Dynamic Contact Networks in Confined Spaces: Synthesizing Micro-Level Encounter Patterns through Human Mobility Models from Real-World Data.

This study advances the field of infectious disease forecasting by introducing a novel approach to micro-level contact modeling, leveraging human movement patterns to generate realistic temporal-dynamic networks. Through the incorporation of human mobility models and parameter tuning, this research presents an innovative method for simulating micro-level encounters that closely mirror infection dynamics within confined spaces. Central to our methodology is the application of Bayesian optimization for parameter selection, which refines our models to emulate both the properties of real-world infection curves and the characteristics of network properties.

High-throughput rapid amplicon sequencing for multilocus sequence typing of from archived clinical DNA samples.

Introduction: Spillover events of have devastating effects on the wild sheep populations. Multilocus sequence typing (MLST) is used to monitor spillover events and the spread of between the sheep populations. Most studies involving the typing of have used Sanger sequencing.

Discovery of the sEH Inhibitor Epoxykynin as a Potent Kynurenine Pathway Modulator.

Disease-related phenotypic assays enable unbiased discovery of novel bioactive small molecules and may provide novel insights into physiological systems and unprecedented molecular modes of action (MMOA). Herein, we report the identification and characterization of epoxykynin, a potent inhibitor of the soluble epoxide hydrolase (sEH). Epoxykynin was discovered by means of a cellular assay monitoring modulation of kynurenine (Kyn) levels in BxPC-3 cells upon stimulation with the cytokine interferon-γ (IFN-γ) and subsequent target identification employing affinity-based chemical proteomics.

FUBP1 is a general splicing factor facilitating 3' splice site recognition and splicing of long introns.

Splicing of pre-mRNAs critically contributes to gene regulation and proteome expansion in eukaryotes, but our understanding of the recognition and pairing of splice sites during spliceosome assembly lacks detail. Here, we identify the multidomain RNA-binding protein FUBP1 as a key splicing factor that binds to a hitherto unknown cis-regulatory motif. By collecting NMR, structural, and in vivo interaction data, we demonstrate that FUBP1 stabilizes U2AF2 and SF1, key components at the 3' splice site, through multivalent binding interfaces located within its disordered regions.