
Recent data from two independent laboratories have shed new light on the molecular mechanisms by which mixed lineage kinase domain-like (MLKL) promotes a peculiar form of regulated necrosis known as necroptosis. Upon phosphorylation by receptor-interacting protein kinase 3 (RIPK3), MLKL appears indeed to form oligomers that localize to the plasma membrane and compromise its ability to preserve ionic homeostasis.
Cell Membrane Permeability, Cell Membrane, Sodium, TRPM Cation Channels, Apoptosis, Protein Serine-Threonine Kinases, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins, Inhibitor of Apoptosis Proteins, Necrosis, Receptor-Interacting Protein Serine-Threonine Kinases, Humans, Calcium, Phosphorylation, HT29 Cells, Protein Kinases
Cell Membrane Permeability, Cell Membrane, Sodium, TRPM Cation Channels, Apoptosis, Protein Serine-Threonine Kinases, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins, Inhibitor of Apoptosis Proteins, Necrosis, Receptor-Interacting Protein Serine-Threonine Kinases, Humans, Calcium, Phosphorylation, HT29 Cells, Protein Kinases
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| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
