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Ryanodine receptors (RYRs) on the ER have multiple allosteric Ca2+ binding sites responsible for triggering Ca2+- induced Ca2+ release (CICR) into the cytosol [19], [20], [21], [22].
Moreover, residues close to the binding sites responsible for protein-protein interactions show higher co-evolution signals than residues outside the binding region [25].
Furthermore, creatinine is removed by hemodialytic strategies [42] but under diseased states uremic compounds of low molecular mass can displace strongly albumin-bound drugs from binding sites responsible for the binding defect of various drugs in uremic sera.
We used transient transfections of promoter-reporter constructs in order to identify putative transcription factor binding sites responsible for such indirect Smad4 effects.
A key objective of global gene expression studies is the identification of transcription factors and their DNA binding sites responsible for co-expression of genes.
Here we identify the putative transcription factor binding sites responsible for this distal cis-acting regulation, and use that information to identify a regulatory region of the human APP gene.
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Indeed PHD2 promoter contains HRE binding site responsible for the induction of human PHD2 gene by hypoxia [41] [43].
The binding site responsible for the increased O2* production is, likely, site L1, since the non-occupancy of site L2 did not significantly affect photobleaching in recombinant LHCII [ 9, 18].
The RyR family has three isoforms, all expressed in the brain, and has multiple allosteric Ca2+-binding sites responsible for triggering Ca2+-induced Ca2+ release (CICR) to the cytosol.
The two exposed loops Asn-Val-Asp Phe-Arg-Gly-Asp-Asp of PAN1 or Asp-Lys-Asp Tyr-Arg-Gly-Asn-Asp of PAN2, and Ser-Gly-Thr-Gly-Thr-Arg-Thr of PAN1 or Ser-Ala-Ala-Gly-Thr-Ala-Thr of PAN2, fulfill these structural requirements and thereby could act as the carbohydrate-binding sites responsible for the hemagglutinating activity of CBEL [ 18, 41].
This raises the possibility that in addition to the H and ACA boxes, the snR30 snoRNA contains at least one protein-binding site responsible for the recruitment of snR30-specific snoRNP proteins.
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