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Scanning and transmission electron microscopic analyses showed that the dispersed phase consist of mainly few layered graphene nanoflakes.
Unexpectedly, light microscopic analyses showed a dramatic loss of the dendrites themselves and immunofluorescence revealed that cytoskeletal elements crucial for the formation and maintenance of dendrites are disrupted in viral Ag-positive cells.
Immunodepletion, subcellular fractionation, and confocal microscopic analyses showed that the HGF-induced C/EBP DNA binding activity depended on nuclear translocation of C/EBPβ.
Transmission electron microscopic analyses showed that HPC moxifloxacin conjugates self-assembled into nanowires of ∼30 nm diameters while HEC moxifloxacin conjugates self-assembled into nanoparticles of 150 350 nm.
Gross and light microscopic analyses showed corneal decompensation and vascularization, peripheral anterior and posterior synechiae, iris thinning, significant changes in the iris pigmented layer, fibrous tissue on the anterior surface of the iris, and Soemmerring ring formation in the periphery of capsular bag remnants.
Immunofluorescence confocal microscopic analyses showed that a substantial population of endogenous Trak1 was localized to MitoTracker-labeled mitochondria in control cells (Fig. 1B).
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Electron microscopic analyses show that the core 3′ processing complex has a distinct "kidney" shape and is ∼250 Å in length.
This observation correlates with CFU determinations and fluorescence microscopic analyses shown in Figure 4. Despite the increased bacterial load, the intestinal barrier of LF82-infected nematodes appeared normal with intact terminal web and apical microvilli (Figure 5B).
The microscopic and spectroscopic analyses showed varying amounts of hydration products (primarily calcium hydroxide and calcium silicate hydrate) in the presence of coal fly ash, signifying the influence of pozzolanic reaction.
Our microscopic and genetic analyses showed that such a faint sheen might represent a wide spectrum of organisms, including nematodes.
Microscopic and ChIP analyses showed that the HACs remained mitotically stable and capable of recruiting inner and outer kinetochore proteins CENP-A, -C, -T, hKNL1, Hec1, hDsn1 and hMis12 (Supplementary Figure S9A, B) in the absence of bound exogenous HAT fusion proteins.
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