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Aviram Rasouly

Researcher at New York University

Publications -  19
Citations -  517

Aviram Rasouly is an academic researcher from New York University. The author has contributed to research in topics: RNA polymerase & Heat shock protein. The author has an hindex of 10, co-authored 17 publications receiving 436 citations. Previous affiliations of Aviram Rasouly include Tel Aviv University.

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Rates and mechanisms of bacterial mutagenesis from maximum-depth sequencing

TL;DR: This work directly measures locus-specific mutation rates in Escherichia coli and shows that they vary across the genome by at least an order of magnitude, and suggests specific mechanisms of antibiotic-induced mutagenesis, including downregulation of mismatch repair via oxidative stress, transcription–replication conflicts, and, in the case of fluoroquinolones, direct damage to DNA.
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Structure of RNA polymerase bound to ribosomal 30S subunit.

TL;DR: Cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit provide a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation.
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Light affects motility and infectivity of Agrobacterium tumefaciens.

TL;DR: Proteomics analyses revealed a significant reduction of FlaA and FlaB - proteins of the flagellum - when the cells were grown in light, which reduced the attachment of A. tumefaciens to tomato roots and the virulence of the bacteria in a cucumber infection assay.
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YbeY, a Heat Shock Protein Involved in Translation in Escherichia coli

TL;DR: Evidence is provided that YbeY, a conserved heat shock protein with unknown function, is involved in the translation process and is an important factor for bacterial translation even at 37 degrees C but becomes essential at high temperatures.
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The Heat Shock Protein YbeY Is Required for Optimal Activity of the 30S Ribosomal Subunit

TL;DR: In vitro activity of the translation machinery of the ybeY deletion mutants is significantly lower than that of the wild type, and the lower efficiency is due to impaired 30S small ribosomal subunits.