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Figure 1 ETS domain secondary structure.
The Munc18b promoter is controlled by INR (initiator), Sp1 (specificity protein 1), Ets, CRE (cAMP-response element), GRE (glucocorticoid-response element), GATA and E-box elements in airway epithelial cells; however, protein levels did not change during mucous metaplasia induced by allergic inflammation.
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In the present study we use a computational approach complimented by steady-state kinetic experiments to extend our understanding further to elucidate a more detailed model for the binding of residues 1 138 of Ets-1 (Ets) to ERK2.
The transcription factor v-ets erythroblastosis virus E26 oncogene homolog 1 (Ets-1) is a member of the Ets family that contains a unique DNA binding domain, the Ets domain.
Specifically we address the roles of E26 transformation specific oncogene homolog 1 (Ets-1); Krüppel-like factor 8 (KLF8); nuclear factor kappa-light-chain-enhancer of activated B (NF- κB); NF-E2-related factor 2 (Nrf2); specificity protein 1 (Sp1) and specificity protein 3 (Sp3); and signal transducer and activator of transcription 3 (STAT-3).
Using a docking-based approach, we screened entire libraries of all possible di- and tri-peptides against the Elk-1 ETS domain, targeting the stability region of the domain identified by Shaw et al [21].
However, Saven et al. [23] performed molecular dynamics (MD) simulations of a single Elk-1 ETS domain taken from the dimeric structure.
Interactions between two Elk-1 ETS domains were calculated using the LIGPLOT program [51].
We have conducted molecular dynamics simulations of the Elk-1 ETS domain followed by virtual screening.
(a) An Elk-1 ETS domain bound to its DNA recognition sequence.
(b) An Elk-1 ETS domain dimer complex, showing the α1β1 loops providing the interface.
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