Výsledky vyhledávání - "Cécile Basquin"

Towards Improved Food and Nutrition Security in Sindh Province, Pakistan

Autor: Joanna Friedman, Cécile Basquin, Shahid Fazal, Paola María Valdettaro, Silke Pietzsch

Publikováno v: IDS Bulletin. 44:21-30

The 2011 National Nutrition Survey (NNS) in Pakistan showed that Sindh province continues to have some of the worst undernutrition rates in South Asia. For determinants of acute and chronic malnutrition to be better understood, Action Against Hunger

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e16dfc51d96ec18c673ca1fb3d903a0d
https://doi.org/10.1111/1759-5436.12027

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The Na + /I − symporter (NIS) mediates electroneutral active transport of the environmental pollutant perchlorate

Autor: Orsolya Dohán, L. Mario Amzel, Nancy Carrasco, Cécile Basquin, Andrea Reyna-Neyra, Carla Portulano

Publikováno v: Proceedings of the National Academy of Sciences. 104:20250-20255

The Na + /I − symporter (NIS) is a key plasma membrane protein that mediates active I − uptake in the thyroid, lactating breast, and other tissues with an electrogenic stoichiometry of 2 Na + per I − . In the thyroid, NIS-mediated I − uptake

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ec477718aa744c627de78e049a6b968
https://doi.org/10.1073/pnas.0707207104

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Characterisation of the purified human sodium/iodide symporter reveals that the protein is mainly present in a dimeric form and permits the detailed study of a native C-terminal fragment

Autor: Olivier Averseng, Sylvaine Huc-Brandt, Didier Marcellin, Laurent Bellanger, Valérie Navarro, Patrick Hivin, Fanny Graslin, Cécile Basquin, Thierry Pourcher, Eric Quéméneur, Elisabeth Darrouzet

Publikováno v: Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2011, 1808 (1), pp.65-77. ⟨10.1016/j.bbamem.2010.08.013⟩
Biochimica et Biophysica Acta:Biomembranes, 2011, 1808 (1), pp.65-77. ⟨10.1016/j.bbamem.2010.08.013⟩

The sodium/iodide symporter is an intrinsic membrane protein that actively transports iodide into thyroid follicular cells. It is a key element in thyroid hormone biosynthesis and in the radiotherapy of thyroid tumours and their metastases. Sodium/io

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfaa6211f41dc2c99fe933c349fcdab1
https://pubmed.ncbi.nlm.nih.gov/20797386

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The Na+/I- symporter mediates active iodide uptake in the intestine

Autor: Juan Pablo Nicola, Monika Paroder, Carla Portulano, Cécile Basquin, Nancy Carrasco, Andrea Reyna-Neyra

Publikováno v: American journal of physiology. Cell physiology. 296(4)

Absorption of dietary iodide, presumably in the small intestine, is the first step in iodide (I−) utilization. From the bloodstream, I−is actively taken up via the Na+/I−symporter (NIS) in the thyroid for thyroid hormone biosynthesis and in suc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68b21fc9ab1413d8390c11c923f12deb
https://pubmed.ncbi.nlm.nih.gov/19052257

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Comparison of expressed human and mouse sodium/iodide symporters reveals differences in transport properties and subcellular localization

Autor: Manal A. Dayem, Robert Marsault, Patrick Chang, Valérie Navarro, Patricia Carrier, Cécile Basquin, Thierry Pourcher, Sabine Lindenthal, Elisabeth Darrouzet, Sylvaine Huc

Publikováno v: Journal of Endocrinology
Journal of Endocrinology, BioScientifica, 2008, 197 (1), pp.95-109. ⟨10.1677/JOE-07-0455⟩
Journal of Endocrinology, 2008, 197 (1), pp.95-109. ⟨10.1677/JOE-07-0455⟩

The active transport of iodide from the bloodstream into thyroid follicular cells is mediated by the Na+/I− symporter (NIS). We studied mouse NIS (mNIS) and found that it catalyzes iodide transport into transfected cells more efficiently than human

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab95d182f4451d5c00253e36f50bef39
https://hal.archives-ouvertes.fr/hal-02281985

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The inner interhelix loop 4-5 of the melibiose permease from Escherichia coli takes part in conformational changes after sugar binding

Autor: Gérard Leblanc, Cécile Basquin, Kerstin Meyer-Lipp, Klaus Fendler, Constanta Ganea, Natacha Séry

Publikováno v: The Journal of biological chemistry. 281(36)

Cytoplasmic loop 4–5 of the melibiose permease from Escherichia coli is essential for the process of Na+-sugar translocation (Abdel-Dayem, M., Basquin, C., Pourcher, T., Cordat, E., and Leblanc, G. (2003) J. Biol. Chem. 278, 1518–1524). In the pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ee4f32f97cc62034db0cffeed1269f7
https://pubmed.ncbi.nlm.nih.gov/16822867

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