ArticleBiochemistry2017
Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Mechanism of inhibition of acid-mediated transthyretin aggregation by designed peptides.The Journal of biological chemistry · 2025Article
- Mispacking of the F87 sidechain drives aggregation-promoting conformational fluctuations in the subunit interfaces of the transthyretin tetramer.Protein science : a publication of the Protein Society · 2024Article
- Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.Nature communications · 2024Article
- The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink.Journal of the American Chemical Society · 2022Article
- Development and Validation of Fluorinated, Aromatic Amino Acid Parameters for Use with the AMBER ff15ipq Protein Force Field.The journal of physical chemistry. A · 2022Article
- Fluorine-Containing Drug Administration in Rats Results in Fluorination of Selected Proteins in Liver and Brain Tissue.International journal of molecular sciences · 2022Article
- Small, but powerful and attractive:Structure (London, England : 1993) · 2022Review
- Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.International journal of molecular sciences · 2021Review
- Thermodynamic Stability and Aggregation Kinetics of EF Helix and EF Loop Variants of Transthyretin.Biochemistry · 2021Article
- A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone.Journal of molecular biology · 2020Article
- Prognostic impact of serum transthyretin in patients with non-small cell lung cancer.Molecular and clinical oncology · 2019Article
- Mispacking of the Phe87 Side Chain Reduces the Kinetic Stability of Human Transthyretin.Biochemistry · 2018Article
- Kinetic analysis of the multistep aggregation pathway of human transthyretin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Abnormal deposition of aggregated wild-type (WT) human transthyretin (TTR) and its pathogenic variants is responsible for cardiomyopathy and neuropathy related to TTR amyloidosis. The tryptophan (Trp) fluorescence measurements typically used to study structural changes of TTR do not yield site-specific information on the two Trp residues per TTR protomer. To obtain such information, tryptophan labeled with fluorine at the 5 and 6 positions (5FW and 6FW) was incorporated into TTR. Fluorescence of 5FW and 6FW-labeled WT-TTR (WT-5FW and WT-6FW) and a single-Trp mutant W41Y showed that the photophysics of incorporated fluoro-Trp is consistent with site-specific solvation of the indole ring of W41 and W79.
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Registered trials
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