List of core publications
M. Botou, V. Yalelis, P. Lazou, I. Zantza, K. Papakostas, V. Charalambous, E. Mikros, E. Flemetakis, and S. Frillingos, Specificity profile of NAT/NCS2 purine transporters in Sinorhizobium (Ensifer) meliloti, Mol. Microbiol. (2020) in press.
https://www.ncbi.nlm.nih.gov/pubmed/32198949
F. Komaitis, K. Kalliampakou, M. Botou, M. Nikolaidis, C. Kalloniati, D. Skliros, B. Du, H. Rennenberg, G. D. Amoutzias, S. Frillingos, and E. Flemetakis, Molecular and physiological characterization of the MST gene family in Medicago truncatula, J. Exp. Bot. (2020) in press.
https://www.ncbi.nlm.nih.gov/pubmed/32016431
A. Doukas, E. Karena, M. Botou, K. Papakostas, A. Papadaki, O. Tziouvara, E. Xingi, S. Frillingos, and H. Boleti, Heterologous expressioin of the mammalian sodium-nucleobase transporter rSNBT1 in Leishmania tarentolae, BBA Biomembranes 186, 1546-1557 (2019).
https://www.ncbi.nlm.nih.gov/pubmed/31283918
A. Chaliotis, P. Vlastaridis, C. Ntountoumi, M. Botou, V. Yalelis, P. Lazou, E. Tatsaki, D. Mossialos, S. Frillingos, and G. Amoutzias, NAT/NCS2-hound: A webserver for the detection and evolutionary classification of prokaryotic and eukaryotic nucleobase-cation symporters of the NAT/NCS2 family, GigaScience 7, giy133 (2018) https://www.ncbi.nlm.nih.gov/pubmed/30418564
M. Botou, P. Lazou, K. Papakostas, G. Lambrinidis, T. Evangelidis, E. Mikros, and S. Frillingos, Insight on specificity of uracil permeases of the NAT/NCS2 family from analysis of the transporter encoded in the pyrimidine utilization operon of Escherichia coli. Mol. Microbiol. 108, 204-219 (2018)
http://www.ncbi.nlm.nih.gov/pubmed/29437264
E. Karena, E. Tatsaki, G. Lambrinidis, E. Mikros, and S. Frillingos, Analysis of conserved NCS2 motifs in the Escherichia coli xanthine permease XanQ, Mol. Microbiol. 98, 502-517 (2015) http://www.ncbi.nlm.nih.gov/pubmed/26192456
K. Papakostas, M. Botou, and S. Frillingos, Functional identification of the hypoxanthine/guanine transporters YjcD and YgfQ and the adenine transporters PurP and YicO of Escherichia coli K-12, J. Biol. Chem. 288, 36827-36840 (2013).
http://www.ncbi.nlm.nih.gov/pubmed/24214977
S. Frillingos, Insights to the evolution of Nucleobase-Ascorbate Transporters (NAT/NCS2 family) from the Cys-scanning analysis of xanthine permease XanQ. Int J Biochem Mol Biol. 3, 250-272 (2012). http://www.ncbi.nlm.nih.gov/pubmed/23097742
K. Papakostas and S. Frillingos, Substrate selectivity of YgfU, a uric acid transporter from Escherichia coli, J. Biol. Chem. 287, 15684-15695 (2012).
http://www.ncbi.nlm.nih.gov/pubmed/22437829
E. Karena and S. Frillingos, The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli, J. Biol. Chem. 286, 39595-39605 (2011).
http://www.ncbi.nlm.nih.gov/pubmed/21917919
G. Mermelekas, E. Georgopoulou, A. Kallis, M. Botou, V. Vlantos, and S. Frillingos, «Cysteine-scanning analysis of helices TM8, TM9a, TM9b and intervening loops in the YgfO xanthine permease: a carboxyl group is essential at position Asp-276», J. Biol. Chem. 285, 35011-35020 (2010).
http://www.ncbi.nlm.nih.gov/pubmed/20802252
E. Georgopoulou, G. Mermelekas, E. Karena, and S. Frillingos, «Purine substrate recognition by the nucleobase-ascorbate transporter motif in the YgfO xanthine permease: Asn-325 binds and Ala-323 senses substrate», J. Biol. Chem. 285, 19422-19433 (2010).
http://www.ncbi.nlm.nih.gov/pubmed/20406814
E. Karena, and S. Frillingos, «Role of intramembrane polar residues in the YgfO xanthine permease: His-31 and Asn-93 are crucial for affinity and specificity, and Asp-304 and Glu-272 are irreplaceable», J. Biol. Chem. 284, 24257-24268 (2009).
