Emerging therapeutic targets for Gaucher disease

Bibliography

• Gaucher PCE. De l’epithelioma primitif de la rate. These de Paris: 1882
   Google Scholar
• Brady RO. Introduction: overview and historical perspective. In: Futerman AH, Zimran A, editors. Gaucher disease. Taylor & Francis Group; Boca Raton: 2007. p. 1-12
   Google Scholar
• Aghion E. La maladie de Gaucher dans l’enfance. Faculté de Médecine; Paris: 1934
   Google Scholar
• Brady RO, Kanfer JN, Shapiro D. Metabolism of glucocerebrosides. II. Evidence of an enzymatic deficiency in Gaucher’s disease. Biochem Biophys Res Commun 1965;18:221-5
   PubMed Web of Science ®Google Scholar
• Patrick AD. Short communications: a deficiency of Glucocerebrosidase in Gaucher’s disease. Biochem J 1965;97:17C-8C
   PubMed Web of Science ®Google Scholar
• Weinreb NJ, Brady RO, Tappel AL. The lysosomal localization of sphingolipid hydrolases. Biochim Biophys Acta 1968;159:141-6
   PubMed Web of Science ®Google Scholar
• Sorge J, West C, Westwood B, Beutler E. Molecular cloning and nucleotide sequence of human glucocerebrosidase cDNA. Proc Natl Acad Sci USA 1985;82:7289-93
   PubMed Web of Science ®Google Scholar
• Horowitz M, Wilder S, Horowitz Z, et al. The human glucocerebrosidase gene and pseudogene: structure and evolution. Genomics 1989;4:87-96
   PubMed Web of Science ®Google Scholar
• Hruska KS, LaMarca ME, Scott CR, et al. Gaucher disease: mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA). Hum Mutat 2008;29:567-83
   PubMed Web of Science ®Google Scholar
• Dvir H, Harel M, McCarthy AA, et al. X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease. EMBO Rep 2003;4:704-9
   PubMed Web of Science ®Google Scholar
• Premkumar L, Sawkar AR, Boldin-Adamsky S, et al. X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease. J Biol Chem 2005;280:23815-19
   PubMed Web of Science ®Google Scholar
• Burns GF, Cawley JC, Flemans RJ, et al. Surface marker and other characteristics of Gaucher’s cells. J Clin Pathol 1977;30:981-8
   PubMed Web of Science ®Google Scholar
• Boven LA, van Meurs M, Boot RG, et al. Gaucher cells demonstrate a distinct macrophage phenotype and resemble alternatively activated macrophages. Am J Clin Pathol 2004;122:359-69
   PubMed Web of Science ®Google Scholar
• Beutler E, Grabowski GA. Gaucher disease. In: Sciver CR, Beaudet AL, Sly WS, Valle D, editors. The metabolic and molecular bases of inherited diseases. 8th edition. McGraw-Hill; New York: 2001. p. 3635
   Google Scholar
• Fuller M, Meikle PJ, Hopwood JJ. Epidemiology of lysosomal storage diseases: an overview. In: Mehta A, Beck M, Sunder-Plassmann G, editors. Fabry disease: perspectives from 5 years of FOS. Oxford PharmaGenesis; Oxford: 2006
   Google Scholar
• Ratjen F, Doring G. Cystic fibrosis. Lancet 2003;361:681-9
   PubMed Web of Science ®Google Scholar
• Walker FO. Huntington’s disease. Lancet 2007;369:218-28
   PubMed Web of Science ®Google Scholar
• Deegan PB, Cox TM. Imiglucerase in the treatment of Gaucher disease: a history and perspective. Drug Des Devel Ther 2012;6:81-106
   PubMed Web of Science ®Google Scholar
• Hruska KS, Goker-Alpan O, Sidransky E. Gaucher disease and the synucleinopathies. J Biomed Biotechnol 2006;2006:78549
   PubMedGoogle Scholar
• Sidransky E, Nalls MA, Aasly JO, et al. Multicenter analysis of glucocerebrosidase mutations in Parkinson’s disease. N Engl J Med 2009;361:1651-61
