Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Ekaterini, Karena"'
Autor:
Haralabia Boleti, Anargyros Doukas, Stathis Frillingos, Amalia Papadaki, Olympia Tziouvara, Evaggelia Xingi, Ekaterini Karena, Konstantinos Papakostas, Maria Botou
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1861:1546-1557
Recombinant expression systems for mammalian membrane transport proteins are often limited by insufficient yields to support structural studies, inadequate post-translational processing and problems related with improper membrane targeting or cytotox
Publikováno v:
Molecular Microbiology. 98:502-517
The xanthine permease XanQ of Escherichia coli is a paradigm for transporters of the evolutionarily broad family nucleobase-cation symporter-2 (NCS2) that transport key metabolites or anti-metabolite analogs. Most functionally known members are xanth
Publikováno v:
Journal of Biological Chemistry. 285:19422-19433
The nucleobase-ascorbate transporter (NAT) signature motif is a conserved 11-amino acid sequence of the ubiquitous NAT/NCS2 family, essential for function and selectivity of both a bacterial (YgfO) and a fungal (UapA) purine-transporting homolog. We
Autor:
Stathis Frillingos, Ekaterini Karena
Publikováno v:
Journal of Biological Chemistry. 284:24257-24268
Using the YgfO xanthine permease of Escherichia coli as a bacterial model for the study of the evolutionarily ubiquitous nucleobase-ascorbate transporter (NAT/NCS2) family, we performed a systematic Cys-scanning and site-directed mutagenesis of 14 pu
Autor:
Ekaterini, Karena, Ekaterini, Tatsaki, George, Lambrinidis, Emmanuel, Mikros, Stathis, Frillingos
Publikováno v:
Molecular microbiology. 98(3)
The xanthine permease XanQ of Escherichia coli is a paradigm for transporters of the evolutionarily broad family nucleobase-cation symporter-2 (NCS2) that transport key metabolites or anti-metabolite analogs. Most functionally known members are xanth
Autor:
Stathis Frillingos, Ekaterini Karena
The xanthine permease XanQ of Escherichia coli is used as a study prototype for function-structure analysis of the ubiquitous nucleobase-ascorbate transporter (NAT/NCS2) family. Our previous mutagenesis study of polar residues of XanQ has shown that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::519cbcee8dbfe62e9d84b58a0c75bc9d
http://olympias.lib.uoi.gr/jspui/handle/123456789/22654
http://olympias.lib.uoi.gr/jspui/handle/123456789/22654
Publikováno v:
The Journal of biological chemistry. 285(25)
The nucleobase-ascorbate transporter (NAT) signature motif is a conserved 11-amino acid sequence of the ubiquitous NAT/NCS2 family, essential for function and selectivity of both a bacterial (YgfO) and a fungal (UapA) purine-transporting homolog. We
Autor:
Ekaterini, Karena, Stathis, Frillingos
Publikováno v:
The Journal of biological chemistry. 284(36)
Using the YgfO xanthine permease of Escherichia coli as a bacterial model for the study of the evolutionarily ubiquitous nucleobase-ascorbate transporter (NAT/NCS2) family, we performed a systematic Cys-scanning and site-directed mutagenesis of 14 pu