ArticleBiochemistry2016
Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.
Article in Biochemistry, 2016. 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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Who cites it
20 citing papers in PubMed.
- Identification of the interfacial regions in misfolded transthyretin oligomers.Biochimica et biophysica acta. Proteins and proteomics · 2024Article
- The Regulatory Mechanism of Transthyretin Irreversible Aggregation through Liquid-to-Solid Phase Transition.International journal of molecular sciences · 2023Article
- Toxic Misfolded Transthyretin Oligomers with Different Molecular Conformations Formed through Distinct Oligomerization Pathways.Biochemistry · 2022Article
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
- Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform.Nature communications · 2022Article
- Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.International journal of molecular sciences · 2021Review
- Aggregation-Prone Structural Ensembles of Transthyretin Collected With Regression Analysis for NMR Chemical Shift.Frontiers in molecular biosciences · 2021Article
- Edge Strand Dissociation and Conformational Changes in Transthyretin under Amyloidogenic Conditions.Biophysical journal · 2020Article
- Structural Characterization of Cardiac Ex Vivo Transthyretin Amyloid: Insight into the Transthyretin Misfolding Pathway In Vivo.Biochemistry · 2020Article
- Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis.Nature communications · 2019Article
- Atomic force microscopy for single molecule characterisation of protein aggregation.Archives of biochemistry and biophysics · 2019Review
- 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
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- 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
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- 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
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7 authors.
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Abstract
Structural characterization of amyloid rich in cross-β structures is crucial for unraveling the molecular basis of protein misfolding and amyloid formation associated with a wide range of human disorders. Elucidation of the β-sheet structure in noncrystalline amyloid has, however, remained an enormous challenge. Here we report structural analyses of the β-sheet structure in a full-length transthyretin amyloid using solid-state NMR spectroscopy. Magic-angle-spinning (MAS) solid-state NMR was employed to investigate native-like β-sheet structures in the amyloid state using selective labeling schemes for more efficient solid-state NMR studies. Analyses of extensive long-range (13)C-(13)C correlation MAS spectra obtained with selectively (13)CO- and (13)Cα-labeled TTR reveal that the two main β-structures in the native state, the CBEF and DAGH β-sheets, remain intact after amyloid formation. The tertiary structural information would be of great use for examining the quaternary structure of TTR amyloid.
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