3D Modeling of the Magnetization of Superconducting Rectangular-Based Bulks and Tape Stacks

In recent years, numerical models have become popular and powerful tools to investigate the electromagnetic behavior of superconductors. One domain where this advances are most necessary is the 3D modeling of the electromagnetic behavior of superconductors. For this purpose, a benchmark problem consisting of superconducting cube subjected to an AC magnetic field perpendicular to one of its faces has been recently defined and successfully solved. In this work, a situation more relevant for applications is investigated: a superconducting parallelepiped bulk with the magnetic field parallel to two of its faces and making an angle with the other one without and with a further constraint on the possible directions of the current. The latter constraint can be used to model the magnetization of a stack of high-temperature superconductor tapes, which are electrically insulated in one direction. For the present study three different numerical approaches are used: the Minimum Electro-Magnetic Entropy Production (MEMEP) method, the $H$-formulation of Maxwell's equations and the Volume Integral Method (VIM) for 3D eddy currents computation. The results in terms of current density profiles and energy dissipation are compared, and the differences in the two situations of unconstrained and constrained current flow are pointed out. In addition, various technical issues related to the 3D modeling of superconductors are discussed and information about the computational effort required by each model is provided. This works constitutes a concrete result of the collaborative effort taking place within the HTS numerical modeling community and will hopefully serve as a stepping stone for future joint investigations

Proton-gated coincidence detection is a common feature of GPCR signaling

Abstract The evolutionary expansion of G protein-coupled receptors (GPCRs) has produced a rich diversity of transmembrane sensors for many physical and chemical signals. In humans alone, over 800 GPCRs detect stimuli such as light, hormones, and metabolites to guide cellular decision making primarily using intracellular G protein signaling networks. This diversity is further enriched by GPCRs that function as molecular logic gates capable of discerning multiple inputs to transduce cues encoded in complex, context-dependent signals. Here, we show that many GPCRs are switch-like Boolean-gated coincidence detectors that link proton (H+) binding to GPCR signaling. Using a panel of 28 receptors, covering 280 individual GPCR-Gα coupling combinations, we show that H+ gating both positively and negatively modulates and controls GPCR signaling. Notably, these observations extend to all modes of GPCR pharmacology including ligand efficacy, potency, and cooperativity. Additionally, we show that GPCR antagonism and constitutive activity are regulated by H+ gating and report the discovery of a new acid sensor, the adenosine A2a receptor (ADORA2A), which can be activated solely by acidic pH. Together, these findings establish a new paradigm for GPCR biology and pharmacology in acidified microenvironments such as endosomes, synapses, tumors, and ischemic vasculature. Competing Interest Statement The authors have declared no competing interest

ATS Core Curriculum 2020. Adult Pulmonary Medicine

The American Thoracic Society Core Curriculumupdates clinicians annually in adult and pediatric pulmonary disease, medical critical care, and sleep medicine in a 3- to 4-year recurring cycle of topics. The topics of the 2020 Pulmonary Core Curriculum include pulmonary vascular disease (submassive pulmonary embolism, chronic thromboembolic pulmonary hypertension, and pulmonary hypertension) and pulmonary infections (community-acquired pneumonia, pulmonary nontuberculous mycobacteria, opportunistic infections in immunocompromised hosts, and coronavirus disease [COVID-19]). Copyright © 2020 by the American Thoracic Society.Open access journalThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at [email protected]