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Article

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

Protein science : a publication of the Protein Society - 1 Feb 2010

Rodrigues J Rui, Simões Carlos J V, Silva Cândida G, Brito Rui M M

Abstract excerpt

Protein aggregation into insoluble fibrillar structures known as amyloid characterizes several neurodegenerative diseases, including Alzheimer's, Huntington's and Creutzfeldt-Jakob. Transthyretin (TTR), a homotetrameric plasma protein, is known to be the causative agent of amyloid pathologies such as FAP (familial amyloid polyneuropathy), FAC (familial amyloid cardiomiopathy) and SSA (senile systemic...

Topics

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Amyloid
Crystallography, X-Ray
Hydrogen Bonding
Molecular Dynamics Simulation
Nuclear Magnetic Resonance, Biomolecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Folding

Protein Structure, Secondary

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Open in PubMed Open full text

Identifiers

PMID: 19937650
DOI: 10.1002/pro.289
PMCID: PMC2865717

Genes

TTR
FAP

Variants

Provenance

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Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.PMID 19937650Read ↗

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