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16 results on '"R. Fernandez-Munoz"'

1. GRBS FOLLOWED-UP BY THE BOOTES NETWORK

Author

S. Guziy, A. Castro-Tirado, M. Jelinek, J. Gorosabel, P. Kubanek, R. Cunniffe, O. Lara-Gil, O. Rabaza-Castillo, A. de Ugarte Postigo, R. Sanchez-Ramirez, J. Tello, C. Perez del Pulgar, S. Castillo-Carrion, J. Castro Cerion, T. de J. Mateo Sanguino, R. Hudec, S. Vitek, B. de la Morena Carretero, J. Diaz Andreu, R. Fernandez-Munoz, D. Perez-Ramirez, P. Yock, W. Allen, I. Bond, I. Kheyfets, G. Christie, L. Sabau-Graziati, C. Cui, Y. Fan, and I. H. Park

Published
2020

2. Subacute Sclerosing Panencephalitis and Other Lethal Encephalitis Caused by Measles Virus Infection: Pathogenesis and New Approaches to Treatment

Author

R., Fernandez-Munoz, primary, Caballero M., Carabana J., additional, J., Ortego, additional, P.B., Liton, additional, B.M, Duque, additional, A., Martin-Cortes, additional, A., Serrano-Pardo, additional, M.A., Munoz-Alia, additional, R., Porras-Mansilla, additional, J.C., Alvarez-Cermeno, additional, and M.L., Celma, additional

Published
2011
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4. Toxicidad pulmonar por interleucina-2

Author

Y. R. Fernandez Munoz, M. J. Tolon Herrera, M. A. De La Torre Ramos, and A. Moneo Gonzalez

Subjects
medicine.medical_specialty, business.industry, Internal medicine, Medicine, Critical Care and Intensive Care Medicine, business, Gastroenterology
Published
2007

5. Virus y desmielinización: ¿por qué sospechar la implicación de virus en la etiología de la esclerosis múltiple?

Author

R. Fernandez-Munoz and M. L. Celma-Serrat

Subjects
business.industry, viruses, Multiple sclerosis, Central nervous system, General Medicine, Virus multiplication, Autoimmune responses, Disease, medicine.disease, Virology, Virus, Myelin, medicine.anatomical_structure, Immunology, Etiology, Medicine, Neurology (clinical), business
Abstract

Introduction. Epidemiological data indicate that environmentalfactors, possibly infections, are associated with the development of multiple sclerosis. Different viruses are known to produce demyelination in natural and experimental animal infections. In humanssome virus cause acute or chronic diseases that course with central nervous system demyelination. A series of virus have been claimed to be etiological agents of multiple sclerosis, although a causal role for any of them has so far been demonstrated. Method The mechanisms of viral demyelination are diverse, ranging from direct destruction of infected oligodendrocytes to triggering autoimmune responses without virus multiplication in target cells. The potential indirect mechanisms of viral demyelination and the heterogeneous histopathology shown in multiple sclerosis patients, suggesting an heterogeneus etiology, might explain why not a single virus has been as yet identified as the cause of this disease. Conclusions. Viral infections that cause demyelination in animals and humans are briefly reviewed, focusing on the potential myelin destruction mechanisms and obstacles to the identifying viruses that might cause multiple sclerosis.

Published
2002

6. Intracellular forms of simian virus 40 nucleoprotein complexes. I. Methods of isolation and characterization in CV-1 cells

Author

M Coca-Prados, M T Hsu, and R Fernandez-Munoz

Subjects
viruses, Immunology, Simian virus 40, Biology, Kidney, Microbiology, Virus, Cell Line, Viral Proteins, chemistry.chemical_compound, Virology, Methods, Animals, DNA replication, RNA, Haplorhini, Molecular biology, Nucleoprotein, Metabolic pathway, chemistry, Cell culture, Insect Science, DNA, Viral, Intracellular, DNA, Research Article
Abstract

A new method was developed for isolation of intracellular forms of simian virus 40 (SV40) nucleoprotein complexes from SV40-infected CV-1 cells late in the infectious cycle. In contrast to the Triton extraction method, which yields only a 60-70S complex, this new procedure yielded three forms of SV40 nucleoprotein complexes: complex I, complex II, and the nature virion (V). The three nucleoprotein complexes differed in physical as well as biochemical properties. Complex I, which is only a small portion of the total SV42 nucleoprotein complexes late during infection, was active in synthesizing both SV40-specific DNA and RNA. Pulse-labeling experiments suggest the following metabolic pathway: I leads to II leads to V. Conversion of complex I to II occurred shortly after the completion of SV40 DNA replication and resulted in the inactivation of the biosynthetic activities of I.

