Zobrazeno 1 - 4
of 4
pro vyhledávání: '"MESH: Protoporphyrins"'
Autor:
Bo Lönnerdal, Michael Ristow, Alan R. Buckpitt, Robert Schoenfeld, Alice Wong, Hélène Puccio, Eleonora Napoli, Shan Zhan, Franco Taroni, Laurence Reutenauer, Dexter Morin, Gino A Cortopassi
Publikováno v:
Human Molecular Genetics
Human Molecular Genetics, Oxford University Press (OUP), 2005, 14 (24), pp.3787-99. ⟨10.1093/hmg/ddi393⟩
Human Molecular Genetics, Oxford University Press (OUP), 2005, 14 (24), pp.3787-99. ⟨10.1093/hmg/ddi393⟩
International audience; Deficiency of the frataxin mRNA alters the transcriptome, triggering neuro- and cardiodegeneration in Friedreich's ataxia. We microarrayed murine frataxin-deficient heart tissue, liver tissue and cardiocytes and observed a tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::423543045f02c60929eda695ff8bc85a
https://doi.org/10.1093/hmg/ddi393
https://doi.org/10.1093/hmg/ddi393
Publikováno v:
Microbiology
Microbiology, 2008, 154 (Pt 12), pp.3707-14. ⟨10.1099/mic.0.2008/018705-0⟩
Microbiology, 2008, 154 (Pt 12), pp.3707-14. ⟨10.1099/mic.0.2008/018705-0⟩
International audience; During haem and chlorophyll biosynthesis, flavin-dependent protoporphyrinogen IX oxidase catalyses the six-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. In the following step, iron is inserted into pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9681678baa5495b139cf221163ca7971
https://pubmed.ncbi.nlm.nih.gov/19047738
https://pubmed.ncbi.nlm.nih.gov/19047738
Publikováno v:
Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Proteins-Structure, Function and Bioinformatics, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Proteins-Structure, Function and Bioinformatics, Wiley, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Proteins-Structure, Function and Bioinformatics, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Heme catalases are homotetrameric enzymes with a highly conserved complex quaternary structure, and their functional role is still not well understood. Proteus mirabilis catalase (PMC), a heme enzyme belonging to the family of NADPH-binding catalases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b60851ca3a8e31e3be81587cc64470c
https://hal.archives-ouvertes.fr/hal-00173312
https://hal.archives-ouvertes.fr/hal-00173312
Autor:
Deniau, Clarisse, Couprie, Joël, Simenel, Catherine, Kumar, Vera, Stojiljkovic, Igor, Wandersman, Cécile, Delepierre, Muriel, Lecroisey, Anne
Publikováno v:
Journal of Biomolecular NMR
Journal of Biomolecular NMR, 2001, 21 (2), pp.189-90. ⟨10.1023/A%3A1012426928104⟩
Journal of Biomolecular NMR, Springer Verlag, 2001, 21 (2), pp.189-90. ⟨10.1023/A%3A1012426928104⟩
Journal of Biomolecular NMR, 2001, 21 (2), pp.189-90. ⟨10.1023/A%3A1012426928104⟩
Journal of Biomolecular NMR, Springer Verlag, 2001, 21 (2), pp.189-90. ⟨10.1023/A%3A1012426928104⟩
International audience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::4333e3b87ef34cd5f573b1ad7930b7e0
https://hal-pasteur.archives-ouvertes.fr/pasteur-00370325
https://hal-pasteur.archives-ouvertes.fr/pasteur-00370325