Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics.

PloS one - 1 Jan 2017

Saldaño Tadeo E, Zanotti Giuseppe, Parisi Gustavo, Fernandez-Alberti Sebastian

Abstract excerpt

Native transthyretin (TTR) homotetramer dissociation is the first step of the fibrils formation process in amyloid disease. A large number of specific point mutations that destabilize TTR quaternary structure have shown pro-amyloidogenic effects. Besides, several compounds have been proposed as d...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Algorithms
Share to Binding Sites
Share to Ligands

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Prealbumin

Share to Protein Stability

Share to Protein Structure, Quaternary

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 28704493
DOI: 10.1371/journal.pone.0181019
PMCID: PMC5509292

Genes

TTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Prepared record publication-28704493-2026-09-05.1. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics.PMID 28704493Read ↗

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 ↗

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

Comparative MD analysis of the stability of transthyretin providing insight into the fibrillation mechanism.Semantic proximity Read ↗

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

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

Characterization of Transthyretin Mutation G47V Associated with Hereditary Cardiac Amyloidosis.Semantic proximity Read ↗

Different disease-causing mutations in transthyretin trigger the same conformational conversion.Semantic proximity Read ↗

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

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation.Semantic proximity Read ↗

Conformational Dynamics of an Amyloidogenic Intermediate of Transthyretin: Implications for Structural Remodeling and Amyloid Formation.Semantic proximity Read ↗

Thermodynamic Stability and Aggregation Kinetics of EF Helix and EF Loop Variants of Transthyretin.Semantic proximity Read ↗

A comparative analysis of 23 structures of the amyloidogenic protein transthyretin.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.