Twenty years of protein interaction studies for biological function deciphering.
Intensive methodological developments and technology innovation have been devoted to protein-protein interaction studies over 20years. Genetic indirect assays and sophisticated large scale biochemical analyses have jointly contributed to the elucidation of protein-protein interactions, still with a lot of drawbacks despite heavy investment in human resources and technologies. With the most recent developments in mass spectrometry and computational tools for studying protein content of complex samples, the initial goal of deciphering molecular bases of biological functions is now within reach. Here, we described the various steps of this process and gave examples of key milestones in this scientific story line. This article is part of a Special Issue entitled: 20years of Proteomics in memory of Viatliano Pallini. Guest Editors: Luca Bini, Juan J. Calvete, Natacha Turck, Denis Hochstrasser and Jean-Charles Sanchez.
Ecole polytechnique, Palaiseau, France. Electronic address: pierre.legrain@polytechnique.edu.
Pierre
P
Legrain
Hybrigenics, Paris, France.
Jean-Christophe
JC
Rain
D000818:Animals; D000846:Anniversaries and Special Events; D019295:Computational Biology / Q000266:history / Q000379:methods; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D013058:Mass Spectrometry / Q000266:history / Q000379:methods; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040901:Proteomics / Q000266:history / Q000379:methods
D011506:Proteins
Affinity-purification followed by mass spectrometry; Multimolecular complexes; Protein interactions; Protein network; Yeast two-hybrid