Pharmaceuticals | Free Full-Text | Identification of a Thyroid Hormone Derivative as a Pleiotropic Agent for the Treatment of Alzheimer’s Disease
PDF) A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease
Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method | Science Advances
PDF) Delivery of Native Proteins into C. Elegans Using a Transduction Protocol Based on Lipid Vesicles
Two decades of new drug discovery and development for Alzheimer's disease - RSC Advances (RSC Publishing) DOI:10.1039/C6RA26737H
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers | PNAS
Drug discovery: Insights from the invertebrate Caenorhabditis elegans - Giunti - 2021 - Pharmacology Research & Perspectives - Wiley Online Library
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease | Science Advances
Glycation affects fibril formation of Aβ peptides - ScienceDirect
PDF) Drug discovery: Insights from the invertebrate Caenorhabditis elegans
PDF) Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease | Science Advances
Perphenazine–Macrocycle Conjugates Rapidly Sequester the Aβ42 Monomer and Prevent Formation of Toxic Oligomers and Amyloid | ACS Chemical Neuroscience
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. - Abstract - Europe PMC
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease | Science Advances
PDF) Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method
![Hexahydropyrrolo[2,3-b]indole Compounds as Potential Therapeutics for Alzheimer's Disease | ACS Chemical Neuroscience](https://pubs.acs.org/cms/10.1021/acschemneuro.9b00297/asset/images/medium/cn9b00297_0007.gif "Hexahydropyrrolo[2,3-b]indole Compounds as Potential Therapeutics for Alzheimer's Disease | ACS Chemical Neuroscience")
Hexahydropyrrolo[2,3-b]indole Compounds as Potential Therapeutics for Alzheimer's Disease | ACS Chemical Neuroscience
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. - Abstract - Europe PMC
PDF) Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
A spiral microfluidic device for rapid sorting, trapping, and long-term live imaging of Caenorhabditis elegans embryos | Microsystems & Nanoengineering
C-Terminal Fragment, Aβ39–42-Based Tetrapeptides Mitigates Amyloid-β Aggregation-Induced Toxicity | ACS Omega
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease | Science Advances
Genetic and Pharmacological Discovery for Alzheimer's Disease Using Caenorhabditis elegans | ACS Chemical Neuroscience
A spiral microfluidic device for rapid sorting, trapping, and long-term live imaging of Caenorhabditis elegans embryos | Microsystems & Nanoengineering
