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Google Citation Profile   http://scholar.google.com/citations?user=jTdMuycAAAAJ

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   ResearcherID: F-2946-2013

   Scopus Author ID: 35268584800

   ORCID Author ID: 0000-0002-7219-3863

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[63] New mammalian target of rapamycin (mTOR) modulators derived from natural product databases and marine extracts by using molecular docking techniques. Ruiz-Torres, V., Losada-Echeberría, M., Herranz-López, M., Barrajón-Catalán, E., Galiano, V., Micol, V., Encinar, J.A. 2018. Mar. Drugs 2018, 16(10), 385.
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DOI: 10.3390/md16100385
Supplemental Material: Tables S1/S7 and Figures S1/S2
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[62] Antimicrobial Capacity of Plant Polyphenols against Gram-positive Bacteria: a Comprehensive Review. Álvarez-Martínez, F.J., Barrajón-Catalán, E., Encinar, J.A., Rodríguez-Díaz, J.C., Micol, V. 2018. Current Medicinal Chemistry. In the press.
DOI: 10.2174/0929867325666181008115650
Supplemental Material: http://dockingfiles.umh.es/bcwall/phenol/
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[61] Chromatin immunoprecipitation and high throughput sequencing of SVCV-infected zebrafish reveals novel epigenetic histone methylation patterns involved in antiviral immune response. Medina-Gali, R.M., Bello-Pérez, M., Martínez-López, A., Falcó, A., Ortega-Villaizan, M.M., Encinar, J.A., Novoa, B., Coll, J., & Perez, L. 2018. Fish Shellfish Immunol. 82: 514-521.
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SCOPUS: 2-s2.0-85052647666
PUBMED: 30170110
DOI: 10.1016/j.fsi.2018.08.056
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[60] Turbot (Scophthalmus maximus) Nk-lysin induces protection against the pathogenic parasite Philasterides dicentrarchi via membrane disruption. Lama, R., Pereiro, P., Costa, M.M., Encinar, J.A., Medina-Gali, R.M., Pérez, L., Lamas, J., Figueras, A., Novoa, B. 2018. Fish Shellfish Immunol. 82: 190-199.
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SCOPUS: 2-s2.0-85051674016
PUBMED: 30086378
DOI: 10.1016/j.fsi.2018.08.004
Supplementary Data: supplementary data related to this article.
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[59] Discovery of non-nucleoside inhibitors of the polymerase of infectious pancreatic necrosis virus (IPNV). Bello-Perez, M., Falco, A., Galiano, V., Coll, J., Perez, L. and Encinar, J.A. 2018. Drug Design, Development and Therapy, 12: 2337-2359.
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PUBMED: 30104863
DOI: 10.2147/DDDT.S171087
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[58] Plant-Derived Polyphenols in Human Health: Biological Activity, Metabolites and Putative Molecular Targets. Olivares-Vicente, M., Barrajón-Catalán, E., Herranz-López, M., Segura-Carretero, A., Joven, J., Encinar, J.A. and Micol, V. 2018. Current Drug Metabolism, 19: 351-369.
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SCOPUS: 2-s2.0-85048992337
PUBMED: 29468962
DOI: 10.2174/1389200219666180220095236
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[57] Nutraceuticals molecular targets (III) - targeting protein receptors with polyphenols as new anti-obesity therapies. Micol, V., Encinar, J.A. and Herranz-López, M.. 2017. Agro FOOD Industry Hi Tech - vol. 28(5) - September/October 2017.
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Website of the publication: http://www.teknoscienze.com/
SCOPUS: 2-s2.0-85033694815
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[56] Neutralization of viral infectivity by zebrafish C-reactive protein isoforms. Bello-Perez, M., Falco, A., Medina-Gali, R., Pereiro, P., Encinar, J.A., Novoa, B., Perez, L., Coll, J. 2017. Molecular Immunology 91: 145-155.
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SCOPUS: 2-s2.0-85029186314
PUBMED: 28915434
DOI: 10.1016/j.molimm.2017.09.005
Supplementary Material: S1, S2, S3 Figures and Legends.
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[55] Multi-targeted molecular effects of Hibiscus sabdariffa polyphenols: an opportunity for a global approach to obesity. Herranz-López, M., Olivares-Vicente, M., Encinar, J.A., Barrajón-Catalán, E., Segura-Carretero, A., Joven, J. and Micol, V. 2017. Nutrients, 9(8), 907.
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SCOPUS: 2-s2.0-85028087858
PUBMED: 28825642
DOI: 10.3390/nu9080907
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[54] Nutraceuticals molecular targets (II). A novel way of approaching health by using nutraceuticals: Combined -omics and virtual screening. Micol, V. and Encinar, J.A.. 2017. Agro FOOD Industry Hi Tech - vol. 28(2) - March/April 2017.
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Website of the publication: www.teknoscienze.com
SCOPUS: 2-s2.0-85031772569
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[53] An updated review on marine anticancer compounds: the use of virtual screening for the discovery of small-molecule cancer drugs. Ruiz-Torres, V., Encinar, J.A., Herranz López, M., Perez-Sánchez, A., Galiano, V., Barrajón-Catalán, E., Micol, V. 2017. Molecules, 22(7): 1037.
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SCOPUS: 2-s2.0-85021642641
PUBMED: 28644406
DOI: 10.3390/molecules22071037
Supplemental Material: http://docking.umh.es/chemlib/mnplib and
http://dockingfiles.umh.es/anticancer-drugs/Anticancer_drugslist.asp
