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Several mutations in the RIG-I regulatory domain that affected RNA binding have been characterized [6], [7], [14].
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For Dsg 1, Ca2+-dependency of homophilic binding has been characterized in more detail.
The anion binding has been characterized to be mediated by anion type, protein conformation and surface electrostatic potential.
Host guest binding interactions have been characterized using simple spectroscopic techniques viz.
Several XA21 binding proteins have been characterized, however the early events governing XA21 signaling have not been fully elucidated.
Conformation-specific antibody probe of DR1 structure also are available, although the binding sites have been characterized only by domain-swap or mutagenesis experiments.
Activities of Scaffold/Matrix Attachment Region (SAR/MAR) binding proteins have been characterized biochemically; although it is still unclear how are they are involved in gene regulation, they have been proposed to contribute to chromatin structure by mediating the attachment of chromatin to the nuclear scaffold thereby folding chromatin into topologically independent loop domains[14], [17].
However, binding sites have been characterized for some factors.
The PtdIns4 P and ARF1 binding sites have been characterized in FAPP1-PH [14].
Although numerous plant proteins with in vitro telomeric DNA binding activity have been characterized, many of them do not appear to act at telomeres, and may rather represent transcription factors [50].
Furthermore, multiple transcription factor-binding sites have been characterized in the upstream regulatory region of the MMP-9 gene, including binding sites for the AP-1 and NF-kappaB transcription factors [ 8, 49, 50].
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