   PubMed Web of Science ®Google Scholar
• Schiffmann R, Vellodi A. Neuronopathic gaucher disease. In: Futerman AH, Zimran A, editors. Gaucher disease. Taylor & Francis Group; Boca Raton: 2007. p. 175-96
   Google Scholar
• Futerman AH, Sussman JL, Horowitz M, et al. New directions in the treatment of Gaucher disease. Trends Pharmacol Sci 2004;25:147-51
   PubMed Web of Science ®Google Scholar
• Cox TM. Gaucher disease: clinical profile and therapeutic developments. Biologics 2010;4:299-313
   PubMedGoogle Scholar
• Pastores GM, Hughes DA. Gaucher disease. In: GeneReviews® [Internet] Pagon RA, Adam MP, Ardinger HH, et al. editors. University of Washington: Seattle: 1993
   Google Scholar
• Pentchev PG, Brady RO, Hibbert SR, et al. Isolation and characterization of glucocerebrosidase from human placental tissue. J Biol Chem 1973;248:5256-61
   PubMed Web of Science ®Google Scholar
• Zimran A, Elstein D, Levy-Lahad E, et al. Replacement therapy with imiglucerase for type 1 Gaucher’s disease. Lancet 1995;345:1479-80
   PubMed Web of Science ®Google Scholar
• Gonzalez DE, Turkia HB, Lukina EA, et al. Enzyme replacement therapy with velaglucerase alfa in Gaucher disease: results from a randomized, double-blind, multinational, Phase 3 study. Am J Hematol 2013;88:166-71
   PubMed Web of Science ®Google Scholar
• Zimran A, Pastores GM, Tylki-Szymanska A, et al. Safety and efficacy of velaglucerase alfa in Gaucher disease type 1 patients previously treated with imiglucerase. Am J Hematol 2013;88:172-8
   PubMed Web of Science ®Google Scholar
• Ben Turkia H, Gonzalez DE, Barton NW, et al. Velaglucerase alfa enzyme replacement therapy compared with imiglucerase in patients with Gaucher disease. Am J Hematol 2013;88:179-84
   PubMed Web of Science ®Google Scholar
• Brumshtein B, Salinas P, Peterson B, et al. Characterization of gene-activated human acid-beta-glucosidase: crystal structure, glycan composition, and internalization into macrophages. Glycobiology 2010;20:24-32
   PubMed Web of Science ®Google Scholar
• Zimran A, Loveday K, Fratazzi C, et al. A pharmacokinetic analysis of a novel enzyme replacement therapy with Gene-Activated human glucocerebrosidase (GA-GCB) in patients with type 1 Gaucher disease. Blood Cells Mol Dis 2007;39:115-18
   PubMed Web of Science ®Google Scholar
• Grabowski GA, Golembo M, Shaaltiel Y. Taliglucerase alfa: an enzyme replacement therapy using plant cell expression technology. Mol Genet Metab 2014;112:1-8
   PubMed Web of Science ®Google Scholar
• Hollak CEM, Dahl vom S, Aerts JMFG, et al. Force majeure: therapeutic measures in response to restricted supply of imiglucerase (Cerezyme) for patients with Gaucher disease. Blood Cells Mol Dis 2010;44:41-7
   PubMed Web of Science ®Google Scholar
• Cox T, Lachmann R, Hollak C, et al. Novel oral treatment of Gaucher’s disease with N-butyldeoxynojirimycin (OGT 918) to decrease substrate biosynthesis. Lancet 2000;355:1481-5
   PubMed Web of Science ®Google Scholar
• Platt FM, Cox TM. Substrate reduction therapy. In: Futerman AH, Zimran A, editors. Gaucher disease. Taylor & Francis Group; Boca Raton: 2007. p. 355-76
   Google Scholar
• Zimran A. How I treat Gaucher disease. Blood 2011;118:1463-71
   PubMed Web of Science ®Google Scholar
• Platt FM, Neises GR, Dwek RA, et al. N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis. J Biol Chem 1994;269:8362-5
   PubMed Web of Science ®Google Scholar
