An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease | Science Advances
Pharmaceuticals | Free Full-Text | Identification of a Thyroid Hormone Derivative as a Pleiotropic Agent for the Treatment of Alzheimer’s Disease
Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method | Science Advances
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
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
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![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
Glycation affects fibril formation of Aβ peptides - ScienceDirect
PDF) Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers | PNAS
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) Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
PDF) Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic A 42 aggregates linked with Alzheimers disease – topic of research paper in Biological sciences. Download scholarly
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. - Abstract - Europe PMC
Two decades of new drug discovery and development for Alzheimer's disease - RSC Advances (RSC Publishing) DOI:10.1039/C6RA26737H
Two decades of new drug discovery and development for Alzheimer's disease
Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease | Science Advances
PDF) Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease
PDF) Small molecule-mediated co-assembly of amyloid-β oligomers reduces neurotoxicity through promoting non-fibrillar aggregation
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 | PNAS
Moxifloxacin Disrupts and Attenuates Aβ42 Fibril and Oligomer Formation: Plausibly Repositioning an Antibiotic as Therapeutic against Alzheimer's Disease | ACS Chemical Neuroscience
A spiral microfluidic device for rapid sorting, trapping, and long-term live imaging of Caenorhabditis elegans embryos | Microsystems & Nanoengineering
IJMS | Free Full-Text | Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers
PDF) A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease
PDF) Delivery of Native Proteins into C. Elegans Using a Transduction Protocol Based on Lipid Vesicles
Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease | Science Advances
