Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation (Q24311960)

identical protein binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

1 reference

Nelson Ferreira

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Maria Rosário Almeida

object named as

Maria Rosário Almeida

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Maria João Saraiva

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language of work or name

English

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publication date

4 August 2011

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2 July 2011

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Europe PubMed Central

PubMed publication ID

21740906

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21740906

full work available at URL

6 December 2024

https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2011.06.030

1 reference

DOI

https://api.crossref.org/works/10.1016/J.FEBSLET.2011.06.030

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2011.06.030

6 December 2024

1 reference

DOI

https://api.crossref.org/works/10.1016/J.FEBSLET.2011.06.030

6 December 2024

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585

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issue

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page(s)

2424-30

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cites work

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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

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Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses

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Evaluating the binding selectivity of transthyretin amyloid fibril inhibitors in blood plasma

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4 ′‐iodo‐4′‐Deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters

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Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative

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Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity

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Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo

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Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for alpha-synuclein fibrils in vitro

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Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design

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Transthyretin oligomers induce calcium influx via voltage-gated calcium channels.

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Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways

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Binding and stabilization of transthyretin by curcumin.

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The crystal structure of the green tea polyphenol (-)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site

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Curcumin reduces alpha-synuclein induced cytotoxicity in Parkinson's disease cell model

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EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

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Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model.

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The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution

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Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils

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inferred from DOI database lookup

7 January 2021

based on heuristic

Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates

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inferred from DOI database lookup

7 January 2021

based on heuristic

The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils

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inferred from DOI database lookup

7 January 2021

based on heuristic

Small transthyretin (TTR) ligands as possible therapeutic agents in TTR amyloidoses

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The dark side of curcumin.

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