Harvard Catalyst Profiles
Contact, publication, and social network information about Harvard faculty and fellows.
Open Source Software
to edit your profile (add a photo, awards, links to other websites, etc.)
Edit My Profile
My Person List (
Return to Top
Search Result Details
Back to Search Results
This page shows the details of why an item matched the keywords from your search.
One or more keywords matched the following items that are connected to
The influence of the central region containing residues 19-25 on the aggregation properties and secondary structure of Alzheimer's beta-amyloid peptide.
A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils.
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
Human anti-Aß IgGs target conformational epitopes on synthetic dimer assemblies and the AD brain-derived peptide.
Role of aromatic side chains in amyloid ß-protein aggregation.
Aggregation and metal-binding properties of mutant forms of the amyloid A beta peptide of Alzheimer's disease.
An improved method of preparing the amyloid beta-protein for fibrillogenesis and neurotoxicity experiments.
N-Terminal Extensions Retard Aß42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aß42.
The Aggregation Paths and Products of Aß42 Dimers Are Distinct from Those of the Aß42 Monomer.