Chemical and structural characterization of hemicellulose from date fruits (<i>Phoenix dactylifera</i> L.). [PDF]
Okonkwo CE +7 more
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Shaken batch cultures of <i>Pseudomonas aeruginosa</i> contain biofilm-like heterogeneity. [PDF]
Fritz BG +6 more
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Proposal of <i>Limosilactobacillus secundus</i> sp. nov., <i>Limosilactobacillus reuteri</i> subsp. <i>pararodentium</i> subsp. nov., <i>Limosilactobacillus reuteri</i> subsp. <i>peregrinus</i> subsp. nov. and <i>Limosilactobacillus reuteri</i> subsp. <i>simiae</i> subsp. nov., isolated from the gastrointestinal tract of vertebrate hosts. [PDF]
Guo X +6 more
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Protocol for condensate-based stabilization of gene circuit dynamics under growth-mediated dilution in E. coli. [PDF]
Zhang R, Tian XJ.
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An engineered bacterial symbiont maps micron-scale sugar gradients in the honeybee gut
Chhun A +7 more
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Programmable bacterial adhesion to plastic surfaces for enhanced biodegradation
Schneier A +3 more
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A green fluorescent protein for live imaging in hyperthermophiles
Kuo Y +9 more
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Arabinose C Protein: Regulation of the Arabinose Operon in vitro
Nature New Biology, 1971The detection of the gene ara C protein using a DNA-dependent in vitro protein synthesizing system represents the first isolation of an operon specific positive regulator with an in vivo role that has been genetically defined.
J, Greenblatt, R, Schleif
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An l-arabinose binding protein and arabinose permeation in Escherichia coli
Journal of Molecular Biology, 1969Abstract A search was made for proteins of the arabinose system which bind arabinose, as it is expected that the permease and possibly the C protein could be identified by arabinose binding. One protein was found and this is most probably part of the arabinose permease. It is inducible, can be removed from cells by osmotic shock and easily purified,
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AraC protein, which regulates expression of the l-arabinose operon in Escherichia coli, is a dimer whose DNA binding affinity for pairs of DNA half-sites is controlled by arabinose. Here we have addressed the question of whether the arabinose response of AraC requires the binding of one or two molecules of arabinose.
Michael E, Rodgers, Robert, Schleif
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