http://www.ncbi.nlm.nih.gov/pubmed/19581302
N. Lemuh, G. Diallinas, S. Frillingos, G. Mermelekas, A. D. Karagouni, and D. G. Hatzinikolaou, «Purification and partial characterization of the xanthine – uric acid transporter (UapA) of Aspergillus nidulans», Prot. Expr. Purif. 63, 33-39 (2009).
http://www.ncbi.nlm.nih.gov/pubmed/18824106
K. Papakostas, E. Georgopoulou, and S. Frillingos, «Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: Ile-432 and Asn-430 are important», J. Biol. Chem. 283, 13666-13678 (2008).
http://www.ncbi.nlm.nih.gov/pubmed/18359771
S. Tavoulari, and S. Frillingos, «Substrate selectivity of the melibiose permease (MelY) from Enterobacter cloacae», J. Mol. Biol. 376, 681-693 (2008).
http://www.ncbi.nlm.nih.gov/pubmed/18177889
A. Kallimanis, S. Frillingos, C. Drainas, and A. Koukkou, «Taxonomic
identification, phenanthrene uptake activity and membrane lipid alterations of the PAH degrading Arthrobacter sp. strain Sphe3», Appl. Microbiol. Biotechnol. 76, 709- 717(2007).
http://www.ncbi.nlm.nih.gov/pubmed/17583808
P. Kafasla, D. Bouzarelou, S. Frillingos, and V. Sophianopoulou, «The proline permease of Aspergillus nidulans: functional replacement of the cysteine residues and properties of a cysteine-less transporter», Fung. Genet. Biol. 44, 615-626 (2007).
http://www.ncbi.nlm.nih.gov/pubmed/17350864
H. R. Kaback, R. Dunten, S. Frillingos, P. Venkatesan, I. Kwaw, W. Zhang, and N. Ermolova, «Site-directed alkylation and the alternating access model for LacY», Proc. Natl. Acad. Sci. USA 104,491-494 (2007).
http://www.ncbi.nlm.nih.gov/pubmed/17172438
P. Karatza, P. Panos, E. Georgopoulou, and S. Frillingos, «Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential and Ile-329–Val-339 form an alpha-helix». J. Biol. Chem. 281, 39881-39890 (2006).
http://www.ncbi.nlm.nih.gov/pubmed/17077086
S. Goudela, P. Karatza, M. Koukaki, S. Frillingos, and G. Diallinas, «Comparative substrate recognition by bacterial and fungal purine transporters of the NAT/NCS2 family», Mol. Membr. Biol. 22, 263-275 (2005).
http://www.ncbi.nlm.nih.gov/pubmed/16096268
P. Karatza, and S. Frillingos, «Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli», Mol. Membr. Biol. 22, 251-261 (2005).
http://www.ncbi.nlm.nih.gov/pubmed/16096268
S. Tavoulari, S. Frillingos, P. Karatza, I. Messinis, and K. Seferiadis, «The recombinant subdomain IIIB of human serum albumin displays activity of gonadotrophin surge attenuating factor», Human Reproduction 19, 849-858 (2004).
http://www.ncbi.nlm.nih.gov/pubmed/15016777
M. Sahin-Tόth, S. Frillingos, M. C. Lawrence, and H. R. Kaback, «The sucrose permease of Escherichia coli: Functional significance of the Cys residues and properties of a Cys-less transporter», Biochemistry 39, 6164-6169 (2000).
http://www.ncbi.nlm.nih.gov/pubmed/10821690
S. Frillingos, A. Linden, F. Niehaus, C. Vargas, J. J. Nieto, A. Ventosa, G. Antranikian, and C. Drainas, «Cloning and expression of α-amylase from the hyperthermophilic archaeon Pyrococcus woesei in the moderately halophilic bacterium Halomonas elongata», J. Appl. Microbiol. 88, 495-503 (2000).
http://www.ncbi.nlm.nih.gov/pubmed/10747230
E. Douka, A. I. Koukkou, G. Vartholomatos, S. Frillingos, E. M. Papamichael, and C. Drainas, «A Zymomonas mobilis mutant with delayed growth on high glucose concentrations», J. Bacteriology 181, 4598-4604 (1999).
http://www.ncbi.nlm.nih.gov/pubmed/10419959
S. Frillingos, M. Sahin-Tόth, J. Wu, and H. R. Kaback, «Cys-scanning mutagenesis: a novel approach to structure-function relationships in membrane proteins», FASEB J. 12, 1281-1299 (1998).
http://www.ncbi.nlm.nih.gov/pubmed/9761772
S. Frillingos, A. Gonzalez, and H. R. Kaback, «Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli», Biochemistry 36, 14284-14290 (1997).
