Do Catechins (ECG and EGCG) Bind to the Same Site as Thioflavin T (ThT) in Amyloid Fibril? Answer From Saturation Transfer Difference NMR

Natural Product Communications - United States
doi 10.1177/1934578x19849791
Full Text
Abstract

Available in full text

Date
Authors
Publisher

SAGE Publications

Related search

Variable Binding of Thioflavin T to Amyloid Fibrils

Biophysical Journal
Biophysics
2019English

Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils

Biochimica et Biophysica Acta - Proteins and Proteomics
BiochemistryAnalytical ChemistryMolecular BiologyBiophysics
2010English

Protein-Induced Photophysical Changes to the Amyloid Indicator Dye Thioflavin T

Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
2010English

Protein-Induced Photophysical Changes to the Amyloid Indicator Dye, Thioflavin T

2010English

Saturation Transfer Difference NMR to Study Substrate and Product Binding to Human UDP-xylose Synthase (hUXS1A) During Catalytic Event

RSC Advances
ChemistryChemical Engineering
2015English

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

2020English

ECG Dilemma-Answer

American Journal of Hospital Medicine
2017English

Destruction of Amyloid Fibrils of Keratoepithelin Peptides by Laser Irradiation Coupled With Amyloid-Specific Thioflavin T

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2011English

Investigating the Interaction Mechanism of Fluorescent Whitening Agents to Human Serum Albumin Using Saturation Transfer Difference-Nmr, Multi-Spectroscopy, and Docking Studies

RSC Advances
ChemistryChemical Engineering
2017English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy