A motif within the armadillo repeat of Parkinson’s-linked LRRK2 interacts with FADD to hijack the extrinsic death pathway

[1]  G. Hadjigeorgiou,et al.  Activation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 Mutations , 2016, PloS one.

[2]  Robert F Gahl,et al.  Bcl-2 proteins bid and bax form a network to permeabilize the mitochondria at the onset of apoptosis , 2016, Cell Death and Disease.

[3]  Young Ho Suh,et al.  Interplay between Leucine-Rich Repeat Kinase 2 (LRRK2) and p62/SQSTM-1 in Selective Autophagy , 2016, PloS one.

[4]  M. Ueffing,et al.  Structural model of the dimeric Parkinson’s protein LRRK2 reveals a compact architecture involving distant interdomain contacts , 2016, Proceedings of the National Academy of Sciences.

[5]  Matthias Mann,et al.  Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases , 2016, eLife.

[6]  D. Longley,et al.  DED or alive: assembly and regulation of the death effector domain complexes , 2015, Cell Death and Disease.

[7]  H. Miyatake,et al.  Crystal Structure of Human Importin-α1 (Rch1), Revealing a Potential Autoinhibition Mode Involving Homodimerization , 2015, PloS one.

[8]  J. Martinou,et al.  Involvement of cardiolipin in tBID-induced activation of BAX during apoptosis. , 2014, Chemistry and physics of lipids.

[9]  G. Garden,et al.  Bax Interacting Factor-1 Promotes Survival and Mitochondrial Elongation in Neurons , 2014, The Journal of Neuroscience.

[10]  Marta Tormos-Pérez,et al.  Structural and functional in silico analysis of LRRK2 missense substitutions , 2014, Molecular Biology Reports.

[11]  M. Cookson,et al.  Mutant LRRK2 Toxicity in Neurons Depends on LRRK2 Levels and Synuclein But Not Kinase Activity or Inclusion Bodies , 2014, The Journal of Neuroscience.

[12]  Marta Tormos-Pérez,et al.  Structural and functional in silico analysis of LRRK 2 missense substitutions , 2014 .

[13]  M. Cookson,et al.  Biochemical Characterization of Highly Purified Leucine-Rich Repeat Kinases 1 and 2 Demonstrates Formation of Homodimers , 2012, PloS one.

[14]  T. Yeh,et al.  (G2019S) LRRK2 activates MKK4-JNK pathway and causes degeneration of SN dopaminergic neurons in a transgenic mouse model of PD , 2012, Cell Death and Differentiation.

[15]  Mark Ellisman,et al.  LRRK2 Parkinson disease mutations enhance its microtubule association. , 2011, Human molecular genetics.

[16]  Wei Lu,et al.  The kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel disease , 2011, Nature Immunology.

[17]  Zhiheng Xu,et al.  Expression of leucine-rich repeat kinase 2 (LRRK2) inhibits the processing of uMtCK to induce cell death in a cell culture model system. , 2011, Bioscience reports.

[18]  C. Schnell,et al.  LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice , 2011, Human molecular genetics.

[19]  H. Walczak,et al.  Caspase-8 and bid: caught in the act between death receptors and mitochondria. , 2011, Biochimica et biophysica acta.

[20]  張文騰 台灣族群帕金森氏症Leucine-Rich Repeat Kinase 2 (LRRK2) 基因變異的分子功能研究 , 2011 .

[21]  F. Sun,et al.  Expression, purification and preliminary biochemical studies of the N-terminal domain of leucine-rich repeat kinase 2. , 2010, Biochimica et biophysica acta.

[22]  U. Stochaj,et al.  Dissecting the Signaling Events That Impact Classical Nuclear Import and Target Nuclear Transport Factors , 2009, PloS one.

[23]  G. Gores,et al.  Life and death by death receptors , 2009, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[24]  W. Lasoń,et al.  Protective Effect of Memantine Against Doxorubicin Toxicity in Primary Neuronal Cell Cultures: Influence a Development Stage , 2009, Neurotoxicity Research.

