Zobrazeno 1 - 10
of 12
pro vyhledávání: '"MESH: Flavin-Adenine Dinucleotide"'
Autor:
Manuel Maestre-Reyna, Cheng-Han Yang, Eriko Nango, Wei-Cheng Huang, Eka Putra Gusti Ngurah Putu, Wen-Jin Wu, Po-Hsun Wang, Sophie Franz-Badur, Martin Saft, Hans-Joachim Emmerich, Hsiang-Yi Wu, Cheng-Chung Lee, Kai-Fa Huang, Yao-Kai Chang, Jiahn-Haur Liao, Jui-Hung Weng, Wael Gad, Chiung-Wen Chang, Allan H. Pang, Michihiro Sugahara, Shigeki Owada, Yuhei Hosokawa, Yasumasa Joti, Ayumi Yamashita, Rie Tanaka, Tomoyuki Tanaka, Fangjia Luo, Kensuke Tono, Kai-Cheng Hsu, Stephan Kiontke, Igor Schapiro, Roberta Spadaccini, Antoine Royant, Junpei Yamamoto, So Iwata, Lars-Oliver Essen, Yoshitaka Bessho, Ming-Daw Tsai
Publikováno v:
Nature Chemistry
Nature Chemistry, 2022, 14 (6), pp.677-685. ⟨10.1038/s41557-022-00922-3⟩
Nature Chemistry, 2022, 14 (6), pp.677-685. ⟨10.1038/s41557-022-00922-3⟩
International audience; Flavin coenzymes are universally found in biological redox reactions. DNA photolyases, with their flavin chromophore (FAD), utilize blue light for DNA repair and photoreduction. The latter process involves two single-electron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ab1ccc473a4c1aff447bbd9403e54d0
https://hal.science/hal-03716098
https://hal.science/hal-03716098
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2013, 52 (49), pp.8949-8956. 〈10.1021/bi4013879〉
Biochemistry, American Chemical Society, 2013, 52 (49), pp.8949-8956. ⟨10.1021/bi4013879⟩
Biochemistry, 2013, 52 (49), pp.8949-8956. ⟨10.1021/bi4013879⟩
Biochemistry, American Chemical Society, 2013, 52 (49), pp.8949-8956. 〈10.1021/bi4013879〉
Biochemistry, American Chemical Society, 2013, 52 (49), pp.8949-8956. ⟨10.1021/bi4013879⟩
Biochemistry, 2013, 52 (49), pp.8949-8956. ⟨10.1021/bi4013879⟩
International audience; TrmFO is a tRNA methyltransferase that uses methylenetetrahydrofolate (CH2THF) and flavin adenine dinucleotide hydroquinone as cofactors. We have recently shown that TrmFO from Bacillus subtilis stabilizes a TrmFO-CH2-FADH add
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::569c75d096d6fc0e4062c0c8b37545a7
https://doi.org/10.1021/bi4013879
https://doi.org/10.1021/bi4013879
Autor:
Béatrice Benayoun, Anna Tury, Georges Mairet-Coello, Pierre-Yves Risold, Dominique Fellmann, B. Griffond, Annick Esnard-Fève
Publikováno v:
Cell and Tissue Research
Cell and Tissue Research, Springer Verlag, 2006, 323 (1), pp.91-103. ⟨10.1007/s00441-005-0043-x⟩
Cell and Tissue Research, Springer Verlag, 2006, 323 (1), pp.91-103. ⟨10.1007/s00441-005-0043-x⟩
International audience; Rat quiescin/sulphydryl oxidase (rQSOX) introduces disulphide bridges into peptides and proteins with the reduction of molecular oxygen to hydrogen peroxide. Its occurrence has been previously highlighted in a wide range of or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e0c1c7d1c07ed0747065c0d184f6d56
https://doi.org/10.1007/s00441-005-0043-x
https://doi.org/10.1007/s00441-005-0043-x
Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain
Autor:
Michèle Jouvenot, Dominique Fellmann, Franck Thiebault, Georges Mairet-Coello, Didier Colin, Jean Radom, Mai J. Dognin-Bergeret, Annick Esnard-Fève
