Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis

Global analysis of protein phosphorylation by mass spectrometry proteomic techniques has emerged in the last decades as a powerful tool in biological and biomedical research. However, there are several factors that make the global study of the phosphoproteome more challenging than measuring non-modi...

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Autores: Colomé, Núria, Abián, Joaquín, Aloria, Kerman, Arizmendi, Jesús M., Barceló Batllori, Sílvia, Braga Lagache, Sophie, Burlet Schiltz, Odile, Carrascal, Montse, Casal, J. Ignacio, Chicano Gálvez, Eduard, Chiva, Cristina, Clemente, Luis Felipe, Elortza, Felix, Estanyol i Ullate, Josep Maria, Fernandez Irigoyen, Joaquín, Fernández Puente, Patricia, Fidalgo, María José, Froment, Carine, Fuentes, Manuel, Fuentes Almagro, Carlos, Gay, Marina, Hainard, Alexandre, Heller, Manfred, Hernández, María Luisa, Ibarrola, Nieves, Iloro, Ibon, Kieselbach, Thomas, Lario, Antonio, Locard Paulet, Marie, Marina Ramírez, Anabel, Martín, Luna, Morato López, Esperanza, Muñoz, Javier, Navajas, Rosana, Odena, M. Antonia, Odriozola, Leticia, Oliveira, Eliandre, Paradela, Alberto, Pasquarello Mosimann, Carla, Rios, Vivian de los, Ruiz Romero, Cristina, Sabidó Aguadé, Eduard, Sánchez del Pino, Manuel, Sancho, Jaime, Santamaría, Enrique, Schaeffer Reiss, Christine, Schneider, Justine, Torre, Carolina de la, Valero, M. Luz, Vilaseca, Marta, Wu, Shuai, Wu, Linfeng, Ximénez Embún, Pilar, Canals, Francesc, Corrales, Fernando
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/181798
Acceso en línea:https://hdl.handle.net/2445/181798
Access Level:acceso abierto
Palabra clave:Proteòmica
Normalització
Proteomics
Standardization
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spelling Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysisColomé, NúriaAbián, JoaquínAloria, KermanArizmendi, Jesús M.Barceló Batllori, SílviaBraga Lagache, SophieBurlet Schiltz, OdileCarrascal, MontseCasal, J. IgnacioChicano Gálvez, EduardChiva, CristinaClemente, Luis FelipeElortza, FelixEstanyol i Ullate, Josep MariaFernandez Irigoyen, JoaquínFernández Puente, PatriciaFidalgo, María JoséFroment, CarineFuentes, ManuelFuentes Almagro, CarlosGay, MarinaHainard, AlexandreHeller, ManfredHernández, María LuisaIbarrola, NievesIloro, IbonKieselbach, ThomasLario, AntonioLocard Paulet, MarieMarina Ramírez, AnabelMartín, LunaMorato López, EsperanzaMuñoz, JavierNavajas, RosanaOdena, M. AntoniaOdriozola, LeticiaOliveira, EliandreParadela, AlbertoPasquarello Mosimann, CarlaRios, Vivian de losRuiz Romero, CristinaSabidó Aguadé, EduardSánchez del Pino, ManuelSancho, JaimeSantamaría, EnriqueSchaeffer Reiss, ChristineSchneider, JustineTorre, Carolina de laValero, M. LuzVilaseca, MartaWu, ShuaiWu, LinfengXiménez Embún, PilarCanals, FrancescCorrales, FernandoProteòmicaNormalitzacióProteomicsStandardizationGlobal analysis of protein phosphorylation by mass spectrometry proteomic techniques has emerged in the last decades as a powerful tool in biological and biomedical research. However, there are several factors that make the global study of the phosphoproteome more challenging than measuring non-modified proteins. The low stoichiometry of the phosphorylated species and the need to retrieve residue specific information require particular attention on sample preparation, data acquisition and processing to ensure reproducibility, qualitative and quantitative robustness and ample phosphoproteome coverage in phosphoproteomic workflows. Aiming to investigate the effect of different variables in the performance of proteome wide phosphoprotein analysis protocols, ProteoRed-ISCIII and EuPA launched the