Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Daria Picchioni"'
Autor:
Daria Picchioni, Albert Antolin-Fontes, Noelia Camacho, Claus Schmitz, Alba Pons-Pons, Marta Rodríguez-Escribà, Antigoni Machallekidou, Merve Nur Güler, Panagiota Siatra, Maria Carretero-Junquera, Alba Serrano, Stacy L. Hovde, Philip A. Knobel, Eva M. Novoa, Maria Solà-Vilarrubias, Laurie S. Kaguni, Travis H. Stracker, Lluís Ribas de Pouplana
Publikováno v:
Cell Reports, Vol 27, Iss 1, Pp 40-47.e5 (2019)
Summary: The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARSs) is a central reaction in biology. Multiple regulatory pathways use the aminoacylation status of cytosolic tRNAs to monitor and regulate metabolism. The existence of equivalent
Externí odkaz:
https://doaj.org/article/4bd6ef76423646f5a93ac1cb397bb7ac
Autor:
Sameena Khan, Ankur Garg, Arvind Sharma, Noelia Camacho, Daria Picchioni, Adélaïde Saint-Léger, Lluís Ribas de Pouplana, Manickam Yogavel, Amit Sharma
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e66224 (2013)
Specific activation of amino acids by aminoacyl-tRNA synthetases (aaRSs) is essential for maintaining fidelity during protein translation. Here, we present crystal structure of malaria parasite Plasmodium falciparum tryptophanyl-tRNA synthetase (Pf-W
Externí odkaz:
https://doaj.org/article/a86cd5e76c5c484da3af81fee0fa99f5
Autor:
Laurie S. Kaguni, Alba Serrano, Philip A. Knobel, Maria Carretero-Junquera, Merve Nur Güler, Daria Picchioni, Panagiota Siatra, Alba Pons-Pons, Eva Maria Novoa, Stacy Hovde, Maria Solà-Vilarrubias, Marta Rodríguez-Escribà, Claus A. Schmitz, Lluís Ribas de Pouplana, Antigoni Machallekidou, Travis H. Stracker, Noelia Camacho, Albert Antolin-Fontes
Publikováno v:
Cell Reports, Vol 27, Iss 1, Pp 40-47.e5 (2019)
Digital.CSIC. Repositorio Institucional del CSIC
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Digital.CSIC. Repositorio Institucional del CSIC
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© 2019 The Authors.
The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARSs) is a central reaction in biology. Multiple regulatory pathways use the aminoacylation status of cytosolic tRNAs to monitor and regulate metabolism. The existen
The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARSs) is a central reaction in biology. Multiple regulatory pathways use the aminoacylation status of cytosolic tRNAs to monitor and regulate metabolism. The existen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::097e6f51103c59f85ab1597bcb23a888
http://www.sciencedirect.com/science/article/pii/S2211124719303298
http://www.sciencedirect.com/science/article/pii/S2211124719303298
Autor:
Claus A. Schmitz, María del Mar Carretero, Stacy Hovde, Maria Solà-Vilarrubias, Philip A. Knobel, Merve Nur Güler, Eva Maria Novoa, Marta Rodríguez-Escribà, Alba Serrano, Lluís Ribas de Pouplana, Travis H. Stracker, Noelia Camacho, Daria Picchioni, Antigoni Machallekidou, Laurie S. Kaguni, Alba Pons-Pons, Albert Antolin-Fontes
Publikováno v:
SSRN Electronic Journal.
The aminoacylation of tRNAs by aminoacyl-tRNA synthetases (ARS) is a central reaction in biology. Multiple regulatory pathways utilize the aminoacylation status of cytosolic tRNAs to monitor and regulate metabolism. The existence of equivalent regula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba9a70b3fe2a4218aec93e7246aca151
https://doi.org/10.2139/ssrn.3305578
https://doi.org/10.2139/ssrn.3305578
Publikováno v:
Nucleic Acids Research
The translation of genes encoded in the mitochondrial genome requires specific machinery that functions in the organelle. Among the many mutations linked to human disease that affect mitochondrial translation, several are localized to nuclear genes c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6648237866a1177f369ffddbe89e8a70
https://doi.org/10.1093/nar/gkt402
https://doi.org/10.1093/nar/gkt402
Autor:
Giovanni, Messina, Elisabetta, Damia, Laura, Fanti, Maria Teresa, Atterrato, Emanuele, Celauro, Francesca Romana, Mariotti, Maria Carmela, Accardo, Matthias, Walther, Fiammetta, Vernì, Daria, Picchioni, Roberta, Moschetti, Ruggiero, Caizzi, Lucia, Piacentini, Giovanni, Cenci, Ennio, Giordano, Patrizio, Dimitri
The evolutionarily conserved family of Bucentaur (BCNT) proteins exhibits a widespread distribution in animal and plants, yet its biological role remains largely unknown. Using Drosophila melanogaster as a model organism, we investigated the in vivo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::c92d6c326fe5971393b57063bfa36bc6
https://hdl.handle.net/10281/413016
https://hdl.handle.net/10281/413016
Autor:
Ennio Giordano, Elisabetta Damia, Lucia Piacentini, Maria Teresa Atterrato, Patrizio Dimitri, Laura Fanti, Fiammetta Vernì, Daria Picchioni, Emanuele Celauro, Maria Carmela Accardo, Roberta Moschetti, Giovanni Cenci, Francesca Romana Mariotti, Giovanni Messina, Ruggiero Caizzi, Matthias Walther
Publikováno v:
Journal of Cell Science.
The evolutionarily conserved family of Bucentaur (BCNT) proteins exhibits a widespread distribution in animal and plants, yet its biological role remains largely unknown. Using Drosophila melanogaster as a model organism, we investigated the in vivo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc17fb1d02b3ecbf3e9d5545b210c921
https://doi.org/10.1242/jcs.150243
https://doi.org/10.1242/jcs.150243
Autor:
Ankur Garg, Lluís Ribas de Pouplana, Amit Sharma, Noelia Camacho, Daria Picchioni, Adélaïde Saint-Léger, Sameena Khan, Manickam Yogavel, Arvind Sharma
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 6, p e66224 (2013)
'PloS One ', vol: 8, pages: e66224-1-e66224-11 (2013)
PLoS ONE, Vol 8, Iss 6, p e66224 (2013)
'PloS One ', vol: 8, pages: e66224-1-e66224-11 (2013)
Specific activation of amino acids by aminoacyl-tRNA synthetases (aaRSs) is essential for maintaining fidelity during protein translation. Here, we present crystal structure of malaria parasite Plasmodium falciparum tryptophanyl-tRNA synthetase (Pf-W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24d023f983656e11e313ddaf39851057
https://pubmed.ncbi.nlm.nih.gov/23776638
https://pubmed.ncbi.nlm.nih.gov/23776638