8 results match your criteria: "UT MD Anderson Cancer Center UTHealth Houston[Affiliation]"

Magnetic resonance (MR)-guided radiation therapy (RT) is enhancing head and neck cancer (HNC) treatment through superior soft tissue contrast and longitudinal imaging capabilities. However, manual tumor segmentation remains a significant challenge, spurring interest in artificial intelligence (AI)-driven automation. To accelerate innovation in this field, we present the Head and Neck Tumor Segmentation for MR-Guided Applications (HNTS-MRG) 2024 Challenge, a satellite event of the 27th International Conference on Medical Image Computing and Computer Assisted Intervention.

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The Dice Similarity Coefficient (DSC) is the current standard to determine agreement between a reference segmentation and one generated by manual / auto-contouring approaches. This metric is useful for non-spatially important images; however, radiation therapy requires consideration of nearby Organs-at-Risk (OARs) and their radiosensitivity which are currently unaccounted for with the traditional DSC. In this work, we introduce the OAR-DSC which accounts for nearby OARs and their radiosensitivity when computing the DSC.

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Stem cell activity-coupled suppression of endogenous retrovirus governs adult tissue regeneration.

Cell

December 2024

Department of Cancer Biology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA; Graduate School of Biomedical Sciences, UT MD Anderson Cancer Center UTHealth Houston, Houston, TX, USA. Electronic address:

Mammalian retrotransposons constitute 40% of the genome. During tissue regeneration, adult stem cells coordinately repress retrotransposons and activate lineage genes, but how this coordination is controlled is poorly understood. Here, we observed that dynamic expression of histone methyltransferase SETDB1 (a retrotransposon repressor) closely mirrors stem cell activities in murine skin.

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Article Synopsis
  • - Eukaryotic genomes usually have one enzyme from the DXO/Dxo1/Rai1 family that helps break down non-standard RNA ends, while some yeasts have two copies, including Dxo1, which is essential for processing 25S rRNA.
  • - The study finds that the ability to process 25S rRNA evolved specifically in budding yeasts, not in other organisms, and this developed alongside a gene duplication event.
  • - Interestingly, different types of budding yeasts have independently evolved similar traits by duplicating their DXO/Dxo1/Rai1 gene and allowing one copy to gain new functions for processing 25S rRNA, illustrating a case of parallel evolution.
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Objective: The purpose of this study was to investigate the technical feasibility of integrating the quantitative maps available from SyntheticMR into the head and neck adaptive radiation oncology workflow. While SyntheticMR has been investigated for diagnostic applications, no studies have investigated its feasibility and potential for MR-Simulation or MR-Linac workflow. Demonstrating the feasibility of using this technique will facilitate rapid quantitative biomarker extraction which can be leveraged to guide adaptive radiation therapy decision making.

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Fungi of the order Mucorales express a "sealing-only" tRNA ligase.

RNA

March 2024

Department of Microbiology and Molecular Genetics, UT MD Anderson Cancer Center UTHealth Houston Graduate School of Biomedical Sciences, University of Texas Health Science Center, Houston, Texas 77030, USA

Some eukaryotic pre-tRNAs contain an intron that is removed by a dedicated set of enzymes. Intron-containing pre-tRNAs are cleaved by tRNA splicing endonuclease, followed by ligation of the two exons and release of the intron. Fungi use a "heal and seal" pathway that requires three distinct catalytic domains of the tRNA ligase enzyme, Trl1.

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Some eukaryotic pre-tRNAs contain an intron that is removed by a dedicated set of enzymes. Intron-containing pre-tRNAs are cleaved by tRNA splicing endonuclease (TSEN), followed by ligation of the two exons and release of the intron. Fungi use a "heal and seal" pathway that requires three distinct catalytic domains of the tRNA ligase enzyme, Trl1.

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