Author: "Roque, Alicia" - Searchworks@Jio Institute Digital Library Search Results

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123 results on '"Roque, Alicia"'

1. Quantification of Histone H1 Subtypes Using Targeted Proteomics.

Author: López-Gómez, Jordi, Villarreal, Laura, Andrés, Marta, Ponte, Inma, Xicoy, Blanca, Zamora, Lurdes, Vilaseca, Marta, and Roque, Alicia
Subjects: CHRONIC myeloid leukemia, PROTEIN-tyrosine kinase inhibitors, SOMATIC cells, IMATINIB, WESTERN immunoblotting
Abstract: Histone H1 is involved in the regulation of chromatin structure. Human somatic cells express up to seven subtypes. The variability in the proportions of somatic H1s (H1 complement) is one piece of evidence supporting their functional specificity. Alterations in the protein levels of different H1 subtypes have been observed in cancer, suggesting their potential as biomarkers and that they might play a role in disease development. We have developed a mass spectrometry-based (MS) parallel reaction monitoring (PRM) assay suitable for the quantification of H1 subtypes. Our PRM method is based on the quantification of unique peptides for each subtype, providing high specificity. Evaluation of the PRM performance on three human cell lines, HeLa, K562, and T47D, showed high reproducibility and sensitivity. Quantification values agreed with the electrophoretic and Western blot data, indicating the accuracy of the method. We used PRM to quantify the H1 complement in peripheral blood samples of healthy individuals and chronic myeloid leukemia (CML) patients. In CML, the first line of therapy is a tyrosine kinase inhibitor, imatinib. Our preliminary data revealed differences in the H1 complement in CML patients between imatinib responders and non-responders. These results support further research to determine if the H1 content or subtype composition could help predict imatinib response. [ABSTRACT FROM AUTHOR]
Published: 2024
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2. The effects of age-related macular degeneration on quality of life in a Brazilian population

Author: Roque, Alicia Buffoni, da Silva Borges, Géssica Fernandes, Abe, Ricardo Yuji, de Souza, Osias Francisco, Machado, Maria Cecília, Ferreira, Tamara, José, Newton Kara, and de Vasconcellos, José Paulo Cabral
Published: 2021
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3. A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study

Author: Chaves-Arquero, Belén, Pantoja-Uceda, David, Roque, Alicia, Ponte, Inmaculada, Suau, Pedro, and Jiménez, M. Angeles
Published: 2018
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4. Identification of novel post-translational modifications in linker histones from chicken erythrocytes

Author: Sarg, Bettina, Lopez, Rita, Lindner, Herbert, Ponte, Inma, Suau, Pedro, and Roque, Alicia
Published: 2015
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5. Complex Evolutionary History of the Mammalian Histone H1.1–H1.5 Gene Family

Author: Ponte, Inma, Romero, Devani, Yero, Daniel, Suau, Pedro, and Roque, Alicia
Published: 2017
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6. Language Competence and Tradition-Constituted Rationality

Author: Roque, Alicia Juarrero
Published: 1991
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7. Association of genetic variants rs641153 (CFB), rs2230199 (C3), and rs1410996 (CFH) with age-related macular degeneration in a Brazilian population

Author: Neto, Jamil M, primary, Viturino, Marina GM, additional, Ananina, Galina, additional, Bajano, Flávia F, additional, Costa, Sueli M da S, additional, Roque, Alicia B, additional, Borges, Gessica FS, additional, Franchi, Raissa, additional, Rim, Priscila HH, additional, Medina, Flávio M, additional, Costa, Fernando F, additional, Melo, Mônica B de, additional, and de Vasconcellos, José PC, additional
Published: 2021
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8. Towards understanding the regulation of histone H1 somatic subtypes with OMICs

Author: Ministerio de Economía y Competitividad (España), Ponte, I., Andrés, M., Jordan, Albert, Roque, Alicia, Ministerio de Economía y Competitividad (España), Ponte, I., Andrés, M., Jordan, Albert, and Roque, Alicia
Abstract: Histone H1 is involved in the regulation of chromatin higher-order structure and compaction. In humans, histone H1 is a multigene family with seven subtypes differentially expressed in somatic cells. Which are the regulatory mechanisms that determine the variability of the H1 complement is a long-standing biological question regarding histone H1. We have used a new approach based on the integration of OMICs data to address this issue. We have examined the 3D-chromatin structure, the binding of transcription factors (TFs), and the expression of somatic H1 genes in human cell lines, using data from public repositories, such as ENCODE. Analysis of Hi-C, ChIP-seq, and RNA-seq data, have revealed that transcriptional control has a greater impact on H1 regulation than previously thought. Somatic H1 genes located in topologically associated domains (TADs) show higher expression than in boundary regions. H1 genes are targeted by a variable number of transcription factors including cell cycle-related TFs, and tissue-specific TFs, suggesting a fine-tuned, subtype-specific transcriptional control. We describe, for the first time, that all H1 somatic subtypes are under transcriptional co-regulation. The replication-independent subtypes, which are encoded in different chromosomes isolated from other histone genes, are also co-regulated with the rest of the somatic H1 genes, indicating that transcriptional co-regulation extends beyond the histone cluster. Transcriptional control and transcriptional co-regulation explain, at least in part, the variability of H1 complement, the fluctuations of H1 subtypes during development, and also the compensatory effects observed, in model systems, after perturbation of one or more H1 subtypes.
Published: 2021

