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DOI: 10.1016/j.dci.2016.12.001
Impact factor: 3.393, Quartile (WoS): Q2
[50] Looking for inhibitors of the Dengue virus NS5 RNA-dependent RNA-polymerase using a molecular docking approach. Galiano-Ibarra, V., Garcia-Valtanen, P., Micol, V., Encinar, J.A. 2016. Drug Design, Development and Therapy, 10: 3163-3181.
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PUBMED: 27784988
DOI: 10.2147/DDDT.S117369
Supplemental Material: http://docking.umh.es/
[49] In silico approach for the discovery of new PPAR-gamma modulators among plant-derived polyphenols. Encinar, J.A., Fernández-Ballester, G., Galiano-Ibarra, V., and Micol, V. 2015. Drug Design, Development and Therapy. 9: 5877-5895.
SCOPUS: 2-s2.0-84946595271
PUBMED: 26604687
DOI: 10.2147/DDDT.S93449
Supplementary Material: 1, http://goo.gl/Vn8zBU),
Supplemental Material 2 (http://goo.gl/OJEgfV),
Supplemental Material 3 (http://goo.gl/KGVJb4).
[48] Competing Lipid-Protein and Protein-Protein Interactions Determine Clustering and Gating Patterns in KcsA. Molina, M.L., Giudici, A.M., Poveda, J.A., Fernández-Ballester, G., Montoya, E., Renart, M.L., Fernández, A.M., Encinar, J.A., Riquelme, G., Morales, A., & González-Ros, J.M. 2015. Journal of Biological Chemistry 290(42): 25745-25755.
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PUBMED: 26336105
DOI: 10.1074/jbc.M115.669598
[47] Nucleotide binding triggers a conformational change of the CBS module of the magnesium transporter CNNM2 from a twisted towards a flat structure. Corral-Rodríguez, M.A., Stuiver, M., Abascal-Palacios, G., Diercks, T., Oyenarte, I., Ereño-Orbea, J., Ibáñez De Opakua, A., Blanco, F.J., Encinar, J.A., Spiwok, V., Terashima, H., Accardi, A., Müller, D., Martinez-Cruz LA. 2014. Biochemical Journal 464: 23-34.
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PUBMED: 25184538
DOI: 10.1042/BJ20140409
[46] Hepatitis C virus polymerase-polymerase contact interface: Significance for virus replication and antiviral design. López-Jiménez, A.J., Clemente-Casaresa, P., Sabariegosa, R., Llanos-Valero, M., Bellón-Echeverría, I., Encinar, J.A., Kaushik-Basue, N., Froeyen, M. and Mas, A. 2014. Antiviral Research 108: 14-24.
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PUBMED: 24815023
DOI: 10.1016/j.antiviral.2014.04.009
[45] Lipid modulation of ion channels through specific binding sites. Poveda JA, Giudici A.M., Renart L., Molina M.L, Montoya E., Fernández A.M., Fernández-Ballester G., Encinar, J.A., González-Ros J.M. 2014. Biochim Biophys Acta. 1838(6): 1560-1567.
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DOI: 10.1016/j.bbamem.2013.10.023
[44] pH-dependent solution structure and activity of the host-defense peptide myticin C (Myt C) from the mussel Mytilus galloprovincialis. Martinez-López, A., Encinar, J.A., Medina-Gali, R.M., Balseiro, P., García-Valtanen, P., Figueras, A., Novoa, B. and Estepa A. 2013. Marine Drugs, 11(7): 2328-2346.
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PUBMED: 23880927
DOI: 10.3390/md11072328
[43] Partitioning of Liquid-ordered / Liquid-disordered Membrane Microdomains Induced by the Fluidifying Effect of 2-Hydroxylated Fatty Acid Derivatives. Maitane Ibarguren, David J. López, José A. Encinar, José M. González-Ros, Xavier Busquets and Pablo V. Escribá. 2013. Biochimica et Biophysica Acta, 1828 (2013): 2553-2563.
SCOPUS: 2-s2.0-84882634594
PUBMED: 23792066
DOI: 10.1016/j.bbamem.2013.06.014
[42] Detergent-labile, supramolecular assemblies of KcsA: Relative abundance and interactions involved. A. Marcela Giudici, M. Luisa Molina, Jose L. Ayala, Estefanía Montoya, M. Lourdes Renart, Asia M. Fernández, José A. Encinar, Antonio V. Ferrer-Montiel, José A. Poveda, José M. González-Ros. 2013. Biochimica et Biophysica Acta - Biomembranes, 1828(2): 193-200.
