Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Carla Carluccio"'
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e79482 (2013)
Phenylalanine hydroxylase (PAH) catalyzes the conversion of L-Phe to L-Tyr. Defects in PAH activity, caused by mutations in the human gene, result in the autosomal recessively inherited disease hyperphenylalaninemia. PAH activity is regulated by mult
Externí odkaz:
https://doaj.org/article/f5b9673aa8cc4585b31bf478efdeb060
Autor:
Marina Capuano, Carmen Maria Garcia-Herrero, Nadia Tinto, Carla Carluccio, Valentina Capobianco, Iolanda Coto, Arturo Cola, Dario Iafusco, Adriana Franzese, Adriana Zagari, Maria Angeles Navas, Lucia Sacchetti
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e38906 (2012)
Type 2 Maturity Onset Diabetes of the Young (MODY2) is a monogenic autosomal disease characterized by a primary defect in insulin secretion and hyperglycemia. It results from GCK gene mutations that impair enzyme activity. Between 2006 and 2010, we i
Externí odkaz:
https://doaj.org/article/ec0db7a59f214113893fab0f52e22940
Autor:
Rosanna Culurciello, Mariateresa Trapani, Irene Russo Krauss, Elio Pizzo, Carla Carluccio, Andrea Bosso, Antonello Merlino, Lelio Mazzarella, Filomena Sica, Romualdo Troisi
Publikováno v:
International Journal of Biological Macromolecules. 182:659-668
The superfamily of vertebrate ribonucleases, a large group of evolutionarily related proteins, continues to provide interesting structural and functional information. In particular, the crystal structure of SS-RNase-2 from Salmo salar (SS2), here pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f54f9001ecb1c82b8aa0df840001c0f9
https://doi.org/10.1016/j.ijbiomac.2021.04.041
https://doi.org/10.1016/j.ijbiomac.2021.04.041
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 34:497-507
The enzyme phenylalanine hydroxylase (PAH) is defective in the inherited disorder phenylketonuria. PAH, a tetrameric enzyme, is highly regulated and displays positive cooperativity for its substrate, Phe. Whether Phe binds to an allosteric site is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a61b7007814fb70ce0338258b59a746a
https://doi.org/10.1080/07391102.2015.1052016
https://doi.org/10.1080/07391102.2015.1052016
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e79482 (2013)
PLoS ONE
PLoS ONE
Phenylalanine hydroxylase (PAH) catalyzes the conversion of L-Phe to L-Tyr. Defects in PAH activity, caused by mutations in the human gene, result in the autosomal recessively inherited disease hyperphenylalaninemia. PAH activity is regulated by mult
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5b695f261f7ece282d2f25b294f8053
http://europepmc.org/articles/PMC3828330?pdf=render
http://europepmc.org/articles/PMC3828330?pdf=render
Autor:
Carla Carluccio, Paola Cavaliere, Francesco Salvatore, Monica Cerreto, Aurora Daniele, Felice Amato, Adriana Zagari
Hyperphenylalaninemias are genetic diseases prevalently caused by mutations in the phenylalanine hydroxylase (PAH) gene. The wild-type PAH enzyme is a homotetramer regulated by its substrate, cofactor and phosphorylation. We reproduced a full-length
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab0e9095e8e197263af169ae13663797
http://hdl.handle.net/11588/404283
http://hdl.handle.net/11588/404283
Autor:
Arturo Cola, Carla Carluccio, Iolanda Coto, Marina Capuano, Valentina Capobianco, Nadia Tinto, Adriana Zagari, María Ángeles Navas, Carmen M. García-Herrero, Lucia Sacchetti, Dario Iafusco, Adriana Franzese
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e38906 (2012)
PLoS ONE
PLoS ONE
Type 2 Maturity Onset Diabetes of the Young (MODY2) is a monogenic autosomal disease characterized by a primary defect in insulin secretion and hyperglycemia. It results from GCK gene mutations that impair enzyme activity. Between 2006 and 2010, we i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40e82ba45e339a38f1230ddec5c9b33e
https://doi.org/10.1371/journal.pone.0038906
https://doi.org/10.1371/journal.pone.0038906