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[52] AMPK modulatory activity of olive-tree leaves phenolic compounds: Bioassay-guided isolation on adipocyte model and in silico approach. Jiménez-Sánchez, C., Olivares-Vicente, M., Rodríguez-Pérez, C., Herranz-López, M., Lozano-Sánchez, J., Segura-Carretero, A., Fernández Gutiérrez, A., Encinar, J.A., Micol, V. 2017. PLoS ONE, 12(3): e0173074.
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SCOPUS: 2-s2.0-85014969519
PUBMED: 28278224
DOI: 10.1371/journal.pone.0173074
Supplementary Material: S1, S2, S3 Figures
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[51] Structure and functionalities of the human c-reactive protein compared to the zebrafish multigene family of c-reactive-like proteins. Bello, M., Falco, A., Medina Gali, R.M., Encinar, J.A., Novoa, B., Perez, L., Coll. 2016. J. Dev Comp Immunol. 69: 33-40.
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SCOPUS: 2-s2.0-85006883474
PUBMED: 27965017
DOI: 10.1016/j.dci.2016.12.001
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[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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SCOPUS: 2-s2.0-84991585010
PUBMED: 27784988
DOI: 10.2147/DDDT.S117369
Supplemental Material: http://docking.umh.es/
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[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.
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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).
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[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. J Biol Chem. 290(42): 25745-25755.
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SCOPUS: 2-s2.0-84944472904
PUBMED: 26336105
DOI: 10.1074/jbc.M115.669598
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[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. Biochem J. 464: 23-34.
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SCOPUS: 2-s2.0-84908383508
PUBMED: 25184538
DOI: 10.1042/BJ20140409
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[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 Res. 108: 14-24.
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SCOPUS: 2-s2.0-84901452169
PUBMED: 24815023
DOI: 10.1016/j.antiviral.2014.04.009
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[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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SCOPUS: 2-s2.0-84899433919
PUBMED: 24211605
DOI: 10.1016/j.bbamem.2013.10.023
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[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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SCOPUS: 2-s2.0-84880882272
PUBMED: 23880927
DOI: 10.3390/md11072328
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[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.
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SCOPUS: 2-s2.0-84882634594
PUBMED: 23792066
DOI: 10.1016/j.bbamem.2013.06.014
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[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. BBA - Biomembranes, 1828(2): 193-200.
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SCOPUS: 2-s2.0-84869884191
PUBMED: 23022492
DOI: 10.1016/j.bbamem.2012.09.020
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[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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SCOPUS: 2-s2.0-84860761010
PUBMED: 22509943
DOI: 10.1021/bi201497n
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[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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SCOPUS: 2-s2.0-84860156451
PUBMED: 22471585
DOI: 10.1021/bi201574t
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[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.
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SCOPUS: 2-s2.0-79954506008
PUBMED: 21490973
DOI: 10.1371/journal.pone.0018515
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[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 Eng Des Sel. 24(1-2): 161-169.
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SCOPUS: 2-s2.0-78650485262
PUBMED: 20959390
DOI: 10.1093/protein/gzq073
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[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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SCOPUS: 2-s2.0-78149323108
PUBMED: 20925387
DOI: 10.1021/bi101235v
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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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SCOPUS: 2-s2.0-77953896086
PUBMED: 20481584
DOI: 10.1021/bi1003712
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[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. J. Mol. Biol. 396(3): 800-820.
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SCOPUS: 2-s2.0-77949314227
PUBMED: 20026078
DOI: 10.1016/j.jmb.2009.12.012
[Movie 1A] [Movie 1B] [Movie 2]
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[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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SCOPUS: 2-s2.0-69849100180
PUBMED: 19602529
DOI: 10.1093/bioinformatics/btp424
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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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SCOPUS: 2-s2.0-71849098809
PUBMED: 19568979
DOI: 10.1080/09687680903081610

