Zobrazeno 1 - 10
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pro vyhledávání: '"M L, Bernardini"'
Autor:
M, Gutierrez, R, De Angelis, M L, Bernardini, E, Filippucci, G, Goteri, G, Brandozzi, G, Lemme, A, Campanati, W, Grassi, A, Offidani
Publikováno v:
The British journal of dermatology. 164(1)
To date, the diagnosis of psoriasis is based on both clinical history and physical examination, and its severity is assessed by the Psoriasis Area and Severity Index (PASI). Continuous technological advances in the field of sonography have led to the
Autor:
C. Cigana, L. Curcuru’, M. R. Leone, T. Ieranò, N. I. Lorè, I. Bianconi, F. Cozzolino, M. L. Bernardini, A. Bragonzi, SILIPO, ALBA, LANZETTA, ROSA, MOLINARO, ANTONIO
Pseudomonas aeruginosa can establish life-long airways chronic infection in patients with cystic fibrosis (CF) with pathogenic variants distinguished from initially acquired strain. Here, we analysed chemical and biological activity of P. aeruginosa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3730::61a0987daa4eee6f1fb015b4db8ad391
http://hdl.handle.net/11588/426056
http://hdl.handle.net/11588/426056
Publikováno v:
Current topics in microbiology and immunology. 180
Akademický článek
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Akademický článek
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Akademický článek
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Autor:
Luisa Sturiale, Luciana Albuquerque, Flaviana Di Lorenzo, Ida Paciello, Maria Lina Bernardini, Antonio Molinaro, Luigi Lembo Fazio, Milton S. da Costa, Rosa Lanzetta, Domenico Garozzo, Michelangelo Parrilli, Dott. Alba Silipo
Publikováno v:
ChemBioChem (Internet) 15 (2014): 2146–2155. doi:10.1002/cbic.201402233
info:cnr-pdr/source/autori:Di Lorenzo F.; Paciello I.; Fazio L.L.; Albuquerque L.; Sturiale L.; da Costa M.S.; Lanzetta R.; Parrilli M.; Garozzo D.; Bernardini M.L.; Silipo D.A.; Molinaro A./titolo:Thermophiles as potential source of novel endotoxin antagonists: The full structure and bioactivity of thelipo-oligosaccharide from thermomonas hydrothermalis/doi:10.1002%2Fcbic.201402233/rivista:ChemBioChem (Internet)/anno:2014/pagina_da:2146/pagina_a:2155/intervallo_pagine:2146–2155/volume:15
info:cnr-pdr/source/autori:Di Lorenzo F.; Paciello I.; Fazio L.L.; Albuquerque L.; Sturiale L.; da Costa M.S.; Lanzetta R.; Parrilli M.; Garozzo D.; Bernardini M.L.; Silipo D.A.; Molinaro A./titolo:Thermophiles as potential source of novel endotoxin antagonists: The full structure and bioactivity of thelipo-oligosaccharide from thermomonas hydrothermalis/doi:10.1002%2Fcbic.201402233/rivista:ChemBioChem (Internet)/anno:2014/pagina_da:2146/pagina_a:2155/intervallo_pagine:2146–2155/volume:15
Thermomonas hydrothermalis is a Gram-negative thermophilic bacterium that is able to live at 50°C. This ability is attributed to chemical modifications, involving those to bacterial cell-wall components, such as proteins and (glyco)lipids. As the ma
Autor:
Luisa Sturiale, Gaëlle Noël, Antonio Molinaro, Valeria Ciancarella, Maria Lina Bernardini, Anna Brotcke Zumsteg, Laura Curcurù, Ida Paciello, Alba Silipo, Luigi Lembo-Fazio
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (46), pp.E4345-54. ⟨10.1073/pnas.1303641110⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (46), pp.E4345-54. ⟨10.1073/pnas.1303641110⟩
Proceedings of the National Academy of Sciences of the United States of America 110 (2013): E4345–E4354. doi:10.1073/pnas.1303641110
info:cnr-pdr/source/autori:Paciello, I; Silipo, A; Lembo-Fazio, L; Curcuru, L; Zumsteg, A; Noel, G; Ciancarella, V; Sturiale, L; Molinaro, A; Bernardini, ML./titolo:Intracellular Shigella remodels its LPS to dampen the innate immune recognition and evade inflammasome activation/doi:10.1073%2Fpnas.1303641110/rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2013/pagina_da:E4345/pagina_a:E4354/intervallo_pagine:E4345–E4354/volume:110