• Boot RG, Verhoek M, Donker-Koopman W, et al. Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J Biol Chem 2007;282:1305-12
   PubMed Web of Science ®Google Scholar
• Kuter DJ, Mehta A, Hollak CEM, et al. Miglustat therapy in type 1 Gaucher disease: clinical and safety outcomes in a multicenter retrospective cohort study. Blood Cells Mol Dis 2013;51:116-24
   PubMed Web of Science ®Google Scholar
• Elstein D, Hollak C, Aerts JMFG, et al. Sustained therapeutic effects of oral miglustat (Zavesca, N-butyldeoxynojirimycin, OGT 918) in type I Gaucher disease. J Inherit Metab Dis 2004;27:757-66
   PubMed Web of Science ®Google Scholar
• Schiffmann R, Fitzgibbon EJ, Harris C, et al. Randomized, controlled trial of miglustat in Gaucher’s disease type 3. Ann Neurol 2008;64:514-22
   PubMed Web of Science ®Google Scholar
• Lukina E, Watman N, Arreguin EA, et al. Improvement in hematological, visceral, and skeletal manifestations of Gaucher disease type 1 with oral eliglustat tartrate (Genz-112638) treatment: 2-year results of a phase 2 study. Blood 2010;116:4095-8
   PubMed Web of Science ®Google Scholar
• Cox TM. Eliglustat tartrate, an orally active glucocerebroside synthase inhibitor for the potential treatment of Gaucher disease and other lysosomal storage diseases. Curr Opin Investig Drugs 2010;11:1169-81
   PubMed Web of Science ®Google Scholar
• Vembar SS, Brodsky JL. One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 2008;9:944-57
   PubMed Web of Science ®Google Scholar
• Hoseki J, Ushioda R, Nagata K. Mechanism and components of endoplasmic reticulum-associated degradation. J Biochem 2010;147:19-25
   PubMed Web of Science ®Google Scholar
• Ron I, Horowitz M. ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum Mol Genet 2005;14:2387-98
   PubMed Web of Science ®Google Scholar
• Goldin E, Zheng W, Motabar O, et al. High throughput screening for small molecule therapy for Gaucher disease using patient tissue as the source of mutant glucocerebrosidase. PLoS One 2012;7:e29861
   PubMed Web of Science ®Google Scholar
• Patnaik S, Zheng W, Choi JH, et al. Discovery, structure-activity relationship, and biological evaluation of noninhibitory small molecule chaperones of glucocerebrosidase. J Med Chem 2012;55:5734-48
   PubMed Web of Science ®Google Scholar
• Sawkar AR, Cheng W-C, Beutler E, et al. Chemical chaperones increase the cellular activity of N370S beta -glucosidase: a therapeutic strategy for Gaucher disease. Proc Natl Acad Sci USA 2002;99:15428-33
   PubMed Web of Science ®Google Scholar
• Benito JM, Garcia Fernandez JM, Ortiz Mellet C. Pharmacological chaperone therapy for Gaucher disease: a patent review. Expert Opin Ther Pat 2011;21:885-903
   PubMed Web of Science ®Google Scholar
• Maegawa GHB, Tropak MB, Buttner JD, et al. Identification and characterization of ambroxol as an enzyme enhancement agent for Gaucher disease. J Biol Chem 2009;284:23502-16
   PubMed Web of Science ®Google Scholar
• Weiser T. Ambroxol: a CNS drug? CNS Neurosci Ther 2008;14:17-24
   PubMed Web of Science ®Google Scholar
• Zimran A, Altarescu G, Elstein D. Pilot study using ambroxol as a pharmacological chaperone in type 1 Gaucher disease. Blood Cells Mol Dis 2013;50:134-7
   PubMed Web of Science ®Google Scholar
• Goker-Alpan O. Commentary on “Pilot study using ambroxol as a pharmacological chaperone in type 1 Gaucher disease” by Zimran et al. Blood Cells Mol Dis 2013;50:138-9
