ArticleThe journal of physical chemistry letters2015
Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.
Article in The journal of physical chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.
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Who cites it
33 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A Systematic and Comprehensive Review on Disease-Causing Genes in Amyotrophic Lateral Sclerosis.Journal of molecular neuroscience : MN · 2020Pooled it
- Protease-Mediated TAR DNA-Binding Protein 43 (TDP-43) Pathogenesis: From Molecular Mechanisms to Therapeutic Opportunities.ACS pharmacology & translational science · 2026Review
- Orientation affects hydrogen bonding cooperativity in polyproline II helical bundles.Communications chemistry · 2025Article
- Hydrogen bonding patterns and cooperativity in polyproline II helical bundles.Communications chemistry · 2024Article
- Review
- Synthetic β-sheets mimicking fibrillar and oligomeric structures for evaluation of spectral X-ray scattering technique for biomarker quantification.Cell & bioscience · 2024Article
- Single-molecule visualization determines conformational substate ensembles in β-sheet-rich peptide fibrils.Science advances · 2023Article
- Head-to-Head Comparison of Tau-PET Radioligands for Imaging TDP-43 in Post-Mortem ALS Brain.Molecular imaging and biology · 2023Article
- Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR.Frontiers in molecular biosciences · 2023Article
- Different Intermolecular Interactions Drive Nonpathogenic Liquid-Liquid Phase Separation and Potentially Pathogenic Fibril Formation by TDP-43.International journal of molecular sciences · 2022Article
- Slow Evolution toward "Super-Aggregation" of the Oligomers Formed through the Swapping of RNase A N-Termini: A Wish for Amyloidosis?International journal of molecular sciences · 2022Article
- Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils.Biophysical journal · 2022Article
- Insights into the aggregation mechanism of RNA recognition motif domains in TDP-43: a theoretical exploration.Royal Society open science · 2021Article
- The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils.International journal of molecular sciences · 2021Review
- Trends in Understanding the Pathological Roles of TDP-43 and FUS Proteins.Advances in experimental medicine and biology · 2021Article
- The mutational landscape of a prion-like domain.Nature communications · 2019Article
- Dysregulation of TDP-43 intracellular localization and early onset ALS are associated with a TARDBP S375G variant.Brain pathology (Zurich, Switzerland) · 2019Article
- Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation.The Journal of biological chemistry · 2019Article
- Morphology and Distribution of TDP-43 Pre-inclusions in Primary Progressive Aphasia.Journal of neuropathology and experimental neurology · 2019Article
- Structural Insights Into TDP-43 and Effects of Post-translational Modifications.Frontiers in molecular neuroscience · 2019Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the putative aggregation domain, engineered repeats of residues 341-366 can recruit endogenous TDP-43 into aggregates inside cells; however, the nature of these aggregates is a debatable issue. Recently, we showed that a coil to β-hairpin transition in a short peptide corresponding to TDP-43 residues 341-357 enables oligomerization. Here we provide definitive structural evidence for amyloid formation upon extensive characterization of TDP-43(341-357) via chromophore and antibody binding, electron microscopy (EM), solid-state NMR, and X-ray diffraction. On the basis of these findings, structural models for TDP-43(341-357) oligomers were constructed, refined, verified, and analyzed using docking, molecular dynamics, and semiempirical quantum mechanics methods. Interestingly, TDP-43(341-357) β-hairpins assemble into a novel parallel β-turn configuration showing cross-β spine, cooperative H-bonding, and tight side-chain packing. These results expand the amyloid foldome and could guide the development of future therapeutics to prevent this structural conversion.
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