Background: Little is known on the effect of glycogen synthase kinase-3ß inhibitors (GSK3Is), as a class, on prostate cancer (PC). We aimed to study this in the Canadian province of Manitoba, because mixed results have been reported on the effect of valproate.
Methods: We conducted a nested case-control study among cancer-free Manitobans with ≥ 5 years of medical history in which we matched all men 40 years or older diagnosed with PC between 2000 and 2018 (N = 11,189) on period, age, length of available drug information to cancer-free controls (N = 55,728).
The ERBB2 is one of the most studied genes in oncology for its significant role in human malignancies. The metastasis-associated properties that facilitate cancer metastasis can be enhanced by activating the ERBB2 receptor signaling pathways. Additionally, therapeutic resistance is conferred by ERBB2 overexpression via receptor-mediated antiapoptotic signals.
View Article and Find Full Text PDFAlthough cellular senescence has been recognized as a hallmark of aging, it is challenging to detect senescence cells (SnCs) due to their high level of heterogeneity at the molecular level. Machine learning (ML) is likely an ideal approach to address this challenge because of its ability to recognize complex patterns that cannot be characterized by one or a few features, from high-dimensional data. To test this, we evaluated the performance of four ML algorithms including support vector machines (SVM), random forest (RF), decision tree (DT), and Soft Independent Modelling of Class Analogy (SIMCA), in distinguishing SnCs from controls based on bulk RNA sequencing data.
View Article and Find Full Text PDFPhoU proteins are negative regulators of the phosphate response, regulate virulence, and contribute to antibiotic resistance. has multiple genes encoding PhoU homologs that regulate persister formation and potentially virulence, but the molecular mechanisms of this regulation are not fully understood. We used a bacterial adenylate cyclase two-hybrid system to assess interactions between PhoU homologs and other proteins known to interact with PhoU from PhoU (also referred to as PhoU1) interacted with PhoU itself; PitR (also referred to as PhoU2) interacted with PitR itself.
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