   PubMed Web of Science ®Google Scholar
• Barranger JA, Rice EO, Dunigan J, et al. Gaucher’s disease: studies of gene transfer to haematopoietic cells. Baillieres Clin Haematol 1997;10:765-78
   PubMedGoogle Scholar
• Enquist IB, Nilsson E, Månsson J-E, et al. Successful low-risk hematopoietic cell therapy in a mouse model of type 1 Gaucher disease. Stem Cells 2009;27:744-52
   PubMed Web of Science ®Google Scholar
• Kim EY, Hong YB, Lai Z, et al. Expression and secretion of human glucocerebrosidase mediated by recombinant lentivirus vectors in vitro and in vivo: implications for gene therapy of Gaucher disease. Biochem Biophys Res Commun 2004;318:381-90
   PubMed Web of Science ®Google Scholar
• Diaz-Font A, Cormand B, Chabas A, et al. Unsuccessful chimeraplast strategy for the correction of a mutation causing Gaucher disease. Blood Cells Mol Dis 2003;31:183-6
   PubMed Web of Science ®Google Scholar
• McEachern KA, Nietupski JB, Chuang W-L, et al. AAV8-mediated expression of glucocerebrosidase ameliorates the storage pathology in the visceral organs of a mouse model of Gaucher disease. J Gene Med 2006;8:719-29
   PubMed Web of Science ®Google Scholar
• Cox TM, Schofield JP. Gaucher’s disease: clinical features and natural history. Baillieres Clin Haematol 1997;10:657-89
   PubMed Web of Science ®Google Scholar
• Bemelmans A-P, Duque S, Riviere C, et al. A single intravenous AAV9 injection mediates bilateral gene transfer to the adult mouse retina. PLoS One 2013;8:e61618
   PubMed Web of Science ®Google Scholar
• Rahim AA, Wong AMS, Hoefer K, et al. Intravenous administration of AAV2/9 to the fetal and neonatal mouse leads to differential targeting of CNS cell types and extensive transduction of the nervous system. FASEB J 2011;25:3505-18
   PubMed Web of Science ®Google Scholar
• Korkotian E, Schwarz A, Pelled D, et al. Elevation of intracellular glucosylceramide levels results in an increase in endoplasmic reticulum density and in functional calcium stores in cultured neurons. Clin Immunol 1999;147:21673-8
   Google Scholar
• Pelled D, Trajkovic-Bodennec S, Lloyd-Evans E, et al. Enhanced calcium release in the acute neuronopathic form of Gaucher disease. Neurobiol Dis 2005;18:83-8
   PubMed Web of Science ®Google Scholar
• Osellame LD, Rahim AA, Hargreaves IP, et al. Mitochondria and quality control defects in a mouse model of Gaucher disease – links to Parkinson’s disease. Cell Metab 2013;17:941-53
   PubMed Web of Science ®Google Scholar
• Farfel-Becker T, Vitner EB, Kelly SL, et al. Neuronal accumulation of glucosylceramide in a mouse model of neuronopathic Gaucher disease leads to neurodegeneration. Hum Mol Genet 2014;23:843-54
   PubMed Web of Science ®Google Scholar
• Ballabio A. Disease pathogenesis explained by basic science: lysosomal storage diseases as autophagocytic disorders. Int J Clin Pharmacol Ther 2009;47(Suppl 1):S34-8
   PubMed Web of Science ®Google Scholar
• Ridley CM, Thur KE, Shanahan J, et al. Beta-Glucosidase 2 (GBA2) activity and imino sugar pharmacology. J Biol Chem 2013;288:26052-66
   PubMed Web of Science ®Google Scholar
• Yildiz Y, Matern H, Thompson B, et al. Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility. J Clin Invest 2006;116:2985-94
   PubMed Web of Science ®Google Scholar
• Citterio A, Arnoldi A, Panzeri E, et al. Mutations in CYP2U1, DDHD2 and GBA2 genes are rare causes of complicated forms of hereditary spastic paraparesis. J Neurol 2014;261:373-81
