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Both molecular modeling and Q189A mutation revealed that Gln189 plays a key role in the binding.
Analysis of cybrids harboring homoplasmic m.3243A>G mutation revealed that the level of aminoacylated tRNALeu UUR) was reduced 70%75%%, which is mainly due to a shortage of tRNALeu UUR), leading to the reduced rate of mitochondrial protein synthesis and respiration defects (Picard et al., 2014).
Our enrichment analyses of the genes significantly affected by the U6atac mutation revealed that many metabolic pathways were affected.
In silico analysis of the discovered new frameshift stop gained mutation revealed that it is a pathogenic mutation that led to nonfunctional sclerostin protein.
Modeling of this mutation revealed that its location was at the base of helix A at the N-terminal part of MEK1 (Fig 4B).
Analysis of dermal biopsies from a patient and his unaffected father, who also carries the mutation, revealed that both display basement membrane (BM) defects.
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Seven out of 21 MC cats with an fHCM diagnosis were not carrying the mutation, revealing that the etiology of fHCM is heterogeneous (i.e. at least one more cause is present) in the MC breed.
Cross-comparison of our transcriptome data with previously identified mutations revealed that most genes from our dataset have not been mutated.
Analysis of the mutations revealed that specific combinations of mutations were particularly important in conferring selective advantage.
The clustering of our DNA sequences into genotype groups corresponded to their respective subtype, that is, adw2 in genotype B, adrq in genotype C and ayw in genotype D. Analysis of the point mutations revealed that five of the sequences contained aa substitutions at immunodominant epitopes involved in B or/and T cell recognition.
Mutation showers were found after analyses of intragenic doublet mutations revealed that they were clustered and chronocoordinate [9].
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