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For both FFPET and frozen samples, the highest proportion of annotated reads mapped to the 3' untranslated region (50% of annotated FFPET reads and 41% of annotated frozen reads), followed by the coding exon (14% FFPET and 22% frozen).
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Human PRNP is localized on chromosome 20 and contains a short un-translated exon I separated from the coding exon II by a 13 kb intron [ 48, 61- 63].
Its possible association with this condition was investigated by sequencing the coding exons of the FU gene in an affected member from the German family [ 17].
Mutational analysis is carried out by sequencing the coding exons and flanking intronic regions of these two genes [ 19, 37, 84].
We identified two types of chimeric transcripts containing all but the last exon of the PPARG gene followed by all the coding exons of the TSEN2 gene (exons 2 to 12).
A total of 240 variants were identified by sequencing the coding exons and flanking intronic regions of the gene in all study participants and then divided into the categories 'rare' and 'common' using a cutoff MAF of 0.5%.
A broad region surrounding the shared region of homozygosity was analysed by sequencing the coding exons and exon-intron junctions of the genes in the region between position 59.6 and 78.0 Mb of ECA1 identified on the Equus caballus reference genome assembly EquCab2.0, annotation release 101.
By sequencing all the coding exons and the untranslated regions in UGDH with pooled DNA of 8 sires represented the separated families detected in our previous studies, a total of ten SNPs were identified and genotyped in 1417 Holstein cows of 8 separation families.
Samples negative by SSCP analysis were subsequently sequenced by Sanger sequencing for the coding exons 2 11.
Mutational analysis in genes GJB2 and GJB6 was brought by direct sequencing of the coding exons including the intron transitions.
By direct sequencing of the coding exons and intron-exon junctions of the candidate genes, we found only known polymorphisms except a novel heterozygous substitution c.250C>T in GUCA1A, replacing leucine with phenylalanine at amino acid residue 84).
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