214 results on '"Abrescia, Nicola G A"'
Search Results
2. Seroprevalence of adeno-associated virus types 1, 2, 3, 4, 5, 6, 8, and 9 in a Basque cohort of healthy donors
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Navarro-Oliveros, Miguel, Vidaurrazaga, Ander, Soares Guerra, Gabriel, Castellana, Donatello, Embade, Nieves, Millet, Oscar, Marigorta, Urko M., and Abrescia, Nicola G. A.
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- 2024
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3. Integrative Approaches to Study Virus Structures
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Stuart, David I., Oksanen, Hanna M., Abrescia, Nicola G. A., Kundu, Tapas K., Series Editor, Harris, J. Robin, Advisory Editor, Holzenburg, Andreas, Advisory Editor, Korolchuk, Viktor, Advisory Editor, Bolanos-Garcia, Victor, Advisory Editor, Marles-Wright, Jon, Advisory Editor, and Mateu, Mauricio G., editor
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- 2024
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4. Membrane-Containing Icosahedral Bacteriophage PRD1: The Dawn of Viral Lineages
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Oksanen, Hanna M., Abrescia, Nicola G. A., COHEN, IRUN R., Editorial Board Member, LAJTHA, ABEL, Editorial Board Member, LAMBRIS, JOHN D., Editorial Board Member, PAOLETTI, RODOLFO, Editorial Board Member, REZAEI, NIMA, Editorial Board Member, and Greber, Urs F., editor
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- 2019
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5. Sensitive detection of SARS-CoV-2 seroconversion by flow cytometry reveals the presence of nucleoprotein-reactive antibodies in unexposed individuals
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Egia-Mendikute, Leire, Bosch, Alexandre, Prieto-Fernández, Endika, Lee, So Young, Jiménez-Lasheras, Borja, García del Río, Ana, Antoñana-Vildosola, Asier, Bruzzone, Chiara, Bizkarguenaga, Maider, Embade, Nieves, Gil-Redondo, Rubén, Martínez-Chantar, María Luz, López-Hoyos, Marcos, Abrescia, Nicola G. A., Mato, José M., Millet, Óscar, and Palazón, Asís
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- 2021
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6. Physical Virology in Spain
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Reguera, David, primary, de Pablo, Pedro J., additional, Abrescia, Nicola G. A., additional, Mateu, Mauricio G., additional, Hernández-Rojas, Javier, additional, Castón, José R., additional, and San Martín, Carmen, additional
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- 2023
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7. A novel Schmallenberg virus subunit vaccine candidate protects IFNAR-/- mice against virulent SBV challenge
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Boshra, Hani, Lorenzo, Gema, Charro, Diego, Moreno, Sandra, Guerra, Gabriel Soares, Sanchez, Isbene, Garrido, Joseba M., Geijo, Marivi, Brun, Alejandro, and Abrescia, Nicola G. A.
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- 2020
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8. Structural basis for assembly of vertical single β-barrel viruses
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Santos-Pérez, Isaac, Charro, Diego, Gil-Carton, David, Azkargorta, Mikel, Elortza, Felix, Bamford, Dennis H., Oksanen, Hanna M., and Abrescia, Nicola G. A.
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- 2019
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9. Four principles to establish a universal virus taxonomy
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Simmonds, Peter, Adriaenssens, Evelien M, Zerbini, F Murilo, Abrescia, Nicola G A, Aiewsakun, Pakorn, Alfenas-Zerbini, Poliane, Bao, Yiming, Barylski, Jakub, Drosten, Christian, Duffy, Siobain, Duprex, W Paul, Dutilh, Bas E, Elena, Santiago F, García, Maria Laura, Junglen, Sandra, Katzourakis, Aris, Koonin, Eugene V, Krupovic, Mart, Kuhn, Jens H, Lambert, Amy J, Lefkowitz, Elliot J, Łobocka, Małgorzata, Lood, Cédric, Mahony, Jennifer, Meier-Kolthoff, Jan P, Mushegian, Arcady R, Oksanen, Hanna M, Poranen, Minna M, Reyes-Muñoz, Alejandro, Robertson, David L, Roux, Simon, Rubino, Luisa, Sabanadzovic, Sead, Siddell, Stuart, Skern, Tim, Smith, Donald B, Sullivan, Matthew B, Suzuki, Nobuhiro, Turner, Dann, Van Doorslaer, Koenraad, Vandamme, Anne-Mieke, Varsani, Arvind, Vasilakis, Nikos, Simmonds, Peter, Adriaenssens, Evelien M, Zerbini, F Murilo, Abrescia, Nicola G A, Aiewsakun, Pakorn, Alfenas-Zerbini, Poliane, Bao, Yiming, Barylski, Jakub, Drosten, Christian, Duffy, Siobain, Duprex, W Paul, Dutilh, Bas E, Elena, Santiago F, García, Maria Laura, Junglen, Sandra, Katzourakis, Aris, Koonin, Eugene V, Krupovic, Mart, Kuhn, Jens H, Lambert, Amy J, Lefkowitz, Elliot J, Łobocka, Małgorzata, Lood, Cédric, Mahony, Jennifer, Meier-Kolthoff, Jan P, Mushegian, Arcady R, Oksanen, Hanna M, Poranen, Minna M, Reyes-Muñoz, Alejandro, Robertson, David L, Roux, Simon, Rubino, Luisa, Sabanadzovic, Sead, Siddell, Stuart, Skern, Tim, Smith, Donald B, Sullivan, Matthew B, Suzuki, Nobuhiro, Turner, Dann, Van Doorslaer, Koenraad, Vandamme, Anne-Mieke, Varsani, Arvind, and Vasilakis, Nikos
- Abstract
A universal taxonomy of viruses is essential for a comprehensive view of the virus world and for communicating the complicated evolutionary relationships among viruses. However, there are major differences in the conceptualisation and approaches to virus classification and nomenclature among virologists, clinicians, agronomists, and other interested parties. Here, we provide recommendations to guide the construction of a coherent and comprehensive virus taxonomy, based on expert scientific consensus. Firstly, assignments of viruses should be congruent with the best attainable reconstruction of their evolutionary histories, i.e., taxa should be monophyletic. This fundamental principle for classification of viruses is currently included in the International Committee on Taxonomy of Viruses (ICTV) code only for the rank of species. Secondly, phenotypic and ecological properties of viruses may inform, but not override, evolutionary relatedness in the placement of ranks. Thirdly, alternative classifications that consider phenotypic attributes, such as being vector-borne (e.g., "arboviruses"), infecting a certain type of host (e.g., "mycoviruses," "bacteriophages") or displaying specific pathogenicity (e.g., "human immunodeficiency viruses"), may serve important clinical and regulatory purposes but often create polyphyletic categories that do not reflect evolutionary relationships. Nevertheless, such classifications ought to be maintained if they serve the needs of specific communities or play a practical clinical or regulatory role. However, they should not be considered or called taxonomies. Finally, while an evolution-based framework enables viruses discovered by metagenomics to be incorporated into the ICTV taxonomy, there are essential requirements for quality control of the sequence data used for these assignments. Combined, these four principles will enable future development and expansion of virus taxonomy as the true evolutionary diversity of viruses becomes a
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- 2023
10. Four principles to establish a universal virus taxonomy
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Theoretical Biology and Bioinformatics, Sub Bioinformatics, Simmonds, Peter, Adriaenssens, Evelien M, Zerbini, F Murilo, Abrescia, Nicola G A, Aiewsakun, Pakorn, Alfenas-Zerbini, Poliane, Bao, Yiming, Barylski, Jakub, Drosten, Christian, Duffy, Siobain, Duprex, W Paul, Dutilh, Bas E, Elena, Santiago F, García, Maria Laura, Junglen, Sandra, Katzourakis, Aris, Koonin, Eugene V, Krupovic, Mart, Kuhn, Jens H, Lambert, Amy J, Lefkowitz, Elliot J, Łobocka, Małgorzata, Lood, Cédric, Mahony, Jennifer, Meier-Kolthoff, Jan P, Mushegian, Arcady R, Oksanen, Hanna M, Poranen, Minna M, Reyes-Muñoz, Alejandro, Robertson, David L, Roux, Simon, Rubino, Luisa, Sabanadzovic, Sead, Siddell, Stuart, Skern, Tim, Smith, Donald B, Sullivan, Matthew B, Suzuki, Nobuhiro, Turner, Dann, Van Doorslaer, Koenraad, Vandamme, Anne-Mieke, Varsani, Arvind, Vasilakis, Nikos, Theoretical Biology and Bioinformatics, Sub Bioinformatics, Simmonds, Peter, Adriaenssens, Evelien M, Zerbini, F Murilo, Abrescia, Nicola G A, Aiewsakun, Pakorn, Alfenas-Zerbini, Poliane, Bao, Yiming, Barylski, Jakub, Drosten, Christian, Duffy, Siobain, Duprex, W Paul, Dutilh, Bas E, Elena, Santiago F, García, Maria Laura, Junglen, Sandra, Katzourakis, Aris, Koonin, Eugene V, Krupovic, Mart, Kuhn, Jens H, Lambert, Amy J, Lefkowitz, Elliot J, Łobocka, Małgorzata, Lood, Cédric, Mahony, Jennifer, Meier-Kolthoff, Jan P, Mushegian, Arcady R, Oksanen, Hanna M, Poranen, Minna M, Reyes-Muñoz, Alejandro, Robertson, David L, Roux, Simon, Rubino, Luisa, Sabanadzovic, Sead, Siddell, Stuart, Skern, Tim, Smith, Donald B, Sullivan, Matthew B, Suzuki, Nobuhiro, Turner, Dann, Van Doorslaer, Koenraad, Vandamme, Anne-Mieke, Varsani, Arvind, and Vasilakis, Nikos
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- 2023
11. Physical Virology in Spain
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Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Human Frontier Science Program, European Commission, Ministerio de Ciencia e Innovación (España), Consejo Superior de Investigaciones Científicas (España), Comunidad de Madrid, Hernández-Rojas, Javier [0000-0003-0610-660X], Castón, José R. [0000-0003-2350-9048], San Martín, Carmen [0000-0001-9799-175X], Reguera, David, Pablo, Pedro J. de, Abrescia, Nicola G. A., Mateu, Mauricio G., Hernández-Rojas, Javier, Castón, José R., San Martín, Carmen, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Human Frontier Science Program, European Commission, Ministerio de Ciencia e Innovación (España), Consejo Superior de Investigaciones Científicas (España), Comunidad de Madrid, Hernández-Rojas, Javier [0000-0003-0610-660X], Castón, José R. [0000-0003-2350-9048], San Martín, Carmen [0000-0001-9799-175X], Reguera, David, Pablo, Pedro J. de, Abrescia, Nicola G. A., Mateu, Mauricio G., Hernández-Rojas, Javier, Castón, José R., and San Martín, Carmen
- Abstract
Virus particles consist of a protein coat that protects their genetic material and delivers it to the host cell for self-replication. Understanding the interplay between virus structure and function is a requirement for understanding critical processes in the infectious cycle such as entry, uncoating, genome metabolism, capsid assembly, maturation, and propagation. Together with well-established techniques in cell and molecular biology, physical virology has emerged as a rapidly developing field, providing detailed, novel information on the basic principles of virus assembly, disassembly, and dynamics. The Spanish research community contains a good number of groups that apply their knowledge on biology, physics, or chemistry to the study of viruses. Some of these groups got together in 2010 under the umbrella of the Spanish Interdisciplinary Network on Virus Biophysics (BioFiViNet). Thirteen years later, the network remains a fertile ground for interdisciplinary collaborations geared to reveal new aspects on the physical properties of virus particles, their role in regulating the infectious cycle, and their exploitation for the development of virus-based nanotechnology tools. Here, we highlight some achievements of Spanish groups in the field of physical virology.