Proceedings of the National Academy of Sciences; Vol 110
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (46), pp.E4345-54. ⟨10.1073/pnas.1303641110⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (46), pp.E4345-54. ⟨10.1073/pnas.1303641110⟩
Proceedings of the National Academy of Sciences of the United States of America 110 (2013): E4345–E4354. doi:10.1073/pnas.1303641110
info:cnr-pdr/source/autori:Paciello, I; Silipo, A; Lembo-Fazio, L; Curcuru, L; Zumsteg, A; Noel, G; Ciancarella, V; Sturiale, L; Molinaro, A; Bernardini, ML./titolo:Intracellular Shigella remodels its LPS to dampen the innate immune recognition and evade inflammasome activation/doi:10.1073%2Fpnas.1303641110/rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2013/pagina_da:E4345/pagina_a:E4354/intervallo_pagine:E4345–E4354/volume:110
Proceedings of the National Academy of Sciences; Vol 110
International audience; LPS is a potent bacterial effector triggering the activation of the innate immune system following binding with the complex CD14, myeloid differentiation protein 2, and Toll-like receptor 4. The LPS of the enteropathogen Shige
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f4459ea70e0e3b8ca3eacdf8a7498e6
https://hal-riip.archives-ouvertes.fr/pasteur-01044866/document
https://hal-riip.archives-ouvertes.fr/pasteur-01044866/document
Autor:
Ida Paciello, Rosa Lanzetta, William D. Grant, Maria Lina Bernardini, Angelo Palmigiano, Antonio Molinaro, Luigi Lembo Fazio, Michelangelo Parrilli, Domenico Garozzo, Alba Silipo, Luisa Sturiale, Flaviana Di Lorenzo
Publikováno v:
European journal of organic chemistry
2013 (2013): 2653–2665. doi:10.1002/ejoc.201201702
info:cnr-pdr/source/autori:Alba Silipo, Flaviana Di Lorenzo, Luigi Lembo Fazio, Ida Paciello, Luisa Sturiale, Angelo Palmigiano, Michelangelo Parrilli, William D Grant, Domenico Garozzo, Rosa Lanzetta, Maria Lina Bernardini, Antonio Molinaro/titolo:Structure and Immunological Activity of the Lipopolysaccharide Isolated from the Species Alkalimonas delamerensis/doi:10.1002%2Fejoc.201201702/rivista:European journal of organic chemistry (Print)/anno:2013/pagina_da:2653/pagina_a:2665/intervallo_pagine:2653–2665/volume:2013
2013 (2013): 2653–2665. doi:10.1002/ejoc.201201702
info:cnr-pdr/source/autori:Alba Silipo, Flaviana Di Lorenzo, Luigi Lembo Fazio, Ida Paciello, Luisa Sturiale, Angelo Palmigiano, Michelangelo Parrilli, William D Grant, Domenico Garozzo, Rosa Lanzetta, Maria Lina Bernardini, Antonio Molinaro/titolo:Structure and Immunological Activity of the Lipopolysaccharide Isolated from the Species Alkalimonas delamerensis/doi:10.1002%2Fejoc.201201702/rivista:European journal of organic chemistry (Print)/anno:2013/pagina_da:2653/pagina_a:2665/intervallo_pagine:2653–2665/volume:2013
We have defined the complete structure and assessed the biological activity of the lipopolysaccharide (LPS) from Alkalimonas delamerensis, an alkaliphilic bacterium isolated from soda lakes in China and East Africa. The structural determination, whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2022c0f4a55d6c6ef9f807d01036081f
http://www.cnr.it/prodotto/i/241705
http://www.cnr.it/prodotto/i/241705
Autor:
Ivan Tattoli, Giacomo Rossi, Antonio Molinaro, Valeria Liparoti, Luigi Lembo Fazio, Maria Lina Bernardini, Cristina De Castro, Giulia Nigro, Dana J. Philpott, Maria Celeste Martino
Bacterial infections trigger the activation of innate immunity through the interaction of pathogen-associated molecular patterns (PAMPs) with pattern recognition molecules (PRMs). The nucleotide-binding oligomerization domain (Nod) proteins are intra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f0e2c7e4a4a96b5e7a52e36e9495e95
http://hdl.handle.net/11581/105496
http://hdl.handle.net/11581/105496