ArticleBiophysical journal2011
Experimentally derived structural constraints for amyloid fibrils of wild-type transthyretin.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Review
- Advances in protein misfolding, amyloidosis and its correlation with human diseases.3 Biotech · 2020Review
- Probing conformational changes of monomeric transthyretin with second derivative fluorescence.Scientific reports · 2019Article
- Anti-prion systems in yeast.The Journal of biological chemistry · 2019Review
- Retinol-Binding Protein Interferes with Transthyretin-Mediated β-Amyloid Aggregation Inhibition.Biochemistry · 2018Article
- Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.Cold Spring Harbor perspectives in medicine · 2018Review
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy.Journal of visualized experiments : JoVE · 2017Article
- Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.Biochemistry · 2017Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.Biochemistry · 2016Article
- Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.Journal of the American Chemical Society · 2016Article
- Transthyretin variants with improved inhibition of β-amyloid aggregation.Protein engineering, design & selection : PEDS · 2016Article
- Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.Biochemistry · 2016Article
- Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid Protofibrils.Scientific reports · 2015Article
- Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Amyloids and yeast prion biology.Biochemistry · 2013Article
- Efficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy.Journal of biomolecular NMR · 2013Article
- Domain swapping and amyloid fibril conformation.Prion · 2012Article
- Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Transthyretin (TTR) is a largely β-sheet serum protein responsible for transporting thyroxine and vitamin A. TTR is found in amyloid deposits of patients with senile systemic amyloidosis. TTR mutants lead to familial amyloidotic polyneuropathy and familial amyloid cardiomyopathy, with an earlier age of onset. Studies of amyloid fibrils of familial amyloidotic polyneuropathy mutant TTR suggest a structure similar to the native state with only a simple opening of a β-strand-loop-strand region exposing the two main β-sheets of the protein for fibril elongation. However, we find that the wild-type TTR sequence forms amyloid fibrils that are considerably different from the previously suggested amyloid structure. Using protease digestion with mass spectrometry, we observe the amyloid core to be primarily composed of the C-terminal region, starting around residue 50. Solid-state NMR measurements prove that TTR differs from other pathological amyloids in not having an in-register parallel β-sheet architecture. We also find that the TTR amyloid is incapable of binding thyroxine as monitored by either isothermal calorimetry or 1,8-anilinonaphthalene sulfonate competition. Taken together, our experiments are consistent with a significantly different configuration of the β-sheets compared to the previously suggested structure.
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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.