Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Séverine Groh"'
Autor:
Henry L. Keen, Pimonrat Ketsawatsomkron, Curt D. Sigmund, Frank M. Faraci, Séverine Groh, Christopher J. Pelham
Publikováno v:
Journal of Biological Chemistry. 285:9311-9316
Peroxisome proliferator-activated receptor-gamma (PPAR gamma) is a ligand-activated transcription factor of the nuclear hormone receptor superfamily. Increasing evidence suggests that PPAR gamma is involved in the regulation of vascular function and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d8bc988711014d2f7a2363d56f50779
https://doi.org/10.1074/jbc.r109.025031
https://doi.org/10.1074/jbc.r109.025031
Autor:
Jeffrey E. Pessin, Kevin P. Campbell, Matthew M. Goddeeris, David Venzke, Haihong Zong, Séverine Groh, Connie S. Lebakken
Publikováno v:
Journal of Biological Chemistry. 284:19178-19182
The sarcoglycans are known as an integral subcomplex of the dystrophin glycoprotein complex, the function of which is best characterized in skeletal muscle in relation to muscular dystrophies. Here we demonstrate that the white adipocytes, which shar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd150a4fab9ca026763b04a5c3a12b28
https://doi.org/10.1074/jbc.c109.010728
https://doi.org/10.1074/jbc.c109.010728
Autor:
Séverine Groh, Dimple Bansal, Steven S. Vogel, Chien-Chang Chen, Roger A. Williamson, Katsuya Miyake, Paul L. McNeil, Kevin P. Campbell
Publikováno v:
Nature. 423:168-172
Muscular dystrophy includes a diverse group of inherited muscle diseases characterized by wasting and weakness of skeletal muscle. Mutations in dysferlin are linked to two clinically distinct muscle diseases, limb-girdle muscular dystrophy type 2B an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5976236d52dfa2e502ad90b68788eb5
https://doi.org/10.1038/nature01573
https://doi.org/10.1038/nature01573
Autor:
Séverine Groh, Norma B. Romero, Michel Villaz, Joelle Henry-Berger, Dominique Thevenon, Michel DeWaard, Isabelle Marty, Sophia Smida-Rezgui, Frédéric Chevessier
Publikováno v:
Biochemical and Biophysical Research Communications. 303:669-675
We obtained the gene organization of human triadin gene by aligning the DNA coding sequence of human 95-kDa triadin (Trisk 95) with human genomic database. We identified a novel human triadin isoform, a potential human homologue of rat Trisk 51. We s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2aa9ba8d39a65810e0e8dc60f793e93e
https://doi.org/10.1016/s0006-291x(03)00406-6
https://doi.org/10.1016/s0006-291x(03)00406-6
Autor:
Curt D. Sigmund, Henry L. Keen, Séverine Groh, Christopher J. Pelham, Stella-Rita C Ibeawuchi, Frank M. Faraci, Justin L. Grobe, Pimonrat Ketsawatsomkron, Eric T. Weatherford, Willem J. de Lange
Publikováno v:
Cell metabolism. 16(4)
SummaryDominant-negative (DN) mutations in the nuclear hormone receptor peroxisome proliferator-activated receptor-γ (PPARγ) cause hypertension by an unknown mechanism. Hypertension and vascular dysfunction are recapitulated by expression of DN PPA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cbf903bb40edd653b191ed8c25dbb82
https://pubmed.ncbi.nlm.nih.gov/23040065
https://pubmed.ncbi.nlm.nih.gov/23040065
Autor:
Kevin P. Campbell, Isabelle Marty, Stéphane Vassilopoulos, Julien Fauré, Julie Brocard, Marine Cacheux, Séverine Groh, Sarah Oddoux
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2010, 49 (29), pp.6130-5. ⟨10.1021/bi100796v⟩
Biochemistry, American Chemical Society, 2010, 49 (29), pp.6130-5. ⟨10.1021/bi100796v⟩
International audience; The triadin isoforms Trisk 95 and Trisk 51 are both components of the skeletal muscle calcium release complex. To investigate the specific role of Trisk 95 and Trisk 51 isoforms in muscle physiology, we overexpressed Trisk 95
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3783aea3462def22ad44fb165b8ece98
https://pubmed.ncbi.nlm.nih.gov/20565104
https://pubmed.ncbi.nlm.nih.gov/20565104
Autor:
Séverine, Groh, Haihong, Zong, Matthew M, Goddeeris, Connie S, Lebakken, David, Venzke, Jeffrey E, Pessin, Kevin P, Campbell
Publikováno v:
The Journal of Biological Chemistry
The sarcoglycans are known as an integral subcomplex of the dystrophin glycoprotein complex, the function of which is best characterized in skeletal muscle in relation to muscular dystrophies. Here we demonstrate that the white adipocytes, which shar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b96782a28b0f77289c46939144152986
https://pubmed.ncbi.nlm.nih.gov/19494113
https://pubmed.ncbi.nlm.nih.gov/19494113
Autor:
Sylvain Sainnier, Mylène Robert, Didier Grunwald, Séverine Groh, Christian Scotto, Dominique Thevenon, Isabelle Marty, Michel Villaz
Publikováno v:
The Journal of biological chemistry. 275(11)
We have shown that several isoforms of triadin, a protein involved in calcium release process through the ryanodine receptor, are expressed in rat skeletal muscle, and we have cloned two of these isoforms. One is the rat homolog of the 95-kDa triadin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c27ae31513dca1d8261af0bce4282679
https://pubmed.ncbi.nlm.nih.gov/10713145
https://pubmed.ncbi.nlm.nih.gov/10713145
Autor:
Michel Ronjat, Michela Ottolia, Isabelle Marty, Agnès Chapel, Michel Villaz, Gianfranco Prestipino, Séverine Groh
Publikováno v:
The Journal of biological chemistry. 274(18)
Triadin has been shown to co-localize with the ryanodine receptor in the sarcoplasmic reticulum membrane. We show that immunoprecipitation of solubilized sarcoplasmic reticulum membrane with antibodies directed against triadin or ryanodine receptor,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed8b6496ae19b734f4eaa799ea362445
https://pubmed.ncbi.nlm.nih.gov/10212196
https://pubmed.ncbi.nlm.nih.gov/10212196
Autor:
Mylène Robert, Susan Treves, Michela Ottolia, Gianfranco Prestipino, Séverine Groh, Michel Ronjat, Erica Scutari, Francesco Zorzato
Publikováno v:
Biochemistry. 36(38)
In the present report we studied the interaction between the skeletal muscle ryanodine receptor and the ubiquitous S100A1 Ca2+ binding protein. S100A1 did not affect equilibrium [3H]ryanodine binding to purified rabbit skeletal muscle terminal cister
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2f04f0b84fb7508ac2cd98185916234
https://pubmed.ncbi.nlm.nih.gov/9298970
https://pubmed.ncbi.nlm.nih.gov/9298970