Exact(1)
The DNA binding domain is essential for interaction with the viral origin of plasmid replication (OriP) [10].
Similar(58)
Taken together, these data suggest that both the VRR_nuc nuclease domain and the SAP DNA binding domain are essential for SpFan1 activity in vivo.
Of the two linkers, one that connects the dimerization and ATP binding domains is essential for both basal autophosphorylation and activation of the kinase.
The P3 P4 linker that connects the dimerization and ATP binding domains is essential for both basal autophosphorylation and activation of the kinase.
A human immunodeficiency virus type 1 Tat-like arginine-rich RNA-binding domain is essential for HEXIM1 to inhibit RNA polymerase II transcription through 7SK snRNA-mediated inactivation of P-TEFb.
We provide data to show that the PDZ-binding domain is essential for the maintenance of cell polarity in both tissues.
This finding supports the view that the PDZ-binding domain is essential for maintenance of apicobasal polarity by stabilizing the Crb-associated comembersembers, including Crb itself, at the plasma membrane.
Using fosmid-based transgenes, we could confirm previous results showing that the PDZ-binding domain is essential for the maintenance of epithelial polarity in the early embryo and for proper invagination of cells of the tracheal and salivary placodes.
Importantly, we revealed that KCBP exhibits non-processive movement by the live-cell, single-molecule (particle) motility assay, and that the second MT-binding domain is essential, based on the genetic complementation tests; our data further support the bundling or crosslinking role of KCBP in the formation of the MT rings at the branching site.
Taken together, the data show that the dimerisation of the actin-binding domain is essential for F-actin binding, in agreement with the recent work of Smith and McCann (2007), and also suggest that the dimerisation domain itself might contribute to binding through electrostatic interactions.
An analysis of a series of truncation variants of pTAL revealed that a region encompassing approximately 150 amino acids upstream of the DNA-binding domain is essential for efficient binding to a target site, whereas the C-terminal domain is dispensable for the interaction with DNA (Miller et al., 2011; Mussolino et al., 2011; Zhang et al., 2011).
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