Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Elisabeth Darrouzet"'
Autor:
Florent Bernaudat, Annie Frelet-Barrand, Nathalie Pochon, Sébastien Dementin, Patrick Hivin, Sylvain Boutigny, Jean-Baptiste Rioux, Daniel Salvi, Daphné Seigneurin-Berny, Pierre Richaud, Jacques Joyard, David Pignol, Monique Sabaty, Thierry Desnos, Eva Pebay-Peyroula, Elisabeth Darrouzet, Thierry Vernet, Norbert Rolland
Publikováno v:
PLoS ONE, Vol 6, Iss 12, p e29191 (2011)
BackgroundMembrane proteins are the targets of 50% of drugs, although they only represent 1% of total cellular proteins. The first major bottleneck on the route to their functional and structural characterisation is their overexpression; and simply c
Externí odkaz:
https://doaj.org/article/24e6ffec5e774736824ebc599b5bb6ee
Autor:
Elisabeth Darrouzet, Thierry Rabilloud, Hélène Diemer, Sarah Cianférani, Christine Cavazza, Julien Pérard, Véronique Collin-Faure
Publikováno v:
Journal of Proteomics
Journal of Proteomics, 2022, 250, pp.104389. ⟨10.1016/j.jprot.2021.104389⟩
Journal of Proteomics, Elsevier, 2022, 250, pp.104389. ⟨10.1016/j.jprot.2021.104389⟩
Journal of Proteomics, 2022, 250, pp.104389. ⟨10.1016/j.jprot.2021.104389⟩
Journal of Proteomics, Elsevier, 2022, 250, pp.104389. ⟨10.1016/j.jprot.2021.104389⟩
International audience; Some carboxydotrophs like Rhodospirillum rubrum are able to grow with CO as their sole source of energy using a Carbone monoxide dehydrogenase (CODH) and an Energy conserving hydrogenase (ECH) to perform anaerobically the so c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d2c7298a55212b31ebcfc9b8e9c4219
https://hal.science/hal-03361906
https://hal.science/hal-03361906
Autor:
Lisa Salleron, Carlos Eduardo Bernal Barquero, Mariano Martín, Juan Pablo Nicola, Victoria Peyret, Thierry Pourcher, Romina Celeste Geysels, Elisabeth Darrouzet, Sabine Lindenthal, Ana María Masini-Repiso
Publikováno v:
FASEB Journal
FASEB Journal, Federation of American Society of Experimental Biology, 2021, 35 (8), pp.e21681. ⟨10.1096/fj.202100303R⟩
FASEB Journal, Federation of American Society of Experimental Biology, 2021, 35 (8), pp.e21681. ⟨10.1096/fj.202100303R⟩
International audience; The sodium/iodide symporter (NIS) expresses at the basolateral plasma membrane of the thyroid follicular cell and mediates iodide accumulation required for normal thyroid hormonogenesis. Loss-of-function NIS variants cause con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e6fae1f075c7c3d6fe7a036a15fea1a
https://doi.org/10.1096/fj.202100303r
https://doi.org/10.1096/fj.202100303r
Autor:
Mariano Martín, Carlos P. Modenutti, Thierry Pourcher, Victoria Peyret, Ana María Masini-Repiso, Juan Pablo Nicola, Romina Celeste Geysels, Elisabeth Darrouzet, Nancy Carrasco, Marcelo A. Martí
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
The Na+/iodide (I2) symporter (NIS), a glycoprotein expressed at the basolateral plasma membrane of thyroid follicular cells, mediates I2 accumulation for thyroid hormonogenesis and radioiodide therapy for differentiated thyroid carcinoma. However, d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ad29577b23864bd36e988c6f31f78f5
https://pubmed.ncbi.nlm.nih.gov/30496374/
https://pubmed.ncbi.nlm.nih.gov/30496374/
Autor:
Thierry Pourcher, Elisabeth Darrouzet, Iulia Tcheremisinova, Didier Marcellin, Lisa Salleron, Philippe Pognonec, Charles Marchetti, Fanny Graslin
Publikováno v:
Biochemical Journal
Biochemical Journal, 2016, 473 (7), pp.919-928. ⟨10.1042/BJ20151086⟩
Biochemical Journal, Portland Press, 2016, 473 (7), pp.919-928. ⟨10.1042/BJ20151086⟩
