ArticleBiochemistry2017
Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Identification of the interfacial regions in misfolded transthyretin oligomers.Biochimica et biophysica acta. Proteins and proteomics · 2024Article
- Oxidative Stress in Transthyretin-Mediated Amyloidosis: An Exploratory Study.Antioxidants (Basel, Switzerland) · 2024Article
- The Regulatory Mechanism of Transthyretin Irreversible Aggregation through Liquid-to-Solid Phase Transition.International journal of molecular sciences · 2023Article
- Identification of predictors for the comprehensive clinical risk and severity of coronary lesions of acute coronary syndrome.Frontiers in cardiovascular medicine · 2023Article
- Toxic Misfolded Transthyretin Oligomers with Different Molecular Conformations Formed through Distinct Oligomerization Pathways.Biochemistry · 2022Article
- Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.International journal of molecular sciences · 2021Review
- Divergence Entropy-Based Evaluation of Hydrophobic Core in Aggressive and Resistant Forms of Transthyretin.Entropy (Basel, Switzerland) · 2021Article
- Structural Characterization of Cardiac Ex Vivo Transthyretin Amyloid: Insight into the Transthyretin Misfolding Pathway In Vivo.Biochemistry · 2020Article
- 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
- Probing conformational changes of monomeric transthyretin with second derivative fluorescence.Scientific reports · 2019Article
- Two distinct aggregation pathways in transthyretin misfolding and amyloid formation.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Transthyretin Aggregation Pathway toward the Formation of Distinct Cytotoxic Oligomers.Scientific reports · 2019Article
- NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations.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
- Inhibition of amyloid beta fibril formation by monomeric human transthyretin.Protein science : a publication of the Protein Society · 2018Article
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Authors and funding
7 authors.
Funding
Abstract
Amyloid formation of natively folded proteins involves global and/or local unfolding of the native state to form aggregation-prone intermediates. Here we report solid-state nuclear magnetic resonance (NMR) structural studies of amyloid derived from wild-type (WT) and more aggressive mutant forms of transthyretin (TTR) to investigate the structural changes associated with effective TTR aggregation. We employed selective
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