Fibrosis results from excessive extracellular matrix (ECM) deposition, causing tissue stiffening and organ dysfunction. Activated fibroblasts, central to fibrosis, exhibit increased migration, proliferation, contraction, and ECM production. However, it remains unclear if the same fibroblast performs all of the processes that fall under the umbrella term of "activation".
View Article and Find Full Text PDFBackground: Infectious diseases remain the leading cause of death among children younger than 5 years due to disparities in access and acceptance of essential interventions. The Community Mobilisation and Community Incentivisation (CoMIC) trial was designed to evaluate a customised community mobilisation and incentivisation strategy for improving coverage of evidence-based interventions for child health in Pakistan.
Methods: CoMIC was a three-arm cluster-randomised, controlled trial in rural areas of Pakistan.
Background: Cancer is a major cause of mortality worldwide, and differences in cancer mortality rates between countries are, in part, due to differences in access to cancer care, including medicines. National essential medicines lists (NEMLs) play a role in prioritization of healthcare expenditure and access to medicines. We examined the association between amenable cancer mortality and listing medicines used in the management of eight cancers (non-melanoma skin, uterine, breast, Hodgkin lymphoma, colon, leukemia, cervical, and testicular) in national essential medicines lists of 158 countries and summarized changes to the inclusion of cancer treatments in NEMLs.
View Article and Find Full Text PDFThe receptor tyrosine kinase AXL promotes tumor progression, metastasis, and therapy resistance through the induction of epithelial-mesenchymal transition (EMT). Here, we found that activation of AXL resulted in the phosphorylation of TANK-binding kinase 1 (TBK1) and the downstream activation of AKT3 and Snail, a transcription factor critical for EMT. Mechanistically, we showed that TBK1 directly bound to and phosphorylated AKT3 in a manner dependent on the multiprotein complex mTORC1.
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