Publications by authors named "J M Simonet"
Arginine methylation is catalyzed by protein arginine methyltransferases (PRMTs) and is involved in various cellular processes, including cancer development. PRMT2 expression is increased in several cancer types although its role in acute myeloid leukemia (AML) remains unknown. Here, we investigate the role of PRMT2 in a cohort of patients with AML, PRMT2 knockout AML cell lines as well as a Prmt2 knockout mouse model.
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- Citizen science allows non-scientists to contribute to research, particularly in addressing issues relevant to their communities, typically designed by experienced scientists.
- Challenges arise when citizens try to design their own research due to limited training and access to necessary tools, which can lead to overlooked community experiences in health research.
- This approach engages participants from Grade 5 to adults in studying diet and disease using the genetics of Drosophila, empowering them to lead research projects and incorporate community relevance into the findings.
Arginine methylation is a common post-translational modification affecting protein activity and the transcription of target genes when methylation occurs on histone tails. There are nine protein arginine methyltransferases (PRMTs) in mammals, divided into subgroups depending on the methylation they form on a molecule of arginine. During the formation and maturation of the different types of blood cells, PRMTs play a central role by controlling cell differentiation at the transcriptional level.
View Article and Find Full Text PDFInosine-5'-monophosphate dehydrogenase (IMPDH), a key regulatory enzyme in purine nucleotide biosynthesis, dynamically assembles filaments in response to changes in metabolic demand. Humans have two isoforms: IMPDH2 filaments reduce sensitivity to feedback inhibition, while IMPDH1 assembly remains uncharacterized. IMPDH1 plays a unique role in retinal metabolism, and point mutants cause blindness.
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- T-cell and B-cell acute lymphoblastic leukemias (T-ALL, B-ALL) are aggressive cancers caused by the buildup of immature T or B cells, and current treatments still need improvement for high-risk patients.
- Research shows that ALL cells are sensitive to NVP-BEP800, a drug that inhibits Heat shock protein 90 (HSP90), which helps maintain the stability of certain proteins crucial for cancer cell survival.
- In experiments with patient-derived models, treatment with NVP-BEP800 slowed down ALL progression, suggesting that targeting the relationship between HSP90 and specific kinases could lead to better therapies for leukemia.