[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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SCOPUS: 2-s2.0-65249117438
PUBMED: 19267448
DOI: 10.1021/bi801920r

[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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SCOPUS: 2-s2.0-56449111038
PUBMED: 19008030
DOI: 10.1016/j.bpc.2008.10.003

[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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SCOPUS: 2-s2.0-45449119278
PUBMED: 18294450
DOI: 10.1016/j.bbamem.2008.01.021

[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. J. Biol. Chem. 283(26): 18076-18085.
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SCOPUS: 2-s2.0-49649103285
PUBMED: 18430729
DOI: 10.1074/jbc.M710132200

[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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SCOPUS: 2-s2.0-71849098809
PUBMED: 17545235
DOI: 10.1529/biophysj.106.101196

[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).
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DOI: 10.1007/3-540-28435-4_8
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[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. J. Mol. Neurosci. 30(1-2): 121-124.
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SCOPUS: 2-s2.0-33845956512
PUBMED: 17192656
DOI: 10.1385/JMN:30:1:121

[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. J. Mol. Neurosci. 30(1-2): 5-6.
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SCOPUS: 2-s2.0-33845959640
PUBMED: 17192603
DOI: 10.1385/JMN:30:1:5

[24] The XII International Symposium on Cholinergic Mechanisms. J. M. Gonzalez-Ros, J.A. Encinar, H. Soreq, and A. G. Karczmar. 2006. J. Mol Neurosci. 30(1-2): 1-2.
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SCOPUS: 2-s2.0-33845935460
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. J. Biol. Chem. 281(40): 29905-29915.
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SCOPUS: 2-s2.0-33749575060
PUBMED: 16815844
DOI: 10.1074/jbc.M602636200

[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. J. Biol. Chem. 281(27): 18837-18848.
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SCOPUS: 2-s2.0-33745870439
PUBMED: 16670090
DOI: 10.1074/jbc.M600342200

[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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SCOPUS: 2-s2.0-27444441821
PUBMED: 16245951
DOI: 10.1021/bi050845t

[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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SCOPUS: 2-s2.0-24944476565
PUBMED: 16150445
DOI: 10.1016/j.febslet.2005.08.038

[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).
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[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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SCOPUS: 2-s2.0-9744272384
PUBMED: 15554699
DOI: 10.1021%2Fbi048889%2B

[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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SCOPUS: 2-s2.0-0042848686
PUBMED: 12873149
DOI: 10.1021/bi0343121

