Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Laurence Deneubourg"'
Autor:
Jean-Marie Vanderwinden, Christophe Erneux, Laurence Deneubourg, Colette Moreau, William's Elong Edimo
Publikováno v:
Cellular Signalling. 26:1193-1203
The SH2 containing inositol 5-phosphatase SHIP2 is a member of the mammalian phosphoinositide polyphosphate 5-phosphatase family. It is a multi-domain protein comprising a central catalytic domain, an SH2 domain at its N-terminus, proline rich sequen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c37f205bc335e85365990f3a10a87d1
https://doi.org/10.1016/j.cellsig.2014.02.005
https://doi.org/10.1016/j.cellsig.2014.02.005
Autor:
Laurence Deneubourg, Sebastian Ralea, Christophe Erneux, Ramon Parsons, Petra Gromova, Jean-Marie Vanderwinden
Publikováno v:
Cellular Signalling. 23:1857-1868
Gastrointestinal stromal tumors (GISTs) are the most common mesenchymal tumors of the gastrointestinal tract. Approximately 85% of GISTs harbor activating mutations of the KIT or PDGFRA receptor tyrosine kinases. PTEN and SHIP2 are major phosphatases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43315dd5a4446f47c73a304af33943ab
https://doi.org/10.1016/j.cellsig.2011.06.023
https://doi.org/10.1016/j.cellsig.2011.06.023
Publikováno v:
Journal of Cellular Biochemistry. 112:2203-2209
The SH2 domain containing inositol 5-phosphatase 2 (SHIP2) belongs to the family of the mammalian inositol polyphosphate 5-phosphatases. The two closely related isoenzymes SHIP1 (or SHIP) and SHIP2 contain a N-terminal SH2 domain, a catalytic domain,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a2c7233d51a8749397b2a676b43e9c5
https://doi.org/10.1002/jcb.23146
https://doi.org/10.1002/jcb.23146
Autor:
Joanne Rasschaert, Laurence Deneubourg, Xavier Pesesse, Zhenan Liu, Jing Zhang, Christophe Erneux, Stéphane Schurmans, Daniel Blero
Publikováno v:
Cellular Signalling. 19:2194-2200
Reactive oxygen species (ROS) are known to be involved in redox signalling pathways that may contribute to normal cell function as well as disease progression. The tumour suppressor PTEN and the inositol 5-phosphatase SHIP2 are critical enzymes in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::826ceee63f5965866bbd6a900ca5a808
https://doi.org/10.1016/j.cellsig.2007.06.022
https://doi.org/10.1016/j.cellsig.2007.06.022
Publikováno v:
Journal of cellular biochemistry. 112(9)
The SH2 domain containing inositol 5-phosphatase 2 (SHIP2) belongs to the family of the mammalian inositol polyphosphate 5-phosphatases. The two closely related isoenzymes SHIP1 (or SHIP) and SHIP2 contain a N-terminal SH2 domain, a catalytic domain,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e4988f061dc4d1b6d787a4946e6ae3cb
https://pubmed.ncbi.nlm.nih.gov/21503961
https://pubmed.ncbi.nlm.nih.gov/21503961
Autor:
Edith Charlier, Patrizia Agostinis, Alain Chariot, Laurence Deneubourg, Stuart M. Haslam, Souad Rahmouni, Christophe Erneux, Anne Dell, Geoffrey Gloire, Joseph M. Penninger, P-C Pang, Cecilia B Conde, Jacques Piette, E Di Valentin, Junyu Zhang
Publikováno v:
Leukemia. 24(4)
SHIP-1 (SH2 (Src homology 2)-containing inositol 5'-phosphatase-1) functions as a negative regulator of immune responses by hydrolyzing phosphatidylinositol-3,4,5-triphosphate generated by phosphoinositide-3 (PI 3)-kinase activity. As a result, SHIP-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb4667af33303e56a24a72353700ad2e
https://pubmed.ncbi.nlm.nih.gov/20147977
https://pubmed.ncbi.nlm.nih.gov/20147977
Publikováno v:
Advances in enzyme regulation. 50(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56c39440863866e6283bc57ded0e2743
https://pubmed.ncbi.nlm.nih.gov/19895833
https://pubmed.ncbi.nlm.nih.gov/19895833
Autor:
Zhongchun Zhang, Johannes L. Bos, Laurence Deneubourg, Holger Rehmann, J.H. Raaijmakers, Christophe Erneux, John P. de Koning, Sonja Krugmann
Publikováno v:
Cellular signalling, 19(6), 1249. Elsevier
Arap3 is a phosphoinositide (PI) 3 kinase effector that serves as a GTPase activating protein (GAP) for both Arf and Rho G-proteins. The protein has multiple pleckstrin homology (PH) domains that bind preferentially phosphatidyl-inositol-3,4,5-trisph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d010d2379c7133b00218210a2d76874a
https://dspace.library.uu.nl/handle/1874/35664
https://dspace.library.uu.nl/handle/1874/35664