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- 2023
12. Molecular Recognition of Glycan-Bearing Glycomacromolecules Presented at Membrane Surfaces by Lectins: An NMR View
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Química Orgánica e Inorgánica, Kimika Organikoa eta Ez-Organikoa, Gutiérrez Lete, Marta, Hoffmann, Miriam, Schomann, Nils, Martínez Castillo, Ane, Peccati, Francesca, Konietzny, Patrick B., Delgado, Sandra, Snyder, Nicole L., Jiménez Oses, Gonzalo, Abrescia, Nicola G. A., Ardá, Ana, Hartmann, Laura, Jiménez Barbero, Jesús, Química Orgánica e Inorgánica, Kimika Organikoa eta Ez-Organikoa, Gutiérrez Lete, Marta, Hoffmann, Miriam, Schomann, Nils, Martínez Castillo, Ane, Peccati, Francesca, Konietzny, Patrick B., Delgado, Sandra, Snyder, Nicole L., Jiménez Oses, Gonzalo, Abrescia, Nicola G. A., Ardá, Ana, Hartmann, Laura, and Jiménez Barbero, Jesús
- Abstract
Lectin–glycan interactions are at the heart of a multitude of biological events. Glycans are usually presented in a multivalent manner on the cell surface as part of the so-called glycocalyx, where they interact with other entities. This multivalent presentation allows us to overcome the typical low affinities found for individual glycan–lectin interactions. Indeed, the presentation of glycans may drastically impact their binding by lectins, highly affecting the corresponding binding affinity and even selectivity. In this context, we herein present the study of the interaction of a variety of homo- and heteromultivalent lactose-functionalized glycomacromolecules and their lipid conjugates with two human galectins. We have employed as ligands the glycomacromolecules, as well as liposomes decorated with those structures, to evaluate their interactions in a cell-mimicking environment. Key details of the interaction have been unravelled by NMR experiments, both from the ligand and receptor perspectives, complemented by cryo-electron microscopy methods and molecular dynamics simulations.
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- 2023
13. Molecular Recognition of Glycan-Bearing Glycomacromolecules Presented at Membrane Surfaces by Lectins: An NMR View
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Lete, Marta G., primary, Hoffmann, Miriam, additional, Schomann, Nils, additional, Martínez-Castillo, Ane, additional, Peccati, Francesca, additional, Konietzny, Patrick B., additional, Delgado, Sandra, additional, Snyder, Nicole L., additional, Jiménez-Oses, Gonzalo, additional, Abrescia, Nicola G. A., additional, Ardá, Ana, additional, Hartmann, Laura, additional, and Jiménez-Barbero, Jesús, additional
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- 2023
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14. Combined Approaches to Study Virus Structures
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Badia-Martinez, Daniel, Oksanen, Hanna M., Stuart, David I., Abrescia, Nicola G. A., and Mateu, Mauricio G., editor
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- 2013
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15. Four principles to establish a universal virus taxonomy
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Simmonds, Peter, primary, Adriaenssens, Evelien M., additional, Zerbini, F. Murilo, additional, Abrescia, Nicola G. A., additional, Aiewsakun, Pakorn, additional, Alfenas-Zerbini, Poliane, additional, Bao, Yiming, additional, Barylski, Jakub, additional, Drosten, Christian, additional, Duffy, Siobain, additional, Duprex, W. Paul, additional, Dutilh, Bas E., additional, Elena, Santiago F., additional, García, Maria Laura, additional, Junglen, Sandra, additional, Katzourakis, Aris, additional, Koonin, Eugene V., additional, Krupovic, Mart, additional, Kuhn, Jens H., additional, Lambert, Amy J., additional, Lefkowitz, Elliot J., additional, Łobocka, Małgorzata, additional, Lood, Cédric, additional, Mahony, Jennifer, additional, Meier-Kolthoff, Jan P., additional, Mushegian, Arcady R., additional, Oksanen, Hanna M., additional, Poranen, Minna M., additional, Reyes-Muñoz, Alejandro, additional, Robertson, David L., additional, Roux, Simon, additional, Rubino, Luisa, additional, Sabanadzovic, Sead, additional, Siddell, Stuart, additional, Skern, Tim, additional, Smith, Donald B., additional, Sullivan, Matthew B., additional, Suzuki, Nobuhiro, additional, Turner, Dann, additional, Van Doorslaer, Koenraad, additional, Vandamme, Anne-Mieke, additional, Varsani, Arvind, additional, and Vasilakis, Nikos, additional
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- 2023
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16. New Glucosamine-Based TLR4 Agonists: Design, Synthesis, Mechanism of Action, and In Vivo Activity as Vaccine Adjuvants
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Romerio, Alessio, primary, Gotri, Nicole, additional, Franco, Ana Rita, additional, Artusa, Valentina, additional, Shaik, Mohammed Monsoor, additional, Pasco, Samuel T., additional, Atxabal, Unai, additional, Matamoros-Recio, Alejandra, additional, Mínguez-Toral, Marina, additional, Zalamea, Juan Diego, additional, Franconetti, Antonio, additional, Abrescia, Nicola G. A., additional, Jimenez-Barbero, Jesus, additional, Anguita, Juan, additional, Martín-Santamaría, Sonsoles, additional, and Peri, Francesco, additional
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- 2023
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17. Capsid-deficient alphaviruses generate propagative infectious microvesicles at the plasma membrane
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Ruiz-Guillen, Marta, Gabev, Evgeni, Quetglas, Jose I., Casales, Erkuden, Ballesteros-Briones, María Cristina, Poutou, Joanna, Aranda, Alejandro, Martisova, Eva, Bezunartea, Jaione, Ondiviela, Marina, Prieto, Jesus, Hernandez-Alcoceba, Ruben, Abrescia, Nicola G. A., and Smerdou, Cristian
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- 2016
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18. Insights into Hepatitis C Virus E2core Interactions with Human Cellular Receptor CD81 at Different pHs from Molecular Simulations
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Risueño, Cristina, primary, Abrescia, Nicola G A, additional, and Coluzza, Ivan, additional
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- 2022
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19. Mitochondrial bioenergetics boost macrophage activation, promoting liver regeneration in metabolically compromised animals
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Goikoetxea-Usandizaga, Naroa, Serrano-Maciá, Marina, Delgado, Teresa C., Simón, Jorge, Fernández-Ramos, David, Barriales, Diego, Cornide, Maria E., Jiménez, Mónica, Pérez-Redondo, Marina, Lachiondo-Ortega, Sofía, Rodríguez-Agudo, Rubén, Bizkarguenaga, Maider, Zalamea, Juan Diego, Pasco, Samuel T., Caballero-Díaz, Daniel, Alfano, Benedetta, Bravo, Miren, González-Recio, Irene, Mercado-Gomez, María, Gil-Pitarch, Clàudia, Mabe, Jon, Gracia-Sancho, Jordi, Abecia, Leticia, Lorenzo, Óscar, Martín-Sanz, Paloma, Abrescia, Nicola G. A., Sabio, Guadalupe, Rincón, Mercedes, Anguita, Juan, Miñambres, Eduardo, Martín, César, Berenguer, Marina, Fabregat, Isabel, Casado, Marta, Peralta, Carmen, Varela-Rey, Marta, Martínez-Chantar, María Luz, Goikoetxea-Usandizaga, Naroa, Serrano-Maciá, Marina, Delgado, Teresa C., Simón, Jorge, Fernández-Ramos, David, Barriales, Diego, Cornide, Maria E., Jiménez, Mónica, Pérez-Redondo, Marina, Lachiondo-Ortega, Sofía, Rodríguez-Agudo, Rubén, Bizkarguenaga, Maider, Zalamea, Juan Diego, Pasco, Samuel T., Caballero-Díaz, Daniel, Alfano, Benedetta, Bravo, Miren, González-Recio, Irene, Mercado-Gomez, María, Gil-Pitarch, Clàudia, Mabe, Jon, Gracia-Sancho, Jordi, Abecia, Leticia, Lorenzo, Óscar, Martín-Sanz, Paloma, Abrescia, Nicola G. A., Sabio, Guadalupe, Rincón, Mercedes, Anguita, Juan, Miñambres, Eduardo, Martín, César, Berenguer, Marina, Fabregat, Isabel, Casado, Marta, Peralta, Carmen, Varela-Rey, Marta, and Martínez-Chantar, María Luz
- Abstract
[Background and aims ]Hepatic ischemia-reperfusion injury (IRI) is the leading cause of early posttransplantation organ failure as mitochondrial respiration and ATP production are affected. A shortage of donors has extended liver donor criteria, including aged or steatotic livers, which are more susceptible to IRI. Given the lack of an effective treatment and the extensive transplantation waitlist, we aimed at characterizing the effects of an accelerated mitochondrial activity by silencing methylation-controlled J protein (MCJ) in three preclinical models of IRI and liver regeneration, focusing on metabolically compromised animal models., [Approach and results] Wild-type (WT), MCJ knockout (KO), and Mcj silenced WT mice were subjected to 70% partial hepatectomy (Phx), prolonged IRI, and 70% Phx with IRI. Old and young mice with metabolic syndrome were also subjected to these procedures. Expression of MCJ, an endogenous negative regulator of mitochondrial respiration, increases in preclinical models of Phx with or without vascular occlusion and in donor livers. Mice lacking MCJ initiate liver regeneration 12 h faster than WT and show reduced ischemic injury and increased survival. MCJ knockdown enables a mitochondrial adaptation that restores the bioenergetic supply for enhanced regeneration and prevents cell death after IRI. Mechanistically, increased ATP secretion facilitates the early activation of Kupffer cells and production of TNF, IL-6, and heparin-binding EGF, accelerating the priming phase and the progression through G1 /S transition during liver regeneration. Therapeutic silencing of MCJ in 15-month-old mice and in mice fed a high-fat/high-fructose diet for 12 weeks improves mitochondrial respiration, reduces steatosis, and overcomes regenerative limitations., [Conclusions] Boosting mitochondrial activity by silencing MCJ could pave the way for a protective approach after major liver resection or IRI, especially in metabolically compromised, IRI-susceptible organs.
