Is Your Product Really Green? A Content Analysis to Reassess Green Advertising

This article investigates the changes in green advertising by conceptually replicating and extending Carlson, Grove, and Kangun's 1993 study. A content analysis of 433 unique ads from 18 magazine titles published in 2009 and 2010 demonstrates that advertisers attempted to address growing public concern for the environment and the demand for green products and services as emerge from the analyses of the ads' target, objective, and the executional elements. Contrary to Carlson, Grove, and Kangun's findings, the majority of environmental claims were deemed acceptable, implying a trend toward more trustworthy and reliable green advertising

Measuring Activity in the Ubiquitin–Proteasome System: From Large Scale Discoveries to Single Cells Analysis

The ubiquitin proteasome system (UPS) is the primary pathway responsible for the recognition and degradation of misfolded, damaged, or tightly regulated proteins in addition to performing essential roles in DNA repair, cell cycle regulation, cell migration, and the immune response. While traditional biochemical techniques have proven useful in the identification of key proteins involved in this pathway, the implementation of novel reporters responsible for measuring enzymatic activity of the UPS have provided valuable insight into the effectiveness of therapeutics and role of the UPS in various human diseases such as multiple myeloma and Huntington’s disease. These reporters, usually consisting of a recognition sequences fused to an analytical handle, are designed to specifically evaluate enzymatic activity of certain members of the UPS including the proteasome, E3 ubiquitin ligases, and deubiquitinating enzymes (DUBs). This review highlights the more commonly used reporters employed in a variety of scenarios ranging from high-throughput screening of novel inhibitors to single cell microscopy techniques measuring E3 ligase or proteasome activity. Finally, recent work is presented highlighting the development of novel degron-based substrate designed to overcome the limitations of current reporting techniques in measuring E3 ligase and proteasome activity in patient samples