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Firstly, we investigate the plasticity of a class II major histocompatibility complex in the absence of a bound peptide.
Some CC isomerization could be detected during the course of 1-dodecene hydrogenation, and (1) gave a dihydride complex in the absence of alkene.
It was concluded that the presence of the XL-domain in these isoforms is not relevant for the formation of the calpain/calpastatin complex in the absence of calcium, that is the interaction of calpastatin with inactive calpain.
Moreover, TgDLC could also not be detected in basal complex in the absence of MORN1 [28].
Constructing such an index remains very complex in the absence of consensus on the choice of parameters to incorporate and their corresponding weight [46].
This outgrowth is clearly seen in Fig. 3 A and B. Formation of LRP at both low and high auxin modalities is attenuated 2 3 fold by the G protein complex in the absence of glucose (Fig 3B).
An alternative explanation for the apparent stability of the peptide/MHCII complex in the absence of competitor peptide might be that the unlabeled peptide serves to prevent rebinding of the freshly dissociated pre-bound peptide.
In contrast, aggregates of non-native VAMP2 were not dispersed by the CHL1ID/CSP complex in the absence of nucleotides or in the presence of ADP, or by the CHL1ID/Hsc70/αSGT complex in the presence of ATP.
Consistent with this view, the crystal structure of the eIF4AIII-MLN51 complex in the absence of ATP, showed that eIF4AIII adopts an open conformation in which the RNA-binding site is disrupted [17].
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The source of these complexes in the absence of etoposide is not yet clear.
Surprisingly, high serum concentrations increased transfection efficiency of DC complexes in the absence of protamine sulfate.
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