Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson's disease

[1]  E. Kuusisto,et al.  Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation , 2002, Neuropathology and applied neurobiology.

[2]  K. Zatloukal,et al.  Mallory body—A disease‐associated type of sequestosome , 2002, Hepatology.

[3]  M. W. Wooten,et al.  Structure and functional properties of the ubiquitin binding protein p62 , 2002, FEBS letters.

[4]  Kurt Zatloukal,et al.  p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases. , 2002, The American journal of pathology.

[5]  M. Spillantini,et al.  α‐Synuclein metabolism and aggregation is linked to ubiquitin‐independent degradation by the proteasome , 2001, FEBS letters.

[6]  V. Lee,et al.  Parkin and the Molecular Pathways of Parkinson's Disease , 2001, Neuron.

[7]  M. W. Wooten,et al.  Nerve growth factor stimulates the interaction of ZIP/p62 with atypical protein kinase C and targets endosomal localization: Evidence for regulation of nerve growth factor‐induced differentiation , 2001, Journal of cellular biochemistry.

[8]  D. Sulzer,et al.  Proteasomal inhibition leads to formation of ubiquitin/α‐synuclein‐immunoreactive inclusions in PC12 cells , 2001, Journal of neurochemistry.

[9]  D. Dickson,et al.  Alpha-synuclein and the Lewy body disorders. , 2001, Current opinion in neurology.

[10]  Barry Halliwell,et al.  Failure of the ubiquitin–proteasome system in Parkinson's disease , 2001, Nature Reviews Neuroscience.

[11]  E. Kuusisto,et al.  Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies , 2001, Neuroreport.

[12]  Michel Goedert,et al.  Alpha-synuclein and neurodegenerative diseases , 2001, Nature Reviews Neuroscience.

[13]  P. Barker,et al.  The Atypical Protein Kinase C-interacting Protein p62 Is a Scaffold for NF-κB Activation by Nerve Growth Factor* , 2001, The Journal of Biological Chemistry.

[14]  E. Kuusisto,et al.  Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. , 2001, Biochemical and biophysical research communications.

[15]  J. Lowe,et al.  Ubiquitin and the molecular pathology of neurodegenerative diseases. , 2001, Advances in experimental medicine and biology.

[16]  J. Andersen What causes the build-up of ubiquitin-containing inclusions in Parkinson’s disease? , 2000, Mechanisms of Ageing and Development.

[17]  Ken Itoh,et al.  Transcription Factor Nrf2 Coordinately Regulates a Group of Oxidative Stress-inducible Genes in Macrophages* , 2000, The Journal of Biological Chemistry.

[18]  K. Nakashima,et al.  Oxidative stress-related proteins A170 and heme oxygenase-1 are differently induced in the rat cerebellum under kainate-mediated excitotoxicity , 2000, Neuroscience Letters.

[19]  H. Osada,et al.  p62 functions as a p38 MAP kinase regulator. , 2000, Biochemical and biophysical research communications.

[20]  R. Terry,et al.  Do neuronal inclusions kill the cell? , 2000, Journal of neural transmission. Supplementum.

[21]  M. Li,et al.  Differential stimulation of PKC phosphorylation of potassium channels by ZIP1 and ZIP2. , 1999, Science.

[22]  K. Nakashima,et al.  Effects of kainate-mediated excitotoxicity on the expression of rat counterparts of A170 and MSP23 stress proteins in the brain. , 1999, Brain research. Molecular brain research.

[23]  R. Kopito,et al.  Aggresomes: A Cellular Response to Misfolded Proteins , 1998, The Journal of cell biology.

[24]  Jaekyoon Shin P62 and the sequestosome, a novel mechanism for protein metabolism , 1998, Archives of pharmacal research.

[25]  M. Figueiredo-Pereira,et al.  Ubiquitin, cellular inclusions and their role in neurodegeneration , 1998, Trends in Neurosciences.

[26]  A. Puls,et al.  Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[27]  T. Reinheckel,et al.  Degradation of oxidized proteins in mammalian cells , 1997, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[28]  H. Yoshida,et al.  Low micromolar levels of hydrogen peroxide and proteasome inhibitors induce the 60-kDa A170 stress protein in murine peritoneal macrophages. , 1997, Biochemical and biophysical research communications.

[29]  J. Seita,et al.  Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p56lck-associated protein in response to oxidative stress. , 1996, Biochemical and biophysical research communications.

[30]  J. Strominger,et al.  p62, a Phosphotyrosine-independent Ligand of the SH2 Domain of p56lck, Belongs to a New Class of Ubiquitin-binding Proteins* , 1996, The Journal of Biological Chemistry.

[31]  J. Strominger,et al.  Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[32]  E. Kieff,et al.  A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes , 1996, Journal of virology.