Pandemics, policy, and pluralism: A Feyerabend-inspired perspective on COVID-19.

We analyse insufficient epistemic pluralism and associated problems in science-based policy advice during the COVID-19 pandemic drawing on specific arguments in Paul Feyerabend's philosophy. Our goal is twofold: to deepen our understanding of the epistemic shortcomings in science-based policy during the pandemic, and to assess the merits and problems of Feyerabend's arguments for epistemic pluralism as well as their relevance for policy-making. We discuss opportunities and challenges of integrating a plurality of viewpoints from within and outside science into policy advice thus contributing to discussions about normative issues concerning evidence and expertise in policy-making.

The COVID-19 pandemic: a case for epistemic pluralism in public health policy.

This paper uses the example of the COVID-19 pandemic to analyse the danger associated with insufficient epistemic pluralism in evidence-based public health policy. Drawing on certain elements in Paul Feyerabend's political philosophy of science, it discusses reasons for implementing more pluralism as well as challenges to be tackled on the way forward.

Failure in Science and Why It Is a Good Thing.

Stuart Firestein's book Failure: Why Science Is So Successful (2015) presents an image of science that includes failure in its diverse forms as an essential feature of scientific practice. Firestein makes it clear that failure is a frequently underappreciated component in popular as well as professional accounts of scientific knowledge production. This review essay provides an analysis of Firestein's considerations from a philosophical perspective and assesses its quality and originality as a contribution to the age-old philosophical question of what science is and how it works.

Risk, Uncertainty and Precaution in Science: The Threshold of the Toxicological Concern Approach in Food Toxicology.

Environmental risk assessment is often affected by severe uncertainty. The frequently invoked precautionary principle helps to guide risk assessment and decision-making in the face of scientific uncertainty. In many contexts, however, uncertainties play a role not only in the application of scientific models but also in their development. Building on recent literature in the philosophy of science, this paper argues that precaution should be exercised at the stage when tools for risk assessment are developed as well as when they are used to inform decision-making. The relevance and consequences of this claim are discussed in the context of the threshold of the toxicological concern approach in food toxicology. I conclude that the approach does not meet the standards of an epistemic version of the precautionary principle.

Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide.

The multifunctional Ewing Sarcoma (EWS) protein, a member of a large family of RNA-binding proteins, is extensively asymmetrically dimethylated at arginine residues within RGG consensus sequences. Using recombinant proteins we examined whether type I protein arginine methyltransferase (PRMT)1 or 3 is responsible for asymmetric dimethylations of the EWS protein. After in vitro methylation of the EWS protein by GST-PRMT1, we identified 27 dimethylated arginine residues out of 30 potential methylation sites by mass spectrometry-based techniques (MALDI-TOF MS and MS/MS). Thus, PRMT1 recognizes most if not all methylation sites of the EWS protein. With GST-PRMT3, however, only nine dimethylated arginines, located mainly in the C-terminal region of EWS protein, could be assigned, indicating that structural determinants prevent complete methylation. In contrary to previous reports this study also revealed that trypsin is able to cleave after methylated arginines. Pull-down experiments showed that endogenous EWS protein binds efficiently to GST-PRMT1 but less to GST-PRMT3, which is in accordance to the in vitro methylation results. Furthermore, methylation of a peptide containing different methylation sites revealed differences in the site selectivity as well as in the kinetic properties of GST-PRMT1 and GST-PRMT3. Kinetic differences due to an inhibition effect of the methylation inhibitor S-adenosyl-L-homocysteine could be excluded by determining the corresponding K(i) values of the two enzymes and the K(d) values for the methyl donor S-adenosyl-L-methionine. The study demonstrates the strength of MS-based methods for a qualitative and quantitative analysis of enzymic arginine methylation, a posttranslational modification that becomes more and more the object of investigations.