Publications by authors named "I Sharon"

Article Synopsis
  • Metabolic interactions between bacteria in the rhizosphere impact plant-related functions and understanding these interactions can enhance microbial community functionality.
  • A new framework using genomics and modeling has been developed to study these interactions, focusing on bacteria in apple rhizospheres linked to disease outcomes.
  • This research enables the identification of specific microbial species and compounds that could either suppress or support diseases, providing insights for targeted manipulation of microbiomes across various environments.
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Autotrophy is the basis for complex life on Earth. Central to this process is rubisco-the enzyme that catalyzes almost all carbon fixation on the planet. Yet, with only a small fraction of rubisco diversity kinetically characterized so far, the underlying biological factors driving the evolution of fast rubiscos in nature remain unclear.

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Reversible genomic DNA inversions control the expression of numerous gut bacterial molecules, but how this impacts disease remains uncertain. By analyzing metagenomic samples from inflammatory bowel disease (IBD) cohorts, we identified multiple invertible regions where a particular orientation correlated with disease. These include the promoter of polysaccharide A (PSA) of Bacteroides fragilis, which induces regulatory T cells (Tregs) and ameliorates experimental colitis.

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Aim: The aim of this study was to test a moderated-mediation model, explaining how and under which circumstances a process- or an outcome-accountability focus affects performance.

Design: Randomized controlled design, using screen-based simulations.

Methods: Data were collected during 2021.

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Covering: 1878 to early 2023Cyanophycin is a biopolymer consisting of a poly-aspartate backbone with arginines linked to each Asp sidechain through isopeptide bonds. Cyanophycin is made by cyanophycin synthetase 1 or 2 through ATP-dependent polymerization of Asp and Arg, or β-Asp-Arg, respectively. It is degraded into dipeptides by exo-cyanophycinases, and these dipeptides are hydrolyzed into free amino acids by general or dedicated isodipeptidase enzymes.

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