Journal: British journal of pharmacology

Article Title: Quantitative assessment of oligomeric amyloid β peptide binding to α7 nicotinic receptor.

doi: 10.1111/bph.14688

Figure Lengend Snippet: FIGURE 3 Effect of well‐characterized compounds on the Aβ/α7nAChR interaction. Competition for Aβ1–42‐FAM binding to Tb‐ SNAP‐α7nAChR by non‐labelled Aβ1–42 (reference, dotted line) and by the compounds (a) S24795 (n = 5), (b) PNU‐282987 (n = 5), (c) EVP‐6124 (n = 5), (d) S65050 (n = 5), (e) anti‐ Aβ antibody (20 μg·ml−1; n = 5), by the α7nAChR type II PAM (f) PNU‐120596 (n = 5) and type I PAM (g) NS1738 (n = 4); (h) model of the α7nAChR homo‐pentamer illustrating the localization of the orthosteric binding site, the proposed allosteric binding sites for NS1738 and PNU‐120596, and the binding site of the channel blocker mecamylamine (adapted from Corradi & Bouzat, 2016; Spurny et al., 2015). All data are expressed as mean ± SEM

Article Snippet: Epibatidine, α‐bungarotoxin, methyllycaconitine, PNU‐282987, PNU‐120596, and NS1738 were purchased from Tocris Bioscience (Bristol, UK).

Techniques: Binding Assay

Journal: Pharmacological Reviews

Article Title: More than Smoke and Patches: The Quest for Pharmacotherapies to Treat Tobacco Use Disorder

doi: 10.1124/pr.119.018028

Figure Lengend Snippet: Positive allosteric modulators of neuronal nAChRs and studies investigating them as pharmacotherapies for tobacco use disorder

Article Snippet: In this study, it was found that NS1738 has three theoretical binding sites ( Kuang et al., 2016 ).

Techniques: Activity Assay, In Vivo