Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Bénédicte Thiebot"'
Publikováno v:
ACS Central Science, Vol 10, Iss 6, Pp 1167-1178 (2024)
Externí odkaz:
https://doaj.org/article/6171cf0c62c2474c8ae3a4281ef1467a
Autor:
Chloé Talarmin-Gas, Georges Smolyakov, Cleo Parisi, Cyril Scandola, Valérie Andrianasolonirina, Cloé Lecoq, Valentine Houtart, Song-Hua Lee, Homa Adle-Biassette, Bénédicte Thiébot, Timothy Ganderton, Philippe Manivet
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-15 (2024)
Abstract MandibuloAcral Dysplasia associated to MTX2 gene (MADaM) is a recently described progeroid syndrome (accelerated aging disease) whose clinical manifestations include skin abnormalities, growth retardation, and cardiovascular diseases. We pre
Externí odkaz:
https://doaj.org/article/1dbb1081659043f4b03a5d849a79099d
Publikováno v:
MicroTAS
MicroTAS, Oct 2020, on-line, France
HAL
MicroTAS, Oct 2020, on-line, France
HAL
International audience; We show the capture and analysis single cells, in particular human sinonasal squamous cell carcinomas (SCC), by the combination of di-electrophoresis (DEP) force and electrorotation, within a microfluidic device. A set of 4 pl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::808a6476c53e211744afa73bea58b8a4
https://hal.science/hal-03078871
https://hal.science/hal-03078871
Autor:
Hajar Mamad-Hemouch, Gilles Patriarche, Laurent Bacri, Juan Pelta, Cédric Przybylski, Nathalie Jarroux, Bénédicte Thiebot
Publikováno v:
Faraday Discussions
Faraday Discussions, 2018, 210, pp.41-54. ⟨10.1039/C8FD00030A⟩
Faraday Discussions, Royal Society of Chemistry, 2018, 210, pp.41-54. ⟨10.1039/C8FD00030A⟩
Faraday Discussions, 2018, 210, pp.41-54. ⟨10.1039/C8FD00030A⟩
Faraday Discussions, Royal Society of Chemistry, 2018, 210, pp.41-54. ⟨10.1039/C8FD00030A⟩
International audience; Biomimetic ion channels can be made to display the high sensitivity of natural protein nanopores and to develop new properties as a function of the material used. How to design the best future biomimetic channels? The main cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::963dfc36f091431f5bdf44575e743034
https://hal.science/hal-02006444
https://hal.science/hal-02006444
Publikováno v:
European Physical Journal E: Soft matter and biological physics
European Physical Journal E: Soft matter and biological physics, EDP Sciences: EPJ, 2018, 41 (5), ⟨10.1140/epje/i2018-11661-4⟩
European Physical Journal E: Soft matter and biological physics, EDP Sciences: EPJ, 2018, 41 (58), ⟨10.1140/epje/i2018-11661-4⟩
European Physical Journal E: Soft matter and biological physics, 2018, 41 (58), ⟨10.1140/epje/i2018-11661-4⟩
European Physical Journal E: Soft matter and biological physics, EDP Sciences: EPJ, 2018, 41 (5), ⟨10.1140/epje/i2018-11661-4⟩
European Physical Journal E: Soft matter and biological physics, EDP Sciences: EPJ, 2018, 41 (58), ⟨10.1140/epje/i2018-11661-4⟩
European Physical Journal E: Soft matter and biological physics, 2018, 41 (58), ⟨10.1140/epje/i2018-11661-4⟩
International audience; We describe the behaviour of a polyelectrolyte in confined geometry. The transport of a polyelectrolyte, dextran sulfate, through a recombinant protein channel, aerolysin, inserted into a planar lipid bilayer is studied as a f
Autor:
Nathalie Jarroux, Laurent Bacri, Juan Pelta, Hajar Mamad-Hemouch, Cécile Huin, Gilles Patriarche, Cédric Przybylski, Bénédicte Thiebot
Publikováno v:
Nanoscale
Nanoscale, 2018, 10 (32), pp.15303-15316. ⟨10.1039/C8NR02623H⟩
Nanoscale, Royal Society of Chemistry, 2018, 10 (32), pp.15303-15316. ⟨10.1039/C8NR02623H⟩
Nanoscale, 2018, 10 (32), pp.15303-15316. ⟨10.1039/C8NR02623H⟩
Nanoscale, Royal Society of Chemistry, 2018, 10 (32), pp.15303-15316. ⟨10.1039/C8NR02623H⟩
International audience; Biomimetic ion channels with different materials have been extensively designed to study the dynamics in a confined medium. These channels allow the development of several applications, such as ultra-fast sequencing and biomar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::416f0445aea876fb87fabc4aff779194
https://hal.sorbonne-universite.fr/hal-01955731
https://hal.sorbonne-universite.fr/hal-01955731
Autor:
Sid Labdi, Bénédicte Thiebot, Juan Pelta, Georgiy Smolyakov, Childérick Séverac, Clément Campillo, Etienne Dague
Publikováno v:
ACS Applied Materials & Interfaces
ACS Applied Materials & Interfaces, 2016, 8 (41), pp.27426-27431. ⟨10.1021/acsami.6b07698⟩
ACS Applied Materials & Interfaces, Washington, D.C. : American Chemical Society, 2016, 8 (41), pp.27426-27431. ⟨10.1021/acsami.6b07698⟩
ACS Applied Materials & Interfaces, 2016, 8 (41), pp.27426-27431. ⟨10.1021/acsami.6b07698⟩
ACS Applied Materials & Interfaces, Washington, D.C. : American Chemical Society, 2016, 8 (41), pp.27426-27431. ⟨10.1021/acsami.6b07698⟩
International audience; We use single-cell force spectroscopy to compare elasticity, adhesion, and tether extrusion on four breast cancer cell lines with an increasing invasive potential. We perform cell attachment/detachment experiments either on fi
Autor:
Olek Maciejak, Jérôme Mathé, Céline Merstorf, Juan Pelta, Philippe Savarin, Bénédicte Thiebot, Patrick A. Curmi, Marie-Jeanne Clément, Manuela Pastoriza-Gallego, Loïc Auvray
Publikováno v:
Biochemistry
Biochemistry, 2012, 51 (44), pp.8919-8930. ⟨10.1021/bi3003605⟩
Biochemistry, American Chemical Society, 2012, 51 (44), pp.8919-8930. ⟨10.1021/bi3003605⟩
Biochemistry, 2012, 51 (44), pp.8919-8930. ⟨10.1021/bi3003605⟩
Biochemistry, American Chemical Society, 2012, 51 (44), pp.8919-8930. ⟨10.1021/bi3003605⟩
International audience; Being able to differentiate local fluctuations from global folding−unfolding dynamics of a protein is of major interest for improving our understanding of structure−function determinants. The maltose binding protein (MBP),
Autor:
Françoise Gisou van der Goot, Juan Pelta, Leila Rabah, Jean-Michel Betton, Bénédicte Thiebot, Manuela Pastoriza-Gallego, Gabriel Gibrat, Loïc Auvray
Publikováno v:
Journal of the American Chemical Society
Protein export is an essential mechanism in living cells and exported proteins are usually translocated through a protein-conducting channel in an unfolded state. Here we analyze, by electrical detection, the entry and transport of unfolded proteins,
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788:1377-1386
We determined the ability of Maltose Binding Protein and the polyelectrolyte dextran sulfate to enter into and interact with channels formed by Staphylococcus aureus alpha-hemolysin. The entry of either macromolecule in the channel pore causes transi