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dc.contributor.authorHildebrand, JM
dc.contributor.authorLucet, IS
dc.contributor.authorMurphy, JM
dc.date.accessioned2021-02-12T00:25:23Z
dc.date.available2021-02-12T00:25:23Z
dc.date.issued2015-01-01
dc.identifierpii: 985550
dc.identifier.citationHildebrand, J. M., Lucet, I. S. & Murphy, J. M. (2015). Flicking the molecular switch underlying MLKL-mediated necroptosis. MOLECULAR & CELLULAR ONCOLOGY, 2 (3), https://doi.org/10.4161/23723556.2014.985550.
dc.identifier.issn2372-3556
dc.identifier.urihttp://hdl.handle.net/11343/260592
dc.description.abstractThe pseudokinase domain of the necroptosis effector mixed lineage kinase domain-like (MLKL) functions as a latch to restrain the unleashing of its N-terminal 4-helix bundle (4HB) domain. Cell death mediated by the 4HB domain relies on membrane association and oligomerization, which can be inhibited by an ATP-mimetic small molecule that binds the pseudokinase domain of MLKL.
dc.languageEnglish
dc.publisherTAYLOR & FRANCIS INC
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0
dc.titleFlicking the molecular switch underlying MLKL-mediated necroptosis
dc.typeJournal Article
dc.identifier.doi10.4161/23723556.2014.985550
melbourne.affiliation.departmentMedical Biology (W.E.H.I.)
melbourne.affiliation.facultyMedicine, Dentistry & Health Sciences
melbourne.source.titleMolecular and Cellular Oncology
melbourne.source.volume2
melbourne.source.issue3
dc.rights.licenseCC BY-NC
melbourne.elementsid1072918
melbourne.contributor.authorLucet, Isabelle
melbourne.contributor.authorHildebrand, Joanne
melbourne.contributor.authorMurphy, James
dc.identifier.eissn2372-3548
melbourne.accessrightsOpen Access


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