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PUBMED: 23022492
DOI: 10.1016/j.bbamem.2012.09.020
[41] Contribution of ion binding affinity to ion selectivity and permeation in KcsA, a model potassium channel. Renart, M.L., Montoya, E., Fernández, A.M., Molina, M.L., Poveda, J.A., Encinar, J.A., Ayala, J.L., Ferrer-Montiel, A.V., Gómez, J., Morales, A. and González-Ros, J.M. 2012. Biochemistry, 51: 3891-3900.
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DOI: 10.1021/bi201497n
[40] Mutation of Ser-50 and Cys-66 in Snapin Modulate Protein Structure and Stability. Navarro, A., Encinar, J.A., López, B., Aguado-Llera, D., Prieto, J., Gómez, J., Martínez-Cruz, L.A., Millet, O., González-Ros, J.M., Fernández-Ballester, G., Neira, J.L., and Ferrer-Montiel, A. 2012. Biochemistry, 51: 3470-3484.
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PUBMED: 22471585
DOI: 10.1021/bi201574t
[39] De novo polymerase activity and oligomerization of Hepatitis C Virus RNA-dependent RNApolymerases from genotypes 1 to 5. Clemente-Casares, P., López-Jiménez, A.J., Bellón-Echeverría, I., Encinar, J.A., Martínez-Alfaro, E., Pérez-Flores, R., & Mas, A. 2011. PLoS ONE 6(4): e18515.
SCOPUS: 2-s2.0-79954506008
PUBMED: 21490973
DOI: 10.1371/journal.pone.0018515
[38] Nucleotide-induced conformational transitions in the CBS domain protein MJ0729 of Methanocaldococcus jannaschii. Martínez-Cruz, L.A., Encinar, J.A., Sevilla-Sierra, P., Oyenarte, I., Gómez-García, I., Aguado-Llera, D., García-Blanco, F., Gómez, J. and Neira, J.L. 2011. Protein Engineering, Design and Selection 24(1-2): 161-169.
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PUBMED: 20959390
DOI: 10.1093/protein/gzq073
[37] Ion binding to KcsA: implications in ion selectivity and channel gating. Renart, M.L., Triano, I., Poveda, J.A., Encinar, J.A., Fernandez, A.M., Ferrer-Montiel, A.V., Gomez, J., González-Ros J.M. 2010. Biochemistry. 49(44): 9480-9487.
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PUBMED: 20925387
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[36] Occupancy of non-annular lipid binding sites on KcsA greatly increases the stability of the tetrameric protein. Triano, I., Barrera, F.N., Renart, M.L., Molina, M.L., Fernandez-Ballester, G., Poveda, J.A., Fernandez, A.M., Encinar, J.A., Ferrer-Montiel, A.V., Otzen, D. and Gonzalez-Ros, J.M. 2010. Biochemistry. 49(25): 5397-5404.
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PUBMED: 20481584
DOI: 10.1021/bi1003712
[35] Binding of 5´-methylthioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-close conformational change in its CBS motif pair. M. Lucas, J. A. Encinar, I. Oyenarte, I. Gómez García, E. Astigarraga Arribas, D. Kortazar, J. A. Fernández, J. M. Mato, M. L. Martínez-Chantar and Luis A. Martínez-Cruz. 2010. Journal of Molecular Biology 396(3): 800-820.
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DOI: 10.1016/j.jmb.2009.12.012
[Movie 1A] [Movie 1B] [Movie 2]
[34] ADAN: A database for prediction of protein-protein interaction of modular domains mediated by linear motifs. J. A. Encinar, Fernandez-Ballester G., Sánchez I.E., Hurtado-Gomez E., Stricher F., Beltrao P., Serrano L. 2009. Bioinformatics. 25(18): 2418-2424.
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PUBMED: 19602529
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[33] Interaction of transmembrane-spanning segments of the α2-adrenergic receptor with model membranes. J. Prades, J. A. Encinar, J. M. González-Ros, P. V. Escribá and F. Barceló. 2009. Molecular Membrane Biology 26(5-7): 265-278.
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[32] The CBS-domain protein MJ0729 of Methanococcus jannaschii is a thermostable protein with pH-dependent homooligomeric species. L.A. Martínez-Cruz, J. A. Encinar, D. Kortazar, J. Prieto, J. Gómez, P. Fernández-Millán, M. Lucas, E. Astigarraga Arribas, J. A. Fernández, M. L. Martínez-Chantar, J. M. Mato and J. L. Neira. 2009. Biochemistry, 48: 2760-2776.
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[31] Metal-triggered changes in the stability and secondary structure of a tetrameric dihydropyrimidinase: a biophysical characterization. S. Martínez-Rodríguez, J. A. Encinar, E. Hurtado-Gómez, J. Prieto, J. M. Clemente-Jiménez, F. J. Las Heras-Vázquez, F. Rodríguez-Vico and J. L. Neira. 2009. Biophysical Chemistry. 139(1): 42-52.
