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However, the remeasurement of substantially similar proteomes, for example those generated by perturbation experiments in systems biology, at high reproducibility and throughput remains challenging. Here, we apply a directed MS strategy to detect and quantify sets of pre-determined peptides in tryptic digests of cells of the human pathogen Leptospira interrogans at 25 different states. We show that in a single LC-MS/MS experiment around 5000 peptides, covering 1680 L. interrogans proteins, can be consistently detected and their absolute expression levels estimated, revealing new insights about the proteome changes involved in pathogenic progression and antibiotic defense of L. interrogans. This is the first study that describes the absolute quantitative behavior of any proteome over multiple states, and represents the most comprehensive proteome abundance pattern comparison for any organism to date."],"pubmed_title":["Absolute quantification of microbial proteomes at different states by directed mass spectrometry."],"pubmed_authors":["Schmidt Alexander A, Beck Martin M, Malmström Johan J, Lam Henry H, Claassen Manfred M, Campbell David D, Aebersold Ruedi R"],"additional_accession":[]},"is_claimable":false,"name":"LInterrogans_1D-LC","description":"L. interrogans 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