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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
Moxifloxacin Disrupts and Attenuates Aβ42 Fibril and Oligomer Formation: Plausibly Repositioning an Antibiotic as Therapeutic against Alzheimer's Disease | ACS Chemical Neuroscience
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A spiral microfluidic device for rapid sorting, trapping, and long-term live imaging of Caenorhabditis elegans embryos | Microsystems & Nanoengineering
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
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease | Science Advances
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. - Abstract - Europe PMC
A spiral microfluidic device for rapid sorting, trapping, and long-term live imaging of Caenorhabditis elegans embryos | Microsystems & Nanoengineering
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers | PNAS
![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 | PNAS
Pharmaceuticals | Free Full-Text | Identification of a Thyroid Hormone Derivative as a Pleiotropic Agent for the Treatment of Alzheimer’s Disease
Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease | Science Advances
Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method | Science Advances
Two decades of new drug discovery and development for Alzheimer's disease
Kinetic fingerprints differentiate anti-Aβ therapies
Glycation affects fibril formation of Aβ peptides - ScienceDirect
IJMS | Free Full-Text | Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers
PDF) Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
PDF) A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease
Perphenazine–Macrocycle Conjugates Rapidly Sequester the Aβ42 Monomer and Prevent Formation of Toxic Oligomers and Amyloid | ACS Chemical Neuroscience
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease | Science Advances