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- 2022
20. Assessing the Mobility of Severe Acute Respiratory Syndrome Coronavirus-2 Spike Protein Glycans by Structural and Computational Methods
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Stagnoli, Soledad, primary, Peccati, Francesca, additional, Connell, Sean R., additional, Martinez-Castillo, Ane, additional, Charro, Diego, additional, Millet, Oscar, additional, Bruzzone, Chiara, additional, Palazon, Asis, additional, Ardá, Ana, additional, Jiménez-Barbero, Jesús, additional, Ereño-Orbea, June, additional, Abrescia, Nicola G. A., additional, and Jiménez-Osés, Gonzalo, additional
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- 2022
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21. Solvent-induced allosteric transition of the Hepatitis C virus human cellular receptor CD81 large extracellular loop
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Risueno, Cristina, primary, Charro, Diego, additional, Abrescia, Nicola G. A., additional, and Coluzza, Ivan, additional
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- 2022
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22. Mitochondrial bioenergetics boost macrophage activation, promoting liver regeneration in metabolically compromised animals
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Goikoetxea‐Usandizaga, Naroa, primary, Serrano‐Maciá, Marina, additional, Delgado, Teresa C., additional, Simón, Jorge, additional, Fernández Ramos, David, additional, Barriales, Diego, additional, Cornide, Maria E., additional, Jiménez, Mónica, additional, Pérez‐Redondo, Marina, additional, Lachiondo‐Ortega, Sofia, additional, Rodríguez‐Agudo, Rubén, additional, Bizkarguenaga, Maider, additional, Zalamea, Juan Diego, additional, Pasco, Samuel T., additional, Caballero‐Díaz, Daniel, additional, Alfano, Benedetta, additional, Bravo, Miren, additional, González‐Recio, Irene, additional, Mercado‐Gómez, Maria, additional, Gil‐Pitarch, Clàudia, additional, Mabe, Jon, additional, Gracia‐Sancho, Jordi, additional, Abecia, Leticia, additional, Lorenzo, Óscar, additional, Martín‐Sanz, Paloma, additional, Abrescia, Nicola G. A., additional, Sabio, Guadalupe, additional, Rincón, Mercedes, additional, Anguita, Juan, additional, Miñambres, Eduardo, additional, Martín, César, additional, Berenguer, Marina, additional, Fabregat, Isabel, additional, Casado, Marta, additional, Peralta, Carmen, additional, Varela‐Rey, Marta, additional, and Martínez‐Chantar, María Luz, additional
- Published
- 2021
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23. Chemoenzymatic synthesis of complex N-glycans of the parasite S.mansoni to examine the importance of epitope presentation on DC-SIGN recognition
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Srivastava, Apoorva D, Unione, Luca, Bunyatov, Mehman, Gagarinov, Ivan A, Abrescia, Nicola G A, Delgado, Sandra, Arda, Ana, Boons, Geert-Jan, Afd Chemical Biology and Drug Discovery, Sub Chemical Biology and Drug Discovery, and Chemical Biology and Drug Discovery
- Subjects
glycan ,Chemistry(all) ,glycosyl transferase ,cryo-EM ,chemoenzymatic synthesis ,NMR ,Catalysis - Abstract
The importance of multivalency for N-glycan-protein interactions has primarily been studied by attachment of minimal epitopes to artificial multivalent scaffold and not in the context of multi-antennary glycans. N-glycans can be modified by bisecting GlcNAc, core xylosides and fucosides, and extended N-acetyl lactosamine moieties. The impact of such modifications on glycan recognition are also not well understood. We describe here a chemoenzymatic methodology that can provide N-glycans expressed by the parasitic worm S. mansoni having unique epitopes at each antenna and containing core xyloside. NMR, computational and electron microscopy were employed to investigate recognition of the glycans by the human lectin DC-SIGN. It revealed that core xyloside does not influence terminal epitope recognition. The multi-antennary glycans bound with higher affinity to DC-SIGN compared to mono-valent counterparts, which was attributed to proximity-induced effective concentration. The multi-antennary glycans cross-linked DC-SIGN into a dense network, which likely is relevant for antigen uptake and intracellular routing.
- Published
- 2021
24. Chemoenzymatic Synthesis of Complex N ‐Glycans of the Parasite S. mansoni to Examine the Importance of Epitope Presentation on DC‐SIGN recognition
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Srivastava, Apoorva D., primary, Unione, Luca, additional, Bunyatov, Mehman, additional, Gagarinov, Ivan A., additional, Delgado, Sandra, additional, Abrescia, Nicola G. A., additional, Ardá, Ana, additional, and Boons, Geert‐Jan, additional
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- 2021
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25. Cross-Linking Effects Dictate the Preference of Galectins to Bind LacNAc-Decorated HPMA Copolymers
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Bertuzzi, Sara, primary, Gimeno, Ana, additional, Martinez-Castillo, Ane, additional, Lete, Marta G., additional, Delgado, Sandra, additional, Airoldi, Cristina, additional, Rodrigues Tavares, Marina, additional, Bláhová, Markéta, additional, Chytil, Petr, additional, Křen, Vladimír, additional, Abrescia, Nicola G. A., additional, Ardá, Ana, additional, Bojarová, Pavla, additional, and Jiménez-Barbero, Jesús, additional
- Published
- 2021
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26. Insights into Hepatitis C Virus E2core Interactions with Human Cellular Receptor CD81 at Different pHs from Molecular Simulations.
- Author
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Risueño, Cristina, Abrescia, Nicola G A, and Coluzza, Ivan
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- 2022
- Full Text
- View/download PDF
27. Chemoenzymatic synthesis of complex N-glycans of the parasite S.mansoni to examine the importance of epitope presentation on DC-SIGN recognition
- Author
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Afd Chemical Biology and Drug Discovery, Sub Chemical Biology and Drug Discovery, Chemical Biology and Drug Discovery, Srivastava, Apoorva D, Unione, Luca, Bunyatov, Mehman, Gagarinov, Ivan A, Abrescia, Nicola G A, Delgado, Sandra, Arda, Ana, Boons, Geert-Jan, Afd Chemical Biology and Drug Discovery, Sub Chemical Biology and Drug Discovery, Chemical Biology and Drug Discovery, Srivastava, Apoorva D, Unione, Luca, Bunyatov, Mehman, Gagarinov, Ivan A, Abrescia, Nicola G A, Delgado, Sandra, Arda, Ana, and Boons, Geert-Jan
- Published
- 2021
28. Bacteriophage PRD1 as a nanoscaffold for drug loading
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Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), European Commission, Eusko Jaurlaritza, CIC bioGUNE, Wellcome, Medical Research Council (UK), Duyvesteyn, Helen M. E., Santos-Pérez, Isaac, Peccati, Francesca, Martínez-Castillo, Ane, Walter, Thomas S., Reguera, David, Goñi, Félix M., Jiménez-Osés, Gonzalo, Oksanen, Hanna M., Stuart, David I., Abrescia, Nicola G. A., Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), European Commission, Eusko Jaurlaritza, CIC bioGUNE, Wellcome, Medical Research Council (UK), Duyvesteyn, Helen M. E., Santos-Pérez, Isaac, Peccati, Francesca, Martínez-Castillo, Ane, Walter, Thomas S., Reguera, David, Goñi, Félix M., Jiménez-Osés, Gonzalo, Oksanen, Hanna M., Stuart, David I., and Abrescia, Nicola G. A.
