title: The importance of being chaperoned: HSP90 and necroptosis.
abstract: Necroptosis is a form of regulated cell death implicated in a range of inflammatory diseases. In this issue of Cell Chemical Biology, Li et al. (2016) describe a novel inhibitor of necroptosis that targets the chaperone protein HSP90.
authors.affiliation: The Walter and Eliza Hall Institute of Medical Research, Melbourne, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Melbourne, Australia.
authors.forename: Annette V
authors.initials: AV
authors.lastname: Jacobsen
authors.affiliation: The Walter and Eliza Hall Institute of Medical Research, Melbourne, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Melbourne, Australia. Electronic address: silke@wehi.edu.au.
authors.forename: John
authors.initials: J
authors.lastname: Silke
mesh_terms: D017209:Apoptosis; D016923:Cell Death; D045744:Cell Line, Tumor; D002470:Cell Survival; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D050884:HSP72 Heat-Shock Proteins / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D009336:Necrosis / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D053422:Receptor-Interacting Protein Serine-Threonine Kinases / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D018840:HSP70 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; D011494:Protein Kinases; D053422:Receptor-Interacting Protein Serine-Threonine Kinases