Publikováno v:
BBA-Molecular Cell Research
BBA-Molecular Cell Research, Elsevier, 2006, 1759 (5), pp.225-33. 〈10.1016/j.bbaexp.2006.04.008〉
Biochimica et Biophysica Acta-Molecular Cell Research
Biochimica et Biophysica Acta-Molecular Cell Research, Elsevier, 2006, 1759 (5), pp.225-33. ⟨10.1016/j.bbaexp.2006.04.008⟩
BBA-Molecular Cell Research, Elsevier, 2006, 1759 (5), pp.225-33. 〈10.1016/j.bbaexp.2006.04.008〉
Biochimica et Biophysica Acta-Molecular Cell Research
Biochimica et Biophysica Acta-Molecular Cell Research, Elsevier, 2006, 1759 (5), pp.225-33. ⟨10.1016/j.bbaexp.2006.04.008⟩
Flavoproteins of the quiescin/sulfhydryl oxidase (QSOX) family catalyze oxidation of peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. We report here the molecular cloning of a new putative sulfhydryl oxidase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a3f399f5bd36cdb8bb400ab5b5f4416
https://hal.archives-ouvertes.fr/hal-00482217
https://hal.archives-ouvertes.fr/hal-00482217
Autor:
Hajj Chehade, Mahmoud, Loiseau, Laurent, Lombard, Murielle, Pecqueur, Ludovic, Ismail, Alexandre, Smadja, Myriam, Golinelli-Pimpaneau, Béatrice, Mellot-Draznieks, Caroline, Hamelin, Olivier, Aussel, Laurent, Kieffer-Jaquinod, Sylvie, Labessan, Natty, Barras, Frédéric, Fontecave, Marc, Pierrel, Fabien
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (27), pp.20085-92. ⟨10.1074/jbc.M113.480368⟩
Journal of Biological Chemistry, 2013, 288 (27), pp.20085-92. ⟨10.1074/jbc.M113.480368⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (27), pp.20085-92. ⟨10.1074/jbc.M113.480368⟩
Journal of Biological Chemistry, 2013, 288 (27), pp.20085-92. ⟨10.1074/jbc.M113.480368⟩
International audience; Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::6b4f6b11a40315ebf5c93db707fb4b39
https://hal.archives-ouvertes.fr/hal-00904907/file/manuscript.pdf
https://hal.archives-ouvertes.fr/hal-00904907/file/manuscript.pdf
Autor:
Rui Tada, Isabel Valsecchi, Giovanni Gadda, Andrea Pennati, Stephen Sherman, Hajime Sato, Jean-Paul Latgé, Karine Lambou, Rémi Beau
Publikováno v:
Eukaryotic Cell
Eukaryotic Cell, American Society for Microbiology, 2013, 12 (6), pp.853-863. ⟨10.1128/EC.00348-12⟩
Eukaryotic Cell, 2013, 12 (6), pp.853-863. ⟨10.1128/EC.00348-12⟩
Eukaryotic Cell, American Society for Microbiology, 2013, 12 (6), pp.853-863. ⟨10.1128/EC.00348-12⟩
Eukaryotic Cell, 2013, 12 (6), pp.853-863. ⟨10.1128/EC.00348-12⟩
The choline oxidase ( CHOA ) and betaine aldehyde dehydrogenase ( BADH ) genes identified in Aspergillus fumigatus are present as a cluster specific for fungal genomes. Biochemical and molecular analyses of this cluster showed that it has very specif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d5f1a7bb4b99fd4ba4143e66f3a2763
https://hal.archives-ouvertes.fr/hal-02468278
https://hal.archives-ouvertes.fr/hal-02468278
Autor:
Marie-Claire Dagher, Sylvain Beaumel, Antoine Picciocchi, Marie José Stasia, Didier Grunwald, Franck Debeurme, Algirdas J. Jesaitis
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (32), pp.28357-69. ⟨10.1074/jbc.M111.220418⟩
Journal of Biological Chemistry, 2011, 286 (32), pp.28357-69. ⟨10.1074/jbc.M111.220418⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (32), pp.28357-69. ⟨10.1074/jbc.M111.220418⟩