Published
1979

7. Content of N-6 methyl adenylic acid in heterogeneous nuclear and messenger RNA of HeLa cells

Author

James E. Darnell, R. Fernandez-Munoz, and U. Lavi

Subjects
Cell Nucleus, chemistry.chemical_classification, Messenger RNA, Polyadenylation, RNA, Nuclease protection assay, Methylation, Biology, Ribosome, Molecular biology, Adenosine Monophosphate, Ribonucleases, chemistry, Biochemistry, Genetics, Nucleotide, RNA, Messenger, Poly A, Precursor mRNA, Research Article, HeLa Cells
Abstract

With the aid of a suitable thin layer chromatographic procedure, the N-6 methyl adenylic acid (m6A), content of a variety of 32P labeled RNA species from HeLa cells has been measured. Poly(A)-containing (poly(A)+) cytoplasmic RNA has on the average one m6Ap per 800 to 900 nucleotides. This value is independent of the length of the molecules. The proportion of m6Ap in poly(A)+ cytoplasmic RNA does not change between 4 and 18 hours of labeling with 32P, suggesting that the majority of the messenger RNA molecules may have a similar level of internal methylation regardless of their half-life. The non-polyadenylated, non-ribosomal cytoplasmic RNA fraction sedimenting from 10S TO 28S is less methylated with approximately one m6A per 2,700 nucleotides. Heterogeneous nuclear RNA molecules (DMSO treated) which sediment from 28S to 45S have approximately one m6Ap per 3,000 nucleotides. The hnRNA molecules sedimenting from 10S to 28S have one m6Ap per 1,800 nucleotides. Poly(A)+ nuclear RNA is enriched in m6A, containing 1 residue of m6A per 700 to 800 nucleotides, a value close to that obtained for the polyadenylated cytoplasmic RNA.

Published
1977

8. 5' Caps in hnRNA: absence of m32, 2, 7G and size distribution of capped molecules

Author

R. Fernandez-Munoz, U. Lavi, and James E. Darnell

Subjects
Cell Nucleus, Messenger RNA, Oligoribonucleotides, Guanosine, RNA, Ribonucleotides, Biology, Adenosine, Molecular biology, Uridine, chemistry.chemical_compound, Cell nucleus, Ribonucleases, medicine.anatomical_structure, chemistry, Cytoplasm, Genetics, medicine, RNA, Messenger, RNA, Neoplasm, Precursor mRNA, HeLa Cells, medicine.drug
Abstract

In HeLa cells the "small nuclear" RNA has a cap II 5' structure (8)-- m32,2,7G(5') pppXmpYmp-- where X and Y are 2'0 methylated adenosine and uridine. In contrast hnRNA contains only cap I structures were the 2'0 methylated residue may be any base as was earlier reported for cytoplasmic mRNA (8,9,11). With a clear distinction between the source of these two caps an analysis of the size distribution of capped hnRNA could be performed which revealed over 65% of the capped hnRNA molecules were larger than cytoplasmic mRNA.

Published
1977

9. Structural difference between the 5' termini of viral and cellular mRNA in poliovirus-infected cells: possible basis for the inhibition of host protein synthesis

Author

J E Darnell and R Fernandez-Munoz

Subjects
Five-prime cap, Uracil Nucleotides, viruses, Immunology, RNA-dependent RNA polymerase, Biology, Virus Replication, Guanidines, Microbiology, Virology, Polysome, Protein biosynthesis, RNA, Messenger, RNA, Neoplasm, Messenger RNA, RNA, Molecular biology, Guanine Nucleotides, Neoplasm Proteins, Poliovirus, Viral replication, RNA editing, Polyribosomes, Protein Biosynthesis, Insect Science, Dactinomycin, RNA, Viral, Puromycin, Poly A, Research Article, HeLa Cells
Abstract

Host protein synthesis in poliovirus-infected HeLa cells is interrupted, but the host mRNA appears to remain completely intact and unmodified. The average size and poly (A) content of host mRNA was previously known to be unchanged (Koschel, 1974; Leibowitz and Penman, 1971), and this was confirmed. In addition, the 5' terminal methylated "cap" structures remained intact, and no further base modifications at the level of 1 base in 1,000 could be detected. Poliovirus RNA from viruses was previously shown not to have "caps" (Wimmer, 1972), and in this work poliovirus RNA from polyribosomes was found to have pUp at its 5' end. Since, initiation of protein synthesis is probably the basis for the inhibition of cellular protein synthesis in infected cells, the difference in the 5' ends of the host cell and viral RNA could be the basis of selective translation of viral RNA during infection.

