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AATATT triplet repeats may behave like some disease causing trinucleotide repeats, showing expansion and contraction instabilities.
The non-B structures formed by AATTTA triplet repeats were found to be similar to those of non-B secondary structures formed by disease causing trinucleotide repeats such as CAG·CTG, CGG·CCG and GAA·TTC, which are associated with more than 40 human genetic diseases, including Huntington's disease or fragile X syndrome [8], [13].
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Whereas multiple genes have been associated with PD and AD, HD is an autosomal dominant disease caused by trinucleotide expansion [cytosine, adenine, and guanine (CAG)] within a single gene, huntingtin (Htt).
HD is an autosomal dominant disease caused by a trinucleotide (CAG) repeat expansion beyond 36 in the Huntingtin (htt) gene that produces an altered form of the Htt protein.
In Huntington's disease (HD), a neurodegenerative disease caused by a trinucleotide repeat expansion, miRNA dyregulation has been reported, which may impact gene expression and modify the progression and severity of HD.
Treat the disease causing the jaundice.
This study reveals a novel role for XPG in genome-maintenance and implicates XPG in diseases caused by trinucleotide repeat expansion.
Huntington disease (HD) is a late manifesting inheritable neurodegenerative disease caused by an expanded trinucleotide repeat in the coding region of the HD gene (HDCRG 1993; Vonsattel and DiFiglia 1998).
Huntington's disease (HD) is a progressive neurodegenerative disease caused by an unstable CAG trinucleotide repeat expansion.
Spinocerebellar ataxia 2 (SCA2) is an autosomal dominant disease caused by an expanded CAG trinucleotide repeat encoding glutamine within the open reading frame of the gene encoding the ataxin 2 protein, ATAXIN2 (ATXN2) [10] [12].
Friedreich ataxia (FA) is a progressive neurodegenerative disease caused by expansion of a trinucleotide repeat within the first intron of the gene that encodes frataxin.
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