[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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SCOPUS: 2-s2.0-0038470046
PUBMED: 12795608
DOI: 10.1021/bi027183h

[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. J. Gen. Virol. 83: 2671-2681.
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SCOPUS: 2-s2.0-18644374984
PUBMED: 12388802
DOI: 10.1099/0022-1317-83-11-2671

[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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SCOPUS: 2-s2.0-0037044328
PUBMED: 12356328
DOI: 10.1021/bi0200099

[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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SCOPUS: 2-s2.0-18644376936
PUBMED: 12356329
DOI: 10.1021/bi020188u

[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. J. Biol. Chem. 276: 46268-46275.
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SCOPUS: 2-s2.0-0035824655
PUBMED: 11590161
DOI: 10.1074/jbc.M108682200

[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) J. Biol. Chem. 276: 2742-2751.
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SCOPUS: 2-s2.0-0035951881
PUBMED: 11056169
DOI: 10.1074/jbc.M008594200
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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 Arch, 438: 879-882.
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SCOPUS: 2-s2.0-0010670867
PUBMED: 10591078
DOI: 10.1007/s004249900138

[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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DOI: 10.1016/S0928-4257(99)80046-1

[8] Structural stabilization of botulinum neurotoxins by tyrosine phosphorylation. Encinar, J.A., Fernández, A.M., DasGupta, B.R., Ferragut, J.A., Montal, M., González-Ros, J.M. and Ferrer-Montiel, A.V. 1998. FEBS lett. 429: 78-82.
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SCOPUS: 2-s2.0-0345294418
PUBMED: 9657387
DOI: 10.1016/S0014-5793(98)00571-7

[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. Biochem. J. 331: 497-504.
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SCOPUS: 2-s2.0-0032522766
PUBMED: 9531490
DOI: 10.1042/bj3310497

[6] Lipid-protein interactions in reconstituted membranes containing nicotinic Acetylcholine Receptor. Encinar, J.A., Fernández, A.M., Poveda, J.A. and González-Ros, J.M. (1997). 7th European Conference on Spectroscopy of Biological Moleculas. Spectroscopy of Biological Molecules: Modern Trends. P. Carmona, R. Navarro and A.Herranz (Eds) Ed: KLUWER ACADEMIC PUBLISHERS. (ISBN: 0-7923-4685-8) pp 339-340.
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DOI: 10.1007/978-94-011-5622-6_152

[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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SCOPUS: 2-s2.0-0000080520
DOI: 10.1002/(SICI)1520-6343(1997)3:6<469::AID-BSPY6>3.0.CO;2-W
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[4] Synthesis of a photoaffinity labeling analogue of the inactivating peptide of the Shaker B potassium channel. Fernández, A.M., Molina, A., Encinar, J.A., Gavilanes, F., López-Barneo, J. and González-Ros, J.M. 1996. FEBS lett. 389: 81-86.
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SCOPUS: 2-s2.0-0043100163
PUBMED: 8946957
DOI: 10.1016/S0014-5793(96)01186-6
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[3] Structural properties of hepetitis B virus fusion peptide upon interaction with lipids: a FTIR and CD spectroscopy study. Rodríguez-Crespo, I., Gómez-Gutiérrez, J., Encinar, J.A., González-Ros, J.M., Albar, J.P., Peterson, D.L. and Gavilanes, F. 1996. Eur. J. Biochem. 242: 243-248.
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SCOPUS: 2-s2.0-0029781536
PUBMED: 8973639
DOI: 10.1111/j.1432-1033.1996.0243r.x
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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. Biophys. J. 71: 1313-1323.
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SCOPUS: 2-s2.0-0029781536
PUBMED: 8874005
DOI: 10.1016/S0006-3495(96)79331-1
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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. Eur. J. Clin. Chem. Clin. Biochem. 34: 9-15.
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SCOPUS: 2-s2.0-85025278635
PUBMED: 8704043
DOI: 10.1515/cclm.1996.34.1.9
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