Published
1976

11. The tomato genome sequence provides insights into fleshy fruit evolution

Author

Sato, Shusei, Tabata, Satoshi, Hirakawa, Hideki, Asamizu, Erika, Shirasawa, Kenta, Isobe, Sachiko, Kaneko, Takakazu, Nakamura, Yasukazu, Shibata, Daisuke, Aoki, Koh, Egholm, Michael, Knight, James, Bogden, Robert, Changbao, Shuang, Yang, Xun, Pan, Shengkai, Cheng, Shifeng, Liu, Xin, Ren, Yuanyuan, Wang, Jun, Albiero, Alessandro, Dal Pero, Francesca, Todesco, Sara, Van Eck, Joyce, Buels, Robert M., Bombarely, Aureliano, Gosselin, Joseph R., Huang, Minyun, Leto, Jonathan A., Menda, Naama, Strickler, Susan, Mao, Linyong, Gao, Shan, Tecle, Isaak Y., York, Thomas, Zheng, Vrebalov, Julia T., Lee, JeMin, Zhong, Silin, Mueller, Lukas A., Stiekema, Willem J., Ribeca, Paolo, Alioto, Tyler, Wencai, Sanwen, Yongchen, Zhang, Zhonghua, Jianchang, Guo, Yanmei, Xiaoxuan, Ying, Chuanyou, Zhukuan, Zuo, Jianru, Jianfeng, Zhao, Jiuhai, Yan, Liuhua, Jiang, Hongling, Bao, Hongshuang, Zhenjun, Fuyou, Chen, Bingtang, Han, Bin, Feng, Fan, Danlin, Ling, Hongqing, Xue, Yongbiao, Ware, Doreen, McCombie, W. Richard, Lippman, Zachary B., Chia, Jer-Ming, Pasternak, Shiran, Gelley, Laura, Kramer, Melissa, Anderson, Lorinda K., Chang, Song-Bin, Royer, Suzanne M., Shearer, Lindsay A., Stack, Stephen M., Rose, Jocelyn K. C., Yimin, Eannetta, Nancy, Matas, Antonio J., McQuinn, Ryan, Tanksley, Steven D., Camara, Francisco, Guigo, Roderic, Rombauts, Stephane, Fawcett, Jeffrey, Van de Peer, Yves, Zamir, Dani, Liang, Chunbo, Spannagl, Manuel, Gundlach, Heidrun, Bruggmann, Remy, Mayer, Klaus, Jia, Zhiqi, Junhong, Zhibiao, Bishop, Gerard J., Butcher, Sarah, Lopez-Cobollo, Rosa, Buchan, Daniel, Filippis, Ioannis, Abbott, Dixit, Rekha, Singh, Manju, Archana, Pal, Jitendra Kumar, Pandit, Awadhesh, Pradeep Kumar, Mahato, Ajay Kumar, Dogra, Vivek, Gaikwad, Kishor, Sharma, Tilak Raj, Mohapatra, Trilochan, Nagendra Kumar, Causse, Mathilde, Rothan, Christophe, Schiex, Noirot, Celine, Bellec, Arnaud, Klopp, Delalande, Corinne, Berges, Helene, Mariette, Jerome, Frasse, Pierre, Vautrin, Sonia, Zouine, Mohamed, Latche, Alain, Rousseau, Christine, Regad, Farid, Pech, Jean-Claude, Philippot, Murielle, Bouzayen, Mondher, Pericard, Osorio, Fernandez del Carmen, Asuncion, Monforte, Antonio, Granell, Fernandez-Munoz, Rafael, Conte, Mariana, Lichtenstein, Gabriel, Carrari, Fernando, De Bellis, Gianluca, Fuligni, Fabio, Peano, Clelia, Grandillo, Silvana, Termolino, Pasquale, Pietrella, Marco, Fantini, Elio, Falcone, Giulia, Fiore, Alessia, Giuliano, Giovanni, Lopez, Loredana, Facella, Perrotta, Gaetano, Daddiego, Loretta, Bryan, Glenn, Orozco, Modesto, Pastor, Xavier, Torrents, David, van Schriek, Keygene N. V. Marco G. M., Feron, Richard M. C., van Oeveren, Jan, de Heer, Peter, daPonte, Lorena, Jacobs-Oomen, Saskia, Cariaso, Mike, Prins, Marcel, van Eijk, Michiel J. T., Janssen, Antoine, van Haaren, Mark J. J., Sung-Hwan, Kim, Jungeun, Kwon, Suk-Yoon, Sangmi, Koo, Dal-Hoe, Sanghyeob, Hur, Cheol-Goo, Clouser, Christopher, Rico, Hallab, Asis, Gebhardt, Christiane, Klee, Kathrin, Joecker, Anika, Warfsmann, Jens, Goebel, Ulrike, Kawamura, Shingo, Yano, Kentaro, Sherman, Jamie D., Fukuoka, Hiroyuki, Negoro, Satomi, Bhutty, Sarita, Chowdhury, Parul, Chattopadhyay, Debasis, Datema, Erwin, Smit, Sandra, Schijlen, Eliog. W. M., van de Belt, Jose, van Haarst, Jan C., Peters, Sander A., van Staveren, Marjo J., Henkens, Marleen H. C., Mooyman, Paul J. W., Hesselink, Thamara, van Ham, Roeland C. H. J., Guoyong, Droege, Marcus, Choi, Doil, Kang, Byung-Cheol, Byung Dong, Park, Minkyu, Seungill, Yeom, Seon-In, Yong-Hwan, Yang-Do, Guangcun, Jianwei, Yongsheng, Shengxiong, Fernandez-Pedrosa, Victoria, Collado, Carmen, Zuniga, Sheila, Guoping, Cade, Rebecca, Dietrich, Robert A., Rogers, Jane, Knapp, Fei, Zhangjun, White, Ruth A., Thannhauser, Theodore W., Giovannoni, James J., Angel Botella, Miguel, Gilbert, Louise, Gonzalez, Ramon, Goicoechea, Jose Luis, Yeisoo, Kudrna, Collura, Kristi, Wissotski, Marina, Wing, Rod, Schoof, Heiko, Meyers, Blake C., Gurazada, Aishwarya Bala, Green, Pamela J., Mathur, Saloni, Vyas, Shailendra, Solanke, Amolkumar U., Kumar, Rahul, Gupta, Vikrant, Arun K., Khurana, Paramjit, Jitendra P., Tyagi, Akhilesh K., Dalmay, Tamas, Mohorianu, Irina, Walts, Brandon, Chamala, Srikar, Barbazuk, W. Brad, Jingping, Hui, Tae-Ho, Yupeng, Dong, Paterson, Andrew H., Xiyin, Tang, Haibao, Barone, Amalia, Chiusano, Maria Luisa, Ercolano, Maria Raffaella, D'Agostino, Nunzio, Di