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[30] Protein-promoted membrane domains. J. A. Poveda, A.M. Fernandez, J. A. Encinar, and J. M. González-Ros. 2008. Biochimica et Biophysica Acta, 1778: 1583-1590.
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[29] N-type inactivation of the potassium channel KcsA by the Shaker B “ball” peptide: Mapping the inactivating peptide binding epitope. M. L. Molina, F. N. Barrera, J. A. Encinar, M. L. Renart, A. M. Fernández, J. A. Poveda, J. Santoro, M. Bruix, F. Gavilanes, Fernández-Ballester, G. J., J. L. Neira, and J. M. González-Ros. 2008. Journal of Biological Chemistry 283(26): 18076-18085.
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PUBMED: 18430729
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[28] Interaction of the c-terminal region of the gamma-protein with model membranes. F. Barceló, J. Prades, J. A. Encinar, S. S. Funari, J. Manuel González-Ros and Pablo V. Escribá. (2007). Biophysical Journal, 93: 2530-2541.
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[27] Structural and functional modulation of ion channels by specific lipids: from model systems to cell membranes. A. M. Fernández, J. A. Poveda, J. A. Encinar, A. Morales and J. M. González-Ros (2006). Protein lipid-interactions: New approaches and emerging concepts. CR Mateo, Gomez J., Villalain J and Gonzalez-Ros JM Eds. Springer. pp. 203-233. (ISSN:0932-2353).
DOI: 10.1007/3-540-28435-4_8
[26] Structural and functional changes induced in the nicotinic acetylcholine receptor by membrane phospholipids. A. M. Fernández-Carvajal, J. A. Encinar, J.A. Poveda, E. de Juan, J. Martínez-Pinna, I. Ivorra, J. A. Ferragut, A. Morales and J. M. González-Ros. 2006. Journal of Molecular Neuroscience 30(1-2): 121-124.
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[25] Nicotinic acetylcholine receptor properties are modulated by surrounding lipids: an “in vivo” study. A. Morales, E. de Juan, A. Fernández, J. Martínez-Pinna, J.A. Poveda, J.A. Encinar, I. Ivorra and J. M. González-Ros. 2006. Journal of Molecular Neuroscience 30(1-2): 5-6.
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[24] The XII International Symposium on Cholinergic Mechanisms. J. M. Gonzalez-Ros, J.A. Encinar, H. Soreq, and A. G. Karczmar. 2006. Journal of Molecular Neuroscience 30(1-2): 1-2.
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DOI: 10.1385/JMN:30:1:1
[23] Effects of conducting and blocking ions on the structure and stability of the potassium channel kcsa. M. L. Renart, F. N. Barrera, M. L. Molina, J. A. Encinar, J. A. Poveda, A. M. Fernández, J. Gómez and J. M. González-Ros. 2006. Journal of Biological Chemistry 281(40): 29905-29915.
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[22] Clustering and Coupled Gating Modulate the Activity in KcsA, a Potassium Channel Model. M. L. Molina, F. N. Barrera, Asia M. Fernández, Jose A. Poveda, Maria L. Renart, J. A. Encinar, Gloria Riquelme, and Jose M. González-Ros. 2006. Journal of Biological Chemistry 281(27): 18837-18848.
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[21] Unfolding and refolding in vitro of a tetrameric, alpha-helical membrane protein: the prokaryotic potassium channel KcsA. F.N. Barrera, M. L. Renart, M. L. Molina, J. A. Poveda, J. A. Encinar, A. M. Fernández, J. L. Neira and J. M. González-Ros. 2005. Biochemistry. 44(43): 14344-14352.
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[20] The influence of a membrane environment on the structure and stability of a prokaryotic potassium channel, KcsA. J. A. Encinar, M. L. Molina, J. A. Poveda, F. N. Barrera, M. L. Renart, A. M. Fernández and J. M. González-Ros. 2005. FEBS letters. 579: 5199-5204.
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[19] Segregation of phosphatidic acid-rich domains in reconstituted acetylcholine receptor membranes. Poveda, J.A., Encinar, J.A., Fernández, A.M., Mateo C.R. González-Ros, J.M.. (2004). In "Cholynergic mechanism: Function and dysfunction". I. Silman, H. Soreq, L. Anglister, D. Michaelson and A. Fisher; Eds. Ed. Taylor & Francis Group, pp. 665-669. (ISBN:1841840750).
[18] Influence of C-terminal protein domains and protein-lipid interactions on tetramerization and stability of the potassium channel KcsA. Molina, M.L., Encinar, J.A., Barrera, F.N., Fernández-Ballester, G., Riquelme, G., González-Ros, J.M. 2004. Biochemistry. 43(47): 14924-14931.
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[17] Probing The Channel-Bound Shaker B Inactivating Peptide By Stereoisomeric Substitution At A trategic Tyrosine Residue. J. A. Encinar, A. M. Fernández, J. A. Poveda, M. L. Molina, J. P. Albar, F. Gavilanes and J. M. Gonzalez-Ros. 2003. Biochemistry. 42: 8879-8884.
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[16] Intrinsic Tyrosine Fluorescence as a Tool To Study the Interaction of the Shaker B "Ball" Peptide with Anionic Membranes. J. A. Poveda, M. Prieto, J. A. Encinar, J. M. González-Ros, and C. Reyes Mateo. 2003. Biochemistry. 42: 7124-7132.
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[15] Salmonid viral haemorrhagic septicaemia virus: fusion-related enhancement of virus infectivity by peptides derived from viral glycoprotein G or a combinatorial library. V. Mas, L. Perez, J. A. Encinar, M. T. Pastor, A. Rocha, E. Perez-Paya, A. Ferrer-Montiel, J. M. Gonzalez Ros, A. Estepa and J. M. Coll. 2002. Journal of General Virology 83: 2671-2681.
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[14] Segregation of Phosphatidic Acid-Rich Domains in Reconstituted Acetylcholine Receptor Membranes. Poveda, J. A., Encinar, J. A., Fernandez, A. M., Mateo, C. R.; Ferragut, J. A., Gonzalez-Ros, J. M. 2002. Biochemistry 41: 12253-12262.
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[13] Tyrosine Phosphorylation of the Inactivating Peptide of the Shaker B Potassium Channel: A Structural-Functional Correlate. Encinar, J. A., Fernandez, A. M., Molina, M. L., Molina, A., Poveda, J. A., Albar, J. P., Lopez-Barneo, J., Gavilanes, F., Ferrer-Montiel, A. V., Gonzalez-Ros, J. M. 2002. Biochemistry, 41: 12263-12269.
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[12] A Protein G Fragment from the Salmonid Viral Hemorrhagic Septicemia Rhabdovirus Induces Cell-to-Cell Fusion and Membrane Phosphatidylserine Translocation at Low pH. Estepa, A., Rocha, A.I., Mas, V., Pérez, L., Encinar, J.A., Elena Nuñez, Asia Fernandez, Jose M. Gonzalez Ros, F. Gavilanes and Julio M. Coll. 2001. Journal of Biological Chemistry 276: 46268-46275.
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[11] Human p8 is a HMG-like protein with DNA-binding activity enhanced by phosphorylation. Encinar, J.A., Mallo, G.V., Mizyrycki, C., Giono, L., Gonzalez-Ros, J.M., Rico, M., Canepa, E., Moreno, S., Neira, J.L., Iovanna, J.L. (2001) Journal of Biological Chemistry 276: 2742-2751.
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[10] Effect of the inactivating "ball" peptide of Shaker B on intermediate conductance Ca2+-dependent inwardly rectifying K+ channels of HeLa cells. Riquelme, G., Fernandez, A.M., Encinar, J.A., Gonzalez-Ros, J.M. and Sepulveda F.V. 1999. Pflugers Archiv European Journal of Physiology, 438: 879-882.
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[9] The segregation of a lipid domain underlies structural and functional modulation of acetylcholine receptor in reconstituted membranes. González-Ros, J.M.; Fernández, A.M., Encinar, J.A., Poveda, J.A. 1998. Journal of Physiology-Paris. 92(5-6): 432-433.
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[7] Inactivating peptide of the Shaker B potassium channel: conformational preferences inferred from studies on simple model systems. Encinar, J.A., Fernández, A.M., Gil-Martín, E., Gavilanes, F., Albar, J.P., Ferragut, J.A. and González-Ros, J.M. 1998. Biochemical Journal 331: 497-504.
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[5] Removal of Spectral Noise in the Quantitation of Protein Structure Through Infrared Band Decomposition. Echabe, I., Encinar, J.A. and Arrondo, J. L. R. 1997. Biospectroscopy, 3: 469-475.
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[2] Interaction between ion channel-inactivating peptides and anionic phospholipid vesicles as model targets. Encinar, J. A., Fernández, A. M., Gavilanes, F., Albar, J. P., Ferragut, J. A. and González-Ros, J. M. 1996. Biophysical Journal 71: 1313-1323.
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[1] Enzymatic determination of phosphatidylcholine, sphingomyelin and phosphatidylglycerol in lipid dispersions, blood cell membranes and rat pulmonary surfactant. Encinar, J.A., Ludeña, M. D., Sánchez-Yayüe, J. and Llanillo, M. 1996. Clinical Chemistry and Laboratory Medicine 34: 9-15.
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