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We postulated that CFTR participates in the regulation of eicosanoid release by direct interaction with a complex containing ANXA1, p11 and cPLA2α.
Interaction with a complex formed by uPA and its inhibitor PAI-1 induces cell surface down regulation and recycling of the receptor via the clathrin-coated pathway, a process dependent on the association to LRP-1.
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We found that the surface functional groups and the ligand density at the periphery of these QDs significantly dictated their interactions with a complex biological matrix called biofilm.
For example, the S100B protein induces a helical structure, while interaction with the Cdk2 cyclin A complex leads to an irregular ι-MoRF.
The increased expression of dynamin-1 might be explained by other mechanisms like its direct interaction with a chaperone complex reported to stabilize its level at the synapse49.
Therefore, one possible explanation for our results is that MAG signals via interaction with a multimeric complex containing both NgR1 and NgR2 receptors.
In general, a low cytoplasmic level of β-catenin is maintained through interaction with a protein complex consisting of adenomatous polyposis coli, Axin, PP2A, and GSK-3β (Ding et al. 2000).
A recent discovery that has major implications in the pathogenesis and therapy of gout is the demonstration that MSU crystals are capable of triggering IL-1β release by its interaction with a cytoplasmic complex called the 'inflammasome'inflammasome
In order to unravel the molecular mechanism underlying the observed effects of Abp1 knock down on axon development, we therefore tested the hypothesis of an indirect association with the Arp2/3 complex and of a potential activity modulation of the Arp2/3 complex by an Abp1 interaction with an Arp2/3 complex activator.
Upon interaction with a ligand, a complex cleavage process of the Notch receptor is initiated, resulting in the release of the intracellular c-terminal domain (approximately 110 kDa).
Interestingly, it has recently been shown that histone deacetylase 1, another class I histone deacetylase, which was considered to be exclusively nuclear, is present in a cytoplasmic protein complex by virtue of interaction with a cellular phosphatase complex [ 41].
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