Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Chafik Harrathi"'
Autor:
Natalia Fernández-Borges, Hasier Eraña, Saioa R. Elezgarai, Chafik Harrathi, Mayela Gayosso, Joaquín Castilla
Publikováno v:
International Journal of Cell Biology, Vol 2013 (2013)
Prions are considered the best example to prove that the biological information can be transferred protein to protein through a conformational change. The term “prion-like” is used to describe molecular mechanisms that share similarities with the
Externí odkaz:
https://doaj.org/article/06de1e13d78f480d8ae29e3221cfefd6
Autor:
Chafik Harrathi, Saioa R. Elezgarai, Jorge M. Charco, Joaquín Castilla, Hasier Eraña, Vanessa Venegas, Natalia Fernández-Borges
Publikováno v:
Molecular Neurobiology
The large chronic wasting disease (CWD)-affected cervid population in the USA and Canada, and the risk of the disease being transmitted to humans through intermediate species, is a highly worrying issue that is still poorly understood. In this case,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40a2076d50961a89453ad1dcbf2a178c
https://pubmed.ncbi.nlm.nih.gov/30592012
https://pubmed.ncbi.nlm.nih.gov/30592012
Autor:
Saioa R. Elezgarai, Chafik Harrathi, Natalia Fernández-Borges, Joaquín Castilla, Jorge M. Charco, Oscar Millet, Francesca Chianini, Mark P. Dagleish, Gabriel Ortega, Hasier Eraña
Publikováno v:
Journal of Virology. 91
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of rare progressive neurodegenerative disorders caused by an abnormally folded prion protein (PrP Sc ). This is capable of transforming the normal cellular prion protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11784192b76549cd0aeb7a50cd7adcb2
https://doi.org/10.1128/jvi.01543-17
https://doi.org/10.1128/jvi.01543-17
Autor:
Natalia, Fernández-Borges, Hasier, Eraña, Saioa R, Elezgarai, Chafik, Harrathi, Vanesa, Venegas, Joaquín, Castilla
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1658
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative diseases where the misfolding of the prion protein (PrP) is a crucial event. Based on studies in TSE-affected humans and the generation of transgenic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d58318915c46a263265e11a847db4c6a
https://pubmed.ncbi.nlm.nih.gov/28861792
https://pubmed.ncbi.nlm.nih.gov/28861792
Autor:
Joaquín Castilla, Alejandro M. Sevillano, Jorge M. Charco, Hasier Eraña, Jesús R. Requena, Qingzhong Kong, Paula Saá, Chafik Harrathi, David Gil, Saioa R. Elezgarai, Olivier Andreoletti, Natalia Fernández-Borges
Publikováno v:
Scientific Reports
Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname
Scientific Reports, Vol 7, Iss 1, Pp 1-18 (2017)
Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname
Scientific Reports, Vol 7, Iss 1, Pp 1-18 (2017)
Human transmissible spongiform encephalopathies (TSEs) or prion diseases are a group of fatal neurodegenerative disorders that include Kuru, Creutzfeldt-Jakob disease, Gerstmann-SträusslerScheinker syndrome (GSS), and fatal familial insomnia. GSS is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7363a586c29016122ea041db1982993
https://doi.org/10.1038/s41598-017-09489-3
https://doi.org/10.1038/s41598-017-09489-3
Autor:
Beatriz Parra, Jorge M. Charco, Manuel Sánchez-Martín, Umberto Agrimi, Natalia Fernández-Borges, Claudia D'Agostino, Michele Angelo Di Bari, Tomás Mayoral, Gabriele Vaccari, Laura Pirisinu, Joaquín Castilla, Vanessa Venegas, Hasier Eraña, Chafik Harrathi, Jesús R. Requena, David Gil, Romolo Nonno, Saioa R. Elezgarai, Rafael López-Moreno, Ilaria Vanni
Publikováno v:
Acta neuropathologica. 135(2)
Prion diseases are caused by a misfolding of the cellular prion protein (PrP) to a pathogenic isoform named PrPSc. Prions exist as strains, which are characterized by specific pathological and biochemical properties likely encoded in the three-dimens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::983ffd5014b0afc3a9eaaf753c218fa9
https://pubmed.ncbi.nlm.nih.gov/29094186
https://pubmed.ncbi.nlm.nih.gov/29094186
Autor:
Joaquín Castilla, Natalia Fernández-Borges, Hasier Eraña, Saioa R. Elezgarai, Vanesa Venegas, Chafik Harrathi
Publikováno v:
Prions ISBN: 9781493972425
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative diseases where the misfolding of the prion protein (PrP) is a crucial event. Based on studies in TSE-affected humans and the generation of transgenic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b60acff2ffca0d6abecbc0c5309c913
https://doi.org/10.1007/978-1-4939-7244-9_15
https://doi.org/10.1007/978-1-4939-7244-9_15
Autor:
Natalia Fernández-Borges, Joaquín Castilla, Vanesa Venegas, Hasier Eraña, Chafik Harrathi, Saioa R. Elezgarai
Publikováno v:
Virus research. 207
Prion diseases or Transmissible Spongiform Encephalopathies (TSEs) are a group of fatal neurodegenerative disorders affecting several mammalian species being Creutzfeldt-Jacob Disease (CJD) the most representative in human beings, scrapie in ovine, B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0855dd3be8014eb8b053a8cb1d1b80a7
https://pubmed.ncbi.nlm.nih.gov/25907990
https://pubmed.ncbi.nlm.nih.gov/25907990
Autor:
Mayela Gayosso, Joaquín Castilla, Natalia Fernández-Borges, Hasier Eraña, Chafik Harrathi, Saioa R. Elezgarai
Publikováno v:
International Journal of Cell Biology
International Journal of Cell Biology, Vol 2013 (2013)
International Journal of Cell Biology, Vol 2013 (2013)
Prions are considered the best example to prove that the biological information can be transferred protein to protein through a conformational change. The term “prion-like” is used to describe molecular mechanisms that share similarities with the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fd6120b1fb6972ead74fd5d0ddc6977
https://pubmed.ncbi.nlm.nih.gov/24187553
https://pubmed.ncbi.nlm.nih.gov/24187553