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Ruiz, F.M, Huecas, S., Santos-Aledo, A., Prim, E.A., Andreu, J.M., Fernández-Tornero, C.
[2022]. FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics. PLoS Biology 20:e3001497
Nguyen, P.Q., Conesa, C., Rabut, E., Bragagnolo, G., Gouzerh, C., Fernández-Tornero, C., Lesage, P., Reguera, J., Acker, J.
[2021]. Ty1 integrase is composed of an active N-terminal domain and a large disordered C-terminal module dispensable for its activity in vitro. J. Biol. Chem. 297:101093
Huecas, S., Araújo-Bazán, L., Ruiz, F.M., Ruiz-Ávila, L.B., Martínez, R.F., Escobar-Peña, A., Artola, M., Vázquez-Villa, H., Martín-Fontecha, M., Fernández-Tornero, C.*, López-Rodríguez, M.L.*, Andreu, J.M.*
[2021]. Targeting the FtsZ Allosteric Binding Site with a Novel Fluorescence Polarization Screen, Cytological and Structural Approaches for Antibacterial Discovery. J. Med. Chem. 64:5730–5745.
Huecas, S., Canosa-Valls, A.J., Araújo-Bazán, L., Ruiz, F.M., Laurents, D.V., Fernández-Tornero, C.*, Andreu, J.M.*
[2020]. Nucleotide-induced folding of cell division protein FtsZ from Staphylococcus aureus. FEBS J. 287:4048-4067.
González-Corrochano, R., Ruiz, F.M., Taylor, N.M.I., Huecas, S., Drakulic, S., Spínola-Amilibia, M., Fernández-Tornero, C.
[2020]. The crystal structure of human XPG, the xeroderma pigmentosum group G endonuclease, provides insight into nucleotide excision DNA repair. Nucleic Acids Res. 48:9943-9958.
Darrière, T., Pilsl, M., Sarthou, M.-K., Chauvier, A., Genty, T., Audibert, S., Dez, C., Léger-Silvestre, I., Normand, C., Henras, A.K., Kwapisz, M., Calvo, O., Fernandez-Tornero, C., Tschochner, H., Gadal, O.
[2019]. Genetic analyses led to the discovery of a super-active mutant of the RNA polymerase I. PLoS Genetics. 15:e1008157.
Sanz-Murillo, M., Xu, J., Belogurov, G.A., Calvo, O., Gil-Carton, D., Moreno-Morcillo, M., Wang, D., Fernández-Tornero, C.
[2018]. Structural basis of RNA polymerase I stalling at UV light-induced DNA damage. Proc. Nat. Acad. Sci. USA. 115:8972-8977.
Torreira, E., Louro, J.A., Pazos, I., González-Polo, N., Gil-Carton, D., Duran, A.G., Tosi, S., Gallego, O., Calvo, O., Fernández-Tornero, C.
[2017]. The dynamic assembly of distinct RNA polymerase i complexes modulates rDNA transcription. eLife. 6:e20832
Canales, Á., Rösinger, M., Sastre, J., Felli, I.C., Jiménez-Barbero, J., Giménez-Gallego, G., Fernández-Tornero, C.
[2017]. Hidden α-helical propensity segments within disordered regions of the transcriptional activator CHOP. PLoS ONE. 12:e0189171.
Garavís, M., González-Polo, N., Allepuz-Fuster, P., Louro, J.A., Fernández-Tornero, C., Calvo, O.
[2017]. Sub1 contacts the RNA polymerase II stalk to modulate mRNA synthesis. Nucleic Acids Res. 45:2458-2471.
Moreno-Morcillo, M., Taylor, N.M., Gruene, T., Legrand, P., Rashid, U.J., Ruiz, F.M., Steuerwald, U., Müller, C.W., Fernández-Tornero C.
[2014]. Solving the RNA polymerase I structural puzzle. Acta Cryst. D70:2570-2582
Basu, R.S., Warner, B.A., Molodtsov, V., Pupov, D., Esyunina, D., Fernández-Tornero, C., Kulbachinskiy, A., Murakami K.S.
[2014]. Structural basis of transcription initiation by bacterial RNA polymerase holoenzyme. J. Biol. Chem. 289:24549-24559
Torreira, E., Seabra, A.R., Marriott, H., Zhou, M., Llorca, O., Robinson, C.V., Carvalho, H.G., Fernández-Tornero, C.*, Pereira, P.J.*
[2014]. The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture. Acta Cryst. D70:981-993
Fernández-Tornero, C.*, Moreno-Morcillo, M., Rashid, U.J., Taylor, N.M., Ruiz, F.M., Gruene, T., Legrand, P., Steuerwald, U., Müller, C.W.*
[2013]. Crystal structure of the 14-subunit RNA polymerase I. Nature 502:644-649
Taylor, N.M., Glatt, S., Hennrich, M.L., von Scheven, G., Grötsch, H., Fernández-Tornero, C., Rybin, V., Gavin, A.C., Kolb, P., Müller, C.W.
[2013]. Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. J. Biol. Chem. 288:15110-15120
Lane, L.A., Fernández-Tornero, C., Zhou, M., Morgner, N., Ptchelkine, D., Steuerwald, U., Politis, A., Lindner, D., Gvozdenovic, J., Gavin, A.C., Müller, C.W., Robinson, C.V.
[2011]. Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III. Structure 19:90-100
Gallego, O., Betts, M.J., Gvozdenovic-Jeremic, J., Maeda, K., Matetzki, C., Aguilar-Gurrieri, C., Beltran-Alvarez, P., Bonn, S., Fernández-Tornero, C., Jensen, L.J., Kuhn, M., Trott, J., Rybin, V., Müller, C.W., Bork, P., Kaksonen, M., Russell, R.B., Gavin, A.C.
[2010]. A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol. Syst. Biol. 6:430
Fernández-Tornero C, Böttcher B, Rashid UJ, Steuerwald U, Flörchinger B, Devos DP, Lindner D, Müller CW
[2010]. Conformational flexibility of RNA polymerase III during transcriptional elongation. EMBO J. 29:3762-3772
