Radicalized beliefs, such as those tied to QAnon, Russiagate, and other political conspiracy theories, can lead some individuals and groups to engage in violent behavior, as evidenced in recent months. Understanding the mechanisms by which such beliefs are accepted, spread, and intensified is critical for any attempt to mitigate radicalization and avoid increased political polarization. This article presents and agent-based model of a social media network that enables investigation of the effects of censorship on the amount of dissenting information to which agents become exposed and the certainty of their radicalized views. The model explores two forms of censorship: 1) decentralized censorship-in which individuals can choose to break an online social network tie (unfriend or unfollow) with another individual who transmits conflicting beliefs and 2) centralized censorship-in which a single authority can ban an individual from the social media network for spreading a certain type of belief. This model suggests that both forms of censorship increase certainty in radicalized views by decreasing the amount of dissent to which an agent is exposed, but centralized "banning" of individuals has the strongest effect on radicalization.
We argue that “ecological integrity” is a bad fit as a value for conservation biology and restoration ecology. Both fields are organized around shared values, but it is important to be clear about the specific values and reasons motivating protection of or interventions in specific ecosystems. In practice, appeals to ecological integrity often fail to account for losses in value when ecosystems change. Ultimately, we do not believe ecosystems are the kinds of things that have integrity. Ecosystems are simply too dynamic in space and time, their complex interconnections, including coevolved relationships, ultimately fleeting at the geological scale. Any impression of “wholeness” is an artifact of the brevity of human lives and the shallowness of our historical records. We believe “ecological integrity” as it is currently used is typically a proxy for the values of diversity, complexity, and cultural connections with beloved ecosystem states. We should simply say what we mean and retire the concept of “ecological integrity.”
One hundred sixty years after its discovery, the molecular mechanism of general anesthesia remains a notable mystery. A very wide range of agents ranging from the element xenon to steroids can act as general anesthetics on all animals from protozoa to man, suggesting that a basic cellular mechanism is involved. In this paper, we show that volatile general anesthetics cause large changes in electron spin in Drosophila fruit flies and that the spin responses are different in anesthesia-resistant mutants. We propose that anesthetics perturb electron currents in cells and describe electronic structure calculations on anesthetic–protein interactions that are consistent with this mechanism and account for hitherto unexplained features of general anesthetic pharmacology.
Since 2014, clade 126.96.36.199 has become the dominant epidemic branch of the Asian lineage H5 subtype highly pathogenic avian influenza virus (HPAIV) in southern and eastern China, while the H5N6 subtype is the most prevalent. We have shown earlier that lack of glycosylation at position 158 of the hemagglutinin (HA) glycoprotein due to the T160A mutation is a key determinant of the dual receptor binding property of clade 188.8.131.52 H5NX subtypes. Our present study aims to explore other effects of this site among H5N6 viruses. Here we report that N-linked glycosylation at site 158 facilitated the assembly of virus-like particles and enhanced virus replication in A549, MDCK, and chicken embryonic fibroblast (CEF) cells. Consistently, the HA-glycosylated H5N6 virus induced higher levels of inflammatory factors and resulted in stronger pathogenicity in mice than the virus without glycosylation at site 158. However, H5N6 viruses without glycosylation at site 158 were more resistant to heat and bound host cells better than the HA-glycosylated viruses. H5N6 virus without glycosylation at this site triggered the host immune response mechanism to antagonize the viral infection, making viral pathogenicity milder and favoring virus spread. These findings highlight the importance of glycosylation at site 158 of HA for the pathogenicity of the H5N6 viruses.