Extensive Plasmid Library to Prepare Tau Protein Variants and Study Their Functional Biochemistry
Thomas K. Karikari, Sophie Keeling, Emily Hill, Juan Lantero‐Rodriguez, David A. Nagel, Bruno Becker, Kina Höglund, Henrik Zetterberg, Kaj Blennow, Eric J. Hill, Kevin G. Moffat
Abstract
= 0.002) and mostly wider than WT filaments, explainable by their different principal filament elongation pathways: vertical (end-to-end) and lateral growth for WT and cysteine-modified, respectively. Cysteine rearrangement may therefore induce filament polymorphism. Together, the plasmid library, the protein production methods, and the new insights into cysteine-dependent aggregation should facilitate further studies and the design of antiaggregation agents.
Topics & Concepts
CysteineTau proteinPlasmidMicrotubuleBiochemistryBiologyMicrotubule-associated proteinProtein filamentRecombinant DNAChemistryCell biologyMolecular biologyBiophysicsAlzheimer's diseaseGeneEnzymeMedicinePathologyDiseaseAlzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingMicrotubule and mitosis dynamics