Results 151 to 160 of about 14,072 (183)
Mlkl Knockout Mice Demonstrate the Indispensable Role of Mlkl in Necroptosis [PDF]
Cell Research, 2013 National Basic Research Program of China (973 Program) [2009CB522201]; National Natural Science Foundation of China [91029304, 30830092, 30921005, 81061160512]; Hi-Tech Research and Development Program of China (863 program) [2012AA02A201]; 111 Project ...
Jiahuai Han, Zhe Huang, Zhirong Zhang
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MLKL Forms Cation Channels [PDF]
Cell Research, 2016 The mixed lineage kinase domain-like (MLKL) protein is a key factor in tumor necrosis factor-induced necroptosis. Recent studies on necroptosis execution revealed a commitment role of MLKL in membrane disruption. However, our knowledge of how MLKL functions on membrane remains very limited.
Huayi Wang, Zhaobing Gao, Xueqin Chen
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The Many Faces of MLKL, the Executor of Necroptosis
International Journal of Molecular Sciences, 2023 Necroptosis is a recently discovered form of regulated cell death characterized by the disruption of plasma membrane integrity and the release of intracellular content. Mixed lineage kinase domain-like (MLKL) protein is the main player of this cell death pathway as it mediates the final step of plasma membrane permeabilization.
Uris Ros +2 more
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Necrosome core machinery: MLKL
Cellular and Molecular Life Sciences, 2016In the study of regulated cell death, the rapidly expanding field of regulated necrosis, in particular necroptosis, has been drawing much attention. The signaling of necroptosis represents a sophisticated form of a death pathway. Anti-caspase mechanisms (e.g., using inhibitors of caspases, or genetic ablation of caspase-8) switch cell fate from ...
Jing, Zhang +3 more
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MLKL Requires the Inositol Phosphate Code to Execute Necroptosis [PDF]
Molecular Cell, 2018 Necroptosis is an important form of lytic cell death triggered by injury and infection, but whether mixed lineage kinase domain-like (MLKL) is sufficient to execute this pathway is unknown. In a genetic selection for human cell mutants defective for MLKL-dependent necroptosis, we identified mutations in IPMK and ITPK1, which encode inositol phosphate ...
Scott J Dixon +2 more
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Science Signaling, 2019
TAM family kinases promote necroptosis by stimulating the phosphorylation and oligomerization of the pseudokinase MLKL.
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TAM family kinases promote necroptosis by stimulating the phosphorylation and oligomerization of the pseudokinase MLKL.
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TAM Kinases Promote Necroptosis by Regulating Oligomerization of MLKL [PDF]
Molecular Cell, 2019 Necroptosis, a cell death pathway mediated by the RIPK1-RIPK3-MLKL signaling cascade downstream of tumor necrosis factor α (TNF-α), has been implicated in many inflammatory diseases. Members of the TAM (Tyro3, Axl, and Mer) family of receptor tyrosine kinases are known for their anti-apoptotic, oncogenic, and anti-inflammatory roles.
Ayaz Najafov +2 more
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Detection of MLKL Oligomerization During Programmed Necrosis
2018Programmed necrosis, also known as necroptosis, is a form of regulated necrotic cell death that is mediated by receptor-interacting protein kinases RIP1 (or RIPK1), RIP3 (or RIPK3), and the mixed lineage kinase domain-like protein, MLKL. Following the induction of programmed necrosis, MLKL is phosphorylated by RIP3 and oligomerizes and then the protein
Zhenyu, Cai, Zheng-Gang, Liu
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Detecting phosphorylated MLKL in murine tissues
The programmed cell death process of necroptosis is activated when Receptor Interacting protein Kinase (RIPK)3 phosphorylates its substrate Mixed Lineage Kinase Like protein (MLKL). Phosphorylated MLKL oligomers then traffic to cellular membranes, including the plasma membrane, and perforate these membranes.Riley M, Williams +2 more
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Experimental Cell Research
The dimerization of the MLKL kinase-like domain (KLD) is a crucial step for MLKL activation in necroptosis. In 2014, it was discovered that GW806742X can directly bind to the mouse MLKL KLD via surface plasmon resonance (SPR) (Kd = 9.3 μM), inhibiting TNF-induced membrane translocation of MLKL and necroptosis.
Feiyang, Yuan +5 more
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The dimerization of the MLKL kinase-like domain (KLD) is a crucial step for MLKL activation in necroptosis. In 2014, it was discovered that GW806742X can directly bind to the mouse MLKL KLD via surface plasmon resonance (SPR) (Kd = 9.3 μM), inhibiting TNF-induced membrane translocation of MLKL and necroptosis.
Feiyang, Yuan +5 more
openaire +2 more sources