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Previously, we demonstrated that nasal immunization with a genetically engineered strain in which capsule and O-antigen are no longer expressed (CP923) was immunogenic, generated antibodies that bound a subset of heterologous ExPEC strains, and enhanced neutrophil-mediated bactericidal activity against the homologous and a heterologous strain in vitro.
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Given the variety of engineering strategies afforded through nanoparticle technologies, a significant goal is to tailor nanoparticle surfaces to selectively bind a subset of biomarkers, sequestering them for later study using high sensitivity proteomic tests.
Ultra-low-dose opioid antagonists were initially thought to preferentially bind a subset of MORs [1], and a Gs-coupling MOR subpopulation was again recently proposed [9].
Interestingly, it has often been observed that exogenously added Aβ will selectively bind a subset of hippocampal neurons and neuroblastoma cells in culture [56], [57].
In WT cells, ScPif1 binds a subset of G4 motifs, and this subset is more likely to be associated with fork slowing and DNA breakage in its absence.
This lends further support for the notion that NKX2-5∆HD binds a subset of its off-targets via cofactors interacting with the YRD.
In line of this idea, Itoh et al. raised the possibility that PPARγ covalently binds a subset of fatty acids and that PPARγ can bind two ligand molecules at the same time [33].
If individual Obps bind a subset of odorants, it is reasonable to hypothesize, that in tissues with high Or and therefore odor-coding complexity such as the antennae, the Obp landscape would need to be similarly complex in order to bind the required range of odorants.
These antibodies also bound to a subset of heterologous ExPEC strains and enhanced neutrophil-mediated bactericidal activity against the homologous and a heterologous strain.
We show that the modulus of the solutions to this problem must approach its least upper bound along a subset of the boundary of the domain large enough so that its A-hull contains a subset of the original a large enough to force the same minimum norm.
PRC2 mediates transcriptional silencing via its H3K27me3 mark, which is either subsequently or independently bound by a subset of Polycomb repressor complex 1 (proteinrotein complexes, leading to further chromatin compaction and acting as a stable silencing mechanism [ 32, 33].
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com