Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Didier Delourme"'
Autor:
Didier Delourme, Laure Brémaud, Idelette Plazanet, Patrick Pélissier, Philippe Label, Nathalie Boizot, Christian Breton, Stéphanie Durand, Guy Costa
Publikováno v:
BMC Genomic Data, Vol 24, Iss 1, Pp 1-4 (2023)
Abstract Objectives Molecular cues linked to heartwood formation open new (complementary) perspectives to genetic breeding programs of Douglas-fir, a tree species largely cultivated in Europe for the natural durability and civil engineering propertie
Externí odkaz:
https://doaj.org/article/f7f78173a3524739ab14e78801ec18de
Autor:
Antoine Péré-Brissaud, Xavier Blanchet, Didier Delourme, Patrick Pélissier, Lionel Forestier, Arnaud Delavaud, Nathalie Duprat, Brigitte Picard, Abderrahman Maftah, Laure Brémaud
Publikováno v:
Open Biology, Vol 5, Iss 9 (2015)
α1-Antichymotrypsin is encoded by the unique SERPINA3 gene in humans, while it is encoded by a cluster of eight closely related genes in cattle. BovSERPINA3 proteins present a high degree of similarity and significant divergences in the reactive cen
Externí odkaz:
https://doaj.org/article/e4b869f4846945f48eabca2d54822064
Autor:
Patrick Trouillas, Didier Delourme, Eric Lapeyronie, Laure Bremaud, Véronique Blanquet, Patrick Pélissier, Montasir Al Mansi, Florent Di Meo, Alexis Parenté
Publikováno v:
FEBS Journal
FEBS Journal, Wiley, 2019, Online Version of Record before inclusion in an issue, 10 p;. ⟨10.1111/febs.15072⟩
FEBS Journal, Wiley, 2019, Online Version of Record before inclusion in an issue, 10 p;. ⟨10.1111/febs.15072⟩
International audience; While GASP-1 and GASP-2 proteins are known to regulate myogenesis by inhibiting myostatin, their structural organization suggests a putative role as multivalent protease inhibitors controlling different protease activities. In
Autor:
Laure Bremaud, Christophe Combet, A Péré-Brissaud, Nathalie Duprat, E Pinault, Ahmed Ouali, Patrick Pélissier, Xavier Blanchet, Didier Delourme, Abderrahman Maftah
Publikováno v:
Protein Science. 21:977-986
The family of serpins is known to fold into a metastable state that is required for the proteinase inhibition mechanism. One of the consequences of this conformational flexibility is the tendency of some mutated serpins to form polymers, which occur
Autor:
Laure Bremaud, Xavier Blanchet, Arnaud Delavaud, Patrick Pélissier, Brigitte Picard, Didier Delourme, Abderrahman Maftah, Antoine Péré-Brissaud, Lionel Forestier, Nathalie Duprat
Publikováno v:
Open Biology
Open biology (5), 1-15. (2015)
Open Biology, Vol 5, Iss 9 (2015)
Open Biology, Royal Society, 2015, 5, pp.1-15. ⟨10.1098/rsob.150071⟩
Open biology (5), 1-15. (2015)
Open Biology, Vol 5, Iss 9 (2015)
Open Biology, Royal Society, 2015, 5, pp.1-15. ⟨10.1098/rsob.150071⟩
α 1 -Antichymotrypsin is encoded by the unique SERPINA3 gene in humans, while it is encoded by a cluster of eight closely related genes in cattle. BovSERPINA3 proteins present a high degree of similarity and significant divergences in the reactive c
Autor:
Katiana Saunier, Hubert Levéziel, Rafael Oriol, Ahmad Oulmouden, Jean-Pierre Barreaud, Didier Delourme, Jacques Souchaire, Jean-Michel Petit, Raymond Julien
Publikováno v:
Glycobiology. 10:611-621
To investigate the synthesis of alpha2-fucosylated epitopes in the bovine species, we have characterized cDNAs from various tissues. We found three distinct alpha2-fucosyltransferase genes, named bovine fut1, fut2, and sec1 which are homologous to hu
Publikováno v:
Acta Botanica Gallica. 146:67-72
L'etude des modes d'action des inhibiteurs de la biosynthese des sterols chez la levure nous a conduits a isoler le gene FEN1. Lorsque celui-ci n'est pas fonctionnel, on assiste a une poly-resistance des levures aux inhibiteurs agissant sur des etape
Publikováno v:
Lipids. 28:907-912
Screening for resistance to fenpropimorph was undertaken in order to isolate yeast mutants affected in the regulation of the ergosterol pathway. Among the mutants isolated, one bearing the recessive fen1-1 mutation was characterized by a 1.5-fold inc
Autor:
Miguel Angel Sentandreu, Gerald Coulis, Didier Delourme, Laure Bremaud, Ahmed Ouali, Abdelghani Boudjellal, Xavier Blanchet, Samira Becila, Patrick Pélissier, Carlos Hernan Herrera-Mendez
Publikováno v:
FEBS Letters
FEBS Letters, Wiley, 2009, 583 (17), pp.2743-2748. ⟨10.1016/j.febslet.2009.07.055⟩
FEBS Letters, Wiley, 2009, 583 (17), pp.2743-2748. ⟨10.1016/j.febslet.2009.07.055⟩
Serpins are a superfamily of structurally conserved proteins. Inhibitory serpins use a suicide substrate-like mechanism. Some are able to inhibit cysteine proteases in cross-class inhibition. Here, we demonstrate for the first time the strong inhibit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be039e870d4a5f141f8290a65e908b7e
https://hal.inrae.fr/hal-02661888
https://hal.inrae.fr/hal-02661888
Autor:
Hubert Levéziel, Patrick Pélissier, Laure Bremaud, Agnès Germot, Didier Delourme, Abderrahman Maftah, Xavier Blanchet, Ahmed Ouali, Samira Becila
Publikováno v:
BMC Genomics
BMC Genomics, BioMed Central, 2008, 9, ⟨10.1186/1471-2164-9-151⟩
BMC Genomics, Vol 9, Iss 1, p 151 (2008)
BMC Genomics (9), . (2008)
BMC Genomics, BioMed Central, 2008, 9, ⟨10.1186/1471-2164-9-151⟩
BMC Genomics, Vol 9, Iss 1, p 151 (2008)
BMC Genomics (9), . (2008)
Background The superfamily of ser ine p roteinase in hibitors (serpins) is involved in numerous fundamental biological processes as inflammation, blood coagulation and apoptosis. Our interest is focused on the SERPINA3 sub-family. The major human pla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d105f3702fa8665ffcc8fd95f433b58d
https://hal.archives-ouvertes.fr/hal-01211893/document
https://hal.archives-ouvertes.fr/hal-01211893/document