Peruvian Food Chain Jenga: Learning Ecosystems with an Interactive Model

A pilot study was conducted on a multimodal educational tool, Peruvian Food Chain Jenga (PFCJ), with 5th‐grade students (N = 54) at a public charter school. The goal was to compare the effectiveness of the multimodal tool to a more traditional presentation of the same materials (food chain) using an experimental/control design. Data collection included a pretest/posttest and a “What I Did/What I Learned” response sheet. Quantitative analysis of pretest/posttest results showed both groups improved from pretest to posttest; however, there was no statistically significant difference between posttest results of experimental and control groups. Qualitative analysis of student open‐ended responses indicated a difference between students who used the PFCJ and students in the control. The most striking difference occurred in how the students perceived the connectedness of species and the awareness of human impact. Our findings suggest that using a model such as PFCJ as a means of teaching and connecting scientific content with practices related to ecosystems is an effective method of engaging students in intelligent discussions about these topics.     

Structure-Activity Relationship of NF023 Derivatives Binding to XIAP-BIR1

Inhibitors of Apoptosis Proteins (IAPs) are conserved E3-ligases that ubiquitylate substrates to prevent apoptosis and activate the NF-kB survival pathway, often deregulated in cancer. IAPs-mediated regulation of NF-kB signaling is based on the formation of protein complexes by their type-I BIR domains. The XIAP-BIR1 domain dimerizes to bind two TAB1 monomers, leading to downstream NF-kB activation. Thus, impairment of XIAP-BIR1 dimerization could represent a novel strategy to hamper cell survival in cancer. To this aim, we previously reported NF023 as a potential inhibitor of XIAP-BIR1 dimerization. Here we present a thorough analysis of NF023 binding to XIAP-BIR1 through biochemical, biophysical and structural data. The results obtained indicate that XIAP-BIR1 dimerization interface is involved in NF023 binding, and that NF023 overall symmetry and the chemical features of its central moiety are essential for an efficient interaction with the protein. Such strategy provides original hints for the development of novel BIR1-specific compounds as pro-apoptotic agents.     

Production of CoAl and CoAlCr FSMAs and determination of their thermal,microstructure, and magnetic properties

Journal of Thermal Analysis and Calorimetry - In this study, some thermal, mechanical, and magnetic properties of Co86Al14 and Co82Al14Cr4 (at.%) alloys have been investigated. The alloys were...