9. Evaluation of APOE polymorphisms and the risk for age-related macular degeneration in a Southeastern Brazilian population

Author: Viturino, Marina GM, primary, Neto, Jamil M, additional, Bajano, Flávia F, additional, Costa, Sueli MS, additional, Roque, Alicia B, additional, Borges, Gessica FS, additional, Ananina, Galina, additional, Rim, Priscila HH, additional, Medina, Flávio M, additional, Costa, Fernando F, additional, Vasconcellos, José PC de, additional, and Melo, Mônica B de, additional
Published: 2021
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10. Towards understanding the Regulation of Histone H1 Somatic Subtypes with OMICs

Author: Ponte, Inma, primary, Andrés, Marta, additional, Jordan, Albert, additional, and Roque, Alicia, additional
Published: 2021
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11. Towards understanding the regulation of histone H1 somatic subtypes with OMICs

Author: Ponte, Inma, primary, Andrés, Marta, additional, Jordan, Albert, additional, and Roque, Alicia, additional
Published: 2020
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12. Histone H1 Post-Translational Modifications: Update and Future Perspectives

Author: Andrés, Marta, primary, García-Gomis, Daniel, additional, Ponte, Inma, additional, Suau, Pedro, additional, and Roque, Alicia, additional
Published: 2020
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13. Psychometric properties of the Portuguese version of the National Eye Institute Visual Function Questionnaire-25

Author: Abe, Ricardo Y., primary, Medeiros, Felipe A., additional, Davi, Milton Agrizzi, additional, Gonçalves, Cecília, additional, Bittencourt, Matheus, additional, Roque, Alicia Buffoni, additional, Boccato, Júlia, additional, Costa, Vital Paulino, additional, and Cabral Vasconcellos, José Paulo, additional
Published: 2019
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14. Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation

Author: Roque, Alicia, Ponte, Inma, Arrondo, José Luis R., and Suau, Pedro
Published: 2008

15. Heterogeneity of the somatic histone H1 complement in cancer cell lines

Author: Lopez, P., Andrés, M., Montufar, S., Salinas, M., Serra, P., García, J., Ponte, I., Jordan, Albert, and Roque, Alicia
Subjects: health services administration, hemic and lymphatic diseases, population characteristics, geographic locations
Abstract: Trabajo presentado en el Genetics and epigenetics of leukemia and lymphoma: from knowledge to applications, celebrado en Barcelona (España), los días 19 y 20 de septiembre de 2019
Published: 2019

16. The preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domain

Author: Roque, Alicia, Orrego, Mary, Ponte, Imma, and Suau, Pedro
Published: 2004

17. Fail-safe versus safe-fail: suggestions toward an evolutionary model of justice.

Author: Juarrero-Roque, Alicia
Subjects: Utopias -- Analysis, Evolution -- Analysis, Law -- Beliefs, opinions and attitudes, Formalism (Philosophy) -- Influence
Published: 1991

18. Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin

Author: Mora Xavier, Buschati Natascha, Roque Alicia, Ponte Imma, Orrego Mary, and Suau Pedro
Subjects: Biology (General), QH301-705.5
Abstract: Abstract Background Histone H1 is involved in the formation and maintenance of chromatin higher order structure. H1 has multiple isoforms; the subtypes differ in timing of expression, extent of phosphorylation and turnover rate. In vertebrates, the amino acid substitution rates differ among subtypes by almost one order of magnitude, suggesting that each subtype might have acquired a unique function. We have devised a competitive assay to estimate the relative binding affinities of histone H1 mammalian somatic subtypes H1a-e and H1° for long chromatin fragments (30–35 nucleosomes) in physiological salt (0.14 M NaCl) at constant stoichiometry. Results The H1 complement of native chromatin was perturbed by adding an additional amount of one of the subtypes. A certain amount of SAR (scaffold-associated region) DNA was present in the mixture to avoid precipitation of chromatin by excess H1. SAR DNA also provided a set of reference relative affinities, which were needed to estimate the relative affinities of the subtypes for chromatin from the distribution of the subtypes between the SAR and the chromatin. The amounts of chromatin, SAR and additional H1 were adjusted so as to keep the stoichiometry of perturbed chromatin similar to that of native chromatin. H1 molecules freely exchanged between the chromatin and SAR binding sites. In conditions of free exchange, H1a was the subtype of lowest affinity, H1b and H1c had intermediate affinities and H1d, H1e and H1° the highest affinities. Subtype affinities for chromatin differed by up to 19-fold. The relative affinities of the subtypes for chromatin were equivalent to those estimated for a SAR DNA fragment and a pUC19 fragment of similar length. Avian H5 had an affinity ~12-fold higher than H1e for both DNA and chromatin. Conclusion H1 subtypes freely exchange in vitro between chromatin binding sites in physiological salt (0.14 M NaCl). The large differences in relative affinity of the H1 subtypes for chromatin suggest that differential affinity could be functionally relevant and thus contribute to the functional differentiation of the subtypes. The conservation of the relative affinities for SAR and non-SAR DNA, in spite of a strong preference for SAR sequences, indicates that differential affinity alone cannot be responsible for the heterogeneous distribution of some subtypes in cell nuclei.
Published: 2007
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19. Influence of Gestational Age at Initiation of Antihypertensive Therapy