   PubMed Web of Science ®Google Scholar
• Martin E, Schüle R, Smets K, et al. Loss of function of glucocerebrosidase GBA2 is responsible for motor neuron defects in hereditary spastic paraplegia. Am J Hum Genet 2013;92:238-44
   PubMed Web of Science ®Google Scholar
• Hammer MB, Eleuch-Fayache G, Schottlaender LV, et al. Mutations in GBA2 cause autosomal-recessive cerebellar ataxia with spasticity. Am J Hum Genet 2013;92:245-51
   PubMed Web of Science ®Google Scholar
• Mistry PK, Liu J, Sun L, et al. Glucocerebrosidase 2 gene deletion rescues type 1 Gaucher disease. Proc Natl Acad Sci USA 2014;111:4934-9
   PubMed Web of Science ®Google Scholar
• Enquist IB, Nilsson E, Ooka A, et al. Effective cell and gene therapy in a murine model of Gaucher disease. Proc Natl Acad Sci USA 2006;103:13819-24
   PubMed Web of Science ®Google Scholar
• Mistry PK, Liu J, Yang M, et al. Glucocerebrosidase gene-deficient mouse recapitulates Gaucher disease displaying cellular and molecular dysregulation beyond the macrophage. Proc Natl Acad Sci USA 2010;107:19473-8
   PubMed Web of Science ®Google Scholar
• Airola MV, Hannun YA. Sphingolipid metabolism and neutral sphingomyelinases. Handb Exp Pharmacol 2013(215):57-76
   PubMedGoogle Scholar
• Kitatani K, Sheldon K, Rajagopalan V, et al. Involvement of acid beta-glucosidase 1 in the salvage pathway of ceramide formation. J Biol Chem 2009;284:12972-8
   PubMed Web of Science ®Google Scholar
• Kitatani K, Sheldon K, Anelli V, et al. Acid beta-glucosidase 1 counteracts p38delta-dependent induction of interleukin-6: possible role for ceramide as an anti-inflammatory lipid. J Biol Chem 2009;284:12979-88
   PubMed Web of Science ®Google Scholar
• Yildiz Y, Hoffmann P, Dahl Vom S, et al. Functional and genetic characterization of the non-lysosomal glucosylceramidase 2 as a modifier for Gaucher disease. Orphanet J Rare Dis 2013;8:151
   PubMed Web of Science ®Google Scholar
• Vitner EB, Salomon R, Farfel-Becker T, et al. RIPK3 as a potential therapeutic target for Gaucher’s disease. Nat Med 2014;20:204-8
   PubMed Web of Science ®Google Scholar
• Moriwaki K, Chan FKM. Necrosis-dependent and independent signaling of the RIP kinases in inflammation. Cytokine Growth Factor Rev 2013;25:167-74
   PubMed Web of Science ®Google Scholar
• Moriwaki K, Chan FK-M. RIP3: a molecular switch for necrosis and inflammation. Genes Dev 2013;27:1640-9
   PubMed Web of Science ®Google Scholar
• Zhou W, Yuan J. Necroptosis in health and diseases. Semin Cell Dev Biol 2014;35C:14-23
   Google Scholar
• Kanfer JN, Legler G, Sullivan J, et al. The Gaucher mouse. Biochem Biophys Res Commun 1975;67:85-90
   PubMed Web of Science ®Google Scholar
• Farfel-Becker T, Vitner EB, Futerman AH. Animal models for Gaucher disease research. Dis Model Mech 2011;4:746-52
   PubMed Web of Science ®Google Scholar
• Kaiser WJ, Sridharan H, Huang C, et al. Toll-like Receptor 3-mediated necrosis via TRIF, RIP3 and MLKL. J Biol Chem 2013;288(43):31268-79
   PubMed Web of Science ®Google Scholar
• Sun L, Wang H, Wang Z, et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 2012;148:213-27
   PubMed Web of Science ®Google Scholar
• Li J-X, Feng J-M, Wang Y, et al. The B-Raf(V600E) inhibitor dabrafenib selectively inhibits RIP3 and alleviates acetaminophen-induced liver injury. Cell Death Dis 2014;5:e1278
   PubMed Web of Science ®Google Scholar