- Abstract
Viruses are very attractive biomaterials owing to their capability as nanocarriers of genetic material. Efforts have been made to functionalize self-assembling viral protein capsids on their exterior or interior to selectively take up different payloads. PRD1 is a double-stranded DNA bacteriophage comprising an icosahedral protein outer capsid and an inner lipidic vesicle. Here, we report the three-dimensional structure of PRD1 in complex with the antipsychotic drug chlorpromazine (CPZ) by cryo-electron microscopy. We show that the jellyrolls of the viral major capsid protein P3, protruding outwards from the capsid shell, serve as scaffolds for loading heterocyclic CPZ molecules. Additional X-ray studies and molecular dynamics simulations show the binding modes and organization of CPZ molecules when complexed with P3 only and onto the virion surface. Collectively, we provide a proof of concept for the possible use of the lattice-like organisation and the quasi-symmetric morphology of virus capsomers for loading heterocyclic drugs with defined properties.
- Published
- 2021
29. Minimal epitope for Mannitou IgM on paucimannose-carrying glycoproteins
- Author
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Robakiewicz, Stefania, primary, Bridot, Clarisse, additional, Serna, Sonia, additional, Gimeno, Ana, additional, Echeverria, Begoña, additional, Delgado, Sandra, additional, de Ruyck, Jérôme, additional, Semwal, Shubham, additional, Charro, Diego, additional, Dansercoer, Ann, additional, Verstraete, Kenneth, additional, Azkargorta, Mikel, additional, van Noort, Kim, additional, Wilbers, Ruud H P, additional, Savvides, Savvas N, additional, Abrescia, Nicola G A, additional, Arda, Ana, additional, Reichardt, Niels C, additional, Jiménez-Barbero, Jesús, additional, and Bouckaert, Julie, additional
- Published
- 2021
- Full Text
- View/download PDF
30. Insights into assembly from structural analysis of bacteriophage PRD1
- Author
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Abrescia, Nicola G. A., Cockburn, Joseph J. B., Grimes, Jonathan M., Sutton, Geoffrey C., Diprose, Jonathan M., Butcher, Sarah J., Fuller, Stephen D., San Martin, Carmen, Burnett, Roger M., Stuart, David I., Bamford, Dennis H., and Bamford, Jaana K. H.
- Subjects
Environmental issues ,Science and technology ,Zoology and wildlife conservation - Abstract
Author(s): Nicola G. A. Abrescia [1, 5]; Joseph J. B. Cockburn [1, 2, 5]; Jonathan M. Grimes [1]; Geoffrey C. Sutton [1]; Jonathan M. Diprose [1]; Sarah J. Butcher [3]; [...]
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- 2004
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- View/download PDF
31. Membrane structure and interactions with protein and DNA in bacteriophage PRD1
- Author
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Cockburn, Joseph J. B., Abrescia, Nicola G. A., Grimes, Jonathan M., Sutton, Geoffrey C., Diprose, Jonathan M., Benevides, James M., Thomas, Jr, George J., Bamford, Jaana K. H., Bamford, Dennis H., and Stuart, David I.
- Subjects
Environmental issues ,Science and technology ,Zoology and wildlife conservation - Abstract
Author(s): Joseph J. B. Cockburn [1, 2]; Nicola G. A. Abrescia [1]; Jonathan M. Grimes [1]; Geoffrey C. Sutton [1]; Jonathan M. Diprose [1]; James M. Benevides [3]; George J. [...]
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- 2004
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- View/download PDF
32. Nickel-guanine interactions in DNA: crystal structure of nickel-d[CGTGTACACG]2
- Author
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Abrescia, Nicola G., Huynh-Dinh, Tam, and Subirana, Juan A.
- Published
- 2002
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- View/download PDF
33. What Does it Take to Make a Virus: The Concept of the Viral 'Self'
- Author
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Abrescia, Nicola G. A., primary, Grimes, Jonathan M., additional, Fry, Elizabeth E., additional, Ravantti, Janne J., additional, Bamford, Dennis H., additional, and Stuart, David I., additional
- Published
- 2010
- Full Text
- View/download PDF
34. Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA
- Author
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Wojtas, Magdalena N., Mogni, Maria, Millet, Oscar, Bell, Stephen D., and Abrescia, Nicola G. A.
- Published
- 2012
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35. Bacteriophage PRD1 as a nanoscaffold for drug loading
- Author
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Duyvesteyn, Helen M. E., primary, Santos-Pérez, Isaac, additional, Peccati, Francesca, additional, Martinez-Castillo, Ane, additional, Walter, Thomas S., additional, Reguera, David, additional, Goñi, Felix M., additional, Jiménez-Osés, Gonzalo, additional, Oksanen, Hanna M., additional, Stuart, David I., additional, and Abrescia, Nicola G. A., additional
- Published
- 2021
- Full Text
- View/download PDF
36. Structural Characterization of N‐Linked Glycans in the Receptor Binding Domain of the SARS‐CoV‐2 Spike Protein and their Interactions with Human Lectins
- Author
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Lenza, Maria Pia, primary, Oyenarte, Iker, additional, Diercks, Tammo, additional, Quintana, Jon Imanol, additional, Gimeno, Ana, additional, Coelho, Helena, additional, Diniz, Ana, additional, Peccati, Francesca, additional, Delgado, Sandra, additional, Bosch, Alexandre, additional, Valle, Mikel, additional, Millet, Oscar, additional, Abrescia, Nicola G. A., additional, Palazón, Asís, additional, Marcelo, Filipa, additional, Jiménez‐Osés, Gonzalo, additional, Jiménez‐Barbero, Jesús, additional, Ardá, Ana, additional, and Ereño‐Orbea, June, additional
- Published
- 2020
- Full Text
- View/download PDF
37. Sensitive detection of SARS-CoV-2 seroconversion by flow cytometry reveals the presence of nucleoprotein-reactive antibodies in unexposed individuals
- Author
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Egia-Mendikute, Leire, primary, Bosch, Alexandre, additional, Prieto-Fernández, Endika, additional, Lee, So Young, additional, Jiménez-Lasheras, Borja, additional, del Río, Ana García, additional, Antoñana-Vildosola, Asier, additional, Bruzzone, Chiara, additional, Bizkarguenaga, Maider, additional, Embade, Nieves, additional, Gil-Redondo, Rubén, additional, Martínez-Chantar, María Luz, additional, López-Hoyos, Marcos, additional, Abrescia, Nicola G A, additional, Mato, Jose M., additional, Millet, Oscar, additional, and Palazón, Asís, additional
- Published
- 2020
- Full Text
- View/download PDF
38. Virus crystallography
- Author
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Fry, Elizabeth E., primary, Abrescia, Nicola G. A., additional, and Stuart, David I., additional
- Published
- 2007
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- View/download PDF
39. The cryo-EM structure of African swine fever virus unravels a unique architecture comprising two icosahedral protein capsids and two lipoprotein membranes
- Author
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Andrés, Germán, Charro, Diego, Matamoros, Tania, Dillard, Rebecca S., and Abrescia, Nicola G. A.
- Subjects
viruses - Abstract
African swine fever virus (ASFV) is a complex nucleocytoplasmic large DNA virus (NCLDV) that causes a devastating swine disease currently present in many countries of Africa, Europe, and Asia. Despite intense research efforts, relevant gaps in the architecture of the infectious virus particle remain. Here, we used single-particle cryo-EM to analyze the three-dimensional structure of the mature ASFV particle. Our results show that the ASFV virion, with a radial diameter of ~2,080 Å, encloses a genome-containing nucleoid surrounded by two distinct icosahedral protein capsids and two lipoprotein membranes. The outer capsid forms a hexagonal lattice (triangulation number T = 277) composed of 8,280 copies of the double jelly-roll major capsid protein (MCP) p72, arranged in trimers displaying a pseudo-hexameric morphology, and of 60 copies of a penton protein at the vertices. The inner protein layer, organized as a T = 19 capsid, confines the core shell, and it is composed of the mature products derived from the ASFV polyproteins pp220 and pp62. Also, an icosahedral membrane lies between the two protein layers, whereas a pleomorphic envelope wraps the outer capsid. This high-level organization confers to ASFV a unique architecture among the NCLDVs that likely reflects the complexity of its infection process and may help explain current challenges in controlling it.
