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Evaluation of ThT augmentation and RLS inner filter effect caused by highly fluorescent coumarin derivative and establishing it as true inhibitor of amyloid fibrillation

https://doi.org/10.1016/j.abb.2021.108981

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Review: Formation and Properties of Amyloid-like Fibrils Derived from α-Synuclein and Related Proteins

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Rayleigh and Mie Scattering

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Dynamic Light Scattering

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On the structural definition of amyloid fibrils and other polypeptide aggregates

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Emulsan quantitation by Nile red quenching fluorescence assay

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Extrinsic Fluorescent Dyes as Tools for Protein Characterization

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Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer’s Disease Immunotherapy

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Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces

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Rapid colorimetric assay for cell growth and survival

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Genetics

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Existence of Different Structural Intermediates on the Fibrillation Pathway of Human Serum Albumin

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Intestinal anti-inflammatory activity of esculetin and 4-methylesculetin in the trinitrobenzenesulphonic acid model of rat colitis

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Small molecule probes of protein aggregation

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Fibrillogenesis of human serum albumin in the presence of levodopa – spectroscopic, calorimetric and microscopic studies

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An insight into the inhibition of fibrillation process verses disaggregation of preformed fibrils of bovine serum albumin by isoprenaline hydrochloride

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Molecular basis of the inhibition and disaggregation of thermally-induced amyloid fibrils of human serum albumin by an anti-Parkinson's drug, benserazide hydrochloride

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Esculetin enhances TRAIL-induced apoptosis through DR5 upregulation in human oral cancer SAS cells

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Amyloid formation of native folded protein induced by peptide‐based graft copolymer

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Using Water Raman Intensities To Determine the Effective Excitation and Emission Path Lengths of Fluorophotometers for Correcting Fluorescence Inner Filter Effect

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Structural Analogue of Thioflavin T, DMASEBT, as a Tool for Amyloid Fibrils Study

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Prevention and Disintegration of Human Serum Albumin Fibrils under Physiological Conditions: Biophysical Aspects

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Probing the Nongeneralized Amyloid Inhibitory Mechanism of Hydrophobic Chaperone

inferredcites →https://doi.org/10.1021/jp064861ropenalex-snapshot

Amyloid Fibril Formation and Other Aggregate Species Formed by Human Serum Albumin Association

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Effects of DHLA-Capped CdSe/ZnS Quantum Dots on the Fibrillation of Human Serum Albumin

inferredcites →https://doi.org/10.1021/jp111528copenalex-snapshot

Insights into the Mechanism of Aggregation and Fibril Formation from Bovine Serum Albumin

inferredcites →https://doi.org/10.1021/jp902224dopenalex-snapshot

Influence of Electrostatic Interactions on the Fibrillation Process of Human Serum Albumin

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Spectral Properties of Thioflavin T in Solvents with Different Dielectric Properties and in a Fibril-Incorporated Form

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Atomic structure and chemistry of human serum albumin

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Vitamin B12 inhibits α-synuclein fibrillogenesis and protects against amyloid-induced cytotoxicity

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Fluorescence “off” and “on” signalling of esculetin in the presence of copper and thiol: a possible implication in cellular thiol sensing

inferredcites →https://doi.org/10.1039/c8ra04637aopenalex-snapshot

Andrographolide inhibits human serum albumin fibril formations through site-specific molecular interactions

inferredcites →https://doi.org/10.1039/c8sc03394copenalex-snapshot

Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways

inferredcites →https://doi.org/10.1073/pnas.1820585116openalex-snapshot

α-Sheet secondary structure in amyloid β-peptide drives aggregation and toxicity in Alzheimer’s disease

inferredcites →https://doi.org/10.1074/jbc.m009596200openalex-snapshot

Thioflavin T Is a Fluorescent Probe of the Acetylcholinesterase Peripheral Site That Reveals Conformational Interactions between the Peripheral and Acylation Sites

inferredcites →https://doi.org/10.1074/jbc.m116.742460openalex-snapshot

Inhibition of Insulin Amyloid Fibrillation by a Novel Amphipathic Heptapeptide

inferredcites →https://doi.org/10.1098/rsos.160696openalex-snapshot

Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation

inferredcites →https://doi.org/10.1111/j.1432-1033.2004.04096.xopenalex-snapshot

Multiple‐probe analysis of folding and unfolding pathways of human serum albumin

inferredcites →https://doi.org/10.1111/j.1742-4658.2009.07307.xopenalex-snapshot

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

inferredcites →https://doi.org/10.1111/j.1742-4658.2010.07889.xopenalex-snapshot

Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity

inferredcites →https://doi.org/10.1121/1.3655229openalex-snapshot

On Rayleigh and Mie scattering

inferredcites →https://doi.org/10.1155/2003/296902openalex-snapshot

Spectroscopic Analysis of Amyloid Fibril Formation in SH3‐Domains

inferredcites →https://doi.org/10.1155/2018/8613209openalex-snapshot

Inhibition of Protein Aggregation by Several Antioxidants

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Effects of the Antioxidant (6,7-Dihydroxycoumarin) Esculetin on the Glutathione System and Lipid Peroxidation in Mice

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Mushroom Tyrosinase Inhibitory Activity of Esculetin Isolated from Seeds of Euphorbia lathyris L.

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Bifunctional Anti-Non-Amyloid Component α-Synuclein Nanobodies Are Protective In Situ

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Inhibition of Human Transthyretin Aggregation by Non-Steroidal Anti-Inflammatory Compounds: A Structural and Thermodynamic Analysis

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Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways

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