Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Christophe Epinette"'
Autor:
Laurence Arnault, Anne-Sophie Domelier, Christophe Epinette, Roland Quentin, Nicole Girard, Nathalie van der Mee-Marquet, Jeremy Loyau, Barbara Losfelt
Publikováno v:
Journal of Clinical Microbiology. 45:851-857
We studied 358 Staphylococcus aureus strains isolated from bloodstream infections (BSI) observed during an epidemiological study covering 2,007,681 days of hospitalization in 32 healthcare institutions (HCIs) between 2004 and 2006. The strains were t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48038a6184e5e58839f567cc9891edef
https://doi.org/10.1128/jcm.02178-06
https://doi.org/10.1128/jcm.02178-06
Histidinylated polylysines: An alternative antibacterial and fluidifying agent in cystic fibrosis.**
Autor:
Eric Morello, Jérôme Montharu, Delphine Fouquenet, Thomas Baranek, Lise Vanderlynden, Christophe Epinette, Clémence Henry, Virginie Hervé, Mustapha Si-Tahar, Francis Gauthier
Publikováno v:
7.3 Cystic Fibrosis.
Introduction: We recently showed that polycationic polymers such as poly-L-Lysines (pLK) were able to compact DNA, liquefy sputum of cystic fibrosis (CF) patients, inhibit bacterial growth (Pseudomonas aeruginosa and Staphylococcus aureus) , and favo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2d37099f090c7b269a3a23287ec780b
https://doi.org/10.1183/13993003.congress-2015.pa2060
https://doi.org/10.1183/13993003.congress-2015.pa2060
Autor:
Dieter E. Jenne, Guillaume Gabant, Christophe Epinette, Magdalena Wysocka, Antonia Vlahou, Sandrine Dallet-Choisy, Carla Guarino, Monika Legowska, Christine Kellenberger, Martine Cadene, Jerome Zoidakis, Brice Korkmaz, Francis Gauthier, Marcin Sieńczyk, Adam Lesner, Sylvain Marchand-Adam
Publikováno v:
J. Biol. Chem. 289, 31777-31791 (2014)
Journal of Biological Chemistry
Journal of Biological Chemistry, 2014, 289 (46), pp.doi: 10.1074/jbc.M114.591339. ⟨10.1074/jbc.M114.591339⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (46), pp.doi: 10.1074/jbc.M114.591339. ⟨10.1074/jbc.M114.591339⟩
Journal of Biological Chemistry
Journal of Biological Chemistry, 2014, 289 (46), pp.doi: 10.1074/jbc.M114.591339. ⟨10.1074/jbc.M114.591339⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (46), pp.doi: 10.1074/jbc.M114.591339. ⟨10.1074/jbc.M114.591339⟩
International audience; The function of neutrophil protease 3 (PR3) is poorly understood despite of its role in autoimmune vasculitides and its possible involvement in cell apoptosis. This makes it different from its structural homologue neutrophil e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d6c4bd49fbc5d49ddaf56f8319471c1
https://europepmc.org/articles/PMC4231656/
https://europepmc.org/articles/PMC4231656/
Autor:
Guillaume Gabant, Alain Roussel, Christine Kellenberger, Christophe Epinette, Brice Korkmaz, Chrystelle Derache, Martine Cadene, Francis Gauthier
Publikováno v:
FEBS Journal
FEBS Journal, Wiley, 2012, 279 (24), pp.4466-78. ⟨10.1111/febs.12033⟩
FEBS Journal, Wiley, 2012, 279 (24), pp.4466-78. ⟨10.1111/febs.12033⟩
International audience; Greglin is an 83-residue serine protease inhibitor purified from the ovaries of the locust Schistocerca gregaria. Greglin is a strong inhibitor of subtilisin and human neutrophil elastase, acting at sub-nanomolar and nanomolar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63cc03f60378b896e6902156f2750c35
https://hal.archives-ouvertes.fr/hal-00817089
https://hal.archives-ouvertes.fr/hal-00817089
Autor:
Brice, Korkmaz, Sylvie, Attucci, Christophe, Epinette, Elodie, Pitois, Marie-Lise, Jourdan, Luiz, Juliano, Francis, Gauthier
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 844
Neutrophil elastase, proteinase 3, and cathepsin G are three hematopoietic serine proteases, large quantities of which are stored in neutrophil cytoplasmic azurophilic granules. They act in combination with reactive oxygen species to degrade engulfed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::21bd43d7892f886238bb193ea7dbab1f
https://pubmed.ncbi.nlm.nih.gov/22262439
https://pubmed.ncbi.nlm.nih.gov/22262439
Autor:
Marie-Lise Jourdan, Sylvie Attucci, Francis Gauthier, Christophe Epinette, Brice Korkmaz, Elodie Pitois, Luiz Juliano
Publikováno v:
Methods in Molecular Biology ISBN: 9781617795268
Neutrophil elastase, proteinase 3, and cathepsin G are three hematopoietic serine proteases, large quantities of which are stored in neutrophil cytoplasmic azurophilic granules. They act in combination with reactive oxygen species to degrade engulfed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::03ec3fe29bce7af20f724877b7e75491
https://doi.org/10.1007/978-1-61779-527-5_9
https://doi.org/10.1007/978-1-61779-527-5_9
Autor:
Martine Cadene, Christine Kellenberger, Brice Korkmaz, Christophe Epinette, Cécile Croix, Marie-Claude Viaud-Massuard, Lucie Jaquillard, Francis Gauthier, Gilles Lalmanach, Sylvain Marchand-Adam
Publikováno v:
Biochemical Pharmacology
Biochemical Pharmacology, Elsevier, 2012, 83 (6), pp.788-96. ⟨10.1016/j.bcp.2011.12.023⟩
Biochemical Pharmacology, Elsevier, 2012, 83 (6), pp.788-96. ⟨10.1016/j.bcp.2011.12.023⟩
International audience; The biological functions of human neutrophil proteinase 3 (PR3) remain unclear because of its close structural resemblance to neutrophil elastase and its apparent functional redundancy with the latter. Thus, all natural inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e737e2d71756a9b26714316ea4cc53dd
https://pubmed.ncbi.nlm.nih.gov/22209715
https://pubmed.ncbi.nlm.nih.gov/22209715