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  1. Home
  2. Structure of Macromolecular Assemblies
  3. Publications

Plaza-Pegueroles, A., Aphasizheva, I., Aphasizhev, R., Fernández-Tornero, C.*, Ruiz, F.M.*  [2024]. The cryo-EM structure of trypanosome 3-methylcrotonyl-CoA carboxylase provides mechanistic and dynamic insights into its enzymatic function. Structure 32:930-940.e3.

Nguyen, P.Q., Huecas, S., Asif-Laidin, A., Plaza-Pegueroles, A., Capuzzi, B., Palmic, N., Conesa, C., Acker, J., Reguera, J., Lesage, P.*, Fernández-Tornero, C.*  [2023]. Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration. Nature Commun. 14:1729.

Andreu, J.M.*, Ruiz, F.M., Fernández-Tornero, C.*  [2023]. Conserved GTPase mechanism in bacterial FtsZ and archaeal tubulin filaments. FEBS J. 290:3527-3532.

Rosell-Garcia, T., Rivas-Muñoz, S., Kin, K., Romero-Albillo, V., Alcaraz, S., Fernandez-Tornero, C., Rodriguez-Pascual, F.  [2023]. Multimerization of HIF enhances transcription of target genes containing the hypoxia ancillary sequence. Biochim Biophys Acta Gene Regul Mech. 1866:194963.

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 Biol. 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.

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.

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.

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 Genet. 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.

Fernández-Tornero, C.*  [2018]. RNA polymerase I activation and hibernation: unique mechanisms for unique genes. Transcription. 9:248-254.

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.

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

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

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