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Even though the dramatic effect of some point mutations on IgE binding has been elucidated using Bet v1 as a model allergen [8], [9], nitration has been discussed to especially alter IgG epitopes [10].
A detailed structural comparison of both monocot and dicot AGPase SS along with their specificity towards substrate (ATP) and inhibitor (sulphate) binding has been elucidated.
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Furthermore, the amino acids directly involved in inhibitor binding have been elucidated in several PRPP synthetases [ 21, 29] and it has been reported that specific subtitutions of the leucine 128 and histidine 192 residues of human PRS1 induce allosteric deregulation and enzyme superactivity [ 9].
In mammalian IGFBPs, amino acid residues responsible for IGF-binding have been elucidated [35].
Recently a C-terminal binding site has been elucidated and a structure bound with novobiocin modeled (Fig. 7a b) [83].
The communication mechanism between the ATP-binding pocket and actin-binding cleft has been elucidated structurally (Coureux et al. 2003; Ecken et al. 2016).
The three-dimensional structure of AMP binding to AMPK has been elucidated (44).
While the whole genome DNA-binding profile for CTCF has been elucidated, this has not been done for CTCFL.
The whole genome DNA-binding profile for CTCF has been elucidated in several cell systems (see, for example, [ 6- 9]).
The molecular basis for loss of binding affinity of pheromones to pheromone-binding proteins at low pH has been elucidated in moths [7], [24], [28] [30].
More recently, the molecular basis of FAPP1-PH binding to ARF and PtdIns4 P has been elucidated in detail leading to the concept that both ligands can be bound simultaneously and independently to determine its multivalent anchoring to TGN membranes [14].
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