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Article

Comparative MD analysis of the stability of transthyretin providing insight into the fibrillation mechanism.

Biopolymers - 1 May 2007

Sørensen Jesper, Hamelberg Donald, Schiøtt Birgit, McCammon J Andrew

Abstract excerpt

Proteins can misfold and aggregate, which is believed to be the cause of a variety of diseases, affecting very diverse organs in the body. Many questions about the nature of aggregation and the proteins that are involved in these events are still left unanswered. One of the proteins that is known to form amyloids is transthyretin (TTR), the secondary transporter of thyroxine, and transporter of retinol-binding...

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Identifiers

PMID: 17315201
DOI: 10.1002/bip.20705

Genes

TTR

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Comparative MD analysis of the stability of transthyretin providing insight into the fibrillation mechanism.PMID 17315201Read ↗

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

Mutation and low pH effect on the stability as well as unfolding kinetics of transthyretin dimer.Semantic proximity Read ↗

Modulation of human transthyretin stability by the mutations at histidine 88 studied by free energy simulation.Semantic proximity Read ↗

Intrinsic versus mutation dependent instability/flexibility: a comparative analysis of the structure and dynamics of wild-type transthyretin and its pathogenic variants.Semantic proximity Read ↗

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

Analysis of amyloidogenic transthyretin mutations using continuum solvent free energy calculations.Semantic proximity Read ↗

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

Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics.Semantic proximity Read ↗

Dynamics and Thermodynamics of Transthyretin Association from Molecular Dynamics Simulations.Semantic proximity Read ↗

Probing the dissociation pathway of a kinetically labile transthyretin mutantSemantic proximity Read ↗

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

Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.Semantic proximity Read ↗

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