- Published
- 2020
40. Contributory presentations/posters
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Gries, A., Singh, Balwinder, Nakazawal, Chicko, Genest, D., Getzoff, E. D., Matsuo, H., Kaur, Harpreet, Borst, J. W., Chadha, K. C., Tingyun, Kuang, Jagannadham, M. V., Leijon, Mikael, Sato, S., Bhakuni, Vlnod, Vijayan, M., Surolia, A., Suguna, K., Manoj, N., Srinivas, V. R., Ravishankar, R., Laggner, P., Prassl, R., Schwarzenbacher, R., Zeth, K., Kostner, G. M., Taylor, Susan S., Xuong, Nguyen-huu, Akamine, Pearl, Sagar, Bidva M., Saikrishnan, K., Purnapatre, K., Handa, P., Roy, S., Varshney, U., Biswal, B. K., Sukumar, N., Rao, J. K. Mohana, Johnson, A., Pattabhi, Vasantha, Murthy, M. R. N., Krishna, Sri S., Savithri, H. S., Sastri, Mira, Hosur, M. V., Pillai, Bindu, Kannan, K. K., Kumar, Mukesh, Patwardhan, Swati, Padmanabhaa, B., Sasaki-Sugio, S., Matsuzaki, T., Nukaga, M., Singh, T. P., Sharma, A. K., Srinivasan, A., Khan, J. A., Paramasivam, M., Kumar, P., Karthikevan, S., Sharma, S., Yadav, S., Srintvasan, A., Alam, Neelima, Gourinath, S., Kaur, Punit, Chandra, Vikas, Betzel, Ch., Ghosh, S., Bera, A. K., Pal, A. K., Baneriee, Asok, Mukhopadhyay, B. P., Bhattacharya, S., Chakraborty, S., Haldar, U., Dey, I., Solovicova, Adriana, Sevcik, Jozef, Sekar, K., Sundaralingam, M., Genov, N., Liang, Dong-cai, Zhang, Ji-ping, Jiang, Tao, Chang, Wen-rui, Blommers, Marcel, Jahnke, Wolfgang, Hosur, R. V., Panchal, S. C., Pillay, Bindu, Jaganathan, N. R., Mathur, Puniti, Srivatsun, S., Joshi, Ratan Mani, Chauhan, V. S., Govil, Girjesh, Atreya, H. S., Sahu, S. C., Quinjou, Éric, Adjadj, Elisabeth, Mispelter, Joël, Izadi-Pruneyre, Nadia, Blouquit, Yves, Heyd, Bernadette, Lerat, Guilhem, Desmadreil, Michel, Milnard, Philippe, Lin, Y., Rao, B. D. Nageswara, Raghunathan, Vidva, Chau, Mei H., Coutinho, Evans, Pesais, Prashant, Srivastava, Sudha, Saran, Anil, Srikrishnan, Thamarapu, Lijima, Herbert, Gesme, Jayson, Sapico, Leizl F., Paxton, Raymond, Grace, C. R., Nagenagowda, G., Lynn, A. M., Cowsik, Sudha M., Govil, G., Sahu, Sarata C., Bhattacharya, A., Chauhan, S., Kumar, Anil, Zuiderweg, Erik R. P., Pellecchia, Maurizio, Nitta, Katsutoshi, Ohnishi, Atsushi, Kawano, Keiichi, Hikichi, Kunio, Fujitani, Naoki, Ohkubo, Tadayasu, Aizawa, Tomoyasu, Kumaki, Yasuhiro, Hayakawa, Yoichi, Parvathy, Rani V., Kini, R. M., Nakagawa, Astushi, Tanaka, Isao, Demura, Makoto, Yao, Min, Koshiba, Takumi, Kobashigawa, Yoshihiro, Kuwajima, Kunihiro, Linge, Jens, Nilges, Michael, Donoghue, Seán O., Chakshusmathi, G., Ratnaparkhi, Girish S., Madhu, P. K., Varadarajan, R., Tetreau, C., Tourbez, M., Lavalette, D., Bulone, D., Manno, M., Emanuele, A., Palma-Vittorelli, M. B., Palma, M. U., Vaiana, S. M., Martorana, V., Biagio, P. L. San, Chang, D. K., Cheng, S. F., Yang, S. H., Francis, S., Trivedi, V. D., Chien, W. J., Manstein, Dietmar J., Batra, Renn, Geeves, Michael A., Geller, Maciej, Trvlska, Joanna, Grochowski, Pawel, Lesyng, B., Ginalski, K., Grochowski, P., Lavalette, P., Blouquit, Y., Roccatano, D., Berendsen, H. J. C., Amadei, A., Nola, Di A., Ho, Bosco, Curmi, P. M. G., Berry, H., Pelta, J., Pauthe, E., Lairez, D., Srinivasan, M., Sahi, Shakti, Kothekar, V., Madhusudnan, Kartha S., Nandel, Fateh S., Jain, D. V. S., Berendsen, Herman J. C., Feenstra, Anton K., Tama, F., Sanejouand, Y.-H., Go, N., Sharma, Deepak, Pasha, Santosh, Sharma, Sunita, Brahmachari, Samir K., Makker, Jyoti, Viiavaraghavan, R., Kumar, S., Dey, Sharmisllia, Krishnamoorthy, G., Lakshmikanth, G. S., Zaitseva, E. M., Mazhul, V. M., Kierdaszuk, Borys, Widengren, J., Rigler, R., Terry, B., Mets, Ü., Swaminathan, R., Yathindra, N., Thamotharan, S., Chosrowjan, H., Mataga, N., Shibata, Y., Morisima, I., Xiao, Ming, Selvin, Paul, Chakraharty, Tania, Cooke, Roger, Faraone, A., Branca, C., Maisano, G., Migliardo, P., Magazù, S., Villari, V., Behere, Digambar V., Deva, Sharique Zahida Waheed M., Vallone, B., Savino, C., Travaglini-Allocatelli, C., Cutruzzolà, F., Brunori, M., Gibson, Q. H., Mazumdar, Shyamalava, Mitra, Samaresh, Prasad, Swati, Soto, P., Fayad, R., Tyulkova, N. A., Sukovataya, I. E., Mamedov, Sh. V., Aksakal, B., Canturk, M., Aktas, B., Yilgin, R., Bogutska, K. I., Miroshnichenko, N. S., Wein, A. J., Hypolite, J. A., DiSanto, M., Chacko, S., Zheng, Y-M., Antosiewicz, J., Wojciechowski, M., Grycuk, T., Di Nola, Alfredo, Ceruso, Marc A., Chatterjee, Bishnu P., Bandvopadhvay, Subhasis, Choudhury, Devapriva, Khight, Stefan, Thompson, Andrew, Stojanoff, Vivian, Pinkner, Jerome, Hultgren, Scott, Flatters, Delphine, Goodfellow, Julia, Takazawatt, Fumi, Kanehisa, Minoru, Sasai, Masaki, Nakamura, Hironori, Wang, Bao Han, Pan, xin Min, Zheng, Yuan, Wang, Zhi Xin, Ahmad, Atta, Kulkarni, Sangeeta, Prakash, Koodathingal, Prajapati, Shashi, Surin, Alexey, Kihara, Hiroshi, Yang, Li, Matsumoto, Tomoharu, Nakagawa, Yuki, Semisotnov, Gennady V., Kimura, Kazumoto, Amemiya, Yoshiyuki, Tayyab, Saad, Muzammil, Salman, Kumar, Yogesh, Bhakuni, Vinod, Sundd, Monica, Kundu, Suman, Jagannadham, Medicherla V., Chandani, Bina, Warrier, Deepti, Sinha, Lalankumar, Dhar, Ruby, Mehrotra, Sonam, Khandelwal, Purnima, Seth, Subhendu, Gidwani, Arun, Prabha, Ratna C., Sasidhar, Y. U., Madhusudan, K. P., Nishikawa, Ken, Kinjo, Akira R., Varadarajan, Raghavan, Chakravarty, Suvobrata, Van Dael, H., Noyelle, K., Joniau, M., Haezebrouck, P., Jha, Indra Brata, Bhat, Rajiv, Dash, Sheffali, Mohanty, Prasanna, Bandyopadhyay, A. K., Sonawat, H. M., Rao, Ch. Mohan, Datta, Siddhartha, Raman, B., Rajaraman, K., Ramakrishna, T., Pande, A., Benedek, G., King, J., Betts, S., Pande, J., Asherie, N., Ogun, O., Kalacheva, G. S., Sokolova, I. V., Mitaku, Shigeki, Sonoyama, Masashi, Taira, Kunihiro, Yokoyama, Yasunori, Sasakil, Takanori, Kamo, Naoki, Mukai, Yuri, Dalal, Seema, Regan, Lynne, Mituku, Shigeki, Kumar, Devesh, Roychoudhury, Mihir, Lőrinczv, Dénes, Könczöl, Franciska, Farkas, László, Belagyi, Joseph, Schick, Christoph, Thomson, Christy A., Ananthanarayanan, Vettai S., Alirzayeva, E. G., Baba-Zade, S. N., Sarai, A., Kono, H., Uedaira, H., An, J., Gromiha, Michael M., Oobatake, M., Yutani, Katsuhide, Takano, Kazufumi, Yamagata, Yuriko, Jas, Gouri S., Hofrichter, James, Muñoz, Victor, Eaton, William A., Penoyar, Jonathan, Lo Verde, Philip T., Bódi, Á., Venekei, I., Kardos, J., Gráf, L., Závodszky, P., Szilágyi, András, Závodszky, Péter, Woolfson, D. N., Walshaw, J., Allan, R. D., Funahashi, Jun, Gupta, Savan, Di Nola, A., Mangoni, M., Roccatano, P., Ramachandraiah, Gosu, Chandra, Nagasuma R., Ciani, Barbara, Woolfson, Derek N., Nair, Usha B., Salunke, Dinakar M., Kaur, Kanwal J., Swaminathan, Chittoor P., Surolia, Avadhesha, Pramanik, A., Jörnvall, H., Nygren, P.-Å., Jonasson, P., Ståhl, S., Johansson, B.