Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Jean-Jacques Bessoule"'
Autor:
Lysiane Brocard, Françoise Immel, Denis Coulon, Nicolas Esnay, Karine Tuphile, Stéphanie Pascal, Stéphane Claverol, Laëtitia Fouillen, Jean-Jacques Bessoule, Claire Bréhélin
Publikováno v:
Frontiers in Plant Science, Vol 8 (2017)
Lipid droplets (LDs) are cell compartments specialized for oil storage. Although their role and biogenesis are relatively well documented in seeds, little is known about their composition, structure and function in senescing leaves where they also ac
Externí odkaz:
https://doaj.org/article/aae2bede5cf54995bae3d663c54e2fbd
Publikováno v:
Journal of Lipid Research, Vol 43, Iss 7, Pp 1150-1154 (2002)
Imidazole catalyzed acylations of lysolipids by acyl-CoAs in water at room temperature and at a pH close to neutrality. In the presence of oleoyl-CoA and either lysophosphatidylcholine, 1-palmitoyl-sn-glycero-3-phosphocholine (LPC); lysophosphatidylg
Externí odkaz:
https://doaj.org/article/8d8945de7100479b8a319a9b10b16f9e
Autor:
Frédéric Gabriel, Isabelle Accoceberry, Jean-Jacques Bessoule, Bénédicte Salin, Marine Lucas-Guérin, Stephen Manon, Karine Dementhon, Thierry Noël
Publikováno v:
PLoS ONE, Vol 9, Iss 12, p e114531 (2014)
It is generally admitted that the ascomycete yeasts of the subphylum Saccharomycotina possess a single fatty acid ß-oxidation pathway located exclusively in peroxisomes, and that they lost mitochondrial ß-oxidation early during evolution. In this w
Externí odkaz:
https://doaj.org/article/a20d8b4510454ee291f1277a62359893
Autor:
Patricia Laquel, Eric Testet, Karine Tuphile, Christophe Cullin, Laetitia Fouillen, Jean‐Jacques Bessoule, François Doignon
Publikováno v:
Traffic. 23:120-136
Cell polarity is achieved by regulators such as small G proteins, exocyst members and phosphoinositides, with the latter playing a key role when bound to the exocyst proteins Sec3p and Exo70p, and Rho GTPases. This ensures asymmetric growth via the r
Autor:
Lethicia Magno Massuia de Almeida, Mathias Coulon, Jean-Christophe Avice, Annette Morvan-Bertrand, Jean-Jacques Bessoule, Marina Le Guédard, Tae Hwan Kim, Alseny Niare, Alain Mollier, Nadia Bertin, Sophie Brunel-Muguet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2138fdc4896716bd04fe98b0aa49ad61
http://hdl.handle.net/20.500.12278/128757
http://hdl.handle.net/20.500.12278/128757
Autor:
Dittrich-Domergue F, Jean-Jacques Bessoule, Le-Guedard M, Lilly Maneta-Peyret, Patrick Moreau, Wattelet-Boyer, Yohann Boutté, Kriechbaumer
Phosphatidic acid (PA) and Lysophosphatidic acid acyltransferases (LPAATs) might be critical for the secretory pathway. Four extra-plastidial LPAATs (numbered 2,3,4 and 5) were identified in A. thaliana. These AtLPAATs, displaying an enzymatic activi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e03fa0b3d51fad11da86a5bc0876f983
https://doi.org/10.1101/2021.06.08.447563
https://doi.org/10.1101/2021.06.08.447563
Autor:
Valérie Wattelet-Boyer, Marina Le Guédard, Franziska Dittrich-Domergue, Lilly Maneta-Peyret, Verena Kriechbaumer, Yohann Boutté, Jean-Jacques Bessoule, Patrick Moreau
Publikováno v:
Journal of experimental botany. 73(5)
Phosphatidic acid (PA) and lysophosphatidic acid acyltransferases (LPAATs) might be critical for the secretory pathway. Four extra-plastidial LPAATs (LPAAT2, 3, 4, and 5) were identified in Arabidopsis thaliana. These AtLPAATs display a specific enzy
Autor:
Marina Le Guédard, Lethicia Magno Massuia de Almeida, Annette Morvan-Bertrand, Tae-Hwan Kim, Alain Mollier, Marie-Hélène Wagner, María Reyes González-Centeno, Jean-Christophe Avice, Sophie Brunel-Muguet, Pierre-Louis Teissedre, Jean-Jacques Bessoule
Publikováno v:
Environmental and Experimental Botany
Environmental and Experimental Botany, Elsevier, 2021, 185, pp.1-14. ⟨10.1016/j.envexpbot.2021.104400⟩
Environmental and Experimental Botany, Elsevier, 2021, 185, pp.104400. ⟨10.1016/j.envexpbot.2021.104400⟩
Environmental and Experimental Botany, Elsevier, 2021, 185, pp.1-14. ⟨10.1016/j.envexpbot.2021.104400⟩
Environmental and Experimental Botany, Elsevier, 2021, 185, pp.104400. ⟨10.1016/j.envexpbot.2021.104400⟩
International audience; High temperatures during the crop reproductive stage impact seed yield and quality. The changing climate will require consideration of the effects of high temperature events that differ from their intensity, their duration and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0457e6065e45b04f60cea9681b042ee7
https://hal.archives-ouvertes.fr/hal-03363680
https://hal.archives-ouvertes.fr/hal-03363680
Autor:
Pierre-Louis Teissedre, Sophie Brunel-Muguet, Annette Morvan-Bertrand, Lethicia Magno Massuia de Almeida, Jean Christophe Avice, Tae-Hwan Kim, María Reyes González-Centeno, Alain Mollier, Jean-Jacques Bessoule, Marina Le Guédard, Marie Hélène Wagner
High temperatures (HTs) during the crop reproductive stage impact seed yield and quality. The changing climate will require consideration of the effects of repeated HT events following evidence for non-additive effects due to beneficial stress memory
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::979ffe28ac0c009bc3739b8bce66087f
https://doi.org/10.22541/au.159076891.17370253
https://doi.org/10.22541/au.159076891.17370253
Autor:
Magali S. Grison, Jean-Jacques Bessoule, Stéphanie Pascal, Lionel Faure, Valerie Wattelet-Boyer, Denis Coulon, Jonathan Clark, Eric Testet, Marina Le Guédard
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 5, p 1654 (2020)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2020, 21, ⟨10.3390/ijms21051654⟩
Volume 21
Issue 5
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2020, 21, ⟨10.3390/ijms21051654⟩
Volume 21
Issue 5
Lyso-lipid acyltransferases are enzymes involved in various processes such as lipid synthesis and remodelling. Here, we characterized the activity of an acyltransferase from Arabidopsis thaliana (LPIAT). In vitro, this protein, expressed in Escherich