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Biology subjects

Hendricks, A.

Publications and source records attributed to Hendricks, A..

2 recordsLinked to original sources

SimMiL: Simulating Microbiome Longitudinal Data

0.Structured AbstractO_ST_ABSMotivationC_ST_ABSThe quantity of statistical tools designed for omics data analysis has grown rapidly with the ability to collect large sets of human health data, particularly longitudinal data sets. Most tools are assessed for performance using simulated datasets constructed to mimic a handful of relevant characteristics from real world data sets. Consequently, the simulated data sets, and their respective simulation frameworks, are too narrow in scope to qualify as a standard for assessment in longitudinal omics analyses. ResultsHere we present the flexible and accessible simulation framework and software package called SimMiL (Simulating Microbiome Longitudinal data) capturing three general components of longitudinal microbiome data: (i) absence/presence of microbes, (ii) individual microbe abundance, and (iii) microbiome community composition over time. The framework is assessed by replicating the Type I error and Power analyses of a broad range of statistical tools (MirKAT, repeated measures permANOVA, and a modified kernel association test). Software AvaliabilityThe simulation framework is at https://github.com/nweaver111/SimMiL

bioinformatics↗

Cell Surface β-Lactamase Recruitment: A Facile Selection to Identify Protein-Protein Interactions

Protein-protein interactions are central to many cellular processes, and the identification of novel protein-protein interactions is a critical step in the discovery of protein therapeutics. Simple methods to identify naturally existing or laboratory evolved protein-protein interactions are therefore valuable research tools. We have developed a facile selection that links protein-protein interaction-dependent {beta}-lactamase recruitment on the surface of E. coli with resistance to ampicillin. Bacteria displaying a protein which form a complex with a specific protein-{beta}-lactamase fusion are protected from ampicillin-dependent cell death. In contrast, bacteria that do not recruit {beta}-lactamase to the cell surface are killed by ampicillin. Given its simplicity and tunability, we anticipate this selection will be a valuable addition to the palette of methods for illuminating and interrogating protein-protein interactions.

biochemistry↗