-L., Kratz, G., Wahren, J., Ekberg, K., Uhlén, M., Jansson, O. T., Uhlén, S., Misselwitz, Rolf, Welfle, Heinz, Welfle, Karin, Höhne, Wolfgang, Kurganov, B. I., Mitskevich, L. G., Fedurkina, N. V., Jarori, Gotam K., Maity, Haripada, Guharay, J., Sengupta, P. K., Sengupta, B., Sridevi, K., Kasturi, S. R., Gupta, S. P., Agarwal, Gunjan, Briehl, Robin W., Kwong, Suzanne, Tyulkova, N A., Ismailova, O. I., Parola, A. H., Yayon, A., Hariharan, C., Pines, D., Pines, E., Zamai, M., Cohen-Luria, R., Woolfeon, D. N., Spooner, G. A., Padya, M. J., Bharadwaj, D. K., Bakshi, Panchan, Jagannathan, N. R., Sharma, U., Srivastava, N., Barthwal, R., Matsuda, Keiko, Nishioka, Takaaki, Go, Nobuhiro, Urata, S., Aita, T., Husimi, Y., Majumder, Mainak, Subirana, Juan A., Malinina, Lucy, Abrescia, Nicola G. A., Aymami, Juan, Coll, Miquel, Eritxa, Ramón, Premraj, B. J., Thenmalarchelvi, R., Gautham, N., Kumar, Satheesh P., Kan, Lou-Sing, Hou, Ming, Lin, Shwu-Bin, Roy, Kanal B., Sana, Tapas, Bruant, N., Flatters, D., Lavery, R., Sklenar, Heinz, Rons, Remo, Lavery, Richard, Thakur, Ashoke Ranjan, Kundu, Sudip, Bandyopadhyay, Debashree, Bhattacharyya, Dhananjay, Majumdar, Rabi, Barceló, F., Portugal, J., Rao, B. J., Ramanathan, Sunita, Gliosli, Mahua, Varshney, Umesh, Kumar, Vinay N., Pataskar, Shashank S., Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Kolmdaivel, P., Maiti, Motilal, Das, Suman, Sen, Anjana, Xodo, Luigi, Suraci, Chiara, Del Terra, Elisa, Quadrifoglio, Franco, Diviacco, Silvia, Ray, Arghya, Rao, Basuthkar J., Karthikeyan, G., Chary, Kandala V. R., Mujeeb, Anwer, James, Thomas L., Bogdanov, A., Zanina, A., Haya, E. E. F., Kasyanenko, N., Cornélio, M. L., Bugs, M. R., Tolstorukov, Ye. M., Sanval, Nitish K., Tiwari, S. N., Sanyal, Nitish K., Choudhury, Mihir Roy, Patel, P. K., Bhavesh, Neel S., Gabrielian, Anna, Rigler, Rudolf, Edman, Lars, Wennmalm, Stefan, Constantinescu, B., Gazdaru, D., Radulcscu, I., Radu, L., Wärmländer, Sebastian, Aoki, Setsuyuki, Ishiura, Masahiro, Kondo, Takao, Pashinskaya, V. A., Kosevich, M. V., Shelkovsky, V. S., Blagoy, Yu. P., Wang, Ji-hua, Malathi, R., Chandrasekhar, K., Kandimalla, E. R., Agrawal, S., Rastogi, V. K., Palafox, Alcolea M., Singh, Chatar, Beniaminov, A. D., Minyat, E. E., Zdobnov, E. M., Ulyanov, N. B., Bondarenko, S. A., Ivanov, V. I., Singh, J. S., Tewari, Ravindra, Sonawane, Kailas D., Grosjean, Henri, Sonavane, Uddhavesh B., Morin, Annie, Doherty, Elizabeth A., Doudna, Jennifer A., Tochio, H., Shirakawa, M., Kyogoku, Y., Das, Achintya, Javaram, B., Kalra, Parul, Shukla, Piyush, Dixit, Surjit B., Beveridge, David L., McConnell, Kevin, Davidson, B. E., Chan, R. Y. S., Sawyer, W. H., Eccelston, J. F., Yan, Yuling, Norden, Bengt, Tuite, Eimer, Nielsen, Peter, Takahashi, Masayuki, Ghosh, Anirban, Bansal, Manju, Pingoud, Alfred, Christ, Frauke, Thole, Hubert, Pingoud, Vera, Wende, Wolfgang, Luthra, Pratibha Mehta, Chandra, Ramesh, Sen, Ranjan, Weisberg, Robert, King, Rodney, Gobets, Bas, van Amerongen, Herbert, van Stokkum, Ivo H. M., Larsen, Olaf F. A., van Grondelle, Rienk, Hilbers, Cornelis W., Heus, Hans A., Berends, Jos, Sngrvan, H E., Khudaverdian, N. V., Babayan, Yu. S., Pichierri, F., Gromiha, M., Prabakaran, P., Aida, M., Sayano, K., Merkienė, Eglė, Vilkaitis, Giedrius, Klimašauskas, Saulius, Serva, Saulius, Weinhold, Elmar, Bandiera, Antonella, Marsich, Eleonora, Manzini, Giorgio, Potikyan, G., Arakelyan, V., Babayan, Yu., Ninaber, Alex, Goodfellow, Julia M., Ohta, Shigeru, Ito, Yoichiro, Husimi, Yuzuru, Usukura, J., Aiba, H., Tagami, H., Nunes, Elia, Suarez, Mougli, Candreva, Carmen E., Keszenman, Deborah, Thyberg, Per, Földes-Papp, Zeno, Joshi, Amita, Singh, Dinesh, Rajeswari, M. R., Amenitsch, H., Pregetter, M., Chapman, J., Mishra, K. P., Pandev, B. N., Tonevitsky, A. G., Pohl, E. E., Agapov, I. I., Sun, J., Pohl, P., Dennison, S. M., Gorbeako, G. P., Dynbko, T. S., Mishra, A. K., Pappavee, N., Luis, Loura, Rodrigo, Almeida, Manuel, Prieto, Gendel, Ya. L., Kleszczyńska, H., Kuczera, J., Przestalski, S., Kral, T., Chernitsky, E. A., Senkovich, O. A., Rosin, V. V., Gasanov, R. A., Allakhverdieva, Y. M., Papageorgiou, G. C., Savopol, Tudor, Apetrei, Calin, Balea, Marius, Cucu, D., Mihailescu, D., Ramanathan, K. V., Bačić, Goran, Genest, Monique, Sajot, Nicolas, Garnier, Norbert, Crouzy, Serge, Zsiros, O., Várkonyi, Z. S., Combos, Z., Farkas, T., Cribier, Sophie, de Paula, F., Fraceto, I. F., Schreier, S., Spisni, A., Sevšek, F., Žekš, B., Gomišček, G., Svetina, S., Arrigler, V., Hotani, Hirokazu, Nomura, Fumimasa, Takiguchi, Kingo, Nagata, Miki, Panicker, Lata, Parvathanathan, P. S., Hotani, H., Takiguchi, K., Ishino, A., Saitoh, A., Afonin, S., Takahashi, A., Takizawa, T., Nakato, Y., Marathe, Dipti, Jørgensen, Kent, Chattopadhyay, Amitabha, Rukmini, R., Rawat, Satinder S., Pečar, S., Štrancar, J., Šentiurc, M., Stolič, Z., Filipin, K., Biswas, S. C., Samanta, Anunay, Sana, Satyen, Kinoshita, Koji, Yamazaki, Masahito, Ohki, Kazuo, Goto, Akira, Kiuchi, Tai, Kumeta, Takaaki, Ohba, Tetsuhiko, Sugar, I. P., Thompson, K. K., Biltonen, R. L., Thompson, T. E., Ichinose, H., Suezaki, Y., Akivama, M., Matuoka, S., Tsuchihashi, K., Gasa, S., Pike, H. M., Mattjus, P., Brown, R. E., Molotkovsky, J. G., Arora, Ashish, Kleinschmidt, Jörg H., Tamm, Lukas K., Kruglyakova, K. E., Luneva, O. G., Fedin, V. A., Kuptsoya, O. S., Visser, A. J. W. G., Visser, N. V., Dyubko, T. S., Ogihara, Toshihiko, Mishima, Kiyoshi, Shvaleva, A. L., Radenović, Č. N., Jeremić, M. G., Radenović, N. Č., Minić, P. M., Salakhutdinov, B. A., Aripov, T. F., Tadjibaeva, E. T., Zamaraeva, M. V., Vagina, O. N., Basak, A. K., Cole, A., Naylor, C., Poppofl, M., Titball, R., Naylor, C. E., Moss, D. S., Eaton, J. T., Justin, N., Titball, R. W., Nomura, F., Nagata, M., Ishjkawa, S., Takahashi, S., Obuchi, Kaoru, Staudegger, Erich, Lohner, Karl, Kriechbaum, Manfred, Waring, Alan J., Lehrer, Robert I., Mayer, Bernd, Köhler, Gottfried, Gangl, Susanne, Shobini, J., Hu, B., Lortz, B., Sackmann, E., Guttenberg, Z., Antonovich, A. N., Slobozhanina, E. I., Lukyanenko, L. M., Kozlova, N. M., Krylov, Andrey V., Kotova, Elena A., Antonenko, Yuri N., Yaroslavov, Alexander A., Ghosh, Subhendu, Bera, Amal K., Das, Sudipto, Urbánková, Eva, Freeman, Karl, Jelokhani-Niaraki, Masood, Jezek, Petr, Usmanov, P. B., Tonkikh, A. K., Ongarbaev, A., Pohl, Peter, Saparov, Sapar M., Harikumar, P., Reeves, J. P., Sikdar, S. K., Rao, S., Ghatpande, A. S., Corsso, C., Varanda, W. A., ElHamel, C., Dé, E., Molle, G., Saint, N., Varshney, Anurae, Mathew, M. K., Isacoff, E. Y., Loots, E., Kasai, Michiki, Yamaguchi, Naohiro, Ghosh, Paramita, Tigyi, Joseph, Miledi, Ricardo, Tigyi, Gabor, Liliom, Karoly, Djurisic, Maja R., Andjus, Pavle R., Shrivastava, Indira H., Sansom, M. S. P., Barrias, C., Oliveira, P. F., Lopes, I. A., Mauricio, A. C., Fedorovich, S. V., Konev, S. V., Sholukh, M. V., Chubanov, V. S., Klevets, M., Fedirko, N., Shvinka, N., Manko, V., Prabhananda, B. S., Kombrabail, Mamata H., Aravamudhan, S., Venegas-Cotero, Berenice, Blake, Ivan Ortega, Zhou, Han-qing, Hu, Xiao-jian, Zhang, Zhi-hong, Feng, Hang-fang, Cheng, Wei-ying, Zalyvsky, I. A., Dubitsky, L. O., Vovkanvch, L. S., Savio-Galimberti, E., Ponce-Homos, J. E., Bonazzola, P., Capurro, Claudia, Parisi, Mario, Toriano, Roxana, Thomas, David D., Ready, Laxma G., Jones, Larry R., Tashmukhamedov, B. A., Sagdullaev, B. T., Heitzmann, D., Bleich, M., Warth, R., Ferreira, H. G., Ferreira, K. T. G., Greger, R., Parola, Abraham H., Alfahel, Essa, Zagoory, Orna, Priel, Zvi, Hama-Inaba, H., Ohyama, H., Hayata, I., Choi, K., Haginoya, K., Mori, M., Wang, R., Yukawa, O., Nakajima, T., Joshi, Nanda B., Kannurpatti, Sridhar K., Sinha, Mau, Joshi, Preeti G., Bei, Ling, Hu, Tianhui, Shen, Xun, Knetsch, Menno L. W., Schäfers, Nicole, Sandblom, John, Galvanovskis, Juris, Kovacs, Eugenia, Dinu, Alexandra, Pologea-Moraru, Roxana, Sanghvi, S. H., Jazbinšek, V., Tronteli, Z., Thiel, G., Wübeller, G., Müller, W., Brumen, Milan, Fajmut, Leš, Marhl, Marko, Volotovski, I. D., Sokolovski, S. G., Knight, M. R., Chalyi, Alexander V., Vasilʼev, Alexei N., Sharma, P., Pant, H. C., Sharma, M., Amin, N. D., Albers, R. W., Steinbach, P. J., Barchir, J., Balasubramanyam, M., Gardner, J. P., Condrescu, M., Pilarczyk, Gotz, Greulich, K. O., Monajembashi, Shamci, El-Awadi, A. I., El-Refaei, F. M., Talaat, M. M., Ali, F. M., Zahradniková, Alexandra, Tahradník, Ivan, Pavelková, Jana, Zhorov, Boris