Endogenous catecholamine enhances the dysfunction of unfolded protein response and α-synuclein oligomerization in PC12 cells overexpressing human α-synuclein

[1]  Y. Itoyama,et al.  Serine 129 Phosphorylation of α-Synuclein Induces Unfolded Protein Response-mediated Cell Death* , 2008, Journal of Biological Chemistry.

[2]  Nobutaka Hattori,et al.  Progress in the pathogenesis and genetics of Parkinson's disease , 2008, Philosophical Transactions of the Royal Society B: Biological Sciences.

[3]  W. Scheper,et al.  Activation of the unfolded protein response in Parkinson's disease. , 2007, Biochemical and biophysical research communications.

[4]  C. Svendsen,et al.  Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation. , 2007, Human molecular genetics.

[5]  S. Lindquist,et al.  α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models , 2006, Science.

[6]  K. Kitaichi,et al.  Methamphetamine‐induced dopaminergic neurotoxicity is regulated by quinone formation‐related molecules , 2006, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[7]  M. Cookson Neurons inflict self-harm , 2005, Nature Medicine.

[8]  D. Selkoe,et al.  Dopamine covalently modifies and functionally inactivates parkin , 2005, Nature Medicine.

[9]  Songsong Cao,et al.  Torsin-Mediated Protection from Cellular Stress in the Dopaminergic Neurons of Caenorhabditis elegans , 2005, The Journal of Neuroscience.

[10]  K. Nakashima,et al.  L‐dopa and dopamine enhance the formation of aggregates under proteasome inhibition in PC12 cells , 2005, FEBS letters.

[11]  R. Kaufman,et al.  ER stress and the unfolded protein response. , 2005, Mutation research.

[12]  R. Kayed,et al.  Permeabilization of Lipid Bilayers Is a Common Conformation-dependent Activity of Soluble Amyloid Oligomers in Protein Misfolding Diseases* , 2004, Journal of Biological Chemistry.

[13]  A Dürr,et al.  Causal relation between α-synuclein locus duplication as a cause of familial Parkinson's disease , 2004, The Lancet.

[14]  Philippe Amouyel,et al.  α-synuclein locus duplication as a cause of familial Parkinson's disease , 2004, The Lancet.

[15]  K. Prasad,et al.  Overexpression of α‐synuclein decreased viability and enhanced sensitivity to prostaglandin E2, hydrogen peroxide, and a nitric oxide donor in differentiated neuroblastoma cells , 2004, Journal of neuroscience research.

[16]  Janel O. Johnson,et al.  α-Synuclein Locus Triplication Causes Parkinson's Disease , 2003, Science.

[17]  K. O’Malley,et al.  Parkinsonian Mimetics Induce Aspects of Unfolded Protein Response in Death of Dopaminergic Neurons* , 2003, Journal of Biological Chemistry.

[18]  Lloyd A Greene,et al.  Endoplasmic Reticulum Stress and the Unfolded Protein Response in Cellular Models of Parkinson's Disease , 2002, The Journal of Neuroscience.

[19]  P. Aebischer,et al.  α-Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[20]  T. Hashikawa,et al.  CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. , 2002, Molecular cell.

[21]  Nancy A. Jenkins,et al.  Human α-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with α-synuclein aggregation in transgenic mice , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[22]  Bruce A. Yankner,et al.  Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease , 2002, Nature Medicine.

[23]  J. Trojanowski,et al.  Neuronal α-Synucleinopathy with Severe Movement Disorder in Mice Expressing A53T Human α-Synuclein , 2002, Neuron.

[24]  Ron Prywes,et al.  The Luminal Domain of ATF6 Senses Endoplasmic Reticulum (ER) Stress and Causes Translocation of ATF6 from the ER to the Golgi* , 2002, The Journal of Biological Chemistry.

[25]  John Q. Trojanowski,et al.  Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease , 2001, Science.

[26]  Peter T. Lansbury,et al.  Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct , 2001, Science.

[27]  N. Hattori,et al.  An Unfolded Putative Transmembrane Polypeptide, which Can Lead to Endoplasmic Reticulum Stress, Is a Substrate of Parkin , 2001, Cell.

[28]  E. Masliah,et al.  α-Synuclein Promotes Mitochondrial Deficit and Oxidative Stress , 2000 .

[29]  L. Mucke,et al.  Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. , 2000, Science.

[30]  R. Crowther,et al.  α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies , 1998 .