Biochemical Journal, 2016, 473 (7), pp.919-928. ⟨10.1042/BJ20151086⟩
Biochemical Journal, Portland Press, 2016, 473 (7), pp.919-928. ⟨10.1042/BJ20151086⟩
The sodium–iodide symporter (NIS) is an integral membrane protein that plays a crucial role in iodide accumulation, especially in the thyroid. As for many other membrane proteins, its intracellular sorting and distribution have a tremendous effect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e48bd699ad1cb91eb4fee47aef1bd42f
https://doi.org/10.1042/bj20151086
https://doi.org/10.1042/bj20151086
Autor:
Didier Marcellin, Jean-Luc Pellequer, Sabine Lindenthal, Thierry Pourcher, Elisabeth Darrouzet
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2014, 1838 (1), pp.244-253. ⟨10.1016/j.bbamem.2013.08.013⟩
Biochimica et Biophysica Acta:Biomembranes, 2014, 1838 (1), pp.244-253. ⟨10.1016/j.bbamem.2013.08.013⟩
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2014, 1838 (1), pp.244-253. ⟨10.1016/j.bbamem.2013.08.013⟩
Biochimica et Biophysica Acta:Biomembranes, 2014, 1838 (1), pp.244-253. ⟨10.1016/j.bbamem.2013.08.013⟩
International audience; The sodium/iodide symporter (NIS or SLC5A5) is an intrinsic membrane protein implicated in iodide uptake into thyroid follicular cells. It plays a crucial role in iodine metabolism and thyroid regulation and its function is wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50c306c343692515f0f0e11f726b78f7
Publikováno v:
Biochemistry. 50:1651-1663
Cytochrome (cyt) bc(1) is a structural dimer with its monomers consisting of the Fe-S protein, cyt b, and cyt c(1) subunits. Its three-dimensional architecture depicts it as a symmetrical homodimer, but the mobility of the head domain of the Fe-S pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98d9e6a5210e9d1f910df61ae2c9fa60
https://doi.org/10.1021/bi101736v
https://doi.org/10.1021/bi101736v
Publikováno v:
FEMS Microbiology Letters. 148:107-114
The NADH-ubiquinone reductase (type I NDH) of Rhodobacter capsulatus is a good model for the genetic study of bacterial homologues of the mitochondrially encoded ND subunits of the mitochondrial complex I. We disrupted the genes nuoH and nuoL which c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89a11c0d8910671148bc56b40cd9c2cb
https://doi.org/10.1111/j.1574-6968.1997.tb10275.x
https://doi.org/10.1111/j.1574-6968.1997.tb10275.x
Autor:
Elisabeth Darrouzet, Eric Quéméneur, Nicole Sage, Frédéric Bérenguer, Véronique Malard, Odette Prat
Publikováno v:
PROTEOMICS. 5:4568-4580
The industrial use of uranium and particularly of depleted uranium, has pinpointed the need to review its chemical impact on human health. A proteomic approach was used to evaluate the response of a human lung cell line (A549) to uranium. We establis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbfe144ae5bd178da09181fa052037e4
https://doi.org/10.1002/pmic.200402038
https://doi.org/10.1002/pmic.200402038
Uncovering the Molecular Mode of Action of the Antimalarial Drug Atovaquone Using a Bacterial System
Autor:
Akhil B. Vaidya, Michael W. Mather, Fevzi Daldal, Jason W. Cooley, Elisabeth Darrouzet, Maria Valkova-Valchanova, Michael T. McIntosh
Publikováno v:
Journal of Biological Chemistry. 280:27458-27465
Atovaquone is an antiparasitic drug that selectively inhibits electron transport through the parasite mitochondrial cytochrome bc1 complex and collapses the mitochondrial membrane potential at concentrations far lower than those at which the mammalia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dab47ac2ad6a1e67eea342696a37283
https://doi.org/10.1074/jbc.m502319200
https://doi.org/10.1074/jbc.m502319200