Found: 10
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Chemo-sensitisation of HeLa cells to Etoposide by a Benzoxazine in the absence of DNA-PK inhibition.
- Published in:
- Investigational New Drugs, 2013, v. 31, n. 6, p. 1466, doi. 10.1007/s10637-013-0031-z
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- Article
Phosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization.
- Published in:
- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-42255-w
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- Article
The Lck inhibitor, AMG-47a, blocks necroptosis and implicates RIPK1 in signalling downstream of MLKL.
- Published in:
- Cell Death & Disease, 2022, v. 13, n. 4, p. 1, doi. 10.1038/s41419-022-04740-w
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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
Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance.
- Published in:
- 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.
- Published in:
- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-22400-z
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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.
- Published in:
- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-16823-3
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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