Proteomics Multicentric Experiment 11 (PME11). A reference sample consisting of a yeast protein extract spiked in with different amounts of a phosphomix standard (Sigma/Merck) was distributed to 31 laboratories around the globe. Thirty-six datasets from 23 laboratories were analyzed. Our results indicate the suitability of the PME11 reference sample to benchmark and optimize phosphoproteomics strategies, weighing the influence of different factors, as well as to rank intra and inter laboratory performance.Elsevier BV2021202120212021info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion6 p.application/pdfhttps://hdl.handle.net/2445/181798Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.1016/j.jprot.2021.104409Journal of Proteomics, 2021, vol. 251https://doi.org/10.1016/j.jprot.2021.104409cc by (c) Colomé, Núria et al, 2021http://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1817982026-05-29T05:05:01Z
dc.title.none.fl_str_mv Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
spellingShingle Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
Colomé, Núria
Proteòmica
Normalització
Proteomics
Standardization
title_short Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_full Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_fullStr Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_full_unstemmed Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
title_sort Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
dc.creator.none.fl_str_mv Colomé, Núria
Abián, Joaquín
Aloria, Kerman
Arizmendi, Jesús M.
Barceló Batllori, Sílvia
Braga Lagache, Sophie
Burlet Schiltz, Odile
Carrascal, Montse
Casal, J. Ignacio
Chicano Gálvez, Eduard
Chiva, Cristina
Clemente, Luis Felipe
Elortza, Felix
Estanyol i Ullate, Josep Maria
Fernandez Irigoyen, Joaquín
Fernández Puente, Patricia
Fidalgo, María José
Froment, Carine
Fuentes, Manuel
Fuentes Almagro, Carlos
Gay, Marina
Hainard, Alexandre
Heller, Manfred
Hernández, María Luisa
Ibarrola, Nieves
Iloro, Ibon
Kieselbach, Thomas
Lario, Antonio
Locard Paulet, Marie
Marina Ramírez, Anabel
Martín, Luna
Morato López, Esperanza
Muñoz, Javier
Navajas, Rosana
Odena, M. Antonia
Odriozola, Leticia
Oliveira, Eliandre
Paradela, Alberto
Pasquarello Mosimann, Carla
Rios, Vivian de los
Ruiz Romero, Cristina
Sabidó Aguadé, Eduard
Sánchez del Pino, Manuel
Sancho, Jaime
Santamaría, Enrique
Schaeffer Reiss, Christine
Schneider, Justine
Torre, Carolina de la
Valero, M. Luz
Vilaseca, Marta
Wu, Shuai
Wu, Linfeng
Ximénez Embún, Pilar
Canals, Francesc
Corrales, Fernando
author Colomé, Núria
author_facet Colomé, Núria
Abián, Joaquín
Aloria, Kerman
Arizmendi, Jesús M.
Barceló Batllori, Sílvia
Braga Lagache, Sophie
Burlet Schiltz, Odile
Carrascal, Montse
Casal, J. Ignacio
Chicano Gálvez, Eduard
Chiva, Cristina
Clemente, Luis Felipe
Elortza, Felix
Estanyol i Ullate, Josep Maria
Fernandez Irigoyen, Joaquín
Fernández Puente, Patricia
Fidalgo, María José
Froment, Carine
Fuentes, Manuel
Fuentes Almagro, Carlos
Gay, Marina
Hainard, Alexandre
Heller, Manfred
Hernández, María Luisa
Ibarrola, Nieves
Iloro, Ibon
Kieselbach, Thomas
Lario, Antonio
Locard Paulet, Marie
Marina Ramírez, Anabel
Martín, Luna
Morato López, Esperanza
Muñoz, Javier
Navajas, Rosana
Odena, M. Antonia
Odriozola, Leticia
Oliveira, Eliandre
Paradela, Alberto
Pasquarello Mosimann, Carla
Rios, Vivian de los
Ruiz Romero, Cristina
Sabidó Aguadé, Eduard
Sánchez del Pino, Manuel
Sancho, Jaime
Santamaría, Enrique
Schaeffer Reiss, Christine
Schneider, Justine
Torre, Carolina de la
Valero, M. Luz
Vilaseca, Marta
Wu, Shuai
Wu, Linfeng
Ximénez Embún, Pilar
Canals, Francesc
Corrales, Fernando
author_role author
author2 Abián, Joaquín
Aloria, Kerman
Arizmendi, Jesús M.
