Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Céline Desbourdes"'
Autor:
Marie-Lise Lacombe, Frederic Lamarche, Olivier De Wever, Teresita Padilla-Benavides, Alyssa Carlson, Imran Khan, Anda Huna, Sophie Vacher, Claire Calmel, Céline Desbourdes, Cécile Cottet-Rousselle, Isabelle Hininger-Favier, Stéphane Attia, Béatrice Nawrocki-Raby, Joël Raingeaud, Christelle Machon, Jérôme Guitton, Morgane Le Gall, Guilhem Clary, Cedric Broussard, Philippe Chafey, Patrice Thérond, David Bernard, Eric Fontaine, Malgorzata Tokarska-Schlattner, Patricia Steeg, Ivan Bièche, Uwe Schlattner, Mathieu Boissan
Publikováno v:
BMC Biology, Vol 19, Iss 1, Pp 1-29 (2021)
Abstract Background Mitochondrial nucleoside diphosphate kinase (NDPK-D, NME4, NM23-H4) is a multifunctional enzyme mainly localized in the intermembrane space, bound to the inner membrane. Results We constructed loss-of-function mutants of NDPK-D, l
Externí odkaz:
https://doaj.org/article/64c3e3bcb5024675ac11f551606b20d8
Autor:
David Bernard, Malgorzata Tokarska-Schlattner, Anda Huna, Patrice Thérond, Isabelle Hininger-Favier, Sophie Vacher, Patricia S. Steeg, Céline Desbourdes, Guilhem Clary, Philippe Chafey, Morgane Le Gall, Imran Khan, Jérôme Guitton, Olivier De Wever, Christelle Machon, Alyssa Carlson, Ivan Bièche, Teresita Padilla-Benavides, Cécile Cottet-Rousselle, Uwe Schlattner, Stéphane Attia, Béatrice Nawrocki-Raby, Cédric Broussard, Frédéric Lamarche, Mathieu Boissan, Joël Raingeaud, Marie-Lise Lacombe, Claire Calmel, Eric Fontaine
Publikováno v:
BMC BIOLOGY
BMC Biology
BMC Biology, BioMed Central, 2021, 19 (1), ⟨10.1186/s12915-021-01155-5⟩
BMC Biology, 2021, 19 (1), ⟨10.1186/s12915-021-01155-5⟩
BMC Biology, Vol 19, Iss 1, Pp 1-29 (2021)
BMC Biology
BMC Biology, BioMed Central, 2021, 19 (1), ⟨10.1186/s12915-021-01155-5⟩
BMC Biology, 2021, 19 (1), ⟨10.1186/s12915-021-01155-5⟩
BMC Biology, Vol 19, Iss 1, Pp 1-29 (2021)
Background Mitochondrial nucleoside diphosphate kinase (NDPK-D, NME4, NM23-H4) is a multifunctional enzyme mainly localized in the intermembrane space, bound to the inner membrane. Results We constructed loss-of-function mutants of NDPK-D, lacking ei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cbd007d0c6d8a5153e3d323369cab8a
https://hdl.handle.net/1854/LU-8738468
https://hdl.handle.net/1854/LU-8738468
Autor:
Juliette Trepreau, Géraldine Sarret, Isabelle Petit-Haertlein, Eve de Rosny, Eric Girard, Antoine P. Maillard, Dietrich H. Nies, Sandra Kuennemann, Cornelia Grosse, Jean-Marie Mouesca, Jacques Covès, Céline Desbourdes
Publikováno v:
Metallomics
Metallomics, Royal Society of Chemistry, 2014, 6 (2), pp.263-273. ⟨10.1039/C3MT00248A⟩
Metallomics, 2014, 6 (2), pp.263-273. ⟨10.1039/C3MT00248A⟩
Metallomics, Royal Society of Chemistry, 2014, 6 (2), pp.263-273. ⟨10.1039/C3MT00248A⟩
Metallomics, 2014, 6 (2), pp.263-273. ⟨10.1039/C3MT00248A⟩
International audience; When CnrX, the periplasmic sensor protein in the CnrYXH transmembrane signal transduction complex of Cupriavidus metallidurans CH34, binds the cognate metal ions Ni(II) or Co(II), the ECF-type sigma factor CnrH is made availab
Autor:
Vladimir A. Tyurin, Yiran Li, Cécile Cottet-Rousselle, Jianfei Jiang, Charleen T. Chu, Zhentai Huang, Amin Cheikhi, Marie-Lise Lacombe, Malgorzata Tokarska-Schlattner, Y.Y. Tyurina, C. St. Croix, Alexander A. Kapralov, Simon C. Watkins, Valerian E. Kagan, Zheni Shen, Manish Verma, Mathieu Boissan, Donna B. Stolz, Gaowei Mao, Miriam L. Greenberg, Céline Desbourdes, Haider H. Dar, Rama K. Mallampalli, Uwe Schlattner, Hülya Bayır, Richard M. Epand
Publikováno v:
Cell Death and Differentiation
Cell Death and Differentiation, Nature Publishing Group, 2016, 23 (7), pp.1140-1151. ⟨10.1038/cdd.2015.160⟩
Cell Death and Differentiation, Nature Publishing Group, 2016, 23 (7), pp.1140-1151. ⟨10.1038/cdd.2015.160⟩
Mitophagy is critical for cell homeostasis. Externalization of the inner mitochondrial membrane phospholipid, cardiolipin (CL), to the surface of the outer mitochondrial membrane (OMM) was identified as a mitophageal signal recognized by the microtub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2d2f32641c3c43198fd097f615cb5be
https://hal.univ-grenoble-alpes.fr/hal-01987526
https://hal.univ-grenoble-alpes.fr/hal-01987526
Autor:
