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http://dx.doi.org/10.1136/bmj.296.6633.1345-a | DOI Listing |
Child Care Health Dev
January 2025
Faculty of Health, Institute for Physical Activity and Nutrition, Deakin University, Geelong, Victoria, Australia.
Background: The study examined the longitudinal associations of sleep time, restrained time, back time and tummy time with development in a sample of infants using compositional data analysis.
Methods: Participants were a subsample of 93 parent-infant dyads from the Early Movers project in Edmonton, Canada. Parents completed a 3-day time-use diary at 2, 4 and 6 months of age.
Cell Death Dis
December 2024
Department of Gynecology, Shanghai First Maternity and Infant Hospital, School of Medicine, Tongji University, Shanghai, China.
Poly (ADP-ribose) polymerase 1 (PARP1) catalyzes poly (ADP) ribosylation reaction, one of the essential post-translational modifications of proteins in eukaryotic cells. Given that PARP1 inhibition can lead to synthetic lethality in cells with compromised homologous recombination, this enzyme has been identified as a potent target for anti-cancer therapeutics. However, the clinical application of existing PARP1 inhibitors is restrained by side effects associated with DNA trapping and off-target effects, highlighting the need for improved therapeutic strategies.
View Article and Find Full Text PDFPediatr Emerg Care
December 2024
Department of Emergency Medicine, Albany Medical Center Albany, NY.
Cell Death Differ
November 2024
Department of Biochemistry and Molecular Biology, International Cancer Center, Guangdong Key Laboratory of Genome Instability and Human Disease Prevention, Marshall Laboratory of Biomedical Engineering, Shenzhen University Medical School, Shenzhen, China.
Repair of double strand breaks (DSBs) by RNA-binding proteins (RBPs) is vital for ensuring genome integrity. DSB repair is accompanied by local transcriptional repression in the vicinity of transcriptionally active genes, but the mechanism by which RBPs regulate transcriptional regulation is unclear. Here, we demonstrated that RBP hnRNPA2B1 functions as a RNA polymerase-associated factor that stabilizes the transcription complex under physiological conditions.
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