Filippo, Miriam, Traini, Alessandra, Sanseverino, Walter, Frusciante, Luigi, Seymour, Graham B., Elharam, Mounir, Hua, Axin, Kenton, Steven, Lewis, Jennifer, Lin, Shaoping, Najar, Fares, Lai, Hongshing, Qin, Baifang, Chunmei, Shi, Ruihua, Douglas, Xing, Yanbo, Keqin, Jing, Yao, Ziyun, Zhou, Liping, Roe, Bruce A., Vezzi, D'Angelo, Michela, Zimbello, Rosanna, Schiavon, Riccardo, Caniato, Elisa, Rigobello, Chiara, Campagna, Davide, Vitulo, Nicola, Valle, Giorgio, Nelson, David R., De Paoli, Emanuele, Szinay, Dora, de Jong, Hans H., Bai, Yuling, Visser, Richard G. F., Lankhorst, Rene M. Klein, Beasley, Helen, McLaren, Karen, Nicholson, Riddle, Claire, Gianese, Giulio, Tomato Genome Consortium, S., Sato, S., Tabata, H., Hirakawa, E., Asamizu, K., Shirasawa, S., Isobe, T., Kaneko, Y., Nakamura, D., Shibata, K., Aoki, M., Egholm, J., Knight, R., Bogden, C. B., Li, Y., Shuang, X., Xu, S. K., Pan, S. F., Cheng, X., Liu, Y. Y., Ren, J., Wang, A., Albiero, F. D., Pero, S., Todesco, J. V., Eck, R. M., Buel, A., Bombarely, J. R., Gosselin, M. Y., Huang, J. A., Leto, N., Menda, S., Strickler, L. Y., Mao, S., Gao, I. Y., Tecle, T., York, Y., Zheng, J. T., Vrebalov, J., Lee, S. L., Zhong, L. A., Mueller, W. J., Stiekema, P., Ribeca, T., Alioto, W. C., Yang, S. W., Huang, Y. C., Du, Z. H., Zhang, J. C., Gao, Y. M., Guo, X. X., Wang, Y., Li, J., He, C. Y., Li, Z. K., Cheng, J. R., Zuo, J. F., Ren, J. H., Zhao, L. H., Yan, H. L., Jiang, B., Wang, H. S., Li, Z. J., Li, F. Y., Fu, B. T., Chen, B., Han, Q., Feng, D. L., Fan, Y., Wang, H. Q., Ling, Y. B., A., D., Ware, W. R., Mccombie, Z. B., Lippman, J. M., Chia, K., Jiang, S., Pasternak, L., Gelley, M., Kramer, L. K., Anderson, S. B., Chang, S. M., Royer, L. A., Shearer, S. M., Stack, J. K., C., Y. M., Xu, N., Eannetta, A. J., Mata, R., Mcquinn, S. D., Tanksley, F., Camara, R., Guigo, S., Rombaut, J., Fawcett, Y. V., De, D., Zamir, C. B., Liang, M., Spannagl, H., Gundlach, R., Bruggmann, K., Mayer, Z. Q., Jia, J. H., Zhang, Z. B., A., G. J., Bishop, S., Butcher, R., Lopez Cobollo, D., Buchan, I., Filippi, J., Abbott, R., Dixit, M., Singh, A., Singh, J. K., Pal, A., Pandit, P. K., Singh, A. K., Mahato, V., Dogra, K., Gaikwad, T. R., Sharma, T., Mohapatra, N. K., Singh, M., Causse, C., Rothan, T., Schiex, C., Noirot, A., Bellec, C., Klopp, C., Delalande, H., Berge, J., Mariette, P., Frasse, S., Vautrin, M., Zouine, A., Latche, C., Rousseau, F., Regad, J. C., Pech, M., Philippot, M., Bouzayen, P., Pericard, S., Osorio, A. F., Del, A., Monforte, A., Granell, R., Fernandez Munoz, M., Conte, G., Lichtenstein, F., Carrari, G. D., Belli, F., Fuligni, C., Peano, S., Grandillo, P., Termolino, M., Pietrella, E., Fantini, G., Falcone, A., Fiore, G., Giuliano, L., Lopez, P., Facella, G., Perrotta, L., Daddiego, G., Bryan, M., Orozco, X., Pastor, D., Torrent, K. N. V., R. M. C., J. v., Oeveren, P. d., Heer, L., Daponte, S., Jacobs Oomen, M., Cariaso, M., Prin, M. J., T., A., Janssen, M. J., J., S. H., Jo, J., Kim, S. Y., Kwon, S., Kim, D. H., Koo, S., Lee, C. G., Hur, C., Clouser, A., Rico, A., Hallab, C., Gebhardt, K., Klee, A., Jocker, J., Warfsmann, U., Gobel, S., Kawamura, K., Yano, J. D., Sherman, H., Fukuoka, S., Negoro, S., Bhutty, P., Chowdhury, D., Chattopadhyay, E., Datema, S., Smit, E. W., M., J. v., De, J. C., Van, S. A., Peter, M. J., Van, M. H. C., P. J. W., T., Hesselink, R. C., H., G. Y., Jiang, M., Droege, D., Choi, B. C., Kang, B. D., Kim, M., Park, S. I., Yeom, Y. H., Lee, Y. D., Choi, G. C., Li, J. W., Gao, Y. S., Liu, S. X., Huang, V., Fernandez Pedrosa, C., Collado, S., Zuniga, G. P., Wang, R., Cade, R. A., Dietrich, J., Roger, S., Knapp, Z. J., Fei, R. A., White, T. W., Thannhauser, J. J., Giovannoni, M. A., Botella, L., Gilbert, R., Gonzalez, J. L., Goicoechea, Y., Yu, D., Kudrna, K., Collura, M., Wissotski, R., Wing, H., Schoof, B. C., Meyer, A. B., Gurazada, P. J., Green, S., Mathur, S., Vya, A. U., Solanke, R., Kumar, V., Gupta, A. K., Sharma, P., Khurana, J. P., Khurana, A. K., Tyagi, T., Dalmay, I., Mohorianu, B., Walt, S., Chamala, W. B., Barbazuk, J. P., Li, H., Guo, T. H., Lee, Y. P., Wang, D., Zhang, A. H., Paterson, X. Y., Wang, H. B., Tang, Barone, Amalia, Chiusano, MARIA LUISA, Ercolano, MARIA RAFFAELLA, D'Agostino, Nunzio, M. D., Filippo, A., Traini, W., Sanseverino, Frusciante, Luigi, G. B., Seymour, M., Elharam, Y., Fu, A., Hua, S., Kenton, J., Lewi, S. P., Lin, F., Najar, H. S., Lai, B. F., Qin, C. M., Qu, R. H., Shi, D., White, J., White, Y. B., Xing, K. Q., Yang, J., Yi, Z. Y., Yao, L. P., Zhou, B. A., Roe, A., Vezzi, M., D'Angelo, R., Zimbello, R., Schiavon, E., Caniato, C., Rigobello, D., Campagna, N., Vitulo, G., Valle, D. R., Nelson, E. D., Paoli, D., Szinay, H. H., De, Y. L., Bai, R. G. F., R. M. K., H., Beasley, K., Mclaren, C., Nicholson, C., Riddle, G., Gianese, Kazusa