Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Nela Klimova"'
Autor:
Nela Klimova, Jana Holubova, Gaia Streparola, Jakub Tomala, Ludmila Brazdilova, Ondrej Stanek, Ladislav Bumba, Peter Sebo
Publikováno v:
PLoS Pathogens, Vol 18, Iss 6, p e1010577 (2022)
The adenylate cyclase (ACT) and the pertussis (PT) toxins of Bordetella pertussis exert potent immunomodulatory activities that synergize to suppress host defense in the course of whooping cough pathogenesis. We compared the mouse lung infection capa
Externí odkaz:
https://doaj.org/article/881f5b46d1f04874b1279ed1b9cd2ffd
Autor:
Anna Malandra, Waheed Ur Rahman, Nela Klimova, Gaia Streparola, Jana Holubova, Adriana Osickova, Simone Bariselli, Peter Sebo, Radim Osicka
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 16, p 9064 (2021)
The mucus layer protects airway epithelia from damage by noxious agents. Intriguingly, Bordetella pertussis bacteria provoke massive mucus production by nasopharyngeal epithelia during the initial coryza-like catarrhal stage of human pertussis and th
Externí odkaz:
https://doaj.org/article/c8c7de1cdf384ae88be2fb1d02340f98
Autor:
Waheed Ur Rahman, Adriana Osickova, Nela Klimova, Jinery Lora, Nataliya Balashova, Radim Osicka
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 23, p 9092 (2020)
The Gram-negative coccobacillus Kingella kingae is increasingly recognized as an important invasive pediatric pathogen that causes mostly bacteremia and skeletal system infections. K. kingae secretes an RtxA toxin that belongs to a broad family of th
Externí odkaz:
https://doaj.org/article/a73ed197928f448db51205bb018adf4a
Publikováno v:
Toxins, Vol 9, Iss 10, p 293 (2017)
Adenylate cyclase toxin (CyaA) is released in the course of B. pertussis infection in the host’s respiratory tract in order to suppress its early innate and subsequent adaptive immune defense. CD11b-expressing dendritic cells (DC), macrophages and
Externí odkaz:
https://doaj.org/article/cbcc855362af4bb1b8135aad040f7b74
Publikováno v:
Journal of Molecular Biology. 432:5696-5710
Repeats-in-Toxin (RTX) proteins of Gram-negative bacteria are excreted through the type I secretion system (T1SS) that recognizes non-cleavable C-terminal secretion signals. These are preceded by arrays of glycine and aspartate-rich nonapeptide repea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4cfa01f086b6ff4a75ccb7c139abe9a
https://doi.org/10.1016/j.jmb.2020.08.020
https://doi.org/10.1016/j.jmb.2020.08.020
Autor:
Nela Klimova, Humaira Khaliq, Peter Sebo, David Jurnecka, Adriana Osickova, Jiri Masin, Radim Osicka
Publikováno v:
J Biol Chem
The Bordetella adenylate cyclase toxin-hemolysin (CyaA) and the α-hemolysin (HlyA) of Escherichia coli belong to the family of cytolytic pore-forming Repeats in ToXin (RTX) cytotoxins. HlyA preferentially binds the α(L)β(2) integrin LFA-1 (CD11a/C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::530c7aa2f5b82f4b74cc9c16010fb520
https://doi.org/10.1074/jbc.ra120.013630
https://doi.org/10.1074/jbc.ra120.013630
Autor:
Nela Klimova, Adriana Osickova, Jinery Lora, Radim Osicka, Nataliya V. Balashova, Waheed Ur Rahman
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 21, Iss 9092, p 9092 (2020)
Volume 21
Issue 23
International Journal of Molecular Sciences, Vol 21, Iss 9092, p 9092 (2020)
Volume 21
Issue 23
The Gram-negative coccobacillus Kingella kingae is increasingly recognized as an important invasive pediatric pathogen that causes mostly bacteremia and skeletal system infections. K. kingae secretes an RtxA toxin that belongs to a broad family of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be3a568aa16b85c9ba4cfe6d1e04b635
http://europepmc.org/articles/PMC7730106
http://europepmc.org/articles/PMC7730106
Autor:
Nela Klimova, Waheed Ur Rahman, Gaia Streparola, Anna Malandra, Adriana Osickova, Simone Bariselli, Radim Osicka, Jana Holubova, Peter Sebo
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 16
International Journal of Molecular Sciences, Vol 22, Iss 9064, p 9064 (2021)
Volume 22
Issue 16
International Journal of Molecular Sciences, Vol 22, Iss 9064, p 9064 (2021)
The mucus layer protects airway epithelia from damage by noxious agents. Intriguingly, Bordetella pertussis bacteria provoke massive mucus production by nasopharyngeal epithelia during the initial coryza-like catarrhal stage of human pertussis and th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a406808fe2e778bc70266935e811a991
https://doi.org/10.3390/ijms22169064
https://doi.org/10.3390/ijms22169064
Autor:
Peter Sebo, Ilona Bibova, Cyril Barinka, Tomas Wald, Pavel Macek, Lucie Bednárová, Nela Klimova, Vaclav Veverka, Lucia Motlova, Jiri Masin, Michael Kachala, Ladislav Bumba, Dmitri I. Svergun
Publikováno v:
Molecular cell 62(1), 47-62 (2016). doi:10.1016/j.molcel.2016.03.018
Molecular cell 62(1), 47 - 62 (2016). doi:10.1016/j.molcel.2016.03.018
Calcium-binding RTX proteins are equipped with C-terminal secretion signals and translocate from the Ca$^{2+}$-depleted cytosol of Gram-negative bacteria directly into the Ca
Calcium-binding RTX proteins are equipped with C-terminal secretion signals and translocate from the Ca$^{2+}$-depleted cytosol of Gram-negative bacteria directly into the Ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d294233611a6d016c9948c6c8aa26ec
https://doi.org/10.1016/j.molcel.2016.03.018
https://doi.org/10.1016/j.molcel.2016.03.018
Publikováno v:
Toxins
Toxins, Vol 9, Iss 10, p 293 (2017)
Toxins, Vol 9, Iss 10, p 293 (2017)
Adenylate cyclase toxin (CyaA) is released in the course of B. pertussis infection in the host’s respiratory tract in order to suppress its early innate and subsequent adaptive immune defense. CD11b-expressing dendritic cells (DC), macrophages and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c02e8c039ab1619d6780cf4174ce9e40
https://doi.org/10.3390/toxins9100293
https://doi.org/10.3390/toxins9100293