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Background and Purpose: The objectives of this study were to implement multiple active learning strategies in pharmacology and evaluate the most effective method to promote understanding., Educational Activity and Setting: A structured, student-centered learning approach was launched. The implemented active learning strategies were Kahoot web-based interactive games, crossword puzzles, an instructional video, a music video, and fill-in-the-blank tables. For three consecutive years, several topics in pharmacology were taught by the same instructor. While traditional teaching was used for the class of 2016, the above-mentioned active learning strategies were utilized for the classes of 2017 and 2018. Student perceptions on traditional teaching vs. active learning and on the different active learning methods were determined by anonymous survey. The effectiveness of active learning on understanding pharmacology concepts was detected by extracting student performance data from ExamSoft item analysis., Findings: Based on exam performance assessment, students in the classes of 2017 and 2018 performed significantly better when fill-in-the-blank activities and videos were utilized. However, students believed that web-based games helped them better understand concepts. Variables between the classes of 2016, 2017, and 2018 were minimized through comparison of the same lecture topics and having the same instructor write exam questions., Summary: Although students perceived Kahoot web-based interactive gaming as the most valuable active learning strategy, fill-in-the-blank activities and videos were more effective in understanding the pharmacology concepts as measured by their exam performance., (Copyright © 2019 Elsevier Inc. All rights reserved.)

BACKGROUND AND PURPOSE Receptor activity-modifying proteins (RAMPs) define the pharmacology of the calcitonin receptor-like receptor (CLR). The interactions of the different RAMPs with this class B GPCR yield high-affinity calcitonin gene-related peptide (CGRP) or adrenomedullin (AM) receptors. However, the mechanism for this is unclear. EXPERIMENTAL APPROACH Guided by receptor models, we mutated residues in the N-terminal helix of CLR, RAMP2 and RAMP3 hypothesized to be involved in peptide interactions. These were assayed for cAMP production with AM, AM2 and CGRP together with their cell surface expression. Binding studies were also conducted for selected mutants. KEY RESULTS An important domain for peptide interactions on CLR from I32 to I52 was defined. Although I41 was universally important for binding and receptor function, the role of other residues depended on both ligand and RAMP. Peptide binding to CLR/RAMP3 involved a more restricted range of residues than that to CLR/RAMP1 or CLR/RAMP2. E101 of RAMP2 had a major role in AM interactions, and F111/W84 of RAMP2/3 was important with each peptide. CONCLUSIONS AND IMPLICATIONS RAMP-dependent effects of CLR mutations suggest that the different RAMPs control accessibility of peptides to binding residues situated on the CLR N-terminus. RAMP3 appears to alter the role of speci?c residues at the CLR-RAMP interface compared with RAMP1 and RAMP2. [ABSTRACT FROM AUTHOR]