Influence of dendrimer’s structure on its activity against amyloid fibril formation

Starburst Dendrimers: Molecular‐Level Control of Size, Shape, Surface Chemistry, Topology, and Flexibility from Atoms to Macroscopic Matter

Donald A. Tomalia, Adel M. Naylor, William A. Goddard · Angewandte Chemie International Edition in English · 1990 · 3.2K citations

Supramolecular Assembly, Abstract Starburst Dendrimers, Engineering +19

Thioflavine T interaction with synthetic Alzheimer's disease <i>β</i>‐amyloid peptides: Detection of amyloid aggregation in solution

Harry LeVine · Protein Science · 1993 · 2.2K citations · Full text

Poly(amidoamine) (PAMAM) dendrimers: from biomimicry to drug delivery and biomedical applications

Roseita Esfand, Donald A. Tomalia · Drug Discovery Today · 2001 · 1.5K citations

Nanomedicine, Polymer Chemistry, Engineering +7

The binding of thioflavin-T to amyloid fibrils: localisation and implications

Mark R.H. Krebs, Elizabeth H. C. Bromley, Athene M. Donald · Journal of Structural Biology · 2004 · 731 citations · Full text

Biochemistry, Protein Folding, Natural Sciences +3

Physical, Morphological and Functional Differences between pH 5.8 and 7.4 Aggregates of the Alzheimer's Amyloid Peptide A β

Stephen Wood, Beverly E. Maleeff, Timothy K. Hart et al. · Journal of Molecular Biology · 1996 · 338 citations

Neurodegenerative Diseases, Alzheimer's Disease, Functional Differences +8