DNA Research Institute (KDRI), 454 Life Sciences, Amplicon Express Inc., Beijing Academy of Agriculture and Forestry Sciences, Chinese Academy of Sciences (CAS), Beijing Genomics Institute [Shenzhen] (BGI), BMR Genomics S.R.L., Partenaires INRAE, Boyce Thompson Inst Plant Res, Cornell University [New York], Centre for Biosystems Genomics, CNAG-CRG, Centre for Genomic Regulation (CRG), Barcelona Institute of Science and Technology (BIST), 08028 Barcelona, Spain, China Agricultural University (CAU), Chinese Academy of Agricultural Sciences (CAAS), Inst Genet & Dev Biol, State Key Lab Plant Cell & Chromosome Engn, Chinese Academy of Sciences [Beijing] (CAS), Cold Spring Harbor, Cold Spring Harbor Laboratory, Colorado State University [Fort Collins] (CSU), National Taiwan University, Génétique et Amélioration des Fruits et Légumes (GAFL), Institut National de la Recherche Agronomique (INRA), Biologie du fruit et pathologie (BFP), Université Bordeaux Segalen - Bordeaux 2-Institut National de la Recherche Agronomique (INRA)-Université Sciences et Technologies - Bordeaux 1, Unité de Biométrie et Intelligence Artificielle (UBIA), Centre National de Ressources Génomiques Végétales (CNRGV), This work was supported by: Argentina: INTA and CONICET. Belgium: Flemish Institute for Biotechnology and Ghent University. China: The State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Ministry of Science and Technology (2006AA10A116, 2004CB720405, 2006CB101907, 2007DFB30080) Ministry of Agriculture (‘948’ Program: 2007-Z5), National Natural Science Foundation (36171319), Postdoctoral Science Foundation (20070420446). European Union: FP6 Integrated Project EU-SOL PL 016214. France: Institute National de la Recherche Agronomique and Agence Nationale de la Recherche. Germany: the Max Planck Society. India: Department of Biotechnology, Government of India, Indian Council of Agricultural Research. Italy: Ministry of Research (FIRB-SOL, FIRB-Parallelomics, ItaLyco and GenoPOM projects), Ministry of Agriculture (Agronanotech and Biomassval projects), FILAS foundation, ENEA, CNR-ENEA project L. 191/2009. Japan: Kazusa DNA Research Institute Foundation and National Institute of Vegetable and Tea Science. Korea: KRIBB Basic Research Fund and Crop Functional Genomics Research Center (CFGC), MEST. Netherlands: Centre for BioSystems Genomics, Netherlands Organization for Scientific Research. Spain: Fundación Genoma España, Cajamar, FEPEX, Fundación Séneca, ICIA, IFAPA, Fundación Manrique de Lara, Instituto Nacional de Bioinformatica. UK: BBSRC grant BB/C509731/1, DEFRA, SEERAD. USA: NSF (DBI-0116076, DBI-0421634, DBI-0606595, IOS-0923312, DBI-0820612, DBI-0605659, DEB-0316614, DBI 0849896 and MCB 1021718), USDA (2007-02773 and 2007-35300-19739), USDA-ARS. We acknowledge the Potato Genome Sequencing Consortium for sharing data before publication, potato RNA-Seq data was provided by C. R. Buell from the NSF-funded Potato Genome Sequence and Annotation project, tomato RNA-Seq data by the USDA-funded SolCAP project, N. Sinha and J. Maloof, the Amplicon Express team for BAC pooling services, construction of the Whole Genome Profiling (WGP) physical map was supported by EnzaZaden, RijkZwaan, Vilmorin & Cie, and Takii & Co. Keygene N.V. owns patents and patent applications covering its AFLP and Whole Genome Profiling technologies, AFLP and Keygene are registered trademarks of Keygene N.V. The following individuals are also acknowledged for their contribution to the work described: J. Park, B. Wang, C. Niu, D. Liu, F. Cojutti, S. Pescarolo, A. Zambon, G. Xiao, J. Chen, J. Shi, L. Zhang, L. Zeng, M. Caccamo, D. Bolser, D. Martin, M. Gonzalez, P. A. Bedinger, P. A. Covey, P. Pachori, R. R. Pousada, S. Hakim, S. Sims, V. Cahais, W. Long, X. Zhou, Y. Lu, W. Haso, C. Lai, S. Lepp, C. Peluso, H. Teramu, H. De Jong, R. Lizarralde, E. R. May and Z. Li. M. Zabeau is thanked for his support and encouragement and S. van den Brink for her secretarial support., Institut National Polytechnique de Toulouse - Toulouse INP (FRANCE), Institut National de la Recherche Agronomique - INRA (FRANCE), Université de Bordeaux 1 (FRANCE), Université de Bordeaux 2 - Victor Segalen (FRANCE), Institut National Polytechnique de Toulouse - INPT (FRANCE), and Universitat de Barcelona

