ABSTRACT
We present VaxConcerns, a taxonomy for vaccine concerns and misinformation. VaxConcerns is an easy-to-teach taxonomy of concerns and misinformation commonly found among online anti-vaccination media and is evaluated to produce high-quality data annotations among crowdsource workers, opening the potential adoption of the framework far beyond just academic or medical communities. The taxonomy shows high agreement among experts and outperforms existing taxonomies for vaccine concerns and misinformation when presented to non-expert users. Our proof-of-concept study on the changes in anti-vaccination content during the COVID-19 pandemic indicate impactful future use cases, such as longitudinal studies of the shift in vaccine concerns over time.
Subject(s)
Crowdsourcing , Vaccines , Humans , Pandemics/prevention & control , Vaccines/adverse effects , Vaccination , CommunicationABSTRACT
SIGNIFICANCE: Collagen is the most abundant protein in vertebrates and is found in tissues that regularly experience tension, compression, and shear forces. However, the underlying mechanism of collagen fibril formation and remodeling is poorly understood. AIM: We explore how a collagen monomer is visualized using fluorescence microscopy and how its spatial orientation is determined. Defining the orientation of collagen monomers is not a trivial problem, as the monomer has a weak contrast and is relatively small. It is possible to attach fluorescence tags for contrast, but the size is still a problem for detecting orientation using fluorescence microscopy. APPROACH: We present two methods for detecting a monomer and classifying its orientation. A modified Gabor filter set and an automatic classifier trained by convolutional neural network based on a synthetic dataset were used. RESULTS: By evaluating the performance of these two approaches with synthetic and experimental data, our results show that it is possible to determine the location and orientation with an error of â¼37 deg of a single monomer with fluorescence microscopy. CONCLUSIONS: These findings can contribute to our understanding of collagen monomers interaction with collagen fibrils surface during fibril formation and remodeling.