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Intermolecular FRET, i.e., protein-protein interactions between donor-labeled and acceptor-labeled proteins, either soluble or associated with membranes can be detected by using genetically expressed fluorescence proteins fused to the target protein pair of interest.
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Classical FRET imaging techniques for in vivo applications have been limited to the detection of intramolecular FRET interactions using genetically expressed biosensor constructs [ 19– 22].
These data provide information about cell growth and, by using genetically encoded fluorescent reporters, gene expression.
The role of human cytochrome P450 (CYP) in the metabolic activation of N-alkylnitrosamines was examined by Ames test using genetically engineered Salmonella typhimurium (S. typhimurium YG7108 cells expressing each form of human CYP together with human NADPH-cytochrome P450 reductase (OR).
Here we present, to our knowledge, the first structure function analysis of CTRP using genetically modified Plasmodium berghei parasites expressing mutant versions of the ctrp gene.
Using genetically labelled mouse myotubes that express yellow fluorescent protein, they observed that the combined chemical treatment induced cellularization, with approximately 10 15% of the myotube nuclei reverting to proliferating mononucleated cells.
Similar findings were obtained by another group using genetically engineered hESCs transplanted into guinea pig hearts.
Recent studies have attempted to dissect PDGFR-specific events using genetically defined mouse embryonic fibroblasts (MEFS) expressing PDGFRα, PDGFRβ, both or neither [ 20].
Using genetically engineered Escherichia coli strain HT115 to express dsRNA is an economical way to produce large quantities of dsRNA.
Interferon-α is produced by a recombinant DNA process using genetically engineered Escherichia coli.
While startup Hampton Creek approaches the problem by favoring plant protein over eggs, Clara Foods concentrates its efforts on liquid alternatives in a lab, using genetically modified yeast.
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