ArticleBiochemistry2018
Mispacking of the Phe87 Side Chain Reduces the Kinetic Stability of Human Transthyretin.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Mechanism of inhibition of acid-mediated transthyretin aggregation by designed peptides.The Journal of biological chemistry · 2025Article
- The conformational landscape of human transthyretin revealed by cryo-EM.Nature structural & molecular biology · 2025Article
- Lysine carbamoylation during urea denaturation remodels the energy landscape of human transthyretin dissociation linked to unfolding.Protein science : a publication of the Protein Society · 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
- 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
- Role of conformational dynamics in pathogenic protein aggregation.Current opinion in chemical biology · 2023Review
- Aggregation-Prone Structural Ensembles of Transthyretin Collected With Regression Analysis for NMR Chemical Shift.Frontiers in molecular biosciences · 2021Article
- Binding of Monovalent and Bivalent Ligands by Transthyretin Causes Different Short- and Long-Distance Conformational Changes.Journal of medicinal chemistry · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Aggregation of transthyretin (TTR) causes TTR amyloidoses. The native TTR tetramer (a dimer of dimers) is stabilized by packing of phenylalanine 87 (F87) into a hydrophobic cavity of a neighboring protomer across the strong dimer interface. X-ray structures at acidic pH show that the side chain of F87 can be displaced from its binding pocket, but the resultant solution conformations remain unknown. Here we used
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Identifiers
What OpenQuestion holds
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.