• Mittapalli RK, Vaidhyanathan S, Dudek AZ, et al. Mechanisms limiting distribution of the threonine-protein kinase B-RaF(V600E) inhibitor dabrafenib to the brain: implications for the treatment of melanoma brain metastases. J Pharmacol Exp Ther 2013;344:655-64
   PubMed Web of Science ®Google Scholar
• Chavez-Valdez R, Martin LJ, Flock DL, et al. Necrostatin-1 attenuates mitochondrial dysfunction in neurons and astrocytes following neonatal hypoxia-ischemia. Neuroscience 2012;219:192-203
   PubMed Web of Science ®Google Scholar
• Rosenbaum DM, Degterev A, David J, et al. Necroptosis, a novel form of caspase-independent cell death, contributes to neuronal damage in a retinal ischemia-reperfusion injury model. J Neurosci Res 2010;88:1569-76
   PubMed Web of Science ®Google Scholar
• Trichonas G, Murakami Y, Thanos A, et al. Receptor interacting protein kinases mediate retinal detachment-induced photoreceptor necrosis and compensate for inhibition of apoptosis. Proc Natl Acad Sci USA 2010;107:21695-700
   PubMed Web of Science ®Google Scholar
• You Z, Savitz SI, Yang J, et al. Necrostatin-1 reduces histopathology and improves functional outcome after controlled cortical impact in mice. J Cereb Blood Flow Metab 2008;28:1564-73
   PubMed Web of Science ®Google Scholar
• Jagtap PG, Degterev A, Choi S, et al. Structure-activity relationship study of tricyclic necroptosis inhibitors. J Med Chem 2007;50:1886-95
   PubMed Web of Science ®Google Scholar
• Zhu S, Zhang Y, Bai G, et al. Necrostatin-1 ameliorates symptoms in R6/2 transgenic mouse model of Huntington’s disease. Cell Death Dis 2011;2:e115
   PubMed Web of Science ®Google Scholar
• Re DB, Le Verche V, Yu C, et al. Necroptosis drives motor neuron death in models of both sporadic and familial ALS. Neuron 2014;81:1001-8
   PubMed Web of Science ®Google Scholar
• Tenev T, Bianchi K, Darding M, et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol Cell 2011;43:432-48
   PubMed Web of Science ®Google Scholar
• Lin Y, Devin A, Rodriguez Y, et al. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev 1999;13:2514-26
   PubMed Web of Science ®Google Scholar
• Cho Y, Challa S, Moquin D, et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 2009;137:1112-23
   PubMed Web of Science ®Google Scholar
• He S, Wang L, Miao L, et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 2009;137:1100-11
   PubMed Web of Science ®Google Scholar
• Declercq W, Vanden Berghe T, Vandenabeele P. RIP kinases at the crossroads of cell death and survival. Cell 2009;138:229-32
   PubMed Web of Science ®Google Scholar
• Vitner EB, Farfel-Becker T, Eilam R, et al. Contribution of brain inflammation to neuronal cell death in neuronopathic forms of Gaucher’s disease. Brain 2012;135:1724-35
   PubMed Web of Science ®Google Scholar
• He S, Liang Y, Shao F, et al. Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3-mediated pathway. Proc Natl Acad Sci USA 2011;108:20054-9
   PubMed Web of Science ®Google Scholar
• Weng D, Marty-Roix R, Ganesan S, et al. Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death. Proc Natl Acad Sci USA 2014;111(20):7391-6
   PubMed Web of Science ®Google Scholar
• Hennessy EJ, Parker AE, O’Neill LAJ. Targeting Toll-like receptors: emerging therapeutics? Nat Rev Drug Discov 2010;9:293-307
   PubMed Web of Science ®Google Scholar
• Thapa RJ, Nogusa S, Chen P, et al. Interferon-induced RIP1/RIP3-mediated necrosis requires PKR and is licensed by FADD and caspases. Proc Natl Acad Sci USA 2013;110:E3109-18
