Publications by authors named "Deborah M Thurtle-Schmidt"

Article Synopsis
  • The study investigates the role of microsatellite instability (MSI-H) in pancreatic cancer (PC) associated with Lynch syndrome (LS), focusing on both germline and somatic variants that affect mismatch repair genes.
  • It involves a retrospective analysis of 55 PC patients at Memorial Sloan Kettering Cancer Center, revealing that a significant portion of those with LS and somatic MMR variants exhibit MSI-H status, which could impact treatment responses to immune therapy.
  • Results showed that 59% of LS cohort patients had MSI-H, whereas 43% in the somatic MMR cohort had the same status, suggesting distinct genetic characteristics and age differences at diagnosis between the two groups.
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To fully appreciate genetics, one must understand the link between genotype (DNA sequence) and phenotype (observable characteristics). Advances in high-throughput genomic sequencing technologies and applications, so-called "-omics," have made genetic sequencing readily available across fields in biology from applications in non-traditional study organisms to precision medicine. Thus, understanding these tools is critical for any biologist, especially those early in their career.

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Disrupting a gene to determine its effect on an organism's phenotype is an indispensable tool in molecular biology. Such techniques are critical for understanding how a gene product contributes to the development and cellular identity of organisms. The explosion of genomic sequencing technologies combined with recent advances in genome-editing techniques has elevated the possibilities of genetic manipulations in numerous organisms in which these experiments were previously not readily accessible or possible.

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As the only catalytic member of the Sir-protein gene-silencing complex, Sir2's catalytic activity is necessary for silencing. The only known role for Sir2's catalytic activity in Saccharomyces cerevisiae silencing is to deacetylate N-terminal tails of histones H3 and H4, creating high-affinity binding sites for the Sir-protein complex, resulting in association of Sir proteins across the silenced domain. This histone deacetylation model makes the simple prediction that preemptively removing Sir2's H3 and H4 acetyl substrates, by mutating these lysines to unacetylatable arginines, or removing the acetyl transferase responsible for their acetylation, should restore silencing in the Sir2 catalytic mutant.

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