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This framework allows speedy modification of either local or global requirements and is highly portable to other complex planning problems.
Using an in vitro pull-down assay, we demonstrate that the interaction between transport inhibitor response 1 (TIR1) and Aux/IAA proteins does not require stable modification of either protein.
Three collapses that occurred at initial 800 m length of southern tunnel necessitated modification of either or both of the support system or excavation sequences.
Since heteromeric assembly of both subunits is required for efficient functional expression, post-transcriptional modification of either subunit would affect NMDA receptor activity.
As shown in Figure 4B, modification of either NrdR1, NrdR2 or both, increased nrdAB transcription, although only the NrdR2 mutant achieved a transcriptional increase similar to that of the ΔnrdR strain.
During this time, HB-19 exerts a differential inhibitory effect on the expression of cytoplasmic/surface nucleolin compared to nuclear nucleolin as shown by the marked reduction of nucleolin in cytoplasmic extracts of cells but without apparent modification of either level (Figure 2B) or nucleolar localization of nuclear nucleolin (Figure 2D), even after 24 48 hours of HB-19 treatment.
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In conclusion, mPEG-modification of either RSV or the host cell is a highly effective prophylactic strategy for preventing viral infection.
It can be proposed that mitosis-specific modifications of either NFAT5 or the chromatin, or a repressor protein interacting with NFAT5 in mitosis might disrupt the binding of this factor to DNA.
Static cysteine modifications of either carbamidomethylation (IAM-alkylation, +57.0215 Da) or ethanolyl (IE-alkylation, +44.0262 Da) were included on the basis of which modifying reagent was used.
Straightforward modifications of either approach allow us to incorporate the positivity and sum to less than or equal to one constraints of linear mixing.
This revealed additional peaks corresponding to mass differences of 178 and 258 Da, which were respectively identified as gluconoyl and phospho-gluconoyl post-translational modifications of either lysine residues and/or the N-terminal methionine residue (Supplementary Figure S3).
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