophilizing and FreezingQuantum confined peptide assemblies with tunable visible to near-infrared spectral rangeInhibition of beta-amyloid aggregation by fluorescent dye labels
P2860
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P2860
A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 16 April 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
A label-free, quantitative ass ...... sed on intrinsic fluorescence.
@en
A label-free, quantitative ass ...... sed on intrinsic fluorescence.
@nl
type
label
A label-free, quantitative ass ...... sed on intrinsic fluorescence.
@en
A label-free, quantitative ass ...... sed on intrinsic fluorescence.
@nl
prefLabel
A label-free, quantitative ass ...... sed on intrinsic fluorescence.
@en
A label-free, quantitative ass ...... sed on intrinsic fluorescence.
@nl
P2093
P2860
P356
P1433
P1476
A label-free, quantitative ass ...... sed on intrinsic fluorescence.
@en
P2093
Clemens F Kaminski
Dorothea Pinotsi
Gabriele S Kaminski Schierle
P2860
P304
P356
10.1002/CBIC.201300103
P577
2013-04-16T00:00:00Z