Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Herve Celia"'
Publikováno v:
Frontiers in Microbiology, Vol 13 (2022)
The Ton complex is a molecular motor at the inner membrane of Gram-negative bacteria that uses a proton gradient to apply forces on outer membrane (OM) proteins to permit active transport of nutrients into the periplasmic space. Recently, the structu
Externí odkaz:
https://doaj.org/article/8e34a36c0cff458faa0414208f304579
Publikováno v:
Journal of Bacteriology.
The outer membranes (OM) of Gram-negative bacteria contain a class of proteins (TBDTs) that require energy for the import of nutrients and to serve as receptors for phages and protein toxins. Energy is derived from the proton motif force (pmf) of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9862411c8008d8c2e3d49dff2bcc3edd
https://doi.org/10.1128/jb.00035-23
https://doi.org/10.1128/jb.00035-23
Autor:
Herve Celia, Vadim Kotov, Oliver Vesper, Maria Garcia-Alai, Stephan Nussberger, Susan K. Buchanan, G. Mlynek, Jiri Wald, C. Loew, Celso M. Teixeira-Duarte, Marina Pletzer, João H. Morais-Cabral, Thomas C. Marlovits, Kristina Djinović-Carugo
Publikováno v:
Protein science 30(1), 201-217 (2021). doi:10.1002/pro.3986
Protein Science : A Publication of the Protein Society
Protein Science : A Publication of the Protein Society
Protein science 30(1), 201 - 217 (2021). doi:10.1002/pro.3986
Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consu
Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::286fe9b9f64775e4766faec078c5cb02
https://doi.org/10.1002/pro.3986
https://doi.org/10.1002/pro.3986
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 2, p 375 (2020)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
The Ton complex is a molecular motor that uses the proton gradient at the inner membrane of Gram-negative bacteria to generate force and movement, which are transmitted to transporters at the outer membrane, allowing the entry of nutrients into the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::664d4b11dbcdbf32301f46b8d13252c1
https://www.mdpi.com/1422-0067/21/2/375
https://www.mdpi.com/1422-0067/21/2/375
Autor:
Jiansen Jiang, Herve Celia, Istvan Botos, Natalia de Val, Tara Fox, Roland Lloubès, Xiaodan Ni, Susan K. Buchanan
Publikováno v:
Communications Biology
Communications Biology, 2019, 2 (1), pp.358. ⟨10.1038/s42003-019-0604-2⟩
Communications Biology, Vol 2, Iss 1, Pp 1-6 (2019)
Communications Biology, 2019, 2 (1), pp.358. ⟨10.1038/s42003-019-0604-2⟩
Communications Biology, Vol 2, Iss 1, Pp 1-6 (2019)
The TonB–ExbB–ExbD molecular motor harnesses the proton motive force across the bacterial inner membrane to couple energy to transporters at the outer membrane, facilitating uptake of essential nutrients such as iron and cobalamine. TonB physical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66fb1fce1e5a060b958796089c1d89a9
https://hal.science/hal-03641644
https://hal.science/hal-03641644
Autor:
Tara Fox, Herve Celia, Roland Lloubès, Istvan Botos, Xiaodan Ni, Susan K. Buchanan, Jiansen Jiang, Natalia de Val
Publikováno v:
Communications Biology, Vol 3, Iss 1, Pp 1-1 (2020)
Communications Biology
Communications Biology
The TonB-ExbB-ExbD molecular motor harnesses the proton motive force across the bacterial inner membrane to couple energy to transporters at the outer membrane, facilitating uptake of essential nutrients such as iron and cobalamine. TonB physically i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9c2ba8a706632be785881bd9349962f
http://link.springer.com/article/10.1038/s42003-020-01427-w
http://link.springer.com/article/10.1038/s42003-020-01427-w
Autor:
