Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo

[1]  B. Chesebro,et al.  Crucial Role for Prion Protein Membrane Anchoring in the Neuroinvasion and Neural Spread of Prion Infection , 2010, Journal of Virology.

[2]  M. Giustetto,et al.  Blocking ADAM10 synaptic trafficking generates a model of sporadic Alzheimer's disease. , 2010, Brain : a journal of neurology.

[3]  I. Zerr,et al.  Cellular prion protein overexpression disturbs cellular homeostasis in SH-SY5Y neuroblastoma cells but does not alter p53 expression: a proteomic study , 2010, Neuroscience.

[4]  E. Kremmer,et al.  ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons , 2010, The EMBO journal.

[5]  G. Weskamp,et al.  The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex , 2010, The Journal of Neuroscience.

[6]  Frank Baumann,et al.  Axonal prion protein is required for peripheral myelin maintenance , 2010, Nature Neuroscience.

[7]  B. Chesebro,et al.  Fatal Transmissible Amyloid Encephalopathy: A New Type of Prion Disease Associated with Lack of Prion Protein Membrane Anchoring , 2010, PLoS pathogens.

[8]  A. Aguzzi,et al.  Unexpected Tolerance of α-Cleavage of the Prion Protein to Sequence Variations , 2010, PloS one.

[9]  E. Kojro,et al.  Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo , 2009, Neurobiology of Disease.

[10]  F. Checler,et al.  The α-Secretase-derived N-terminal Product of Cellular Prion, N1, Displays Neuroprotective Function in Vitro and in Vivo* , 2009, The Journal of Biological Chemistry.

[11]  Alberto Inga,et al.  The expanding universe of p53 targets , 2009, Nature Reviews Cancer.

[12]  N. Hooper,et al.  Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein* , 2009, The Journal of Biological Chemistry.

[13]  J. Grosche,et al.  ADAM10 is the constitutive functional sheddase of CD44 in human melanoma cells. , 2009, The Journal of investigative dermatology.

[14]  P. S. St George-Hyslop,et al.  p53-Dependent Transcriptional Control of Cellular Prion by Presenilins , 2009, The Journal of Neuroscience.

[15]  S. Booth,et al.  Activation of p53-regulated pro-apoptotic signaling pathways in PrP-mediated myopathy , 2009, BMC Genomics.

[16]  John W. Gilbert,et al.  Cellular Prion Protein Mediates Impairment of Synaptic Plasticity by Amyloid-β Oligomers , 2009, Nature.

[17]  N. Hooper,et al.  α-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts , 2009, Molecular and Cellular Neuroscience.

[18]  G. Murphy.  The ADAMs: signalling scissors in the tumour microenvironment , 2008, Nature Reviews Cancer.

[19]  N. Hooper,et al.  Cellular prion protein regulates β-secretase cleavage of the Alzheimer's amyloid precursor protein , 2007, Proceedings of the National Academy of Sciences.

[20]  B. Ghetti,et al.  Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice , 2007, The EMBO journal.

[21]  F. Checler,et al.  The C-terminal Products of Cellular Prion Protein Processing, C1 and C2, Exert Distinct Influence on p53-dependent Staurosporine-induced Caspase-3 Activation* , 2007, Journal of Biological Chemistry.

[22]  J. Lieberman,et al.  Metalloprotease-induced ectodomain shedding of neural cell adhesion molecule (NCAM). , 2006, Journal of neurobiology.

[23]  Andrew D. Steele,et al.  Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. , 2006, Proceedings of the National Academy of Sciences of the United States of America.

[24]  T. Sklaviadis,et al.  The FASEB Journal express article 10.1096/fj.05-4279fje. Published online December 13, 2005. ©2005 FASEB , 2022 .

[25]  F. Checler,et al.  The Disintegrin ADAM9 Indirectly Contributes to the Physiological Processing of Cellular Prion by Modulating ADAM10 Activity* , 2005, Journal of Biological Chemistry.

[26]  J. Hauw,et al.  The N‐terminal cleavage of cellular prion protein in the human brain , 2005, FEBS letters.

[27]  N. Hooper,et al.  Reactive Oxygen Species-mediated β-Cleavage of the Prion Protein in the Cellular Response to Oxidative Stress* , 2005, Journal of Biological Chemistry.

[28]  C. Blobel,et al.  Adam Meets Eph: An ADAM Substrate Recognition Module Acts as a Molecular Switch for Ephrin Cleavage In trans , 2005, Cell.

[29]  M. Schachner,et al.  Electroporation-based gene transfer for efficient transfection of neural precursor cells. , 2005, Brain research. Molecular brain research.

[30]  Austin G Smith,et al.  Niche-Independent Symmetrical Self-Renewal of a Mammalian Tissue Stem Cell , 2005, PLoS biology.

[31]  A. Aguzzi,et al.  Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrPC , 2005, The Journal of Neuroscience.

[32]  N. Hooper,et al.  Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein. , 2005, Biochemical Society transactions.

[33]  B. de Strooper,et al.  ADAM10 cleavage of N‐cadherin and regulation of cell–cell adhesion and β‐catenin nuclear signalling , 2005, The EMBO journal.

[34]  V. Vasioukhin.  Faculty Opinions recommendation of ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling. , 2005 .

[35]  N. Hooper,et al.  Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress. , 2005, The Journal of biological chemistry.

[36]  N. Hooper,et al.  Dual Mechanisms for Shedding of the Cellular Prion Protein* , 2004, Journal of Biological Chemistry.

[37]  J. Bourdon,et al.  Primary Cultured Neurons Devoid of Cellular Prion Display Lower Responsiveness to Staurosporine through the Control of p53 at Both Transcriptional and Post-transcriptional Levels* , 2004, Journal of Biological Chemistry.

[38]  Robin Fahraeus,et al.  Cellular Prion Protein Sensitizes Neurons to Apoptotic Stimuli through Mdm2-regulated and p53-dependent Caspase 3-like Activation* , 2003, The Journal of Biological Chemistry.

[39]  B. de Strooper,et al.  The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts. , 2002, Human molecular genetics.

[40]  M. W. Young,et al.  kuzbanian-mediated cleavage of Drosophila Notch. , 2002, Genes & development.

[41]  B. Strooper,et al.  The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. , 2001, The Journal of biological chemistry.

[42]  F. Heppner,et al.  Sympathetic Innervation of Lymphoreticular Organs Is Rate Limiting for Prion Neuroinvasion , 2001, Neuron.

[43]  Adriano Aguzzi,et al.  Prions: health scare and biological challenge , 2001, Nature Reviews Molecular Cell Biology.

[44]  A. Mangé,et al.  Cleavage of the Amino Terminus of the Prion Protein by Reactive Oxygen Species* , 2001, The Journal of Biological Chemistry.

[45]  J G Flanagan,et al.  Regulated cleavage of a contact-mediated axon repellent. , 2000, Science.

[46]  M. Schachner,et al.  Formation of myelin after transplantation of neural precursor cells into the retina of young postnatal mice , 2000, Glia.

[47]  B. de Strooper,et al.  Presenilin 1 Controls γ-Secretase Processing of Amyloid Precursor Protein in Pre-Golgi Compartments of Hippocampal Neurons , 1999, The Journal of cell biology.

[48]  O. Kretz,et al.  Disruption of the glucocorticoid receptor gene in the nervous system results in reduced anxiety , 1999, Nature Genetics.

[49]  E. Kojro,et al.  Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[50]  B. Ghetti,et al.  Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. , 1998, The American journal of pathology.

[51]  Christian von Mering,et al.  Expression of Amino-Terminally Truncated PrP in the Mouse Leading to Ataxia and Specific Cerebellar Lesions , 1998, Cell.

[52]  M. Metzstein,et al.  SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling. , 1997, Development.

[53]  G. Rubin,et al.  Kuzbanian Controls Proteolytic Processing of Notch and Mediates Lateral Inhibition during Drosophila and Vertebrate Neurogenesis , 1997, Cell.

[54]  A. Aguzzi,et al.  Prion protein (PrP) with amino‐proximal deletions restoring susceptibility of PrP knockout mice to scrapie. , 1996, The EMBO journal.

[55]  D. Teplow,et al.  Truncated Forms of the Human Prion Protein in Normal Brain and in Prion Diseases (*) , 1995, The Journal of Biological Chemistry.

[56]  S. Prusiner,et al.  Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein , 1992, Nature.

[57]  S. Prusiner.  Novel proteinaceous infectious particles cause scrapie. , 1982, Science.