Výsledky vyhledávání - "Rosa Montone"

The ILE56 mutation on different genetic backgrounds of alanine:glyoxylate aminotransferase: Clinical features and biochemical characterization

Autor: Rosa Montone, Giorgia Mandrile, Carolina Conter, Barbara Cellini, Alessandra Pelle, Mirco Dindo, Claudio Costantini, Daniela Giachino

Publikováno v: Molecular Genetics and Metabolism. 131:171-180

Primary Hyperoxaluria type I (PH1) is a rare disease caused by mutations in the AGXT gene encoding alanine:glyoxylate aminotransferase (AGT), a liver enzyme involved in the detoxification of glyoxylate, the failure of which results in accumulation of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0450ffce4b0f922410e6fce7259e6f2
https://doi.org/10.1016/j.ymgme.2020.07.012

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Correlation between the molecular effects of mutations at the dimer interface of alanineâglyoxylate aminotransferase leading to primary hyperoxaluria type I and the cellular response to vitamin B6

Autor: Elisa Oppici, Daniele Dell'Orco, Rosa Montone, Barbara Cellini, Mirco Dindo

Primary hyperoxaluria type I (PH1) is a rare disease caused by the deficit of liver alanine–glyoxylate aminotransferase (AGT). AGT prevents oxalate formation by converting peroxisomal glyoxylate to glycine. When the enzyme is deficient, progressive

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa7c0547cfd518757b151296b5dd784c
http://hdl.handle.net/11391/1425812

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Correlation between the molecular effects of mutations at the dimer interface of alanine-glyoxylate aminotransferase leading to primary hyperoxaluria type I and the cellular response to vitamin B

Autor: Mirco, Dindo, Elisa, Oppici, Daniele, Dell'Orco, Rosa, Montone, Barbara, Cellini

Publikováno v: Journal of inherited metabolic disease. 41(2)

Primary hyperoxaluria type I (PH1) is a rare disease caused by the deficit of liver alanine-glyoxylate aminotransferase (AGT). AGT prevents oxalate formation by converting peroxisomal glyoxylate to glycine. When the enzyme is deficient, progressive c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2c34a92aac77acdf60b5878e5e3952f8
https://pubmed.ncbi.nlm.nih.gov/29110180

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Mutant FGFR3 associated with SADDAN disease causes cytoskeleton disorganization through PLCγ1/Src-mediated paxillin hyperphosphorylation

Autor: Rosa Montone, F. Ferrarini, Maria Grazia Romanelli, Elio Liboi, Patricia M.-J. Lievens, A. Baruzzi

Publikováno v: The international journal of biochemistrycell biology. 95

K650M/E substitutions in the Fibroblast growth factor receptor 3 (FGFR3) are associated with Severe Achondroplasia with Developmental Delay and Acanthosis Nigricans (SADDAN) and Thanatophoric Dysplasia type II (TDII), respectively. Both SADDAN and TD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2b5d5af5b5966a49b6a5e942dddb82e
https://pubmed.ncbi.nlm.nih.gov/29242050

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