Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/181798
Title: Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis
Author: Colomé, Núria
Abián, Joaquín
Aloria, Kerman
Arizmendi, Jesús M.
Barceló Batllori, Silvia
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, 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 de Embún, Pilar
Canals, Francesc
Corrales, Fernando
Keywords: Proteòmica
Normalització
Proteomics
Standardization
Issue Date: 1-Nov-2021
Publisher: Elsevier BV
Abstract: 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.
Note: Reproducció del document publicat a: https://doi.org/10.1016/j.jprot.2021.104409
It is part of: Journal of Proteomics, 2021, vol. 251
URI: http://hdl.handle.net/2445/181798
Related resource: https://doi.org/10.1016/j.jprot.2021.104409
ISSN: 1874-3919
Appears in Collections:Articles publicats en revistes (Centres Científics i Tecnològics de la Universitat de Barcelona (CCiTUB))
Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))
Articles publicats en revistes (IDIBAPS: Institut d'investigacions Biomèdiques August Pi i Sunyer)
Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona))

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