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Our binding data demonstrate that HIV-1 envelope protein gp140 enters cells by protein receptor mediated interactions that are regulated by the conformational state of the gp140 at physiological environment (pH and temperature).
Notably, this competition is alleviated by interspersed cytidines, allowing strong U2AF65 binding in the presence of hnRNP C. Our iCLIP and in vitro binding data demonstrate that hnRNP C blocks U2AF65 from a large number of binding sites.
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In addition, our flow cytometry and DNA binding data demonstrated that DNA could specifically bind to sperm via mAb C from all tested species, from birds to mammals including human.
scatchard analysis of the binding data demonstrated that the cells bound between 4.5 and 27.5 fmol mg-1 protein with a KD ranging from 16 to 40 pM.
Unlike the results obtained with tubulin-binding agents (e.g., PTX), our data demonstrate that the binding of I-Trp to β-tubulin did not alter the dynamics of the microtubule.
These data demonstrate that binding of dTCF to the distal sites is necessary to inhibit dpp transcription.
Collectively, these data demonstrate that binding to the Fas receptor is required for the processing of hFasL by ADAM10.
Taken together, these data demonstrate that binding of antigens through one or more LysM sequences to nonliving, nonrecombinant bacterial particles can generate efficacious subunit vaccines.
Overall, our data demonstrate that binding of Coro1C to F-actin requires both residues in the β-propeller and in the unique region.
In vitro and in vivo data demonstrate that binding of E6 to p53, Bak, hMCM7, E6TP1, and c-myc is facilitated by the E3 ubiquitin ligase moiety, E6-AP [ 77, 78].
Overall these data demonstrate that SEC3 binding does not distinguish between peptide-loaded and peptide-free DR1.
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