The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer of α-Synuclein Amyloid Fibril Formation

The Properties of α-Synuclein Secondary Nuclei Are Dominated by the Solution Conditions Rather than the Seed Fibril Strain

(2020) Alessia Peduzzo et al.   ACS Chemical Neuroscience

Denaturant effect on amyloid fibrils: Declasterization, depolymerization, denaturation and reassembly

(2020) M.I. Sulatsky et al.   INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity

(2019) Malcolm J. Daniels et al.   Scientific Reports

Complex of EGCG with Cu(II) Suppresses Amyloid Aggregation and Cu(II)-Induced Cytotoxicity of α-Synuclein

(2019) Yilong Teng et al.   MOLECULES

An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils

(2019) Emil Dandanell Agerschou et al.   eLife

The growth of amyloid fibrils: rates and mechanisms

(2019) Alexander K. Buell   BIOCHEMICAL JOURNAL

ZPD-2, a Small Compound That Inhibits α-Synuclein Amyloid Aggregation and Its Seeded Polymerization

(2019) Samuel Peña-Díaz et al.   Frontiers in Molecular Neuroscience

The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG

(2019) Tomas Sneideris et al.   Biomolecules

Microfluidic Diffusion Platform for Characterizing the Sizes of Lipid Vesicles and the Thermodynamics of Protein–Lipid Interactions

(2018) Hongze Gang et al.   ANALYTICAL CHEMISTRY

C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH

(2018) Ingrid M. van der Wateren et al.   Chemical Science

Cryo-EM structure of alpha-synuclein fibrils

(2018) Ricardo Guerrero-Ferreira et al.   eLife

Zinc boosts EGCG's hIAPP amyloid Inhibition both in solution and membrane

(2018) Young-Ho Lee et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Suppression, disaggregation, and modulation of γ-Synuclein fibrillation pathway by green tea polyphenol EGCG

(2018) Sneha Roy et al.   PROTEIN SCIENCE

Probing the inhibitory activity of epigallocatechin-gallate on toxic aggregates of mutant (L84F) SOD1 protein through geometry based sampling and steered molecular dynamics

(2017) E. Srinivasan et al.   JOURNAL OF MOLECULAR GRAPHICS & MODELLING

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity

(2017) Michele Perni et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification

(2017) Ricardo Gaspar et al.   QUARTERLY REVIEWS OF BIOPHYSICS

(−)-Epigallocatechin-3-gallate (EGCG) inhibits fibrillation, disaggregates amyloid fibrils of α-synuclein, and protects PC12 cells against α-synuclein-induced toxicity

(2017) Juan Zhao et al.   RSC Advances

A-type dimeric epigallocatechin-3-gallate (EGCG) is a more potent inhibitor against the formation of insulin amyloid fibril than EGCG monomer

(2016) Rong-zu Nie et al.   BIOCHIMIE

Certain (−)-epigallocatechin-3-gallate (EGCG) auto-oxidation products (EAOPs) retain the cytotoxic activities of EGCG

(2016) Yaqing Wei et al.   FOOD CHEMISTRY

Structural disorder of monomeric α-synuclein persists in mammalian cells

(2016) Francois-Xavier Theillet et al.   NATURE

Molecular mechanisms of protein aggregation from global fitting of kinetic models

(2016) Georg Meisl et al.   Nature Protocols

Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson’s Disease

(2016) Yan Xu et al.   NEUROCHEMICAL RESEARCH

Quantitative thermophoretic study of disease-related protein aggregates

(2016) Manuel Wolff  et al.   Scientific Reports

Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions

(2015) Paolo Arosio et al.   ACS Nano

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

(2015) Céline Galvagnion et al.   Nature Chemical Biology

Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity

(2015) Emma V. Yates et al.   Nature Chemistry

Structural characteristics of (−)-epigallocatechin-3-gallate inhibiting amyloid Aβ42 aggregation and remodeling amyloid fibers

(2015) Yun Liu et al.   RSC Advances

The green tea polyphenol (−)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios

(2014) Heike J. Wobst et al.   FEBS LETTERS

The Presence of an Air–Water Interface Affects Formation and Elongation of α-Synuclein Fibrils

(2014) Silvia Campioni et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The amyloid state and its association with protein misfolding diseases

(2014) Tuomas P. J. Knowles et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease

(2014) Gergely Tóth et al.   PLoS One

Solution conditions determine the relative importance of nucleation and growth processes in  -synuclein aggregation

(2014) A. K. Buell et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour

(2014) Giuliana Fusco et al.   Nature Communications

Lysosomes and α-synuclein form a dangerous duet leading to neuronal cell death

(2014) Mathieu Bourdenx et al.   Frontiers in Neuroanatomy

Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson’s disease

(2013) Jens Wagner et al.   ACTA NEUROPATHOLOGICA

Toward the Molecular Mechanism(s) by Which EGCG Treatment Remodels Mature Amyloid Fibrils

(2013) Fernando L. Palhano et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism

(2013) S. I. A. Cohen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes

(2013) Amber N. Murray et al.   PROTEIN SCIENCE

Pathological  -Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

(2012) K. C. Luk et al.   SCIENCE

EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2

(2011) Indu R. Chandrashekaran et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Metastability of Native Proteins and the Phenomenon of Amyloid Formation

(2011) Andrew J. Baldwin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Interactions between Amyloidophilic Dyes and Their Relevance to Studies of Amyloid Inhibitors

(2010) Alexander K. Buell et al.   BIOPHYSICAL JOURNAL

Lysosomal Degradation of α-Synucleinin Vivo

(2010) Sally K. Mak et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Plant Polyphenols as Dietary Antioxidants in Human Health and Disease

(2010) Kanti Bhooshan Pandey et al.   Oxidative Medicine and Cellular Longevity

EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity

(2010) Jan Bieschke et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Parkinson's disease dementia and dementia with Lewy bodies: different aspects of one entity

(2009) Dag Aarsland et al.   INTERNATIONAL PSYCHOGERIATRICS

Tea Catechins Induce the Conversion of Preformed Lysozyme Amyloid Fibrils to Amorphous Aggregates

(2009) Jing He et al.   JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

(−)-Epigallocatechin-3-Gallate (EGCG) Maintains κ-Casein in Its Pre-Fibrillar State without Redirecting Its Aggregation Pathway

(2009) Sean A. Hudson et al.   JOURNAL OF MOLECULAR BIOLOGY

A synergistic small-molecule combination directly eradicates diverse prion strain structures

(2009) Blake E Roberts et al.   Nature Chemical Biology

Charge neutralization and collapse of the C-terminal tail of alpha-synuclein at low pH

(2009) Sebastian McClendon et al.   PROTEIN SCIENCE

Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS

(2008) Hila Shoval et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Green tea extracts interfere with the stress-protective activity of PrPCand the formation of PrPSc

(2008) Angelika S. Rambold et al.   JOURNAL OF NEUROCHEMISTRY

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

(2008) Dagmar E Ehrnhoefer et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY