Zobrazeno 1 - 10 of 22 pro vyhledávání: '"MESH: PrPC Proteins"'
1
Functional mechanisms of the cellular prion protein (PrPC) associated anti-HIV-1 properties
Autor: Pascal Leblanc, Ricardo Soto-Rifo, Henri Gruffat, Evelyne Manet, Graça Raposo, Vincent Balter, Jean-Luc Darlix, Andrea Cimarelli, Théophile Ohlmann, Sandrine Alais, Laurent Schaeffer
Publikováno v: Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences, Springer Verlag, 2012, 69 (8), pp.1331-1352. ⟨10.1007/s00018-011-0879-z⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2012, 69 (8), pp.1331-52. ⟨10.1007/s00018-011-0879-z⟩
Cellular and Molecular Life Sciences, 2012, 69 (8), pp.1331-1352. ⟨10.1007/s00018-011-0879-z⟩
International audience; The cellular prion protein PrP(C)/CD230 is a GPI-anchor protein highly expressed in cells from the nervous and immune systems and well conserved among vertebrates. In the last decade, several studies suggested that PrP(C) disp
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::913f2cada6ecbafd96fa6d04a3c3606b
https://doi.org/10.1007/s00018-011-0879-z
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2
Doppel and PrPC co-immunoprecipitate in detergent-resistant membrane domains of epithelial FRT cells
Autor: Chiara Zurzolo, Maddalena Costanzo, Alessandro Negro, Vincenza Campana, Daniela Sarnataro, M. Catia Sorgato, Anna Caputo
Publikováno v: Biochemical Journal
Biochemical Journal, 2010, 425 (2), pp.341-51. ⟨10.1042/BJ20091050⟩
Biochemical Journal, Portland Press, 2010, 425 (2), pp.341-51. ⟨10.1042/BJ20091050⟩
International audience; Dpl (doppel) is a paralogue of the PrPC (cellular prion protein), whose misfolded conformer (the scrapie prion protein, PrPSc) is responsible for the onset of TSEs (transmissible spongiform encephalopathies) or prion diseases.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b535cf11e1441f046e7235fd030d365
https://doi.org/10.1042/bj20091050
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3
Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles
Autor: Jean-Luc Darlix, Sylvain Lehmann, Dominique Baas, Graça Raposo, Pascal Leblanc, Sandrine Alais, Sabrina Simoes
Publikováno v: Biology of the Cell
Biology of the Cell, Wiley, 2008, 100 (10), pp.603-618. ⟨10.1042/BC20080025⟩
Biology of the Cell, 2008, 100 (10), pp.603-618. ⟨10.1042/BC20080025⟩
Background information. TSEs (transmissible spongiform encephalopathies) are neurodegenerative disorders affecting humans and animals. PrPSc, a conformationally altered isoform of the normal prion protein (PrPC), is thought to be the pathogenic agent
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::869385afe6d133b8c5b6430c5237cb92
https://doi.org/10.1042/bc20080025
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4
Proteomic consequences of expression and pathological conversion of the prion protein in inducible neuroblastoma N2a cells
Autor: Stéphane Roche, Manuela Pastore, Monique Provansal, Sandrine Alais, Maxime Belondrade, Danielle Casanova, Pascal Leblanc, Sylvain Lehmann, Otto Windl
Publikováno v: Prion
Prion, Taylor & Francis, 2014, 4 (4), pp.292-301. ⟨10.4161/pri.4.4.13435⟩
Prion, 2010, 4 (4), pp.4, 4. ⟨10.4161/pri.4.4.13435⟩
Prion, Taylor & Francis, 2010, 4 (4), pp.4, 4. ⟨10.4161/pri.4.4.13435⟩
International audience; Neurodegenerative diseases are often associated with misfolding and deposition of specific proteins in the nervous system. The prion protein, which is associated with transmissible spongiform encephalopathies (TSEs), is one of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::362a1537263c00525c429f13f62a793c
https://hal.archives-ouvertes.fr/hal-02132261
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5
α-Secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid β (Aβ)-associated cell death
Autor: Claire Sunyach, Charlotte Bauer, Sergio T. Ferreira, Aurelie Thevenet, Marie-Victoire Guillot-Sestier, Maria Paz Marzolo, Frédéric Checler
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (7), pp.5021-32. ⟨10.1074/jbc.M111.323626⟩
JOURNAL OF BIOLOGICAL CHEMISTRY
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
International audience; In physiological conditions, both β-amyloid precursor protein (βAPP) and cellular prion (PrP(c)) undergo similar disintegrin-mediated α-secretase cleavage yielding N-terminal secreted products referred to as soluble amyloid
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c9bfc3e54618ef29558dcc4270b42ae
https://europepmc.org/articles/PMC3774388/
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6
Human prion protein binds Argonaute and promotes accumulation of microRNA effector complexes
Autor: Thierry Lagrange, Fabrice Michel, Pascal Leblanc, Florence Jay, Sandrine Alais, Olivier Voinnet, Yannick Schwab, Derrick Gibbings, Dominique Pontier
Publikováno v: Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, Nature Publishing Group, 2012, 19 (5), pp.517-524. ⟨10.1038/nsmb.2273⟩
Nature Structural and Molecular Biology, 2012, 19 (5), pp.517-524. ⟨10.1038/nsmb.2273⟩
Nature Structural and Molecular Biology, Nature Publishing Group, 2012, 19 (5), pp.517-524
International audience; Despite intense research in the context of neurodegenerative diseases associated with its misfolding, the endogenous human prion protein PrP(C) (or PRNP) has poorly understood physiological functions. Whereas most PrP(C) is ex
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d498dea74224c96195bcf1fbaa335c0
https://hal.archives-ouvertes.fr/hal-02328983
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7
The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
Autor: Sabine Scarzello, Charlotte Druon, Claire Sunyach, Frédéric Checler, Marie-Victoire Guillot-Sestier
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (51), pp.35973-86. ⟨10.1074/jbc.M109.051086⟩
International audience; Cellular prion protein (PrP(c)) undergoes a disintegrin-mediated physiological cleavage, generating a soluble amino-terminal fragment (N1), the function of which remained unknown. Recombinant N1 inhibits staurosporine-induced
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d094d9b28dec1225a1c8cbc32d97b7ed
https://hal.archives-ouvertes.fr/hal-00497181
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8
The cellular prion protein interacts with the tissue non-specific alkaline phosphatase in membrane microdomains of bioaminergic neuronal cells
Autor: Myriam Ermonval, Sophie Mouillet-Richard, Jean-Marie Launay, Kimimitsu Oda, Anne Baudry, Florence Baychelier, Elodie Pradines, Odile Kellermann, Benoit Schneider, Mathéa Pietri
Publikováno v: PLoS ONE
PLoS ONE, Public Library of Science, 2009, 4 (8), pp.e6497. ⟨10.1371/journal.pone.0006497⟩
PLoS ONE, 2009, 4 (8), pp.e6497. ⟨10.1371/journal.pone.0006497⟩
PLoS ONE, Vol 4, Iss 8, p e6497 (2009)
International audience; Background: The cellular prion protein, PrP(C), is GPI anchored and abundant in lipid rafts. The absolute requirement of PrP(C) in neurodegeneration associated to prion diseases is well established. However, the function of th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d749fed75a8baa909494a53d46394cb
https://hal-pasteur.archives-ouvertes.fr/pasteur-03204748/file/76804_2_merged_1246616522.pdf
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9
Regulation of betaAPP and PrPc cleavage by alpha-secretase: mechanistic and therapeutic perspectives
Autor: Bruno, Vincent, Moustapha Alfa, Cisse, Claire, Sunyach, Marie-Victoire, Guillot-Sestier, Frédéric, Checler
Publikováno v: Current Alzheimer Research
Current Alzheimer Research, Bentham Science Publishers, 2008, 5 (2), pp.202-11
Alzheimer's disease (AD) is by far the most common form of dementia in the elderly and concerns one out of three individuals over 85. Like other neurodegenerative disorders such as Parkinson, Hungtington or prion diseases, AD is characterized by the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::d064f66fc148b4792976d03baec12563
https://hal.archives-ouvertes.fr/hal-00315595
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10
Truncated PrP(c) in mammalian brain: interspecies variation and location in membrane rafts
Autor: Raymonde Hässig, Stéphane Haïk, Baptiste A Faucheux, Isabelle Laffont-Proust, Jacques Grassi, Caroline Fonta, Kenneth L. Moya, Stéphanie Simon
Publikováno v: Biol Chem
Biol Chem, 2006, 387 (3), pp.297-300. ⟨10.1515/BC.2006.039⟩
A key molecular event in prion diseases is the conversion of cellular prion protein (PrP(c)) into an abnormal misfolded conformer (PrP(sc)). The PrP(c) N-terminal domain plays a central role in PrP(c) functions and in prion propagation. Because mamma
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90d769b67960ddc5844ef0f5f0c1a8fd
https://hal.archives-ouvertes.fr/hal-00111080
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