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References from Field-assisted interfacial passivation: Microwave-enhanced EGCG remodeling of amyloid-β42 aggregates. Local targets link to admitted publications; unresolved targets remain external evidence.
Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade
10.1146/annurev-biochem-061516-045115 · 2017 · External reference
The amyloid state and its association with protein misfolding diseases
10.1038/nrm3810 · 2014 · External reference
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid β-peptide
10.1038/nrm2101 · 2007 · External reference
The toxic aβ oligomer and Alzheimer’s disease: an emperor in need of clothes
10.1038/nn.3028 · 2012 · External reference
Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
10.1074/jbc.m500997200 · 2005 · External reference
Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein Misfolding diseases
10.1074/jbc.c400260200 · 2004 · External reference
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
10.1073/pnas.1218402110 · 2013 · External reference
Molecular mechanisms of protein aggregation from global fitting of kinetic models
10.1038/nprot.2016.010 · 2016 · External reference
Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies
10.1038/s41594-020-0505-6 · 2020 · External reference
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
10.1038/nsmb.1437 · 2008 · External reference
EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
10.1073/pnas.0910723107 · 2010 · External reference
Structural properties of EGCG-induced, nontoxic Alzheimer’s disease aβ oligomers
10.1016/j.jmb.2012.01.013 · 2012 · External reference
Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils
10.1021/ja3115696 · 2013 · External reference
Distinguishing the effect on the rate and yield of Aβ42 aggregation by green tea polyphenol EGCG
10.1021/acsomega.0c02063 · 2020 · External reference
Molecular mechanism for the (−)-epigallocatechin Gallate-induced toxic to nontoxic remodeling of Aβ oligomers
10.1021/jacs.7b05012 · 2017 · External reference
Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways
10.1074/jbc.m110.173856 · 2011 · External reference
Origins of the superiority of oscillating electric fields for disrupting senile plaques: insights from the 7-residue fragment and the full-length Aβ-42 peptide
10.1021/jacs.4c14791 · 2025 · External reference
Cryo-EM structures of amyloid-β 42 filaments from human brains
10.1126/science.abm7285 · 2022 · External reference
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy
10.1126/science.aao2825 · 2017 · External reference
3D structure of Alzheimer’s amyloid-β(1–42) fibrils
10.1073/pnas.0506723102 · 2005 · External reference
Green tea extract EGCG plays a dual role in Aβ42 protofibril disruption and membrane protection: a molecular dynamic study
10.1016/j.chemphyslip.2020.105024 · 2021 · External reference
Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation
10.1098/rsos.160696 · 2017 · External reference
The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds
10.1111/j.1742-4658.2009.07307.x · 2009 · External reference
Structural remodeling mechanism of the toxic amyloid fibrillary mediated by Epigallocatechin-3-gallate
10.1021/acsomega.2c05995 · 2022 · External reference
Understanding the mechanisms of green tea EGCG against amyloid β oligomer neurotoxicity through computational studies
10.1039/d4ra03343d · 2024 · External reference
Green tea extracts EGCG and EGC display distinct mechanisms in disrupting Aβ42 protofibril
10.1021/acschemneuro.0c00277 · 2020 · External reference
Molecular mechanisms of resveratrol and EGCG in the inhibition of aβ 42 aggregation and disruption of aβ 42 protofibril: similarities and differences
10.1039/d1cp01913a · 2021 · External reference
The effect of (−)-Epigallocatechin-3-Gallate on the amyloid-β secondary structure
10.1016/j.bpj.2020.05.033 · 2020 · External reference
The polyphenol EGCG directly targets intracellular amyloid-β aggregates and promotes their lysosomal degradation
10.1111/jnc.15842 · 2023 · External reference
Biosynthesis of nanoparticles with green tea for inhibition of β-amyloid fibrillation coupled with ligands analysis
10.2147/ijn.s451070 · 2024 · External reference
Using circular dichroism spectra to estimate protein secondary structure
10.1038/nprot.2006.202 · 2006 · External reference
10.1016/j.softx.2015.06.001 · 2015 · Admitted local publication
Improved side-chain torsion potentials for the Amber ff99SB protein force field
10.1002/prot.22711 · 2010 · External reference
AmberTools
10.1021/acs.jcim.3c01153 · 2023 · External reference
Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation
10.1002/jcc.10128 · 2002 · External reference
Comparison of simple potential functions for simulating liquid water
10.1063/1.445869 · 1983 · External reference
Particle mesh Ewald: an N ·log(N) method for Ewald sums in large systems
10.1063/1.464397 · 1993 · External reference
Canonical sampling through velocity rescaling
10.1063/1.2408420 · 2007 · External reference
Polymorphic transitions in single crystals: a new molecular dynamics method
10.1063/1.328693 · 1981 · External reference
P-LINCS: a parallel linear constraint solver for molecular simulation
10.1021/ct700200b · 2008 · External reference
