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TIM family proteins exhibit a classical type I membrane protein structure with an N-terminal immunoglobulin variable Ig-like (Ig V) domain, a heavily O-linked-glycosylated mucin-like domain (MLD) and a short C-terminal cytoplasmic tail (Freeman et al., 2010).
It is interesting to note that WT MEF exhibit a classical polarized phenotype, whereas MEFs not expressing Stat3 display a non-polarized phenotype very similar to the one of NIH3T3-derived transformed foci.
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CdMT3 MMP exhibits a classical MMP-fold with similarity to MT1-MMP.
It exhibits a classical low-temperature behavior, with the appearance of a cool flame and a negative temperature coefficient region.
However, we have seen in Sect. 4 that the deterministic dynamics for neural fields frequently exhibits a classical bistable structure with a saddle-state between stable equilibria.
Our observations are intriguing as epithelial cells exhibiting a classical polygonal morphology are believed to achieve intercellular interactions via specialized junctions [29] and have not been reported to exhibit extensive protrusive activity; thus the dynamic protrusive activity that we are observing is novel.
As expected, Dex exhibited a classical dose-dependent inhibition of T-cell proliferation.
Σ1278b exhibits a classical form of decaying oscillations characterized by a large cAMP peak immediately after the stimulus, and dampening oscillations towards a new steady state.
Pure DPPC exhibited a classical endotherm similar to that described in the literature (25): an endothermic pre-transition at 36°C followed by the main transition at 41.5°C.
To redress this, we have shown that compared with macrophages taken from a peritonitis that progressed to systemic inflammation and that exhibited a classical M1 phenotype, macrophages harvested from the resolving phase of acute peritonitis possess a unique phenotype.
SAL1 exhibits a classical structure of lipocalins characterized by a fully conserved N-terminal -G-X-W motypical the typical folding pattern of a nine-stranded antiparallel β-barrel forming an internal ligand binding site for small hydrophobic molecules [ 12], despite relatively low sequence similarity [ 13].
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