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The latter point is also important in view of the differences in plasma protein binding reported for the different bone-seeking 99mTc-labelled agents [36].
Our data are consistent instead with the glycosaminoglycan binding reported for the gp150 homologs of other gamma-2-herpesviruses [47] [49].
The variant allele has been shown to exhibit similar physiological responses when compared with the human polymorphism including a 3.5-fold elevated affinity of the G77 allele encoded protein for β-endorphin (Miller et al., 2004) comparable with the 3-fold increased binding reported for the 118G allele in the original in vitro work (Bond et al., 1998).
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In contrast to the low binding affinity reported for the binding of LG100754 to RARα [14], we show that this ligand binds to RAR with a significant affinity.
Similarly, a requirement that RNA be a minimum length for detectable binding was reported for the purified yeast Pat1-LSm1 7 complex (Chowdhury et al, 2007), suggesting that some of the RNA-binding properties of the complex can be attributed to Pat-C.
A sequential or a partially compulsory order mechanism for substrate binding has been reported for the FGAR-AT in various organisms, with Gln binding first followed by Mg-ATP and FGAR.
Besides KSHV, GAG binding has been reported for the Bovine herpesvirus-4 (BHV-4) gB [11] and the Herpesvirus saimiri ORF51 [12].
However, a decreased binding affinity was reported for the pre- and post-central gyri from people who died as a result of suicide [ 14].
Furthermore, as in our study, cooperative binding was also reported for the two MYB elements of the bean PAL2 promoter in the presence of the pine PtMYB1 protein [ 30].
Although calcium-independent membrane binding has been reported for the C2 domains of dysferlin, neither C2 domain of synaptotagmin I binds appreciably to PS-containing liposomes in the absence of calcium, suggesting a difference in the mechanisms by which synaptotagmin I and otoferlin bind membranes.
Perturbation of the salt bridges upon substrate binding has been also reported for the mitochondrial ADP/ATP carrier (AAC), suggesting a general mechanistic element for how substrate binding, particularly for charged substrates, might facilitate the progression of larger-scale conformational changes.
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