Journal of Biological Chemistry, 2011, 286 (32), pp.28357-69. ⟨10.1074/jbc.M111.220418⟩
International audience; Flavocytochrome b(558) (cytb) of phagocytes is a heterodimeric integral membrane protein composed of two subunits, p22(phox) and gp91(phox). The latter subunit, also known as Nox2, has a cytosolic C-terminal "dehydrogenase dom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70875dcd80b626a26a57b82a3b5ce973
https://www.hal.inserm.fr/inserm-00763368/file/Picciocchi_2011_Role_of_ME.pdf
https://www.hal.inserm.fr/inserm-00763368/file/Picciocchi_2011_Role_of_ME.pdf
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2011, 50 (12), pp.2111-22. ⟨10.1021/bi101772a⟩
Biochemistry, 2011, 50 (12), pp.2111-22. ⟨10.1021/bi101772a⟩
Biochemistry, American Chemical Society, 2011, 50 (12), pp.2111-22. ⟨10.1021/bi101772a⟩
Biochemistry, 2011, 50 (12), pp.2111-22. ⟨10.1021/bi101772a⟩
International audience; Plant-type ferredoxin-NADP(H) reductases (FNRs) are grouped in two classes, plastidic with an extended FAD conformation and high catalytic rates and bacterial with a folded flavin nucleotide and low turnover rates. The 112-123
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bdfc6d69dd75582a2dcaa56eaa12a73
https://hal-riip.archives-ouvertes.fr/pasteur-00685048
https://hal-riip.archives-ouvertes.fr/pasteur-00685048
Autor:
Debeurme, Franck, Picciocchi, Antoine, Dagher, Marie-Claire, Grunwald, Didier, Beaumel, Sylvain, Fieschi, Franck, Stasia, Marie José
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285 (43), pp.33197-208. ⟨10.1074/jbc.M110.151555⟩
Journal of Biological Chemistry, 2010, 285 (43), pp.33197-208. ⟨10.1074/jbc.M110.151555⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285 (43), pp.33197-208. ⟨10.1074/jbc.M110.151555⟩
Journal of Biological Chemistry, 2010, 285 (43), pp.33197-208. ⟨10.1074/jbc.M110.151555⟩
International audience; The X(+)-linked chronic granulomatous disease (X(+)-CGD) variants are natural mutants characterized by defective NADPH oxidase activity but with normal Nox2 expression. According to the three-dimensional model of the cytosolic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::4405f610346c1207df375f3bb14d4117
https://www.hal.inserm.fr/inserm-00763398/document
https://www.hal.inserm.fr/inserm-00763398/document
Autor:
Pierre Briozzo, David Kopečný, Marek Šebela, Lukáš Spíchal, Michel Laloue, Pavel Anzenbacher, Vlastimil Mašek, Nicole Houba-Hérin, Nathalie Joly, Catherine Madzak
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2008, 380 (5), pp.886-99. ⟨10.1016/j.jmb.2008.05.044⟩
Journal of Molecular Biology, Elsevier, 2008, 380 (5), pp.886-99. ⟨10.1016/j.jmb.2008.05.044⟩
International audience; Cytokinin oxidases/dehydrogenases (CKOs) mediate catabolic regulation of cytokinin levels in plants. Several substrate analogs containing an unsaturated side chain were studied for their possible inhibitory effect on maize CKO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28b079c1814b1f15050659443e977376
https://hal.archives-ouvertes.fr/hal-00315536
https://hal.archives-ouvertes.fr/hal-00315536