[25]  W. Dauer,et al.  The Parkinson Disease Protein Leucine-Rich Repeat Kinase 2 Transduces Death Signals via Fas-Associated Protein with Death Domain and Caspase-8 in a Cellular Model of Neurodegeneration , 2009, The Journal of Neuroscience.

[26]  Boguslaw Stec,et al.  The Fas/FADD death domain complex structure unravels signaling by receptor clustering , 2008, Nature.

[27]  M. Cookson,et al.  The Parkinson Disease-associated Leucine-rich Repeat Kinase 2 (LRRK2) Is a Dimer That Undergoes Intramolecular Autophosphorylation* , 2008, Journal of Biological Chemistry.

[28]  M. P. van der Brug,et al.  Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1 , 2007, Journal of neurochemistry.

[29]  P. Barone,et al.  Apoptotic mechanisms in mutant LRRK2-mediated cell death. , 2007, Human molecular genetics.

[30]  Hynek Wichterle,et al.  Astrocytes expressing ALS-linked mutated SOD1 release factors selectively toxic to motor neurons , 2007, Nature Neuroscience.

[31]  K. Lim,et al.  Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity. , 2007, Human molecular genetics.

[32]  J. Johnson,et al.  Screening for SNCA and LRRK2 mutations in Greek sporadic and autosomal dominant Parkinson's disease: identification of two novel LRRK2 variants , 2007, European journal of neurology.

[33]  M. H. Werner,et al.  FADD self-association is required for stable interaction with an activated death receptor , 2006, Cell Death and Differentiation.

[34]  C. Ross,et al.  Kinase activity of mutant LRRK2 mediates neuronal toxicity , 2006, Nature Neuroscience.

[35]  David W. Miller,et al.  Kinase activity is required for the toxic effects of mutant LRRK2/dardarin , 2006, Neurobiology of Disease.

[36]  M. H. Werner,et al.  The structure of FADD and its mode of interaction with procaspase-8. , 2006, Molecular cell.

[37]  Andrew B West,et al.  Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[38]  G. Rosenberg,et al.  Vulnerability of mouse cortical neurons to doxorubicin-induced apoptosis is strain-dependent and is correlated with mRNAs encoding Fas, Fas-Ligand, and metalloproteinases , 2004, Apoptosis.

[39]  Maurizio Pellecchia,et al.  Targeting apoptosis via chemical design: inhibition of bid-induced cell death by small organic molecules. , 2004, Chemistry & biology.

[40]  A J Carlson,et al.  Frederick R. Rickles, MD, FACP, Appointed Executive Director of the Federation of American Societies for Experimental Biology , 2004, Journal of Investigative Medicine.

[41]  J. Cidlowski,et al.  Molecular evidence for the nuclear localization of FADD , 2003, Cell Death and Differentiation.

[42]  L. Stefanis,et al.  Proteasomal Inhibition-Induced Inclusion Formation and Death in Cortical Neurons Require Transcription and Ubiquitination , 2002, Molecular and Cellular Neuroscience.

[43]  J. Tschopp,et al.  Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling , 2002, FEBS letters.

[44]  S. Korsmeyer,et al.  Bax ablation prevents dopaminergic neurodegeneration in the 1-methyl- 4-phenyl-1,2,3,6-tetrahydropyridine mouse model of Parkinson's disease , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[45]  J. Bertin,et al.  Death-effector Filaments: Novel Cytoplasmic Structures that Recruit Caspases and Trigger Apoptosis , 1998, The Journal of cell biology.

[46]  E. White,et al.  E1B 19K Inhibits Fas-mediated Apoptosis through FADD-dependent Sequestration of FLICE , 1998, The Journal of cell biology.

[47]  Stephen W. Fesik,et al.  NMR structure and mutagenesis of the FADD (Mort1) death-effector domain , 1998, Nature.