Author: Pels, Anouk, primary, Mol, Ben Willem J., additional, Singer, Joel, additional, Lee, Terry, additional, von Dadelszen, Peter, additional, Ganzevoort, Wessel, additional, Asztalos, Elizabeth, additional, Magee, Laura A., additional, Gafni, Amiram, additional, Gruslin, Andrée, additional, Helewa, Michael, additional, Hutton, Eileen, additional, Lee, Shoo, additional, Logan, Alexander, additional, Menzies, Jennifer, additional, Moutquin, Jean-Marie, additional, Murphy, Kellie, additional, Rey, Evelyne, additional, Ross, Sue, additional, Sanchez, Johanna, additional, Thornton, Jim G., additional, Welch, Ross, additional, Hoac, Trinh, additional, Kirton, Joanne, additional, Trigiani, Katherine, additional, Zahid, Ainy, additional, Bracken, Michael B., additional, Crowley, Patricia, additional, Duley, Lelia, additional, Ehrenkranz, Richard, additional, Thorpe, Kevin, additional, Chan, Sunny, additional, Shi, Michael, additional, Yu, Shelley, additional, de Lourdes Martin, Raquel, additional, Bassi, Maria Florencia, additional, Caruso, Mirta Clara, additional, Lagunas, Valeria, additional, Vera, Fernando, additional, Mohedano de Duhalde, Maria, additional, Roque, Alicia Beatriz, additional, Roldan, Patricia, additional, Duhalde, Esteban Marcos, additional, Dip, Viviana, additional, Aguirre, Jesus Daniel, additional, Morales, Elba Mirta Alicia, additional, Abreo, Griselda Itati, additional, De Sagastizabal, Teresa, additional, Gomez, Carolina, additional, Rizzi, Nadia, additional, Arias, Carlos, additional, Bruno, Ricardo Antonio, additional, Mahomed, Kassam, additional, Drew, Alison, additional, Green, Ann, additional, Hoare, Jane, additional, Hague, Bill, additional, Coat, Suzette, additional, Crowther, Caroline, additional, Muller, Peter, additional, Trenowden, Sophie, additional, Walters, Barry, additional, Parker, Claire, additional, Graham, Dorothy, additional, Pennell, Craig, additional, Sung, Eileen, additional, Makris, Angela, additional, Lee, Gaksoo, additional, Thornton, Charlene, additional, Hennessy, Annemarie, additional, Farrell, Louise, additional, Sass, Nelson, additional, Korkes, Henri, additional, Ferreira, Dayana Couto, additional, Moreira de Sa, Renato Augusto, additional, Abreu, Monique Schmidt Marques, additional, Bornia, Rita Guerios, additional, da Silva, Nancy Ribeiro, additional, Cardoso, Fernanda Freitas Oliveira, additional, Marques, Caio Coelho, additional, Hornos, Jorge, additional, Davdt, Ricardo Leal, additional, Paula, Letícia Germany, additional, Zanella, Pedro Luis, additional, Inglis, Gabrielle, additional, Dillon, Ruth, additional, Docherty, Ashley, additional, Hutfield, Anna, additional, Still, Keith, additional, Lalji, Sayrin, additional, Van Tent, Tamara, additional, Hotz, Chris, additional, Messmer, Tracy, additional, Ray, Joel G., additional, Berger, Howard, additional, De Souza, Leanne, additional, Lausman, Andrea, additional, Freire-Lizama, Tatiana, additional, Besel, Kate, additional, Gibson, Paul, additional, Ellsworth, Greta, additional, Miller, Leslie, additional, Hawkins, T. Lee-Ann, additional, Hladunewich, Michelle, additional, Rogowsky, Anna, additional, Hui, Dini, additional, Collins, Virginia, additional, Delisle, Isabelle, additional, Fanning, Cora, additional, Demianczuk, Nestor, additional, Khurana, Rshmi, additional, Sia, Winnie, additional, Marnoch, Catherine, additional, Young, Carmen, additional, Lux, Cheryl, additional, Perreault, Sophie, additional, Tremblay, Valerie, additional, Desindes, Sophie, additional, Côté, Anne-Marie, additional, Dagenais, Veronique, additional, Clark, Heather, additional, O’Shea, Elaine, additional, White, Ruth Rennicks, additional, Gandhi, Shital, additional, Martin, Mary-Jean, additional, Brush, Cheryl, additional, Seaward, Gareth, additional, Newstead-Angel, Jill, additional, Brandt, Judy, additional, Martel, Jocelyne, additional, Mytopher, Kristine, additional, Buschau, Elise, additional, Keely, Erin, additional, Waddell, Patti, additional, Shachkina, Svetlana, additional, Karovitch, Alan, additional, Anderson, Robert, additional, Koenig, Nicole, additional, Yong, Theresa, additional, Vasiliou, Marie, additional, Johnson, Peri, additional, Allan, Beth, additional, Natale, Renato, additional, Kennedy, Laura, additional, Opatrny, Lucie, additional, Lavigne, Lorraine, additional, Carson, George, additional, Kelly, Sheila, additional, Crane, Joan, additional, Hutchens, Donna, additional, Kusanovic, Juan Pedro, additional, Figueroa, Christian, additional, Neculman, Karla Silva, additional, Ortiz, Juan Andres, additional, Vargas, Paula, additional, Ferrand, Pedro, additional, Carrillo, Jorge, additional, Borrero, Rodrigo Cifuentes, additional, Gallo, Dahiana Marcela, additional, Moreno, Luisa Fernanda, additional, Kirss, Fred, additional, Rull, Kristiina, additional, Kirss, Anne, additional, Major, Tamas, additional, Fodor, Andrea, additional, Bartha, Tunde, additional, Hallak, Mordechai, additional, Aslih, Nardin, additional, Anabousi-Murra, Saja, additional, Pri-Or, Ester, additional, Harel, Linda, additional, Siev, Sima, additional, Hakim, Marwan, additional, Khoury, Christina Simona, additional, Hamati, Najla, additional, El-Zibdeh, Mazen, additional, Yousef, Lama, additional, Hughes, Ruth, additional, Leishman, Di, additional, Pullar, Barbra, additional, Farrant, Matthew, additional, Swiatkowska-Freund, Malgorzata, additional, Preis, Krzysztof, additional, Traczyk-Los, Anette