Subjects
0106 biological sciences, [SDV]Life Sciences [q-bio], Laboratory of Virology, tomato, 01 natural sciences, Genome, Laboratorium voor Plantenveredeling, Arabidopsis, Genetic Variation, Genome, Plant, Genomics, Lycopersicon esculentum, Molecular Sequence Data, Phylogeny, RNA, Plant, Sequence Analysis, DNA, Solanum tuberosum, Soybeans, Synteny, Evolution, Molecular, Solanum lycopersicum, Génétique des plantes, Tomàquets, Wild tomato, Genome Sequencing, Lycopersicon-esculentum, gene, diversification : arabidopsis, patterns, ortholog, history, sorghum, potato, ComputingMilieux_MISCELLANEOUS, 2. Zero hunger, 0303 health sciences, Multidisciplinary, Solanum chilense, biology, EPS-4, BioSolar Cells, food and beverages, Solanum pimpinellifolium, BIOS Applied Metabolic Systems, Neofunctionalization, Laboratory of Genetics, Sequence Analysis, diversification, Génomique, Transcriptomique et Protéomique, Evolution, Bioinformatics, Laboratorium voor Erfelijkheidsleer, Article, Genètica molecular, Laboratorium voor Virologie, 03 medical and health sciences, BIOS Applied Bioinformatics, Tomatoes, Botany, Bioinformatica, Genetics, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Genomes, Laboratorium voor Nematologie, lycopersicon-esculentum, 030304 developmental biology, fungi, Molecular, Plant, DNA, Genètica evolutiva, 15. Life on land, biology.organism_classification, Tomato genome, Plant Breeding, arabidopsis, Genòmica, RNA, Solanum, Laboratory of Nematology, Plant sciences, 010606 plant biology & botany
Abstract