   PubMed Web of Science ®Google Scholar
• Robinson N, McComb S, Mulligan R, et al. Type I interferon induces necroptosis in macrophages during infection with Salmonella enterica serovar Typhimurium. Nat Immunol 2012;13:954-62
   PubMed Web of Science ®Google Scholar
• Kirou KA, Gkrouzman E. Anti-interferon alpha treatment in SLE. Clin Immunol 2013;148:303-12
   PubMed Web of Science ®Google Scholar
• Kang T-B, Yang S-H, Toth B, et al. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 2013;38:27-40
   PubMed Web of Science ®Google Scholar
• Yang Y, Ma J, Chen Y, et al. Nucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): identification of novel nuclear export and import signals in RIP3. J Biol Chem 2004;279:38820-9
   PubMed Web of Science ®Google Scholar
• Dondelinger Y, Declercq W, Montessuit S, et al. MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates. Cell Rep 2014;7:971-81
   PubMed Web of Science ®Google Scholar
• Wang H, Sun L, Su L, et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol Cell 2014;54:133-46
   PubMed Web of Science ®Google Scholar
• Vince JE, Wong WW, Gentle I, et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity 2012;36:215-27
   PubMed Web of Science ®Google Scholar
• Kovalenko A, Kim J-C, Kang T-B, et al. Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease. J Exp Med 2009;206:2161-77
   PubMed Web of Science ®Google Scholar
• Lee P, Lee D-J, Chan C, et al. Dynamic expression of epidermal caspase 8 simulates a wound healing response. Nature 2009;458:519-23
   PubMed Web of Science ®Google Scholar
• Kaiser WJ, Upton JW, Long AB, et al. RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature 2011;471:368-72
   PubMed Web of Science ®Google Scholar
• Moll M, Kuemmerle-Deschner JB. Inflammasome and cytokine blocking strategies in autoinflammatory disorders. Clin Immunol 2013;147:242-75
   PubMed Web of Science ®Google Scholar
• Suzuki K, Taniike M. Murine model of genetic demyelinating disease: the twitcher mouse. Microsc Res Tech 1995;32:204-14
   PubMed Web of Science ®Google Scholar
• Enquist IB, Bianco Lo C, Ooka A, et al. Murine models of acute neuronopathic Gaucher disease. Proc Natl Acad Sci USA 2007;104:17483-8
   PubMed Web of Science ®Google Scholar
• Xu Y-H, Reboulet R, Quinn B, et al. Dependence of reversibility and progression of mouse neuronopathic Gaucher disease on acid beta-glucosidase residual activity levels. Mol Genet Metab 2008;94:190-203
   PubMed Web of Science ®Google Scholar
• Xu Y-H, Xu K, Sun Y, et al. Multiple pathogenic proteins implicated in neuronopathic Gaucher disease mice. Hum Mol Genet 2014;23:3943-57
   PubMed Web of Science ®Google Scholar
• Tiscornia G, Vivas EL, Matalonga L, et al. Neuronopathic Gaucher’s disease: induced pluripotent stem cells for disease modelling and testing chaperone activity of small compounds. Hum Mol Genet 2013;22:633-45
   PubMed Web of Science ®Google Scholar
• Aflaki E, Stubblefield BK, Maniwang E, et al. Macrophage models of Gaucher disease for evaluating disease pathogenesis and candidate drugs. Sci Transl Med 2014;6:240ra73
   PubMed Web of Science ®Google Scholar
• Panicker LM, Miller D, Park TS, et al. Induced pluripotent stem cell model recapitulates pathologic hallmarks of Gaucher disease. Proc Natl Acad Sci USA 2012;109:18054-9
   PubMed Web of Science ®Google Scholar