S., Ananthanaravanan, Vettai S., Weiss, D. G., Martin, D., Gornik, E., Neu, E., Michailov, Ch. M., Welscher, U., Seidenbusch, W., Jellali, A., Pattnaik, B. R., Hicks, D., Dreyfus, H., Sahel, J., Picaud, S., Forster, V., Wang, Hong-Wei, Sui, Sen-fang, Luther, Pradeep K., Morris, Ed, Barry, John, Squire, John, Sundari, Sivakama C., Balasubramanian, D., Christlet, Hema Thanka T., Veluraia, K., Suresh, Xavier M., Laretta-Garde, V., Krilov, Dubravka, Herak, Janko N., Stojanović, Nataša, Ferrone, Frank A., Ivanova, Maria, Jasuja, Ravi, Mirchev, Rossen, Stopar, David, Wolfs, Cor J. A. M., Hemminga, Marcus A., Spruijt, Ruud B., Arcovito, G., De Spirito, M., Frank, Joachim, Heagle, Amy B., Grassucci, Robert, Penczek, Pawel, Agrawal, Rajendra K., Sharma, Manjuli R., Wagenknecht, Terence, Jeyakumar, Loice H., Fleischer, Sidney, Knupp, Carlo, Squire, John M., Ezra, Eric, Munro, Peter M. G., Kitazawa, Hidefumi, Ichihara, Koji, Itoh, Tomohiko J., Iguchi, Yusuke, Pifat, Greta, Kveder, Marina, Pečar, Slavko, Schara, Milan, Nair, Deepak, Singh, Kavita, Rao, Kanury V. S., Sundaravadivel, B., Jain, Deepti, Kaur, Kanwaljeet, Salunke, D. M., Goel, Manisha, Kovalenko, E. I., Semenkova, G. N., Cherenkevich, S. N., Loganathan, D., Lakshmanan, T., Sriram, D., Srinivasan, S., Lebrón, J. A., Bjorkman, P. J., Ramalingam, T. S., Singh, A. K., Gayatri, T. N., Bisch, Paulo M., Caffarena, Ernesto R., Grigera, Raul J., Fromherz, P., Kiessling, V., Suresh, C. G., Rao, K. N., Khan, M. I., Gaikwad, S. M., Elanthiraiyan, M., Kaliannan, P., Payne, J., Chadha, K., Ambrus, J. L., Nair, M. P. N., Nair, Madhavan P. N., Hewitt, R., Schwartz, S. A., Mahajan, S., Macherel, D., Bourguignon, J., Neuburger, M., Douce, R., Cohen-Addad, C., Faure, M., Ober, R., Sieker, L., Gurumurthy, D. S., Velmurugan, S., Lobo, Z., Phadke, Ratna S., Desai, Prashant, Alieva, D. R., Guseinova, I. M., Zulfugarov, I. S., Aliev, J. A., Ismayilov, M. A., Novruzova, S. N., Savchenko, T. V., Suleimanov, Yu. S., Bartošková, Hana, Nauš, Jan, Ilík, Petr, Kouřil, Roman, Vidyasagar, P. B., Thomas, Sarah, Gaikwad, Jvoti U., Cseh, Z., Mustárdy, L., Garab, G., Simidjiev, I., Rajagopal, S., Várkonyi, Zs., Holzenburg, A., Stoylova, S., Papp, E., Millar, D. P., Bruder, R., Woo, T. T., Genick, U. K., Gerwert, K., Jávorfí, Tamás, Garab, Győző, Naqvi, Razi K., Gaikwad, Jyoti, Kalimullah, Md., Semwal, Manoj, Naus, Man, Ilik, Petr, Kouril, Roman, Horváth, Gábor, Bernard, Gary D., Pomozi, István, Wehner, Rüdiger, Damjanović, Ana, Schulten, Klaus, Ritz, Thorsten, Yandao, Gong, Jushuo, Wang, Nanming, Zhao, Jixiu, Shan, Freiberg, Arvi, Timpmann, Kõu, Woodbury, Neal W., Ruus, Rein, Nemtseva, E. V., Kudryasheva, N. S., Sizykh, A. G., Tikhomirov, A. A., Nesterenko, T. V., Shikhov, V. N., Forti, Giorgio, Furia, Alberto, Finazzi, Giovanni, Barbagallo, Romina Paola, Agalarov, R., Gasanov, R., Iskenderova, S., Nobuhiro, G. O., Osamu, Miyashita, Ramrakhiani, M., Soni, R. K., Yoshida, Masasuke, Akutsu, Hideo, Yagi, Hiromasa, Tozawa, Kacko, Sekino, Nobuaki, Iwabuchi, Tomoyuki, Kaulen, A. D., Avetisyan, A. V., Feniouk, B. A., Skulachev, V. P., Breyton, Cécile, Kühlbrandt, Werner, Gräslund, Astrid, Assarsson, Maria, Libisch, B., Horváth, G., Gombos, Z., Budagovskaya, N. V., Kudryasheva, N., Fukunishi, Arima, Harada, Erisa, Fukuoka, Yuki, Ohmura, Tomoaki, Kawai, Gota, Watanabe, Kimitsuna, Žekš, Boštjan, Božič, Bojan, Derganc, Jure, Svetina, Saša, Hoh, J. F. Y., Li, Z. B., Rossmanith, G. H., Frederix, P. L. T. M., de Beer, E. L., Treijtel, B. W., Blangè, T., Galtet, F., Hénon, S., Isabey, D., Planus, E., Laurent, V., Rath, L. S., Raval, M. K., Dash, P. K., Ramakrishnan, C., Balaram, R., Basak, Kanika, Balaban, Alexandra T., Nandy, Ashesh, Grunwald, Gregory D., Vracko, Marjan, Randic, Milan, Basak, Subhash C., Amic, Dragan, Beslo, Drago, Trinajstic, Nenad, Nikolic, Sonja, Walahaw, J., Lensink, Marc F. J., Reddy, Boojala V. B., Shindylov, Ilya N., Bourne, Philip E., Grigera, J. R., de Xammar Oro, J., Donnamaria, M. C., Neagu, Monica, Neagu, Adrian, Janežič, Dušanka, Praprotnik, Matej, Nilsson, Lennart, Mark, Pekka, Fata, La L., Dardenne, Laurent E., Werneck, Araken S., Neto, Marçal de O., Kannan, N., Vishveshwara, S., Veluraja, K., Opitz, David, Balasubramanian, Krishnan, Gute, Brian D., Mills, Denise, Lungeanu, Diana, Mihalas, G. I., Macovievici, G., Gruia, Raluca, Dalcin, B., Cortez-Maghelly, C., Passos, E. P., Ljubisavljevic, M., Blesic, S., Milosevic, S., Stratimirovic, D. J., Bachhawat, Nandita, Mande, Shekhar C., Nandy, A., Nishigaki, Koichi, Saito, Ayumu, Naimuddin, Mohammed, Takaesu, Hirotomo, Ono, Mitsuo, Hirokawa, Takatsugu, Eissa, A. M., Ahmed, Abdalla S., El Gohary, M. I., Nakashima, Hiroshi, Raghava, G. P. S., Kurgalvuk, N., Goryn, O., Gerstman, Bernard S., Kratasyuk, V. A., Esimbekova, E. N., Gritsenko, E. V., Remmel, N. N., Maznyak, O. M., German, A., Tikhonov, A., Tchitchkan, D., Koulchitsky, S., Pashkevich, S., Pletnev, S., Kulchitsky, V., Pesotskaya, Y., Shapiro, Erik M., Borthakur, Arijitt, Dimitrov, Ivan, Leigh, John S., Rizi, Rahim, Reddy, Ravinder, Charagundla, Sridhar, Duvvuri, Umamaheswar, Degaonkar, M., Khubchandani, M., Kumar, Mahesh, Jagannathan, N R., Raghunathan, P., Jayasundar, Rama, Coshic, O., Rath, O. K., Julka, P. K., Iliescu, Karina Roxana, Sajin, Maria, Petcu, Ileana, Moisoi, Nicolcta, Kuzmenko, A. I., Donchenko, G. V., Nikolenko, I. A., Morozova, R. P., Rahman, M. K., Ahmed, M. M., Watanabe, Takehiro, Uretzky, G., Ammar, R., Sharony, R., Rubin, Y., Gilboa, H., Mallick, H. N., Kumar, Mohan V., Begum, Gulnaz M., Degaonkar, Mahaveer N., Govindasamy, S., Kumosani, T. A., Lupusoru, C., Titescu, G., Haulica, I., Stefanescu, I., Iliescu, R., Nastasa, V., Bild, W., Khetawat, Gopal, Nealen, M., Faraday, N., Bray, P. F., Noga, S., Lycholat, E. A., Ananieva, T. V., Kosevich, M V., Stepanyan, S. G., Antonyuk, S. V., Khachatryan, A., Kumar, A., Arakelian, H., Khachatryan, R., Agadjanyan, S., Ayrapetyan, S., Mkheyan, V., Rajan, S. S., Kabaleeswaran, V., Gopalakrishnan, Geetha, Govindachari, T. R., Ramrakhiani, Meera, Cullen, David C., Lowe, Phillip, Badley, Andrew, Hermel, H., Möhwald, H., Schmahl, W., Singh, Anil K., Das, Joydip, Majumdar, Nirmalya, Dér, András, Oroszi, László, Kelemen, Loránd, Ormos, Pál, Hámori, András, Ramsden, Jeremy J., Mitra, Chanchal K., Savitri, D., Yanagida, Toshio, Esaki, Seiji, Sowa, Yosiyuki, Nishida, Tomoyuki, Kimura, Yuji, Radu, M., Laukhina, E. E., Kasumova, L. A., Koltover, V. K., Bubnov, V. P., Estrin, Ya. I., Dotta, Rajiv, Zahradník, Ivan, Marko, Milan, Novák, Pavel, Miyata, Hidetake, Hirata, Hiroaki, Sengupta, P., Maiti, S., Balaji, J., Banerjee, S., Barker, A. L., Winlove, C. P., OʼHare, D., Macpherson, J. V., Gonsalves, M., Unwin, P. R., Phillip, R., Kumar, Ravindra G., Murata, K., Nagayaka, K., Danev, R., Sugitani, S., Gősch, Michael, Thyberg, P., Földes-Papp, Z., Björk, G., Blom, H., Holm, J., Heino, T., Inagaki, Fuyuhiko, Yokochi, Masashi, Kusunoki, Masami, Matthews, E. K., Pines, J., Chukova, Yu. P., Koltover, Vitaly K., Kang, B. P. S., Bansal, Geetanjali, Bansal, M. P., Singh, U., Singh, Uma, Nakata, Kotoko, Nakano, Tastuya, Kaminuma, Tsuguchika, Kirn, Bonn, Potocnik, Neja, Stare, Vito, Shukla, Latal, Sastry, M. D., Natarajan, V., Devasagayam, T. P. A., Kesavan, P. C., Sayfutdinov, R., Degermendzhy, A. G., Adamovich, V. V., Rogozin, Yu. D., Khetrapal, C. L., Gowda, G. A. Nagana, Ghimire, Kedar Nath, Masaru, Ishida, Fujita, H., Ishiwata, S., Suzuki, M., Kawahara, S., Kirino, Y., Kishimoto, Y., Mori, H., Mishina, M., Ohshima, H., Dukhin, A. S., Goetz, P. J., Shilov, V. N., and Mishra, R. K.
