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Frontiers in Molecular Biosciences|March 21, 2022
Proximity-Dependent Biotinylation Approaches to Explore the Dynamic Compartmentalized ProteomeUgo Dionne, Anne-Claude GingrasFEBS Letters|June 20, 2012
Beyond hairballs: The use of quantitative mass spectrometry data to understand protein-protein interactionsAnne-Claude Gingras, Brian RaughtProteomics|June 20, 2012
History of protein-protein interactions: from egg-white to complex networksPascal Braun, Anne-Claude GingrasMethods (San Diego, Calif.)|May 29, 2007
Affinity-purification mass spectrometry (AP-MS) of serine/threonine phosphatasesGinny I Chen, Anne-Claude GingrasProgress in Molecular Biology and Translational Science|February 21, 2012
Mass spectrometric tools for systematic analysis of protein phosphorylationNicole St-Denis, Anne-Claude GingrasCurrent Opinion in Structural Biology|July 25, 2016
Proteomics approaches to decipher new signaling pathwaysAnne-Claude Gingras, Cassandra Jj WongThe Journal of Physiology|December 22, 2004
Advances in protein complex analysis using mass spectrometryAnne-Claude Gingras, Ruedi Aebersold, Brian RaughtMethods in Molecular Biology (Clifton, N.J.)|September 4, 2023
Studying Cellular Dynamics Using Proximity-Dependent Biotinylation: Somatic Cell ReprogrammingReuben Samson, Francesco Zangari, Anne-Claude GingrasNucleic Acids Research|December 21, 2021
Membrane-dependent relief of translation elongation arrest on pseudouridine- and N1-methyl-pseudouridine-modified mRNAsYuri V Svitkin, Anne-Claude Gingras, Nahum SonenbergPageof 37