This growing collection consists of scholarly works authored by ASU-affiliated faculty, staff, and community members, and it contains many open access articles. ASU-affiliated authors are encouraged to Share Your Work in KEEP.

Displaying 1 - 2 of 2
Filtering by

Clear all filters

Modeling and leveraging intuitive theories to improve vaccine attitudes
Description

Much of the richness of human thought is supported by people’s intuitive theories—mental frameworks capturing the perceived structure of the world. But intuitive theories can sometimes contain and reinforce misconceptions, such as misconceptions about vaccine safety that discourage vaccination. We argue that addressing misconceptions requires awareness of the broader conceptual

Much of the richness of human thought is supported by people’s intuitive theories—mental frameworks capturing the perceived structure of the world. But intuitive theories can sometimes contain and reinforce misconceptions, such as misconceptions about vaccine safety that discourage vaccination. We argue that addressing misconceptions requires awareness of the broader conceptual contexts in which they are embedded. Here, we developed a cognitive model of the intuitive theory surrounding vaccination decisions. Using this model, we were able to make accurate predictions about how people’s beliefs would be revised in light of educational interventions, design an effective new intervention encouraging vaccination, and understand how these beliefs were affected by real-world events. This approach provides the foundation for richer understandings of intuitive theories and belief revision more broadly.

ContributorsPowell, Derek (Author) / Weisman, Kara (Author) / Markman, Ellen M. (Author)
Created2021
128975-Thumbnail Image.png
Description

Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex biological environment. The goal of these studies was to move

Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex biological environment. The goal of these studies was to move a step beyond detection and into the relative quantification of Cys-SOH within specific proteins found in a complex biological setting--namely, human plasma.

Results: This report describes the possibilities and limitations of performing such analyses based on the use of thionitrobenzoic acid and dimedone-based probes which are commonly employed to trap Cys-SOH. Results obtained by electrospray ionization-based mass spectrometric immunoassay reveal the optimal type of probe for such analyses as well as the reproducible relative quantification of Cys-SOH within albumin and transthyretin extracted from human plasma--the latter as a protein previously unknown to be modified by Cys-SOH.

Conclusions: The relative quantification of Cys-SOH within specific proteins in a complex biological setting can be accomplished, but several analytical precautions related to trapping, detecting, and quantifying Cys-SOH must be taken into account prior to pursuing its study in such matrices.

ContributorsRehder, Douglas (Author) / Borges, Chad (Author) / Biodesign Institute (Contributor)
Created2010-07-01