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Article

EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates.

International journal of molecular sciences - 15 Sept 2023

Zou Huizhen, Zhou Shuangyan

Abstract excerpt

Transthyretin amyloidosis (ATTR) is a progressive and systemic disease caused by the misfolding and amyloid aggregation of transthyretin (TTR). Stabilizing the TTR tetramers and disrupting the formed TTR aggregation are treated as a promising strategy for the treatment of ATTR. Previous studies have reported that epigallocatechin gallate (EGCG) can participate in the whole process of TTR aggregation to prevent...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 37762449
DOI: 10.3390/ijms241814146
PMCID: PMC10531593

Genes

TTR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

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EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates.PMID 37762449Read ↗

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The Physical Driving Forces of Conformational Transition for TTR91-96 with Proline Mutations.Semantic proximity Read ↗

Crystal structures of amyloidogenic segments of human transthyretin.Semantic proximity Read ↗

Disruption of the CD Loop by Enzymatic Cleavage Promotes the Formation of Toxic Transthyretin Oligomers through a Common Transthyretin Misfolding Pathway.Semantic proximity Read ↗

Atomic Mechanisms of Transthyretin Tetramer Dissociation Studied by Molecular Dynamics Simulations.Semantic proximity Read ↗

Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity.Semantic proximity Read ↗

The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses.Semantic proximity Read ↗

Inhibition of the Amyloidogenesis of Transthyretin by Natural Products and Synthetic Compounds.Semantic proximity Read ↗

Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Semantic proximity Read ↗

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