The Benefits of a Real-Time Web-Based Response System for Enhancing Engaged Learning in Classrooms and Public Science Events.

Large introduction to neuroscience classes and small science cafés have the same goal: bridging the gap between the presenter and the audience to convey the information while being engaging. Early classroom response systems became the cornerstone of flipped and engaged learning. These "clickers" helped turn lectures into dialogues, allowing the presenter to become a facilitator rather than a "sage on the stage." Rapid technological developments, especially the increase of computing power opened up new opportunities, moving these systems from a clicker device onto cellphones and laptops. This allowed students to use their own devices, and instructors to use new question types, such as clicking on a picture or ranking concepts. A variety of question types makes the learning environment more engaging, allows better examples for creative and critical thinking, and facilitates assessment. Online access makes these response systems scalable, bringing the strength of formative assessments and surveys to public science communication events, neuroscience journal clubs and distance learning. In addition to the new opportunities, online polling systems also create new challenges for the presenters. For example, allowing mobile devices in the classroom can be distracting. Here, a web-based, real-time response system called Poll Everywhere was compared to iClickers, highlighting the benefits and the pitfalls of both systems. In conclusion, the authors observe that the benefits of web-based response systems outweigh the challenges, and this form of digital pedagogy can help create a rich dialogue with the audience in large classrooms as well as in public science events.

Survey of phosphorylation near drug binding sites in the Protein Data Bank (PDB) and their effects.

While it is currently estimated that 40 to 50% of eukaryotic proteins are phosphorylated, little is known about the frequency and local effects of phosphorylation near pharmaceutical inhibitor binding sites. In this study, we investigated how frequently phosphorylation may affect the binding of drug inhibitors to target proteins. We examined the 453 non-redundant structures of soluble mammalian drug target proteins bound to inhibitors currently available in the Protein Data Bank (PDB). We cross-referenced these structures with phosphorylation data available from the PhosphoSitePlus database. Three hundred twenty-two of 453 (71%) of drug targets have evidence of phosphorylation that has been validated by multiple methods or labs. For 132 of 453 (29%) of those, the phosphorylation site is within 12 Å of the small molecule-binding site, where it would likely alter small molecule binding affinity. We propose a framework for distinguishing between drug-phosphorylation site interactions that are likely to alter the efficacy of drugs versus those that are not. In addition we highlight examples of well-established drug targets, such as estrogen receptor alpha, for which phosphorylation may affect drug affinity and clinical efficacy. Our data suggest that phosphorylation may affect drug binding and efficacy for a significant fraction of drug target proteins.