ArticleIUCrJ2014
Binding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein.
Article in IUCrJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR.Journal of applied crystallography · 2025Article
- Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography.Journal of applied crystallography · 2025Article
- In silico prediction of the interaction of legacy and novel per- and poly-fluoroalkyl substances (PFAS) with selected human transporters and of their possible accumulation in the human body.Archives of toxicology · 2024Article
- 3-O-Methyltolcapone and Its Lipophilic Analogues Are Potent Inhibitors of Transthyretin Amyloidogenesis with High Permeability and Low Toxicity.International journal of molecular sciences · 2023Article
- Thyroxine metabolite-derived 3-iodothyronamine (T1AM) and synthetic analogs as efficient suppressors of transthyretin amyloidosis.Computational and structural biotechnology journal · 2023Article
- Article
- Production of perdeuterated fucose from glyco-engineered bacteria.Glycobiology · 2021Article
- Exploration of the Misfolding Mechanism of Transthyretin Monomer: Insights from Hybrid-Resolution Simulations and Markov State Model Analysis.Biomolecules · 2019Article
- Biophysical characterization and modulation of Transthyretin Ala97Ser.Annals of clinical and translational neurology · 2019Article
- Diagnostic and Treatment Approaches Involving Transthyretin in Amyloidogenic Diseases.International journal of molecular sciences · 2019Review
- A molecular mechanism for transthyretin amyloidogenesis.Nature communications · 2019Article
- Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition.Acta crystallographica. Section D, Structural biology · 2018Review
- Dynamics and Thermodynamics of Transthyretin Association from Molecular Dynamics Simulations.BioMed research international · 2018Article
- Back-exchange of deuterium in neutron crystallography: characterization by IR spectroscopy.Journal of applied crystallography · 2017Article
- Review
- Macromolecular structure phasing by neutron anomalous diffraction.Scientific reports · 2016Article
- Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses.Angewandte Chemie (International ed. in English) · 2016Article
- Automated harvesting and processing of protein crystals through laser photoablation.Acta crystallographica. Section D, Structural biology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis. Here, detailed neutron structural studies of perdeuterated transthyretin are described. The analyses, which fully exploit the enhanced visibility of isotopically replaced hydrogen atoms, yield new information on the stability of the protein and the possible mechanisms of amyloid formation. Residue Ser117 may play a pivotal role in that a single water molecule is closely associated with the γ-hydrogen atoms in one of the binding pockets, and could be important in determining which of the two sites is available to the substrate. The hydrogen-bond network at the monomer-monomer interface is more extensive than that at the dimer-dimer interface. Additionally, the edge strands of the primary dimer are seen to be favourable for continuation of the β-sheet and the formation of an extended cross-β structure through sequential dimer couplings. It is argued that the precursor to fibril formation is the dimeric form of the protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.