Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency

Autor: Olsen, R. K., Konarikova, E., Giancaspero, T. A., Mosegaard, S., Boczonadi, V., Matakovic, L., Veauville-Merllie, A., Terrile, C., Schwarzmayr, T., Haack, T. B., Auranen, M., Leone, P., Galluccio, M., Imbard, A., Gutierrez-Rios, P., Palmfeldt, J., Graf, E., Vianey-Saban, Christine, Oppenheim, M., Schiff, M., Pichard, S., Rigal, O., Pyle, A., Chinnery, P. F., Konstantopoulou, V., Moslinger, D., Feichtinger, R. G., Talim, B., Topaloglu, H., Coskun, T., Gucer, S., Botta, A., Pegoraro, E., Malena, A., Vergani, L., Mazza, D., Zollino, M., Ghezzi, D., Acquaviva, C., Tyni, T., Boneh, A., Meitinger, T., Strom, T. M., Gregersen, N., Mayr, J. A., Horvath, R., Barile, M., Prokisch, H.

Publikováno v: American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2016, 98 (6), pp.1130-45
Am. J. Hum. Genet. 98, 1130-1145 (2016)
Olsen, R K J, Koňaříková, E, Giancaspero, T A, Mosegaard, S, Boczonadi, V, Mataković, L, Veauville-Merllié, A, Terrile, C, Schwarzmayr, T, Haack, T B, Auranen, M, Leone, P, Galluccio, M, Imbard, A, Gutierrez-Rios, P, Palmfeldt, J, Graf, E, Vianey-Saban, C, Oppenheim, M, Schiff, M, Pichard, S, Rigal, O, Pyle, A, Chinnery, P F, Konstantopoulou, V, Möslinger, D, Feichtinger, R G, Talim, B, Topaloglu, H, Coskun, T, Gucer, S, Botta, A, Pegoraro, E, Malena, A, Vergani, L, Mazzà, D, Zollino, M, Ghezzi, D, Acquaviva, C, Tyni, T, Boneh, A, Meitinger, T, Strom, T M, Gregersen, N, Mayr, J A, Horvath, R, Barile, M & Prokisch, H 2016, ' Riboflavin-Responsive and-Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency ', American Journal of Human Genetics, vol. 98, no. 6, pp. 1130-45 . https://doi.org/10.1016/j.ajhg.2016.04.006

International audience; Multiple acyl-CoA dehydrogenase deficiencies (MADDs) are a heterogeneous group of metabolic disorders with combined respiratory-chain deficiency and a neuromuscular phenotype. Despite recent advances in understanding the genet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0cbd7b225ccfd8f625782ca638779b5b
https://hal.archives-ouvertes.fr/hal-01850412

Biosynthesis of flavin cofactors in man: implications in health and disease

Autor: Barile M., Giancaspero T. A., Brizio C., Panebianco C., Indiveri C. Galluccio M., Vergani L., Eberini I., Gianazza E.

Publikováno v: Current pharmaceutical design
19 (2013): 2649.
info:cnr-pdr/source/autori:Barile M., Giancaspero T. A., Brizio C., Panebianco C., Indiveri C. Galluccio M., Vergani L., Eberini I., Gianazza E./titolo:Biosynthesis of flavin cofactors in man: implications in health and disease./doi:/rivista:Current pharmaceutical design (Print)/anno:2013/pagina_da:2649/pagina_a:/intervallo_pagine:2649/volume:19

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::cb6a705b7e6f1d08465070bb1117c2ea
https://publications.cnr.it/doc/271753

Succinate dehydrogenase flavoprotein subunit expression in Saccharomyces cerevisiae--involvement of the mitochondrial FAD transporter, Flx1p

Autor: Giancaspero, T, Wait, R, Boles, E, Barile, M

Publikováno v: The FEBS journal. 275(6)

The mitochondrial FAD transporter, Flx1p, is a member of the mitochondrial carrier family responsible for FAD transport in Saccharomyces cerevisiae. It has also been suggested that it has a role in maintaining the normal activity of mitochondrial FAD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::45d4b4cd750abad049b840fd817d8547
http://ora.ox.ac.uk/objects/uuid:ca1c8c44-b963-4f98-9525-4094c8a4489e

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Significance of redox-active cysteines in human FAD synthase isoform 2

Autor: Teresa Anna Giancaspero, Angelica Miccolis, Maria Barile, Michele Galluccio, Francesco Bonomi, Pasquale Ferranti, Chiara Nitride, Stefania Iametti, Cesare Indiveri

Publikováno v: Biochimica et biophysica acta. 1844(12)

FAD synthase (FMN:ATP adenylyl transferase, FMNAT or FADS, EC 2.7.7.2) is the last enzyme in the pathway converting riboflavin into FAD. In humans, FADS is localized in different subcellular compartments and exists in different isoforms. Isoform 2 (4

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7afcc1ace94c59bdea29d6718d26e53a
https://pubmed.ncbi.nlm.nih.gov/25135855