[EN] Tomato (Solanum lycopersicum) is a major crop plant and a model system for fruit development. Solanum is one of the largest angiosperm genera(1) and includes annual and perennial plants from diverse habitats. Here we present a high-quality genome sequence of domesticated tomato, a draft sequence of its closest wild relative, Solanum pimpinellifolium(2), and compare them to each other and to the potato genome (Solanum tuberosum). The two tomato genomes show only 0.6% nucleotide divergence and signs of recent admixture, but show more than 8% divergence from potato, with nine large and several smaller inversions. In contrast to Arabidopsis, but similar to soybean, tomato and potato small RNAs map predominantly to gene-rich chromosomal regions, including gene promoters. The Solanum lineage has experienced two consecutive genome triplications: one that is ancient and shared with rosids, and a more recent one. These triplications set the stage for the neofunctionalization of genes controlling fruit characteristics, such as colour and fleshiness., This work was supported by: Argentina: INTA and CONICET. Belgium: Flemish Institute for Biotechnology and Ghent University. China: The State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences; Ministry of Science and Technology (2006AA10A116, 2004CB720405, 2006CB101907, 2007DFB30080) Ministry of Agriculture ('948' Program: 2007-Z5); National Natural Science Foundation (36171319); Postdoctoral Science Foundation (20070420446). European Union: FP6 Integrated Project EU-SOL PL 016214. France: Institute National de la Recherche Agronomique and Agence Nationale de la Recherche. Germany: the Max Planck Society. India: Department of Biotechnology, Government of India; Indian Council of Agricultural Research. Italy: Ministry of Research (FIRB-SOL, FIRB-Parallelomics, ItaLyco and GenoPOM projects); Ministry of Agriculture (Agronanotech and Biomassval projects); FILAS foundation; ENEA; CNR-ENEA project L. 191/2009. Japan: Kazusa DNA Research Institute Foundation and National Institute of Vegetable and Tea Science. Korea: KRIBB Basic Research Fund and Crop Functional Genomics Research Center (CFGC), MEST. Netherlands: Centre for BioSystemsGenomics, Netherlands Organization for Scientific Research. Spain: Fundacion Genoma Espana; Cajamar; FEPEX; Fundacion Seneca; ICIA; IFAPA; Fundacion Manrique de Lara; Instituto Nacional de Bioinformatica. UK: BBSRC grant BB/C509731/1; DEFRA; SEERAD. USA: NSF (DBI-0116076; DBI-0421634; DBI-0606595; IOS-0923312; DBI-0820612; DBI-0605659; DEB-0316614; DBI 0849896 and MCB 1021718); USDA (2007-02773 and 2007-35300-19739); USDA-ARS. We acknowledge the Potato Genome Sequencing Consortium for sharing data before publication; potato RNA-Seq data was provided by C. R. Buell from the NSF-funded Potato Genome Sequence and Annotation project; tomato RNA-Seq data by the USDA-funded SolCAP project, N. Sinha and J. Maloof; the Amplicon Express team for BAC pooling services; construction of the Whole Genome Profiling (WGP) physical map was supported by EnzaZaden, RijkZwaan, Vilmorin&Cie, and Takii & Co. Keygene N. V. owns patents and patent applications covering its AFLP and Whole Genome Profiling technologies; AFLP and Keygene are registered trademarks of Keygene N. V.

