ArticleAngewandte Chemie (International ed. in English)2016
Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation.The FEBS journal · 2026Article
- From Hummingbird to Elephant: Amyloid Formation in Natural Transthyretin Variants.bioRxiv : the preprint server for biology · 2026Article
- Effects of Hydration on Transthyretin Conformational Dynamics and Oligomerization.Biochemistry · 2025Article
- Hydration (HJournal of the American Chemical Society · 2025Article
- Initiation of transthyretin aggregation at neutral pH by fluid agitation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography.Journal of applied crystallography · 2025Article
- Aggregation of Transthyretin by Fluid Agitation.bioRxiv : the preprint server for biology · 2024Article
- Conformational Dynamics of an Amyloidogenic Intermediate of Transthyretin: Implications for Structural Remodeling and Amyloid Formation.Journal of molecular biology · 2024Article
- Water Plays Key Roles in Stabilities of Wild Type and Mutant Transthyretin Complexes.Journal of the American Society for Mass Spectrometry · 2024Article
- Probing the Dissociation Pathway of a Kinetically Labile Transthyretin Mutant.Journal of the American Chemical Society · 2024Article
- The Complementarity of Nuclear Magnetic Resonance and Native Mass Spectrometry in Probing Protein-Protein Interactions.Advances in experimental medicine and biology · 2024Review
- Article
- DThe journal of physical chemistry. B · 2023Review
- Calcium Binds to Transthyretin with Low Affinity.Biomolecules · 2022Article
- Structural basis for transthyretin amyloid formation in vitreous body of the eye.Nature communications · 2021Article
- The impact of folding modes and deuteration on the atomic resolution structure of hen egg-white lysozyme.Acta crystallographica. Section D, Structural biology · 2021Article
- Article
- Deuteration of nonexchangeable protons on proteins affects their thermal stability, side-chain dynamics, and hydrophobicity.Protein science : a publication of the Protein Society · 2020Article
- A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines.The FEBS journal · 2020Review
- A molecular mechanism for transthyretin amyloidogenesis.Nature communications · 2019Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
It is well established that the formation of transthyretin (TTR) amyloid fibrils is linked to the destabilization and dissociation of its tetrameric structure into insoluble aggregates. Isotope labeling is used for the study of TTR by NMR, neutron diffraction, and mass spectrometry (MS). Here MS, thioflavin T fluorescence, and crystallographic data demonstrate that while the X-ray structures of unlabeled and deuterium-labeled TTR are essentially identical, subunit exchange kinetics and amyloid formation are accelerated for the deuterated protein. However, a slower subunit exchange is noted in deuterated solvent, reflecting the poorer solubility of non-polar protein side chains in such an environment. These observations are important for the interpretation of kinetic studies involving deuteration. The destabilizing effects of TTR deuteration are rather similar in character to those observed for aggressive mutations of TTR such as L55P (associated with familial amyloid polyneuropathy).
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