Aleksandra, additional, Partyka, Anna, additional, Preis-Orlikowska, Joanna, additional, Lukaszuk, Mariusz, additional, Krasomski, Grzegorz, additional, Krekora, Michael, additional, Kedzierska-Markowicz, Anna, additional, Zych-Krekora, Katarzyna, additional, Breborowicz, Grzegorz H., additional, Dera-Szymanowska, Anna, additional, Bakker, Jannet, additional, Akkermans, Joost, additional, van den Akker, Eline, additional, Logtenberg, Sabine, additional, Koenen, Steven, additional, de Reus, Maartje, additional, Borman, David, additional, Oudijk, Martijn A., additional, Bolte, Annemiek, additional, Verfaille, Viki, additional, Graaf, Bart, additional, Porath, Martina, additional, Verhoeven, Corine, additional, Franssen, Maureen T.M., additional, Ulkeman, Lida, additional, Hamming, Ineke, additional, Keurentjes, Jose H.M., additional, van der Wal, Ina, additional, Bijvank, S.W.A. Nij, additional, Lutjes, A.A., additional, Visser, Henricus, additional, Scheepers, Hubertina Catharina Johanna, additional, van Beek, Erik, additional, van Dam, Coby, additional, van den Berg-Swart, Kathy, additional, Pernet, Paula, additional, van der Goes, Birgit, additional, Schuitemaker, Nico, additional, Kleiverda, Gunilla, additional, van Alphen, Marcel, additional, Rosman, Ageeth, additional, Gaugler-Senden, Ingrid, additional, Linders, Marieke, additional, Nelson-Piercy, Catherine, additional, Briley, Annette, additional, Soh, May Ching, additional, Harding, Kate, additional, Tarft, Hayley, additional, Churchill, David, additional, Cheshire, Katherine, additional, Icke, Julia, additional, Ghosh, Mausumi, additional, Thornton, James, additional, Toomassi, Yvonne, additional, Barker, Karen, additional, Fisher, Joanne, additional, Grace, Nicky, additional, Green, Amanda, additional, Gower, Joanne, additional, Molnar, Anna, additional, Parameshwaran, Shobhana, additional, Simm, Andrew, additional, Bugg, George, additional, Davis, Yvette, additional, Desphande, Ruta, additional, Gunn, Yvette, additional, Houda, Mohammed, additional, Jones, Nia, additional, Waugh, Jason, additional, Allan, Carly, additional, Waring, Gareth, additional, Walkinshaw, Steve A., additional, Pascall, Angela, additional, Clement-Jones, Mark, additional, Dower, Michelle, additional, Houghton, Gillian, additional, Longworth, Heather, additional, Purewal, Tej, additional, Tuffnell, Derek, additional, Farrar, Diane, additional, Syson, Jennifer, additional, Butterfield, Gillian, additional, Jones, Vicky, additional, Palethorpe, Rebecca, additional, Germaine, Tracey, additional, Habiba, Marwan, additional, Lee, Debbie, additional, Eniola, Olufemi, additional, Blake, Lynne, additional, Khan, Jane, additional, Cameron, Helen M., additional, Hinshaw, Kim, additional, Bargh, Amanda, additional, Walton, Eileen, additional, Sorinola, Olanrewaju, additional, Guy, Anna, additional, D’Souza, Zoe, additional, Gabriel, Rhiannon, additional, Williams, Jo, additional, Hollands, Heidi, additional, Jibodu, Olujimi, additional, Collier, Sara, additional, Tottie, Pauline, additional, Oxby, Claire, additional, Dwyer, James, additional, Majoko, Franz, additional, Goldring, Helen, additional, Jones, Sharon, additional, Cresswell, Janet, additional, Underwood, Louise, additional, Kelly-Baxter, Mary, additional, Robinson, Rebecca, additional, Anumba, Dilly, additional, Chamberlain, Anne, additional, Pye, Clare, additional, Tower, Clare, additional, Woods, Sue, additional, Horrocks, Lisa, additional, Prichard, Fiona, additional, Moorhead, Lynsey, additional, Lee, Sarah, additional, Stephens, Louise, additional, Taylor, Cara, additional, Thomas, Suzanne, additional, Whitworth, Melissa, additional, Myers, Jenny, additional, Knox, Ellen, additional, Freitas, Katie, additional, Kilby, Mark, additional, Cotterill, Amanda, additional, Abdo, Khalil, additional, Rigby, Katrina, additional, Butler, Julie, additional, Crosfill, Fiona, additional, Hughes, Sean, additional, Prashar, Sanjeev, additional, Soydemir, Fatimah, additional, Ashworth, Janet, additional, Mycock, Lorraine, additional, Smith, Jill, additional, Ikomi, Amaju, additional, Goodsell, Kerry, additional, Byrne, Jean, additional, Masuku, Maxwell, additional, Pilcher, Alice, additional, Khandelwal, Meena, additional, Simpkins, Gunda, additional, Iavicoli, Michelle, additional, Kim, Yon Sook, additional, Fischer, Richard, additional, Perry, Robin, additional, Chang, Eugene Y., additional, Saunders, Tamara D., additional, Oswald, Betty W., additional, Zaks, Kristin D., additional, Rana, Sarosh, additional, McCullough, Dawn, additional, Sfakianaki, Anna, additional, Danton, Cheryl, additional, Kustan, Erin, additional, Coraluzzi, Luisa, additional, How, Helen, additional, Waldon, Christina, additional, Livingston, Jeffrey, additional, Jackson, Sherry, additional, Greene, Lisa, additional, Shah, Dinesh, additional, Tolosa, Jorge E., additional, Rincon, Monica, additional, Pereira, Leonardo, additional, Lawrence, Amy E., additional, Snyder, Janice E., additional, Armstrong, D. Michael, additional, Blue, Teresa, additional, Hester, Austin, additional, and Salisbury, Kathryn, additional
Published: 2018
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20. Disulfide driven folding for a conditionally disordered protein