Alexandr A. Kapralov, Manish Verma, Vladimir A. Tyurina, Cécile Cottet-Rousselle, Jianfei Jiang, Valerian E. Kagan, Céline Desbourdes, Yulia Y. Tyurina, Zhentai Huang, Uwe Schlattner, Hülya Bayır, Marie-Lise Lacombe, Haider H. Dar, Rama K. Mallampalli, Charleen T. Chu
Publikováno v:
60th Annual Meeting of Biophysical Society
60th Annual Meeting of Biophysical Society, Feb 2016, Los Ageles, United States. 110 (3 suppl 1), pp.472a, 2016, Biophysical Journal. ⟨10.1016/j.bpj.2015.11.2528⟩
60th Annual Meeting of Biophysical Society, Feb 2016, Los Ageles, United States. 110 (3 suppl 1), pp.472a, 2016, Biophysical Journal. ⟨10.1016/j.bpj.2015.11.2528⟩
The well-established function of the hexameric intermembrane space protein, NDPK-D/NM23-H4, is phosphotransfer activity as a nucleoside diphosphate kinase. However, recent data revealed a second function in lipid signaling that is involved in mitopha
Publikováno v:
58th Annual Meeting of the Biophysical Society
58th Annual Meeting of the Biophysical Society, Feb 2014, San Francisco, United States. 112 (3 suppl 1), pp.324A-325A, 2017, Biophysical Journal. ⟨10.1016/j.bpj.2016.11.1757⟩
58th Annual Meeting of the Biophysical Society, Feb 2014, San Francisco, United States. 112 (3 suppl 1), pp.324A-325A, 2017, Biophysical Journal. ⟨10.1016/j.bpj.2016.11.1757⟩
The well-established function of the mitochondrial intermembrane space protein NM23-H4/NDPK-D is phosphotransfer activity as a nucleoside diphosphate kinase (NDPK). However, recent data have revealed a second function in lipid signaling that triggers
Autor:
Ioan Lascu, Graça Raposo, Céline Desbourdes, Philippe Chavrier, Nathalie Sauvonnet, Thibault Lagache, Guillaume Montagnac, Jérôme Guitton, Qinfang Shen, Aurélien Roux, Marie-Lise Lacombe, Maryse Romao, Uwe Schlattner, Lorena Griparic, AlexanderM van der Bliek, Mathieu Boissan, Simona Polo
Publikováno v:
Science
Science, American Association for the Advancement of Science, 2014, 344 (6191), pp.1510-1515. ⟨10.1126/science.1253768⟩
Science, Vol. 344, No 6191 (2014) pp. 1510-1515
Science, 2014, 344 (6191), pp.1510-1515. ⟨10.1126/science.1253768⟩
Science, American Association for the Advancement of Science, 2014, 344 (6191), pp.1510-1515. ⟨10.1126/science.1253768⟩
Science, Vol. 344, No 6191 (2014) pp. 1510-1515
Science, 2014, 344 (6191), pp.1510-1515. ⟨10.1126/science.1253768⟩
Supplying power: Right time, right place Cell membranes are very flexible and easily molded to shape; however, to physically pinch off a membrane vesicle from a membrane tube still requires power. A type of molecular machine known as dynamin is invol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7726ff13ddbb69fa06ced235e15f2ddc
https://hal.archives-ouvertes.fr/hal-01870066
https://hal.archives-ouvertes.fr/hal-01870066
Autor:
Marie-Lise Lacombe, Céline Desbourdes, Philippe Chavrier, Jianfei Jiang, Valerian E. Kagan, Mathieu Boissan, Uwe Schlattner, Hülya Bayır, Malgorzata Tokarska-Schlattner, Cécile Cottet-Rousselle
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857:e26
Autor:
Alexander M. van der Bliek, Guillaume Montagnac, Aurélien Roux, Lorena Griparic, Philippe Chavrier, Cécile Cottet-Rousselle, Uwe Schlattner, Yulia Y. Tyurina, Jianfei Jiang, Céline Desbourdes, Mathieu Boissan, Zhentai Huang, Malgorzata Tokarska-Schlattner, Valerian E. Kagan, Marie-Lise Lacombe
Publikováno v:
ResearcherID
59th Annual Meeting of the Biophysical Society
59th Annual Meeting of the Biophysical Society, Feb 2015, Baltimore, United States. Elsevier, 108 (2 suppl 1), pp.369a, 2015, Biophysical Journal. ⟨10.1016/j.bpj.2014.11.2020⟩
59th Annual Meeting of the Biophysical Society
59th Annual Meeting of the Biophysical Society, Feb 2015, Baltimore, United States. Elsevier, 108 (2 suppl 1), pp.369a, 2015, Biophysical Journal. ⟨10.1016/j.bpj.2014.11.2020⟩
NM23-H4/NDPK-D forms symmetrical homohexameric complexes in the mitochondrial inter-membrane space. The well-established function of NM23-H4 is phosphotransfer activity as a nucleoside diphosphate kinase, using mitochondrial ATP to regenerate NTPs, e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98c58321835def5926ff6370d5652458
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000362849400264&KeyUID=WOS:000362849400264
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000362849400264&KeyUID=WOS:000362849400264