Phosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization
Yanxiang Meng(École Polytechnique Fédérale de Lausanne), James M. Murphy(The University of Melbourne)
Cited by 35
Related Papers
MLKL trafficking and accumulation at the plasma membrane control the kinetics and threshold for necroptosis
|Nature Communications|2020|352
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis
|Nature Communications|2018|192
HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death
|Cell Death and Disease|2016|158
Evolutionary divergence of the necroptosis effector MLKL
|Cell Death and Differentiation|2016|128
The brace helices of MLKL mediate interdomain communication and oligomerisation to regulate cell death by necroptosis
|Cell Death and Differentiation|2018|99