RT Journal Article
T1 Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis.
A1 Colome, Núria
A1 Abian, Joaquin
A1 Aloria, Kerman
A1 Arizmendi, Jesus M
A1 Barcelo-Batllori, Silvia
A1 Braga-Lagache, Sophie
A1 Burlet-Schiltz, Odile
A1 Carrascal, Montse
A1 Casal, J Ignacio
A1 Chicano-Galvez, Eduard
A1 Chiva, Cristina
A1 Clemente, Luis Felipe
A1 Elortza, Felix
A1 Estanyol, Josep M
A1 Fernandez-Irigoyen, Joaquin
A1 Fernandez-Puente, Patricia
A1 Fidalgo, Maria Jose
A1 Froment, Carine
A1 Fuentes, Manuel
A1 Fuentes-Almagro, Carlos
A1 Gay, Marina
A1 Hainard, Alexandre
A1 Heller, Manfred
A1 Hernandez, Maria Luisa
A1 Ibarrola, Nieves
A1 Iloro, Ibon
A1 Kieselbach, Thomas
A1 Lario, Antonio
A1 Locard-Paulet, Marie
A1 Marina-Ramirez, Anabel
A1 Martin, Luna
A1 Morato-Lopez, Esperanza
A1 Muñoz, Javier
A1 Navajas, Rosana
A1 Odena, M Antonia
A1 Odriozola, Leticia
A1 de Oliveira, Eliandre
A1 Paradela, Alberto
A1 Pasquarello, Carla
A1 de Los Rios, Vivian
A1 Ruiz-Romero, Cristina
A1 Sabido, Eduard
A1 Sanchez Del Pino, Manuel
A1 Sancho, Jaime
A1 Santamaria, Enrique
A1 Schaeffer-Reiss, Christine
A1 Schneider, Justine
A1 de la Torre, Carolina
A1 Valero, M Luz
A1 Vilaseca, Marta
A1 Wu, Shuai
A1 Wu, Linfeng
A1 Ximénez de Embún, Pilar
A1 Canals, Francesc
A1 Corrales, Fernando J
K1 Laboratories
K1 Phosphoproteins
K1 Phosphorylation
AB 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.
PB Elsevier
YR 2021
FD 2021-10-27
LK http://hdl.handle.net/10668/22333
UL http://hdl.handle.net/10668/22333
LA en
NO Colomé N, Abian J, Aloria K, Arizmendi JM, Barceló-Batllori S, Braga-Lagache S, et al. Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis. J Proteomics. 2022 Jan 16;251:104409
NO We thank Kevin Ray from MilliporeSigma, Saint Louis, MO, for fruitful discussions on the study design, and MilliporeSigma for kindly providing the Phosphomix standards used in the study. ProteoRed, PRB3 is supported by grant PT17/0019/0001, of the PE I+D+i 2013-2016, funded by ISCIII and ERDF.
DS RISalud
RD Apr 7, 2025