✦ LIBER ✦

Specific binding of the alzheimer βA4 amyloid precursor to collagen, laminin, and heparin

✍ Scribed by Gerd Multhaup; Ashley I. Bush; Peter Pollwein; Colin L. Masters; Konrad Beyreuther

Publisher: Springer
Year: 1992
Tongue: English
Weight: 239 KB
Volume: 11
Category: Article
ISSN: 1573-4943
DOI: 10.1007/bf01673756

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Laminin inhibition of β-amyloid protein

Laminin inhibition of β-amyloid protein (Aβ) fibrillogenesis and identification of an Aβ binding site localized to the globular domain repeats on the laminin a chain

✍ Gerardo M. Castillo; Widia Lukito; Elaine Peskind; Murray Raskind; Daniel A. Kir 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 257 KB

␤-Amyloid protein (A␤) is a major component of neuritic plaques and cerebrovascular amyloid deposits in the brains of patients with Alzheimer's disease (AD). Inhibitors of A␤ fibrillogenesis are currently sought as potential future therapeutics for AD and related disorders. In the present study, the

Is the binding of β-amyloid protein to a

Is the binding of β-amyloid protein to antichymotrypsin in Alzheimer plaques mediated by a β-strand insertion?

✍ Christine M. Lukacs; David W. Christianson 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 606 KB

A growing body of experimental evidence demonstrates that the serpin antichymotrypsin plays a regulatory role in Alzheimer plaque physiology by interacting with the 42 residue p-amyloid protein, and we have used molecular modeling and energy minimization techniques to study this interaction. Based o