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During the series of four ECT sessions, we measured plasma concentrations for the sum of sugammadex and sugammadex-rocuronium complex and observed whether possible residual sugammadex affected muscle relaxation during subsequent sessions of ECT.
In addition, we measured plasma concentrations for the sum of sugammadex and sugammadex-rocuronium complex and observed whether possible residual sugammadex affected muscle relaxation during subsequent sessions of ECT.
Moreover, recently we have determined the structure of domain 1 (pdb code 3PIS) which superimposed well with the CrSPI-1 domain 1 of the complex and observed no conformational changes [57].
We examined other strains with LOF for either wdb or other regulatory, scaffold and catalytic subunits of the PP2A complex, and observed enhancement of C96-domR (Table 4).
Cluster controlled trials also require an estimation of the intraclass correlation coefficient (ICC); this is complex, and observed ICCs rarely match their predicted values.
We have performed the alignments for orthologs of PFB0280w in P. berghei (PBANKA_030400), P. chabaudi (PCHAS_030620), P. knowlesi (PKH_041350), P. vivax (PVX_003750) and P. yoelii (PY00069) with yeast AROM complex and observed that the aligned regions had both the SK and EPSP domains with PfFSmat60 matrix while the standard matrix had only the SK domains aligned.
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The rationale for both methodologies was to start with a prebound peptide/MHCII complex and observe the accumulation of free peptide over time in the absence of an exchange peptide, DM, or both.
In order to determine whether or not Gcn5 was being recruited as part of SAGA or SLIK, we tagged unique components of both of these complexes and observed the identical pattern of recruitment only with the SAGA-specific protein (Spt8) and not with the SLIK-specific protein (Rtg2) (which was detected at the SLIK-dependent promoter CIT2) (data not shown).
We first investigated the expression of AM and its receptor complexes and observed pulmonary upregulation of AM in each of both MV and pneumonia.
We performed single-molecule pulling experiments on bound Coh:mutant Doc complexes and observed a strong bias in the probability of two clearly distinguishable unfolding patterns, termed 'single' and 'double' rupture types for each binding mode mutant.
We have analyzed the nucleotide sequences at the binding sites in different pairs of protein-RNA complexes and observed that the binding preference is similar in all the nucleotides.
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