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Inhibitors identify an auxiliary role for mTOR signalling in necroptosis execution downstream of MLKL activation.
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- Biochemical Journal, 2024, v. 481, n. 17, p. 1125, doi. 10.1042/BCJ20240255
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- Article
Phosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization.
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- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-42255-w
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- Article
A common human MLKL polymorphism confers resistance to negative regulation by phosphorylation.
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- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-41724-6
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- Article
Human RIPK3 C-lobe phosphorylation is essential for necroptotic signaling.
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- Cell Death & Disease, 2022, v. 13, n. 6, p. 1, doi. 10.1038/s41419-022-05009-y
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- Article
A family harboring an MLKL loss of function variant implicates impaired necroptosis in diabetes.
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- Cell Death & Disease, 2021, v. 12, n. 4, p. 1, doi. 10.1038/s41419-021-03636-5
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- Article
Co-clustering of EphB6 and ephrinB1 in trans restrains cancer cell invasion.
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- Communications Biology, 2024, v. 7, n. 1, p. 1, doi. 10.1038/s42003-024-06118-4
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- Article
Crystal structure of the hinge domain of Smchd1 reveals its dimerization mode and nucleic acid–binding residues.
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- Science Signaling, 2020, v. 13, n. 636, p. 1, doi. 10.1126/scisignal.aaz5599
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- Article
An immunohistochemical atlas of necroptotic pathway expression.
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- EMBO Molecular Medicine, 2024, v. 16, n. 7, p. 1717, doi. 10.1038/s44321-024-00074-6
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- Article
SMCHD1’s ubiquitin-like domain is required for N-terminal dimerization and chromatin localization.
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- Biochemical Journal, 2021, v. 478, n. 13, p. 2555, doi. 10.1042/BCJ20210278
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- Article
The epigenetic regulator Smchd1 contains a functional GHKL-type ATPase domain.
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- Biochemical Journal, 2016, v. 473, n. 12, p. 1733, doi. 10.1042/BCJ20160189
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- Article
Necroptosis signalling is tuned by phosphorylation of MLKL residues outside the pseudokinase domain activation loop.
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- Biochemical Journal, 2015, v. 471, n. 2, p. 255, doi. 10.1042/BJ20150678
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- Article
Mechanistic insights into activation and SOCS3-mediated inhibition of myeloproliferative neoplasm-associated JAK2 mutants from biochemical and structural analyses.
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- Biochemical Journal, 2014, v. 458, n. 2, p. 395, doi. 10.1042/BJ20131516
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- Article
Insights into the evolution of divergent nucleotide-binding mechanisms among pseudokinases revealed by crystal structures of human and mouse MLKL.
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- Biochemical Journal, 2014, v. 457, n. 3, p. 369, doi. 10.1042/BJ20131270
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- Article
A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties.
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- Biochemical Journal, 2014, v. 457, n. 2, p. 323, doi. 10.1042/BJ20131174
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- Article
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis.
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- Nature Communications, 2018, v. 9, n. 1, p. 1, doi. 10.1038/s41467-018-04714-7
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- Article
Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-23474-5
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- Article
Conformational interconversion of MLKL and disengagement from RIPK3 precede cell death by necroptosis.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-22400-z
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- Article
Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-21191-7
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- Article
Human RIPK3 maintains MLKL in an inactive conformation prior to cell death by necroptosis.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-27032-x
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- Article
MLKL trafficking and accumulation at the plasma membrane control the kinetics and threshold for necroptosis.
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- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-16887-1
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- Article
Distinct pseudokinase domain conformations underlie divergent activation mechanisms among vertebrate MLKL orthologues.
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- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-16823-3
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- Article
A missense mutation in the MLKL brace region promotes lethal neonatal inflammation and hematopoietic dysfunction.
- Published in:
- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-16819-z
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- Article
Oligomerization‐driven MLKL ubiquitylation antagonizes necroptosis.
- Published in:
- EMBO Journal, 2021, v. 40, n. 23, p. 1, doi. 10.15252/embj.2019103718
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- Article