Author: Fraga, Hugo, primary, Pujols, Jordi, additional, Gil-Garcia, Marcos, additional, Roque, Alicia, additional, Bernardo-Seisdedos, Ganeko, additional, Santambrogio, Carlo, additional, Bech-Serra, Joan-Josep, additional, Canals, Francesc, additional, Bernadó, Pau, additional, Grandori, Rita, additional, Millet, Oscar, additional, and Ventura, Salvador, additional
Published: 2017
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21. Self-Organization: Kant's Concept of Teleology and Modern Chemistry

Author: Roqué, Alicia Juarrero
Published: 1985

22. Dispositions, Teleology and Reductionism

Author: ROQUÉ, ALICIA JUARRERO
Published: 1981

23. Additional file 3: Figure S1. of Genome-wide recruitment profiling of transcription factor Crz1 in response to high pH stress

Author: Roque, Alicia, Petrezsélyová, Silvia, Serra-Cardona, Albert, and Ariño, Joaquín
Abstract: Alkaline pH responsiveness of genes involved in trehalose metabolism. (PPTX 64 kb)
Published: 2016
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24. Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1

Author: Roque, Alicia, Ponte, Inma, and Suau, Pedro
Subjects: Histones -- Structure, Histones -- Research, Protein folding -- Research, DNA -- Research, Chemicals, plastics and rubber industries
Published: 2009

25. The subtype-specific role of histone H1.0 in cancer cell differentiation and intratumor heterogeneity

Author: Roque, Alicia, primary, Ponte, Inma, additional, and Suau, Pedro, additional
Published: 2017
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26. Sequence conservation of linker histones between chicken and mammalian species

