Structural Determinants of Tau Aggregation Inhibitor Potency*
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Summary
It is suggested that flat, highly polarizable ligands inhibit Tau aggregation by interacting with folded species in the aggregation pathway and driving their assembly into soluble but highly stable Tau oligomers.
- Type
- article
- Published
- 2013-09-26
- Cited by
- 40
- References
- 78
- Access
- Open access
- OpenAlex
- https://openalex.org/W24072703
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19186131
Keywords
Computer science, Pipeline (software), Data mining, Knowledge extraction, Rule-based system
References
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- Pathways of tau fibrillization.
- Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.
- Inhibition of tau fibrillization by oleocanthal via reaction with the amino groups of tau
- Research Towards Tau Imaging
- Handbook of Molecular Descriptors
- Small Molecule Inhibitors of α-Synuclein Filament Assembly†
- Tau aggregation and toxicity in tauopathic neurodegenerative diseases
- Is Tau Aggregation Toxic or Protective?
- Structural Characteristics of the α-Synuclein Oligomers Stabilized by the Flavonoid Baicalein
- Structure activity relationship of cyclic thiacarbocyanine tau aggregation inhibitors
- Ligand polarizability contributes to tau fibril binding affinity.
- Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro*
- Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps
- Ligand electronic properties modulate tau filament binding site density
- Color and constitution: one hundred years of research.
- Differentiating Alzheimer disease-associated aggregates with small molecules.
- Possible role of each repeat structure of the microtubule-binding domain of the tau protein in in vitro aggregation.
- Cyanine dye N744 inhibits tau fibrillization by blocking filament extension: implications for the treatment of tauopathic neurodegenerative diseases.
- QSAR studies for prediction of cross-β sheet aggregate binding affinity and selectivity
Cited by
- Inhibition of tau aggregation using a naturally-occurring cyclic peptide scaffold.
- Use of Genetically Modified Mesenchymal Stem Cells to Treat Neurodegenerative Diseases
- Structure and mechanism of action of tau aggregation inhibitors
- Cognitive Enhancers (Nootropics). Part 3: Drugs Interacting with Targets other than Receptors or Enzymes. Disease-modifying Drugs
- Tau-directed approaches for the treatment of Alzheimer’s disease: focus on leuco-methylthioninium
- Advances in therapeutics for neurodegenerative tauopathies: moving toward the specific targeting of the most toxic tau species.
- A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.
- Analyzing tau aggregation with electron microscopy
- Tau-Centric Targets and Drugs in Clinical Development for the Treatment of Alzheimer's Disease
- Synthesis and in vitro evaluation of novel rhodanine derivatives as potential cholinesterase inhibitors.
- Tau-based therapeutics for Alzheimer's disease: active and passive immunotherapy.
- Expression and purification of tau protein and its frontotemporal dementia variants using a cleavable histidine tag
- Interactions between Microtubule-Binding Protein Tau (MAPT) and Small Molecules
- Tau peptides and tau mutant protein aggregation inhibition by cationic polyethyleneimine and polyarginine
- Molecular characterization of the Parkinson's associated protein DJ-1
- Glycogen synthase kinase-3 (GSK-3) activity regulates mRNA methylation in mouse embryonic stem cells
- Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer's Disease, Parkinson's Disease, and Amyotrophic Lateral Sclerosis in the Last Decade.
- Cyanine dyes derived inhibition of insulin fibrillization
- Screening of a neuronal cell model of tau pathology for therapeutic compounds.
- The role of annealing and fragmentation in human tau aggregation dynamics
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