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The association of Ring1b to actively transcribed genes is consistent with global and candidate-based binding studies that show overlap between PcG and RNAPII occupancy or association of PcG proteins with expressed genes in mouse and human ES cells, neural progenitor cells and embryonic fibroblasts [20], [25] [27], [64].
On the effector side of loop 2, Cys292 packs against the base of all three effectors, consistent with binding studies that show the affinity for all specificity effectors is decreased when Cys292 is mutated to alanine (Ormö and Sjöberg, 1996).
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Decoration of the abnormal cortical structures by EB1 can be explained by recent studies that show EB1 binding to the lattice as well as the plus ends of growing and shrinking microtubules in the cell periphery (Currie et al., 2011); we also detect EB1 lattice binding to cortical microtubules in wild-type oocytes, making them appear as faint wisplike filaments.
Binding studies that used labeled influenza (H5N1) showed virus attachment to higher and lower respiratory tract tissues.
The binding studies show that the CTD of primase binds with a high affinity to the full length helicase and NTDL; poorly with NTD of HpDnaB alone.
Crystallographic and solution binding studies show that E. coli Hfq has preferences to bind an A-A-N motif on the distal face (Robinson et al., 2013 ).
Comparative analysis of our expression profiling data with previously published global binding studies shows that the genes that are bound by Ring1b in ES cells have bivalent histone marks, i.e. both active H3K4me3 and repressive H3K27me3, or the active H3K4me3 histone mark alone and are associated with CpG-'rich' promoters.
Peptide binding studies show that the overlapped PAM2 motifs of eRF3 binding with significantly (up to 30 fold) higher affinity than the PAM2 motifs of PAN3 and Tob [12], [28], [32].
These binding studies show that attachment of C3b molecules to a surface alters the binding affinity of C5 for C3b.
The structural studies accompanied by FRET, crosslinking and binding studies show that MutS is converted to a sliding clamp conformation to load MutL onto DNA.
Structural determination of a number of IL-4 variants together with in vitro binding studies show that IL-4 and its high-affinity receptor subunit IL-4Rα interact via a modular protein-protein interface consisting of three independently-acting interaction clusters.
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