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By comparing the mechanics and X-ray diffraction patterns of mutated and wild-type muscle fibers, the authors provide evidence that the myosin mutation enhances the amount of strongly bound myosin cross-bridges and facilitates force production at the molecular and cellular level.
HPLC quantification of the electrochemically produced metabolites showed that E158K mutation leads to an impairment of N-oxygenation activity while E308G mutation enhances the same activity.
We propose that the Tyr195Cys mutation enhances the interaction with Ca2 + and affects the packing of the Ca2 + binding loop, consequently increasing protein stability.
The computational results disclose that the non-polar contribution is the major driving force and Y132A mutation enhances the binding affinity for inhibitor 2 bound to HBV.
The R120G mutation enhances the binding capacity of αB-crystallin for desmin and decreases their dissociation constant.
The inlAm mutation enhances the intestinal translocation of L. monocytogenes but has no impact on the outcome of intravenous infection [61].
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In E. coli TC44, mutation of the poxB gene, which encodes pyruvate oxidase, was most beneficial for growth and pyruvate production, as the mutation enhanced the NAD+ concentration in the cells and activated several enzymes involved in the glycolysis pathway.
The abundance and activity of the G1 cyclin Cln1/2 is required for polarization, cell elongation and transcriptional activation of FLO11, whereas Δcln3 mutation enhanced the filamentous growth [41].
When we compared the DNA binding of nuclear extracts from HeLa cells transfected with wild-type and the S369-S373-S377 mutant Runx2 by EMSA, the mutation enhanced the specific Runx2-DNA binding (Fig. 4G).
Interestingly, only 12±2.7% of the homozygous lark1; E74BG01805 double mutants survived to the early pupal stage; i.e., most of them died prior to or at the third-instar larval stage, indicating that the BG01805 mutation enhanced the lethal phenotype of lark1.
However, AMBRA1 mutation enhanced the interaction between BECN1 and PIK3C3 within the Atg14-containing PIK3C3 complex.
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