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Phosphorylation of H3 S10 during G2/M has been found to prevent HP1β from binding to the adjacent H3K9me residue.
Phosphorylation of H3 at serine 28, catalysed by MSK1/2, can displace PRC2, presumably by disrupting binding to the adjacent, methylated residue [ 76, 77].
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The chains are connected into a 3D CdSO4-type array via the second Hg CN 2 unit binding to the chlorides; adjacent chains are inclined at 59.0°.
Some sublines gave spheroids that showed narrow distributions of [3H]misonidazole binding to the cells adjacent to necrosis, whereas other sublines showed a range of binding similar to that seen in spheroids of the parent line.
Of this, −31.6 kJ/mol has been shown to result from interaction with a single CR domain [ 18, 33], almost certainly the result of binding to the only two adjacent lysine residues that have been shown to be critical for binding [ 3, 34].
Opposing effects of Smad2 and Smad3 on transcriptional regulation of the goosecoid gene have been ascribed to competition between Smad3 and Smad4 for binding to the Smad binding element adjacent to the FAST2/Smad2 binding site [ 38].
This might suggest that Chd1 is recruited to the gene body via the elongation complex and is then targeted to the nucleosome substrate via binding to the exposed DNA loop immediately adjacent to the histone octamer to facilitate the in cis transfer of histone octamers.
In particular, a deletion only abolishes ligand binding to the corresponding region but not to adjacent regions.
Further kinetic studies revealed a mutual exclusivity of BQ covalent inactivation and competitive inhibitor binding to sites adjacent to Cys165, refuting the viability of the current strategy for developing more potent irreversible BoNT/A inhibitors.
One possible explanation is that full-length MUC1 contains a self-aggregation domain that likely contributes to the protein's characteristic clustering and could sterically hinder the binding of ligands to the adjacent region which is the Anti-MUC1* epitope.
In previous studies Hirota et al., 2005, found that the phosphorylation of histone H3 at Ser-10 negatively regulated the binding of HP1α to the adjacent methylated Lys-9 of histone H3.
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