Barceló Batllori, Sílvia
Braga Lagache, Sophie
Burlet Schiltz, Odile
Carrascal, Montse
Casal, J. Ignacio
Chicano Gálvez, Eduard
Chiva, Cristina
Clemente, Luis Felipe
Elortza, Felix
Estanyol i Ullate, Josep Maria
Fernandez Irigoyen, Joaquín
Fernández Puente, Patricia
Fidalgo, María José
Froment, Carine
Fuentes, Manuel
Fuentes Almagro, Carlos
Gay, Marina
Hainard, Alexandre
Heller, Manfred
Hernández, María Luisa
Ibarrola, Nieves
Iloro, Ibon
Kieselbach, Thomas
Lario, Antonio
Locard Paulet, Marie
Marina Ramírez, Anabel
Martín, Luna
Morato López, Esperanza
Muñoz, Javier
Navajas, Rosana
Odena, M. Antonia
Odriozola, Leticia
Oliveira, Eliandre
Paradela, Alberto
Pasquarello Mosimann, Carla
Rios, Vivian de los
Ruiz Romero, Cristina
Sabidó Aguadé, Eduard
Sánchez del Pino, Manuel
Sancho, Jaime
Santamaría, Enrique
Schaeffer Reiss, Christine
Schneider, Justine
Torre, Carolina de la
Valero, M. Luz
Vilaseca, Marta
Wu, Shuai
Wu, Linfeng
Ximénez Embún, Pilar
Canals, Francesc
Corrales, Fernando
author2_role author
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dc.subject.none.fl_str_mv Proteòmica
Normalització
Proteomics
Standardization
topic Proteòmica
Normalització
Proteomics
Standardization
description Global analysis of protein phosphorylation by mass spectrometry proteomic techniques has emerged in the last decades as a powerful tool in biological and biomedical research. However, there are several factors that make the global study of the phosphoproteome more challenging than measuring non-modified proteins. The low stoichiometry of the phosphorylated species and the need to retrieve residue specific information require particular attention on sample preparation, data acquisition and processing to ensure reproducibility, qualitative and quantitative robustness and ample phosphoproteome coverage in phosphoproteomic workflows. Aiming to investigate the effect of different variables in the performance of proteome wide phosphoprotein analysis protocols, ProteoRed-ISCIII and EuPA launched the Proteomics Multicentric Experiment 11 (PME11). A reference sample consisting of a yeast protein extract spiked in with different amounts of a phosphomix standard (Sigma/Merck) was distributed to 31 laboratories around the globe. Thirty-six datasets from 23 laboratories were analyzed. Our results indicate the suitability of the PME11 reference sample to benchmark and optimize phosphoproteomics strategies, weighing the influence of different factors, as well as to rank intra and inter laboratory performance.
publishDate 2021
dc.date.none.fl_str_mv 2021
2021
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/181798
url https://hdl.handle.net/2445/181798
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1016/j.jprot.2021.104409
Journal of Proteomics, 2021, vol. 251
https://doi.org/10.1016/j.jprot.2021.104409
dc.rights.none.fl_str_mv cc by (c) Colomé, Núria et al, 2021
http://creativecommons.org/licenses/by/3.0/es/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc by (c) Colomé, Núria et al, 2021
http://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 6 p.
application/pdf
dc.publisher.none.fl_str_mv Elsevier BV
publisher.none.fl_str_mv Elsevier BV
dc.source.none.fl_str_mv Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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