Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Maud Sigoillot"'
Autor:
Maud Sigoillot, Marie Overtus, Magdalena Grodecka, Daniel Scholl, Abel Garcia-Pino, Toon Laeremans, Lihua He, Els Pardon, Ellen Hildebrandt, Ina Urbatsch, Jan Steyaert, John R. Riordan, Cedric Govaerts
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
The leading cause of cystic fibrosis is the deletion of phenylalanine 508 (F508del) in the first nucleotide-binding domain (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR). Here authors we develop nanobodies targeting NBD1 of
Externí odkaz:
https://doaj.org/article/2a36a5cc137946bdbc014d5d58e302cb
Autor:
Cédric Govaerts, Rafael Colomer Martinez, Chloe Martens, Yiting Wang, Maud Sigoillot, Abel Garcia-Pino, Els Pardon, Marie Overtus, Toon Laeremans, Jelle Hendrix, Daniel Scholl, David N. Sheppard, Jan Steyaert
Publikováno v:
Scholl, D, Wang, Y, Sheppard, D N, Govaerts, C & al., E 2021, ' A Topological Switch in CFTR Modulates Channel Activity and Sensitivity to Unfolding ', Nature Chemical Biology, vol. 17, no. 9, pp. 989-997 . https://doi.org/10.1038/s41589-021-00844-0
The cystic fibrosis transmembrane conductance regulator (CFTR) anion channel is essential to maintain fluid homeostasis in key organs. Functional impairment of CFTR due to mutations in the cftr gene leads to cystic fibrosis. Here, we show that the fi
Autor:
Rafael Colomer, David N. Sheppard, Jelle Hendrix, Els Pardon, Abel Garcia-Pino, Yiting Wang, Daniel Scholl, Chloe Martens, Marie Overtus, Toon Laeremans, Jan Steyaert, Maud Sigoillot, Cédric Govaerts
Publikováno v:
Nature Chemical Biology
The cystic fibrosis transmembrane conductance regulator (CFTR) anion channel is essential to maintain fluid homeostasis in key organs such as the lungs or the digestive systems. Functional impairment of CFTR due to mutation in the cftr gene lead to C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d3173971a1993712b6d2fe6e6a2d37b
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/326089
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/326089
Autor:
Daniel, Scholl, Maud, Sigoillot, Marie, Overtus, Rafael Colomer, Martinez, Chloé, Martens, Yiting, Wang, Els, Pardon, Toon, Laeremans, Abel, Garcia-Pino, Jan, Steyaert, David N, Sheppard, Jelle, Hendrix, Cédric, Govaerts
Publikováno v:
Nature chemical biology. 17(9)
The cystic fibrosis transmembrane conductance regulator (CFTR) anion channel is essential to maintain fluid homeostasis in key organs. Functional impairment of CFTR due to mutations in the cftr gene leads to cystic fibrosis. Here, we show that the fi
Autor:
David N. Sheppard, Chloe Martens, Daniel Scholl, Jelle Hendrix, Rafael Colomer Martinez, Marie Overtus, Els Pardon, Toon Laeremans, Yiting Wang, Jan Steyaert, Maud Sigoillot, Abel Garcia-Pino, Cédric Govaerts
Publikováno v:
bioRxiv
Cystic Fibrosis (CF) is a common lethal genetic disorder caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel. Misfolding and degradation of CFTR are the hallmarks of the predominant mutation, F508del, l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5bc13eec7ff6cb9e07655e7c7136749
https://doi.org/10.1101/2020.07.09.195099
https://doi.org/10.1101/2020.07.09.195099
Autor:
Pierre Legrand, Pierre Roblin, Christophe Charron, Anne Brockhoff, Loïc Briand, Maud Sigoillot, Wolfgang Meyerhof, Christine Belloir, Nicolas Poirier, Fabrice Neiers
Publikováno v:
Chemical Senses
Chemical Senses, Oxford University Press (OUP), 2018, 43 (8), pp.635-643. ⟨10.1093/chemse/bjy054⟩
Chemical Senses, Oxford University Press (OUP), 2018, 43 (8), pp.635-643. ⟨10.1093/chemse/bjy054⟩
International audience; Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges th
Publikováno v:
Cahiers de Nutrition et de Diététique
Cahiers de Nutrition et de Diététique, Elsevier Masson, 2015, 50, pp.252-261
www.sciencedirect.com
Cahiers de Nutrition et de Diététique, Elsevier Masson, 2015, 50, pp.252-261
www.sciencedirect.com
This review summarizes and discusses the current knowledge concerning the physiological role of the sweet taste receptor (T1R2/T1R3) and the potential therapeutic perspectives concerning its inhibition. The functional expression of the sweet taste re
Publikováno v:
Bioelectrochemistry. 101:28-34
We developed an electrochemical assay for the detection of odorant molecules based on a rat odorant-binding protein (rOBP3). We demonstrated that rOBP3 cavity binds 2-methyl-1,4-naphtoquinone (MNQ), an electrochemical probe, as depicted from the decr
Publikováno v:
Bioengineered
Bioengineered, 2013, 4 (1), pp.25-9. ⟨10.4161/bioe.21877⟩
Bioengineered, 2013, 4 (1), pp.25-9. 〈10.4161/bioe.21877〉
Bioengineered 1 (4), 25-29. (2013)
Bioengineered, 2013, 4 (1), pp.25-9. ⟨10.4161/bioe.21877⟩
Bioengineered, 2013, 4 (1), pp.25-9. 〈10.4161/bioe.21877〉
Bioengineered 1 (4), 25-29. (2013)
http://www.landesbioscience.com/; International audience; Sweet taste is mediated by a dimeric receptor composed of two distinct subunits, T1R2 and T1R3, whereas the T1R1/T1R3 receptor is involved in umami taste perception. The T1R1, T1R2, and T1R3 s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aee92d97119016ec01c5f1fbc31d1acb
https://hal.archives-ouvertes.fr/hal-00866018
https://hal.archives-ouvertes.fr/hal-00866018
Publikováno v:
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology, Springer Verlag, 2012, 96 (5), pp.1253-63. ⟨10.1007/s00253-012-3897-3⟩
Applied Microbiology and Biotechnology, Springer Verlag, 2012, 96 (5), pp.1253-63. ⟨10.1007/s00253-012-3897-3⟩
International audience; Gurmarin, a 35-residue polypeptide, is known to selectively inhibit responses to sweet substances in rodents without affecting responses to other basic taste stimuli, such as NaCl, HCl, and quinine. Here, we report the heterol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f02b29130c028f32f6fcdeadb011d891
https://hal.archives-ouvertes.fr/hal-00763833
https://hal.archives-ouvertes.fr/hal-00763833