12. 5' Caps in hnRNA: absence of m32,2,7G and size distribution of capped molecules.

Author

Fernandez-Munoz R, Lavi U, and Darnell JE

Subjects
Cell Nucleus analysis, HeLa Cells analysis, Oligoribonucleotides analysis, RNA, Messenger analysis, Ribonucleases, Ribonucleotides analysis, Guanosine analysis, RNA, Neoplasm
Abstract

In HeLa cells the "small nuclear" RNA has a cap II 5' structure (8)-- m32,2,7G(5') pppXmpYmp-- where X and Y are 2'0 methylated adenosine and uridine. In contrast hnRNA contains only cap I structures were the 2'0 methylated residue may be any base as was earlier reported for cytoplasmic mRNA (8,9,11). With a clear distinction between the source of these two caps an analysis of the size distribution of capped hnRNA could be performed which revealed over 65% of the capped hnRNA molecules were larger than cytoplasmic mRNA.

Published
1977
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13. Structural difference between the 5' termini of viral and cellular mRNA in poliovirus-infected cells: possible basis for the inhibition of host protein synthesis.

Author

Fernandez-Munoz R and Darnell JE

Subjects
Dactinomycin pharmacology, Guanidines pharmacology, Guanine Nucleotides analysis, HeLa Cells, Poliovirus growth & development, Poly A analysis, Polyribosomes metabolism, Protein Biosynthesis, Puromycin pharmacology, Uracil Nucleotides analysis, Virus Replication, Neoplasm Proteins biosynthesis, Poliovirus analysis, RNA, Messenger analysis, RNA, Neoplasm analysis, RNA, Viral analysis
Abstract

Host protein synthesis in poliovirus-infected HeLa cells is interrupted, but the host mRNA appears to remain completely intact and unmodified. The average size and poly (A) content of host mRNA was previously known to be unchanged (Koschel, 1974; Leibowitz and Penman, 1971), and this was confirmed. In addition, the 5' terminal methylated "cap" structures remained intact, and no further base modifications at the level of 1 base in 1,000 could be detected. Poliovirus RNA from viruses was previously shown not to have "caps" (Wimmer, 1972), and in this work poliovirus RNA from polyribosomes was found to have pUp at its 5' end. Since, initiation of protein synthesis is probably the basis for the inhibition of cellular protein synthesis in infected cells, the difference in the 5' ends of the host cell and viral RNA could be the basis of selective translation of viral RNA during infection.

Published
1976
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14. Secondary structure in heterogeneous nuclear RNA: involvement of regions from repeated DNA sites.

Author

Jelinek W, Molloy G, Fernandez-Munoz R, Salditt M, and Darnell JE

Subjects
Alkalies, Base Sequence, Centrifugation, Density Gradient, Chemical Phenomena, Chemistry, HeLa Cells, Nucleic Acid Denaturation, Nucleic Acid Hybridization, Poliovirus, RNA, Messenger analysis, RNA, Viral analysis, Ribonucleases, Transcription, Genetic, Tritium, Cell Nucleus analysis, DNA, RNA analysis
Published
1974
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15. Intracellular forms of simian virus 40 nucleoprotein complexes. I. Methods of isolation and characterization in CV-1 cells.

Author

Fernandez-Munoz R, Coca-Prados M, and Hsu MT

Subjects
Animals, Cell Line, DNA, Viral analysis, Haplorhini, Kidney, Methods, Viral Proteins analysis, DNA, Viral isolation & purification, Simian virus 40 analysis, Viral Proteins isolation & purification
Abstract

A new method was developed for isolation of intracellular forms of simian virus 40 (SV40) nucleoprotein complexes from SV40-infected CV-1 cells late in the infectious cycle. In contrast to the Triton extraction method, which yields only a 60-70S complex, this new procedure yielded three forms of SV40 nucleoprotein complexes: complex I, complex II, and the nature virion (V). The three nucleoprotein complexes differed in physical as well as biochemical properties. Complex I, which is only a small portion of the total SV42 nucleoprotein complexes late during infection, was active in synthesizing both SV40-specific DNA and RNA. Pulse-labeling experiments suggest the following metabolic pathway: I leads to II leads to V. Conversion of complex I to II occurred shortly after the completion of SV40 DNA replication and resulted in the inactivation of the biosynthetic activities of I.

Published
1979
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16. Substrate- and antibiotic-binding sites at the peptidyl-transferase centre of Escherichia coli ribosomes. Studies on the chloramphenicol. lincomycin and erythromycin sites.

Author

Fernandez-Munoz R, Monro RE, Torres-Pinedo R, and Vazquez D

Subjects
Binding Sites, Carbon Isotopes, Chloramphenicol metabolism, Erythromycin metabolism, Escherichia coli cytology, Ethanol pharmacology, Lincomycin metabolism, Peptide Chain Elongation, Translational, Peptides, Ribosomes drug effects, Ribosomes enzymology, Anti-Bacterial Agents metabolism, Ribosomes metabolism, Transferases
Published
1971
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