Author: Sarg, Bettina, Lopez, Rita, Lindner, Herbert, Ponte, Inma, Suau, Pedro, and Roque, Alicia
Published: 2014
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27. Regulation of the Na+/K+-ATPase Ena1 Expression by Calcineurin/Crz1 under High pH Stress: A Quantitative Study

Author: Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes, Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia, Ministerio de Ciencia e Innovación, Petrezsélyová, Silvia, López-Malo, María, Canadell, David, Roque, Alicia, Serra-Cardona, Albert, Marques Romero, Mª Carmen, Vilaprinyó, Ester, Alves, Rui, Yenush, Lynne, Ariño, Joaquin, Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes, Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia, Ministerio de Ciencia e Innovación, Petrezsélyová, Silvia, López-Malo, María, Canadell, David, Roque, Alicia, Serra-Cardona, Albert, Marques Romero, Mª Carmen, Vilaprinyó, Ester, Alves, Rui, Yenush, Lynne, and Ariño, Joaquin
Abstract: [EN] Regulated expression of the Ena1 Na+-ATPase is a crucial event for adaptation to high salt and/or alkaline pH stress in the budding yeast Saccharomyces cerevisiae. ENA1 expression is under the control of diverse signaling pathways, including that mediated by the calcium-regulatable protein phosphatase calcineurin and its downstream transcription factor Crz1. We present here a quantitative study of the expression of Ena1 in response to alkalinization of the environment and we analyze the contribution of Crz1 to this response. Experimental data and mathematical models substantiate the existence of two stress-responsive Crz1-binding sites in the ENA1 promoter and estimate that the contribution of Crz1 to the early response of the ENA1 promoter is about 60%. The models suggest the existence of a second input with similar kinetics, which would be likely mediated by high pH-induced activation of the Snf1 kinase.
Published: 2016

28. SETD7 regulates the differentiation of human embryonic stem cells

Author: Ministerio de Ciencia e Innovación (España), Ministerio de Economía y Competitividad (España), Fundació Privada Cellex, Ministerio de Educación y Ciencia (España), Instituto de Salud Carlos III, Castaño, Julio, Morera, Cristina, Sesé, Borja, Boué, Stéphanie, Bonet-Costa, Carles, Martí, Mercè, Roque, Alicia, Jordan, Albert, Barrero, María José, Ministerio de Ciencia e Innovación (España), Ministerio de Economía y Competitividad (España), Fundació Privada Cellex, Ministerio de Educación y Ciencia (España), Instituto de Salud Carlos III, Castaño, Julio, Morera, Cristina, Sesé, Borja, Boué, Stéphanie, Bonet-Costa, Carles, Martí, Mercè, Roque, Alicia, Jordan, Albert, and Barrero, María José
Abstract: The successful use of specialized cells in regenerative medicine requires an optimization in the differentiation protocols that are currently used. Understanding the molecular events that take place during the differentiation of human pluripotent cells is essential for the improvement of these protocols and the generation of high quality differentiated cells. In an effort to understand the molecular mechanisms that govern differentiation we identify the methyltransferase SETD7 as highly induced during the differentiation of human embryonic stem cells and differentially expressed between induced pluripotent cells and somatic cells. Knock-down of SETD7 causes differentiation defects in human embryonic stem cell including delay in both the silencing of pluripotency-related genes and the induction of differentiation genes. We show that SETD7 methylates linker histone H1 in vitro causing conformational changes in H1. These effects correlate with a decrease in the recruitment of H1 to the pluripotency genes OCT4 and NANOG during differentiation in the SETD7 knockdown that might affect the proper silencing of these genes during differentiation.
Published: 2016

29. Genome-wide recruitment profiling of transcription factor Crz1 in response to high pH stress

Author: Roque, Alicia, primary, Petrezsélyová, Silvia, additional, Serra-Cardona, Albert, additional, and Ariño, Joaquín, additional
Published: 2016
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30. Regulation of the Na+/K+-ATPase Ena1 Expression by Calcineurin/Crz1 under High pH Stress: A Quantitative Study

Author: Petrezsélyová, Silvia, primary, López-Malo, María, additional, Canadell, David, additional, Roque, Alicia, additional, Serra-Cardona, Albert, additional, Marqués, M. Carmen, additional, Vilaprinyó, Ester, additional, Alves, Rui, additional, Yenush, Lynne, additional, and Ariño, Joaquín, additional
Published: 2016
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31. Interplay between histone H1 structure and function

Author: Roque, Alicia, primary, Ponte, Inma, additional, and Suau, Pedro, additional
Published: 2016
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32. SETD7 Regulates the Differentiation of Human Embryonic Stem Cells

Author: Castaño, Julio, primary, Morera, Cristina, additional, Sesé, Borja, additional, Boue, Stephanie, additional, Bonet-Costa, Carles, additional, Martí, Merce, additional, Roque, Alicia, additional, Jordan, Albert, additional, and Barrero, Maria J., additional
Published: 2016
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33. Histone H1 Favors Folding and Parallel Fibrillar Aggregation of the 1–42 Amyloid-β Peptide