- Published
- 1999
- Full Text
- View/download PDF
41. Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus
- Author
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Kotecha, Abhay, Wang, Quan, Dong, Xianchi, Ilca, Serban L., Ondiviela, Marina, Zihe, Rao, Seago, Julian, Charleston, Bryan, Fry, Elizabeth E., Abrescia, Nicola G. A., Springer, Timothy A., Huiskonen, Juha T., and Stuart, David I.
- Subjects
Integrins ,Binding Sites ,Science ,viruses ,Amino Acid Motifs ,Cryoelectron Microscopy ,CHO Cells ,biochemical phenomena, metabolism, and nutrition ,Virus Replication ,Article ,Capsid ,Cricetulus ,Antigens, Neoplasm ,Foot-and-Mouth Disease Virus ,Polysaccharides ,Cricetinae ,Animals ,Receptors, Virus ,Capsid Proteins ,Hydrophobic and Hydrophilic Interactions ,Oligopeptides ,Protein Binding - Abstract
Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally αvβ6, via a conserved arginine–glycine–aspartic acid (RGD) motif in the exposed, antigenic, GH loop of capsid protein VP1. Infection can also occur in tissue culture adapted virus in the absence of integrin via acquired basic mutations interacting with heparin sulphate (HS); this virus is attenuated in natural infections. HS interaction has been visualized at a conserved site in two serotypes suggesting a propensity for sulfated-sugar binding. Here we determined the interaction between αvβ6 and two tissue culture adapted FMDV strains by cryo-electron microscopy. In the preferred mode of engagement, the fully open form of the integrin, hitherto unseen at high resolution, attaches to an extended GH loop via interactions with the RGD motif plus downstream hydrophobic residues. In addition, an N-linked sugar of the integrin attaches to the previously identified HS binding site, suggesting a functional role., Foot-and-mouth disease virus binds αvβ6 integrin, via a conserved RGD motif in the flexible, exposed GH loop of capsid protein VP1, for cell entry. Here Kotecha et al. visualize this interaction with the VP1 GH loop extending away from the viral surface, engaging αvβ6 in an open, active state.
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- 2017
42. Membrane-containing virus particles exhibits mechanics of a composite material for genome protection
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Azinas, Stavros, Richter, Ralf P., Abrescia, Nicola G., Bano, Fouzia, Bamford, Dennis Henry, Schwart, Gustavo A., Oksanen, Hanna Maarit, Torca, Ireneo, Esnaola, Jon Ander, Azinas, Stavros, Richter, Ralf P., Abrescia, Nicola G., Bano, Fouzia, Bamford, Dennis Henry, Schwart, Gustavo A., Oksanen, Hanna Maarit, Torca, Ireneo, and Esnaola, Jon Ander
- Abstract
The protection of the viral genome during extracellular transport is an absolute requirement for virus survival and replication. In addition to the almost universal proteinaceous capsids, certain viruses add a membrane layer that encloses their double-stranded (ds) DNA genome within the protein shell. Using the membrane-containing enterobacterial virus PRD1 as a prototype, and a combination of nanoindentation assays by atomic force microscopy and finite element modelling, we show that PRD1 provides a greater stability against mechanical stress than that achieved by the majority of dsDNA icosahedral viruses that lack a membrane. We propose that the combination of a stiff and brittle proteinaceous shell coupled with a soft and compliant membrane vesicle yields a tough composite nanomaterial well-suited to protect the viral DNA during extracellular transport.
- Published
- 2018
43. Identification and characterization of a heterotrimeric archaeal DNA polymerase holoenzyme
- Author
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Yan, Jiangyu, primary, Beattie, Thomas R., additional, Rojas, Adriana L., additional, Schermerhorn, Kelly, additional, Gristwood, Tamzin, additional, Trinidad, Jonathan C., additional, Albers, Sonja V., additional, Roversi, Pietro, additional, Gardner, Andrew F., additional, Abrescia, Nicola G. A., additional, and Bell, Stephen D., additional
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- 2017
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44. The democratization of cryo-EM
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Stuart, David I, primary, Subramaniam, Sriram, additional, and Abrescia, Nicola G A, additional
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- 2016
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45. Lysine Methylation Mapping of Crenarchaeal DNA-Directed RNA Polymerases by Collision-Induced and Electron-Transfer Dissociation Mass Spectrometry
- Author
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Azkargorta, Mikel, primary, Wojtas, Magdalena N., additional, Abrescia, Nicola G. A., additional, and Elortza, Felix, additional
- Published
- 2014
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46. Three-dimensional visualization of forming Hepatitis C virus-like particles by electron-tomography
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Ministerio de Ciencia y Tecnología (España), Eusko Jaurlaritza, Comunidad de Madrid, Badia-Martínez, Daniel, Peralta, Bibiana, Andrés, Germán, Guerra, Milagros, Gil-Cartón, David, Abrescia, Nicola G. A., Ministerio de Ciencia y Tecnología (España), Eusko Jaurlaritza, Comunidad de Madrid, Badia-Martínez, Daniel, Peralta, Bibiana, Andrés, Germán, Guerra, Milagros, Gil-Cartón, David, and Abrescia, Nicola G. A.
- Abstract
Hepatitis C virus infects almost 170 million people per year but its assembly pathway, architecture and the structures of its envelope proteins are poorly understood. Using electron tomography of plastic-embedded sections of insect cells, we have visualized the morphogenesis of recombinant Hepatitis C virus-like particles. Our data provide a three-dimensional sketch of viral assembly at the endoplasmic reticulum showing different budding stages and contiguity of buds. This latter phenomenon could play an important role during the assembly of . wt-HCV and explain the size-heterogeneity of its particles.
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- 2012
47. From lows to highs: using low-resolution models to phase X-ray data
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Stuart, David I., primary and Abrescia, Nicola G. A., additional
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- 2013
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48. Mechanism of Membranous Tunnelling Nanotube Formation in Viral Genome Delivery
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Peralta, Bibiana, primary, Gil-Carton, David, additional, Castaño-Díez, Daniel, additional, Bertin, Aurelie, additional, Boulogne, Claire, additional, Oksanen, Hanna M., additional, Bamford, Dennis H., additional, and Abrescia, Nicola G. A., additional
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- 2013
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49. Structural comparison of the head-subdomain of human CD81 large extra-cellular loop
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Roversi, Pietro, primary, Ondiviela, Marina, additional, and Abrescia, Nicola G. A., additional
- Published
- 2013
- Full Text
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50. Soaking of DNA into crystals of archaeal RNA polymerase achieved by desalting in droplets
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Wojtas, Magdalena N., primary and Abrescia, Nicola G. A., additional
- Published
- 2012
- Full Text
- View/download PDF
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