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Despite the widespread conviction that the mass media tend to "blow risks out of proportion," the question has received little systematic attention. The mass-media literature also presents the opposite argument, namely that the media minimize the kinds of reporting that might upset largescale capitalistic industries. Still other perspectives hold, on the one hand, that media reports tend to have more subtle anti-technology effects, created by "even-handed'' coverage and on the other hand, that reporters give "establishment" figures the opportunity to "keynote" or "put the facts in perspective" in ways that exert a subtly pro-technology effect. Drawing on a systematic sample of 128 hazard events developed by researchers at another university and factually summarized by LEXIS-NEXIS, we analyze the effects of emotionalism on actual levels of coverage; a variety of analyses show that the only variables to exert significant effects are those that involve objective information, such as the number of casualties or the level of damage created. Given the argument that the effects of emotionalism can be conveyed in ways that are largely independent of the facts, e.g., by headlines, photographs, and "loaded" words, we next compare the emotionalism conveyed by factual summaries vs. the original stories and headlines. Even for incidents involving nuclear andor toxic hazards, we find the net effect of the full stories is to lessen the emotionalism. Overall, the hypothesis receiving strongest support is that the "keynoting" helps create an overall impression that the "responsible authorities" are acting more responsibly than might be assumed on the basis of factual summaries alone. The widespread impression within the technical community, while understandable, may well have as much to do with the selective perceptions of scientists and engineers as with the actual pattern of media reporting.In the positive vein, there were a number of thoughtful, knowledgeable editorials, and the editor of one local paper was certainly well informed and played an important role. On the negative side, some reporters were not excessively concerned with validation of information. Words that instill dread were 31 0272-4332/96/0200-0031S09.50/1 0 I996 Society for Risk Analysts 32 Freudenburg, Coleman, Gonzales, and Helgeland prominent--chcmical waste dump, deadly PCB, dioxin, birth defects, poison plant, like an atom bomb, spew. Reporters know that fear has a high potential to entertain. The activities of positive local leaders were rarely seen as newsworthy, while negative voices received disproportionate media attention.'*'

dimers of dimers), and these low-level associations will be demonstrated. These results provide additional insight into the regulation of heterodimers of tubulin from different biological sources, suggesting that monomer exchange may contribute to the sorting of aand b-tubulin monomers that associate following tubulin folding, and that dimer -dimer association may form species important for further polymerization.

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pathways. in recent years, in vivo studies have shown that the protein Histidine triad nucleotide-binding protein 1 (HINT1) inhibits the ubiquitylation activity of various SCF ligases that regulate the NF-kB signaling pathway and cell cycle progression by promoting the degradation of substratesIkBa and p27 Kip1 , respectively. However, the mechanism of interaction between HINT1 and SCF ligases and how HINT1 causes their inhibition is not understood. Many questions remain unanswered such as the specific binding partner of HINT1 within the SCF complex and how HINT1 is able to inhibit the activity of unique SCF ligases. in total, the 173 kDa SCF ligase complex consists of a scaffolding protein, Cullin1 (90 kDa), that utilizes Rbx1 (12 kDa) to recruit E2 ubiquitin conjugating enzymes (e.g. UBE2D2) and substrates through the adaptor and substrate receptor proteins, Skp1 (17 kDa) and b-TrCP1 (54 kDa) respectively, to promote substrate ubiquitylation. Through co-elution in gel-filtration chromatography, I have assembled the SCF E3 ligase that ubiquitylates IkBa and have demonstrated that HINT1 (28 kDa) binds to this ligase. I have performed biochemical experiments to measure ubiquitylation combined with HDX-MS and other biophysical experiments to characterize the binding affinity and the specific binding interface of HINT1 on the SCF E3 ligase. The results shed light on the molecular mechanism of inhibition of SCF E3 ligases by HINT1.