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There are also many instances in which structurally related TFs potentially compete to bind the same site.
ChIP-sequencing and direct ChIP experiments showed that CTCF and CTCFL bind the same site within the Stra8 and Prss50 promoters, but not in the Gal3st1 promoter.
Based on these findings, it is perhaps reasonable to conclude that both ATP and GTP bind the same site, i.e. the G-domain, and the protein preferentially binds and hydrolyses ATP, over GTP.
Synergistic binding was proven for glucocorticoid receptor in Wright and Gustafsson work [ 36] and studies in Ron et al. [ 37] have suggested that there are interactions between NF-κB and other adjacent regulatory factors, so other proteins may bind the same site as does NF-κB.
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Comparison of Stat5a and Stat5b, demonstrated that these highly homologous factors bind the same sites in vivo, albeit with different kinetics that may underlie differences in Stat5 biology [22].
Irf1 and Ir2 appear to bind the same sites [ 34].
M2 and the LIR-containing p62 compete for binding to LC3, indicating that M2 binds the same site as the classical p62 LIR.
The phosphate molecule, binds the same site as the cyclic phosphates, with the same set of interactions (Fig. 6C and Table 2).
As HflX contains a single nucleotide binding domain, i.e. the G-domain, we wished to examine if ATP too binds the same site.
Recently, we have shown that different LA modules bind to the same site on β2GPI and that β2GPI can not simultaneously bind an LA module and a cardiolipin-coated surface [46].
The steroidal inhibitors are analogues of androstenedione and bind to the same site on the aromatase molecule, but unlike androstenedione they bind irreversibly, because of their conversion to reactive intermediates by aromatase.
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