Author: Roque, Alicia, primary, Sortino, Rosalba, additional, Ventura, Salvador, additional, Ponte, Inma, additional, and Suau, Pedro, additional
Published: 2015
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34. Linker histone partial phosphorylation: effects on secondary structure and chromatin condensation

Author: Lopez, Rita, primary, Sarg, Bettina, additional, Lindner, Herbert, additional, Bartolomé, Salvador, additional, Ponte, Inma, additional, Suau, Pedro, additional, and Roque, Alicia, additional
Published: 2015
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35. Dynamics and dispensability of variant‐specific histone H1 Lys‐26/Ser‐27 and Thr‐165 post‐translational modifications

Author: Terme, Jean-Michel, primary, Millán-Ariño, Lluís, additional, Mayor, Regina, additional, Luque, Neus, additional, Izquierdo-Bouldstridge, Andrea, additional, Bustillos, Alberto, additional, Sampaio, Cristina, additional, Canes, Jordi, additional, Font, Isaura, additional, Sima, Núria, additional, Sancho, Mónica, additional, Torrente, Laura, additional, Forcales, Sonia, additional, Roque, Alicia, additional, Suau, Pere, additional, and Jordan, Albert, additional
Published: 2014
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36. Secondary structure of protamine in sperm nuclei : an infrared spectroscopy study

Author: Roque, Alicia, Ponte Marull, Immaculada, Suau, Pedro, Roque, Alicia, Ponte Marull, Immaculada, and Suau, Pedro
Abstract: Protamines are small basic proteins that condense the DNA in mature spermatozoa. Typical protamines are of simple composition and very arginine-rich, usually in the range of 60-80%. Arginine residues are distributed in a number of stretches separated by neutral amino acids. We have used Fourier transform infrared spectroscopy (FTIR) to gain access for the first time to the secondary structure of protamines in sperm nuclei. This technique is particularly well suited to the study of DNA-bound protamine in whole nuclei since it is not affected by turbidity. We show that DNA -bound salmon (salmine) and squid protamines contain α -helix, β -turns and a proportion of other structures not stabilized by intramolecular hydrogen bonding. No β -sheet was observed. In salmine, the α -helix amounted to ~20%, while in squid protamine it reached ~40%. In contrast, the structure not stabilized by intermolecular hydrogen bonding was more abundant in salmine (~40%) than in squid protamine (~20%). Both protamines contained ~40% β -turns. The different helical potential of salmine and squid protamine was confirmed by structure predictions and CD in the presence of trifluoroethanol. DNA-bound protamine in sperm nuclei contains large amounts of defined secondary structure stabilized by intramolecular hydrogen bonding. Both salmine and squid protamine contain similar amounts of β -turns, but differ in the proportions of α -helix and non-hydrogen bonded conformations. In spite of the large differences in the proportions of secondary structure motifs between salmon and squid protamines, they appear to be equally efficient in promoting tight hexagonal packing of the DNA molecules in sperm nuclei.
Published: 2011

37. Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation

Author: Bioquímica y biología molecular, Biokimika eta biologia molekularra, Roque, Alicia, Ponte, Inma, Rodríguez Arrondo, José Luis, Suau, Pedro, Bioquímica y biología molecular, Biokimika eta biologia molekularra, Roque, Alicia, Ponte, Inma, Rodríguez Arrondo, José Luis, and Suau, Pedro
Abstract: Linker histone H1 plays an important role in chromatin folding. Phosphorylation by cyclin-dependent kinases is the main post-translational modification of histone H1. We studied the effects of phosphorylation on the secondary structure of the DNA-bound H1 carboxy-terminal domain (CTD), which contains most of the phosphorylation sites of the molecule. The effects of phosphorylation on the secondary structure of the DNA-bound CTD were site-specific and depended on the number of phosphate groups. Full phosphorylation significantly increased the proportion of -structure and decreased that of -helix. Partial phosphorylation increased the amount of undefined structure and decreased that of -helix without a significant increase in -structure. Phosphorylation had a moderate effect on the affinity of the CTD for the DNA, which was proportional to the number of phosphate groups. Partial phosphorylation drastically reduced the aggregation of DNA fragments by the CTD, but full phosphorylation restored to a large extent the aggregation capacity of the unphosphorylated domain. These results support the involvement of H1 hyperphosphorylation in metaphase chromatin condensation and of H1 partial phosphorylation in interphase chromatin relaxation. More generally, our results suggest that the effects of phosphorylation are mediated by specific structural changes and are not simply a consequence of the net charge.
Published: 2008