http://www.ncbi.nlm.nih.gov/pubmed/9400367
S. Frillingos, J. Wu, P. Venkatesan, and H. R. Kaback, «Binding of ligand or monoclonal antibody 4B1 induces discrete structural changes in the lactose permease of Escherichia coli», Biochemistry 36, 6408-6414 (1997).
http://www.ncbi.nlm.nih.gov/pubmed/9174357
J. Sun, S. Frillingos, and H. R. Kaback, «Binding of monoclonal antibody 4B1 to homologs of the lactose permease of Escherichia coli», Protein Science 6, 1503-1510 (1997).
http://www.ncbi.nlm.nih.gov/pubmed/9232651
S. Frillingos, and H. R. Kaback, «The role of helix VIII in the lactose permease of Escherichia coli: II. Site-directed sulfhydryl modification», Protein Science 6, 438-443 (1997).
http://www.ncbi.nlm.nih.gov/pubmed/9041647
S. Frillingos, M. L. Ujwal, J. Sun, and H. R. Kaback, «The role of helix VIII in the lactose permease of Escherichia coli: I. Cysteine-scanning mutagenesis», Protein Science 6, 431-437 (1997).
http://www.ncbi.nlm.nih.gov/pubmed/9041646
S. Frillingos, J. Sun, A. Gonzalez, and H. R. Kaback, «Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coli», Biochemistry 36, 269-273 (1997).
http://www.ncbi.nlm.nih.gov/pubmed/8993343
S. Frillingos, and H. R. Kaback, «Chemical rescue of mutants Asp237>Ala and Lys358>Ala in the lactose permease of Escherichia coli», Biochemistry 35, 13363-13367 (1996).
http://www.ncbi.nlm.nih.gov/pubmed/8873603
S. Frillingos, and H. R. Kaback, «Monoclonal antibody 4B1 alters the pKa of a carboxylic acid at position 325 (helix X) of the lactose permease of Escherichia coli», Biochemistry 35, 10166-10171 (1996).
http://www.ncbi.nlm.nih.gov/pubmed/8756481
S. Frillingos, and H. R. Kaback, «Cysteine-scanning mutagenesis of helix VI and the flanking hydrophilic domains in the lactose permease of Escherichia coli», Biochemistry 35, 5333-5338 (1996).
http://www.ncbi.nlm.nih.gov/pubmed/8611521
S. Frillingos, and H. R. Kaback, «Probing the conformation of the lactose permease of Escherichia coli by in situ site-directed sulfhydryl modification», Biochemistry 35, 3950-3956 (1996).
http://www.ncbi.nlm.nih.gov/pubmed/8672426
S. Frillingos, M. Sahin-Tόth, J. W. Lengeler, and H. R. Kaback, «Helix packing in the sucrose permease of Escherichia coli: properties of engineered charge pairs between Asn324 (helix VII) and Ser356 (helix XI)», Biochemistry 34, 9368-9373 (1995).
http://www.ncbi.nlm.nih.gov/pubmed/7626606
M. Sahin-Tόth, S. Frillingos, J. W. Lengeler, and H. R. Kaback, «Active transport by the CscB permease in Escherichia coli K12», Biochem. Biophys. Research Commun. 208, 1116-1123 (1995).
http://www.ncbi.nlm.nih.gov/pubmed/7535526
J. Wu, S. Frillingos, and H. R. Kaback, «Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spectroscopy», Biochemistry 34, 8257-8263 (1995).
http://www.ncbi.nlm.nih.gov/pubmed/7599118
J. Wu, S. Frillingos, J. Voss, and H. R. Kaback, «Ligand-induced conformational changes in the lactose permease of Escherichia coli», Protein Science 3, 2294-2301 (1994).
http://www.ncbi.nlm.nih.gov/pubmed/7756985
M. Sahin-Tόth, S. Frillingos, E. Bibi, A. Gonzalez, and H. R. Kaback, «The role of putative transmembrane domain III in the lactose permease of Escherichia coli», Protein Science 3, 2302-2310 (1994).
http://www.ncbi.nlm.nih.gov/pubmed/7756986
H. R. Kaback, S. Frillingos, H. Jung, K. Jung, G. G. Prive, M. L. Ujwal, C. Weitzman, J. Wu, and K. Zen, «The lactose permease meets Frankestein», J. Exp. Biol. 196, 183-195 (1994).
http://www.ncbi.nlm.nih.gov/pubmed/7823021
S. Frillingos, M. Sahin-Tόth, B. Persson, and H. R. Kaback, «Cysteine-scanning mutagenesis of putative helix VII in lactose permease of Escherichia coli», Biochemistry 33, 8074-8081 (1994).
http://www.ncbi.nlm.nih.gov/pubmed/8025113