THSD1 Suppresses Autophagy-Mediated Focal Adhesion Turnover by Modulating the FAK-Beclin 1 Pathway. [PDF]
Xu Z, Lu J, Gao S, Rui YN.
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The Effect of Arsenic Trioxide and Its Combination with Oxaliplatin and Docetaxel on the Induction of Autophagy and Expression of LC3 and Beclin-1 Genes in AGS and MKN-45 Gastric Cancer Cell Lines. [PDF]
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Correction: Caspase 1 activation is protective against hepatocyte cell death by up-regulating beclin 1 protein and mitochondrial autophagy in the setting of redox stress. [PDF]
Sun Q +6 more
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A study on the mechanism of Beclin-1 m6A modification mediated by catalpol in protection against neuronal injury and autophagy following cerebral ischemia. [PDF]
Liu K, Yao X, Gao J, Wang J, Qi J.
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MicroRNA-141-3p reduces pulmonary hypoxia/reoxygenation injury through suppression of Beclin-1-dependent autophagy. [PDF]
Zhan Y +7 more
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Short-peptide-based enteral nutrition affects rats MDP translocation and protects against gut-lung injury via the PepT1-NOD2-beclin-1 pathway in vivo. [PDF]
Pang XF +8 more
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Beclin-1 and LC3A expression in cutaneous malignant melanomas
Melanoma Research, 2011Autophagy is an intracellular pathway for the degradation of long-lived proteins and damaged organelles. It is, in essence, a recycling process allowing cells to survive oxygen and nutrient depletion. The expression of two autophagy-related proteins, beclin 1 and light chain 3A (LC3A) was investigated in 79 nodular cutaneous melanomas. The results were
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Beclin 1 is the first mammalian autophagy protein identified as a novel Bcl-2-interacting protein. Subsequent studies have demonstrated that this landmark protein is essential for autophagy. By investigating the interaction between Bcl-2 and Beclin 1, key molecular mechanisms of mammalian autophagy regulation have been discovered.
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Beclin 1 Complex and Neurodegenerative Disorders
2020Beclin1 is the mammalian orthologue of yeast Atg6/vacuolar protein sorting-30 (VPS30). Beclin1 interacts with various biological macromolecules like ATG14, BIF-1, NRBF2, RUBICON, UVRAG, AMBRA1, HMGB1, PINK1, and PARKIN. Such interactions promote Beclin1-PI3KC3 complex formation.
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