Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Human Rézaei"'
Autor:
Angélique Igel-Egalon, Jan Bohl, Mohammed Moudjou, Laetitia Herzog, Fabienne Reine, Human Rezaei, Vincent Béringue
Publikováno v:
Viruses, Vol 11, Iss 5, p 429 (2019)
Prions are proteinaceous infectious agents responsible for a range of neurodegenerative diseases in animals and humans. Prion particles are assemblies formed from a misfolded, β-sheet rich, aggregation-prone isoform (PrPSc) of the host-encoded cellu
Externí odkaz:
https://doaj.org/article/ac9bd0eaeed948a182684418ef1fbb47
Publikováno v:
Viruses, Vol 11, Iss 3, p 202 (2019)
The abnormal protein aggregates in progressive neurodegenerative disorders, such as Alzheimer’s, Parkinson’s and prion diseases, adopt a generic structural form called amyloid fibrils. The precise amyloid fold can differ between patients and thes
Externí odkaz:
https://doaj.org/article/03e551de4805462cbe1f9674c04748f1
Autor:
Rajesh P Menon, Suran Nethisinghe, Serena Faggiano, Tommaso Vannocci, Human Rezaei, Sally Pemble, Mary G Sweeney, Nicholas W Wood, Mary B Davis, Annalisa Pastore, Paola Giunti
Publikováno v:
PLoS Genetics, Vol 9, Iss 7, p e1003648 (2013)
At least nine dominant neurodegenerative diseases are caused by expansion of CAG repeats in coding regions of specific genes that result in abnormal elongation of polyglutamine (polyQ) tracts in the corresponding gene products. When above a threshold
Externí odkaz:
https://doaj.org/article/160e066247634585a377f084b98468ee
Autor:
Stéphanie Prigent, Annabelle Ballesta, Frédérique Charles, Natacha Lenuzza, Pierre Gabriel, Léon Matar Tine, Human Rezaei, Marie Doumic
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e43273 (2012)
Protein polymerization consists in the aggregation of single monomers into polymers that may fragment. Fibrils assembly is a key process in amyloid diseases. Up to now, protein aggregation was commonly mathematically simulated by a polymer size-struc
Externí odkaz:
https://doaj.org/article/f5c069e2c26242c9a0d45eaf9bbec75a
Autor:
Steve Simoneau, Human Rezaei, Nicole Salès, Gunnar Kaiser-Schulz, Maxime Lefebvre-Roque, Catherine Vidal, Jean-Guy Fournier, Julien Comte, Franziska Wopfner, Jeanne Grosclaude, Hermann Schätzl, Corinne Ida Lasmézas
Publikováno v:
PLoS Pathogens, Vol 3, Iss 8, p e125 (2007)
The mechanisms underlying prion-linked neurodegeneration remain to be elucidated, despite several recent advances in this field. Herein, we show that soluble, low molecular weight oligomers of the full-length prion protein (PrP), which possess charac
Externí odkaz:
https://doaj.org/article/b78586e103e84f01b240feec7e8ce3fb
Autor:
Annick Le Dur, Thanh Lan Laï, Marie-George Stinnakre, Aude Laisné, Nathalie Chenais, Sabine Rakotobe, Bruno Passet, Fabienne Reine, Solange Soulier, Laetitia Herzog, Gaëlle Tilly, Human Rézaei, Vincent Béringue, Jean-Luc Vilotte, Hubert Laude
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
PrPC protein plays a key role in prion transmission across species. Here, the authors compare transmission of a representative scrapie isolate to transgenic mice expressing variable levels of the same Prnp allele as the donor sheep, and find divergen
Externí odkaz:
https://doaj.org/article/010dfaabcfa2495381f0b8a4b4e912ee
Autor:
Annick, Le Dur, Thanh Lan, Laï, Marie-George, Stinnakre, Aude, Laisné, Nathalie, Chenais, Sabine, Rakotobe, Bruno, Passet, Fabienne, Reine, Solange, Soulier, Laetitia, Herzog, Gaëlle, Tilly, Human, Rézaei, Vincent, Béringue, Jean-Luc, Vilotte, Hubert, Laude
Publikováno v:
Nature Communications
Prions induce a fatal neurodegenerative disease in infected host brain based on the refolding and aggregation of the host-encoded prion protein PrPC into PrPSc. Structurally distinct PrPSc conformers can give rise to multiple prion strains. Constrain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::97bf79790ee7b3956058bb0e466b42af
https://pubmed.ncbi.nlm.nih.gov/28112164
https://pubmed.ncbi.nlm.nih.gov/28112164
Autor:
Jessica D. Panes, Paulina Saavedra, Benjamin Pineda, Kathleen Escobar, Magdalena E. Cuevas, Gustavo Moraga-Cid, Jorge Fuentealba, Coralia I. Rivas, Human Rezaei, Carola Muñoz-Montesino
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 14 (2021)
After the discovery of prion phenomenon, the physiological role of the cellular prion protein (PrPC) remained elusive. In the past decades, molecular and cellular analysis has shed some light regarding interactions and functions of PrPC in health and
Externí odkaz:
https://doaj.org/article/87823bf2331544b9a228724798e160fa
Autor:
Mohammed Moudjou, Johan Castille, Bruno Passet, Laetitia Herzog, Fabienne Reine, Jean-Luc Vilotte, Human Rezaei, Vincent Béringue, Angélique Igel-Egalon
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
Prions are pathogenic infectious agents responsible for fatal, incurable neurodegenerative diseases in animals and humans. Prions are composed exclusively of an aggregated and misfolded form (PrPSc) of the cellular prion protein (PrPC). During the pr
Externí odkaz:
https://doaj.org/article/261c56b9f62847aeb90c8156b6830d77
Autor:
Vincent Béringue, Philippe Tixador, Olivier Andréoletti, Fabienne Reine, Johan Castille, Thanh-Lan Laï, Annick Le Dur, Aude Laisné, Laetitia Herzog, Bruno Passet, Human Rezaei, Jean-Luc Vilotte, Hubert Laude
Publikováno v:
PLoS Pathogens, Vol 16, Iss 7, p e1008283 (2020)
Prions are pathogens formed from abnormal conformers (PrPSc) of the host-encoded cellular prion protein (PrPC). PrPSc conformation to disease phenotype relationships extensively vary among prion strains. In particular, prions exhibit a strain-depende
Externí odkaz:
https://doaj.org/article/5a6d7bcf05644281979b0d12312a5022