Herve Celia, Enrica Bordignon, Monica Santamaria, Nicholas Noinaj, Istvan Botos, Stanislov D. Zakarov, Travis J. Barnard, Roland Lloubès, Susan K. Buchanan, William A. Cramer
Publikováno v:
Nature
Nature, Nature Publishing Group, 2016, 538 (7623), pp.60-65. ⟨10.1038/nature19757⟩
Nature, 2016, 538 (7623), pp.60-65. ⟨10.1038/nature19757⟩
Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid
Consejería de Sanidad de la Comunidad de Madrid
Nature, Nature Publishing Group, 2016, 538 (7623), pp.60-65. ⟨10.1038/nature19757⟩
Nature, 2016, 538 (7623), pp.60-65. ⟨10.1038/nature19757⟩
Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid
Consejería de Sanidad de la Comunidad de Madrid
In Gram-negative bacteria, outer membrane transporters import nutrients by coupling to an inner membrane protein complex called the Ton complex. The Ton complex consists of TonB, ExbB, and ExbD, and uses the proton motive force at the inner membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99bc380bc6a9102b48d72a099f1c153e
https://hal-amu.archives-ouvertes.fr/hal-01788473/file/281224_2_merged_1466169008.pdf
https://hal-amu.archives-ouvertes.fr/hal-01788473/file/281224_2_merged_1466169008.pdf
Publikováno v:
EMBO Reports
EMBO Reports, EMBO Press, 2014, 15 (3), pp.315-321. ⟨10.1002/embr.201337936⟩
EMBO Reports, 2014, 15 (3), pp.315--21. ⟨10.1002/embr.201337936⟩
EMBO Reports, 2014, 15 (3), pp.315-321. ⟨10.1002/embr.201337936⟩
EMBO Reports, EMBO Press, 2014, 15 (3), pp.315--21. ⟨10.1002/embr.201337936⟩
EMBO Reports, EMBO Press, 2014, 15 (3), pp.315-321. ⟨10.1002/embr.201337936⟩
EMBO Reports, 2014, 15 (3), pp.315--21. ⟨10.1002/embr.201337936⟩
EMBO Reports, 2014, 15 (3), pp.315-321. ⟨10.1002/embr.201337936⟩
EMBO Reports, EMBO Press, 2014, 15 (3), pp.315--21. ⟨10.1002/embr.201337936⟩
International audience; The Type VI secretion system (T6SS) is a widespread macromolecular structure that delivers protein effectors to both eukaryotic and prokaryotic recipient cells. The current model describes the T6SS as an inverted phage tail co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09281c34d40ccdff3e76316d4407bd36
https://hal-amu.archives-ouvertes.fr/hal-03274782
https://hal-amu.archives-ouvertes.fr/hal-03274782
Autor:
Roland Lloubès, Nadir Seddiki, Eric Cascales, Marthe Gavioli, Xiang Y.-Z. Zhang, Herve Celia, Emilie L. Goemaere
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (13), pp.11756--64. ⟨10.1074/jbc.M110.192773⟩
Journal of Biological Chemistry, 2011, 286 (13), pp.11756--64. ⟨10.1074/jbc.M110.192773⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (13), pp.11756--64. ⟨10.1074/jbc.M110.192773⟩
Journal of Biological Chemistry, 2011, 286 (13), pp.11756--64. ⟨10.1074/jbc.M110.192773⟩
International audience; The tolQRAB-pal operon is conserved in Gram-negative genomes. The TolQRA proteins of Escherichia coli form an inner membrane complex in which TolQR uses the proton-motive force to regulate TolA conformation and the in vivo int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::016a6935a9ddb8fdcde7af4239bd9dca
https://hal.archives-ouvertes.fr/hal-01458273
https://hal.archives-ouvertes.fr/hal-01458273
Autor:
Julian P. Whitelegge, Herve Celia, Monica Santamaria, William A. Cramer, Stanislav D. Zakharov, Kirill A. Datsenko, Roland Lloubès
Publikováno v:
Biophysical Journal. 98(3)
ExbBD/TonB and TolQR/TolA complexes of the cytoplasmic membrane transduce energy stored in the electrochemical proton gradient to drive cellular import of siderophores or maintain outer membrane barrier function. Both complexes are utilized for cellu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5de2e3c2100c9ada007890e96ad8fd14