38. Regulation of the Na+/K+-ATPase Ena1 Expression by Calcineurin/Crz1 under High pH Stress: A Quantitative Study.

Author: Petrezsélyová, Silvia, López-Malo, María, Canadell, David, Roque, Alicia, Serra-Cardona, Albert, Marqués, M. Carmen, Vilaprinyó, Ester, Alves, Rui, Yenush, Lynne, and Ariño, Joaquín
Subjects: SODIUM ions, POTASSIUM ions, ADENOSINE triphosphatase, GENE expression, CALCINEURIN, PH effect, SACCHAROMYCES cerevisiae
Abstract: Regulated expression of the Ena1 Na+-ATPase is a crucial event for adaptation to high salt and/or alkaline pH stress in the budding yeast Saccharomyces cerevisiae. ENA1 expression is under the control of diverse signaling pathways, including that mediated by the calcium-regulatable protein phosphatase calcineurin and its downstream transcription factor Crz1. We present here a quantitative study of the expression of Ena1 in response to alkalinization of the environment and we analyze the contribution of Crz1 to this response. Experimental data and mathematical models substantiate the existence of two stress-responsive Crz1-binding sites in the ENA1 promoter and estimate that the contribution of Crz1 to the early response of the ENA1 promoter is about 60%. The models suggest the existence of a second input with similar kinetics, which would be likely mediated by high pH-induced activation of the Snf1 kinase. [ABSTRACT FROM AUTHOR]
Published: 2016
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39. Contribution of hydrophobic interactions to the folding and fibrillation of histone H1 and its carboxy-terminal domain

Author: Roque, Alicia, primary, Teruel, Nuria, additional, López, Rita, additional, Ponte, Inma, additional, and Suau, Pedro, additional
Published: 2012
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40. Secondary structure of protamine in sperm nuclei: an infrared spectroscopy study

Author: Roque, Alicia, primary, Ponte, Inma, additional, and Suau, Pedro, additional
Published: 2011
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41. The End of Modernity: Nihilism and Hermeneutics in Post-Modern Culture

Author: Juarrero Roque, Alicia
Subjects: The End of Modernity (Book) -- Book reviews, Books -- Book reviews, Philosophy and religion
Published: 1991

42. Philosophy of Science and Its Discontents

Author: Roque, Alicia Juarrero
Subjects: Philosophy of Science and Its Discontents (Book) -- Book reviews, Books -- Book reviews, Philosophy and religion
Published: 1990

43. Macromolecular Crowding Induces a Molten Globule State in the C-Terminal Domain of Histone H1

Author: Roque, Alicia, primary, Ponte, Inma, additional, and Suau, Pedro, additional
Published: 2007
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44. Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin

Author: Orrego, Mary, primary, Ponte, Imma, additional, Roque, Alicia, additional, Buschati, Natascha, additional, Mora, Xavier, additional, and Suau, Pedro, additional
Published: 2007
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45. Histone H1 Favors Folding and Parallel Fibrillar Aggregationof the 1–42 Amyloid-β Peptide.

Author: Roque, Alicia, Sortino, Rosalba, Ventura, Salvador, Ponte, Inma, and Suau, Pedro
Subjects: *HISTONES, *FIBRILLARIN, *AMYLOID, *PEPTIDE receptors, *PROTEIN-protein interactions, *THIOFLAVINS
Abstract: Alzheimer’s disease (AD) isone of the most prevalent neurodegenerativediseases of the central nervous system. The aggregation of the amyloid-βpeptide, Aβ(1–42), is believed to play an important rolein the pathogenesis of AD. Histone H1 is found in the cytoplasm ofneurons in AD, and it has been shown to interact with aggregated amyloid-βpeptides and with amyloid fibrils. We have used Thioflavin T (ThT)fluorescence enhancement, circular dichroism spectroscopy (CD), coprecipitation,and transmission electron microscopy (TEM) to study the interactionof histone H1 with Aβ(1–42). Both freshly prepared (monomeric)Aβ(1–42) and histone H1 solutions showed negative CDbands typical of the random coil. Mixing Aβ(1–42) andhistone H1 led to the loss of the random coil, which was replacedmostly by β-structure. Therefore, both Aβ(1–42)and histone H1 behave as intrinsically disordered proteins with coupledbinding and folding. Mutual structure induction demonstrates the interactionof Aβ(1–42) and histone H1. The interaction was confirmedby coprecipitation followed by SDS-PAGE. Mutual structure inductionwas also observed with the H1 terminal domains. Incubation of Aβ(1–42)for 1 week in the presence of histone H1 led to the formation of laminaraggregates and thick bundles, characterized by the parallel associationof large numbers of fibrils. The aggregates were particularly largeand ordered with the H1 subtype H1.2. Further aging of the complexesled to tight compaction of fibril bundles and to fiber growth. Stabilizationof fibril–fibril interactions appeared to be determined bythe C-terminal domain of histone H1. In summary, these observationsindicate that histone H1 has at least two effects: it helps the foldingof Aβ monomers and stabilizes the parallel association of fibrils. [ABSTRACT FROM AUTHOR]
Published: 2015
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46. DNA-induced Secondary Structure of the Carboxyl-terminal Domain of Histone H1

Author: Roque, Alicia, primary, Iloro, Ibon, additional, Ponte, Imma, additional, Arrondo, José Luis R., additional, and Suau, Pedro, additional
Published: 2005
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