{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bons J"],"funding":["Agence Nationale de la Recherche (ANR)"],"pagination":["1085-1095"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6553941"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(6)"],"pubmed_abstract":["All but thirteen mammalian mitochondrial proteins are encoded by the nuclear genome, translated in the cytosol and then imported into the mitochondria. For a significant proportion of the mitochondrial proteins, import is coupled with the cleavage of a presequence called the transit peptide, and the formation of a new N-terminus. Determination of the neo N-termini has been investigated by proteomic approaches in several systems, but generally in a static way to compile as many N-termini as possible. In the present study, we have investigated how the mitochondrial proteome and N-terminome react to chemical stimuli that alter mitochondrial metabolism, namely zinc ions and rapamycin. To this end, we have used a strategy that analyzes both internal and N-terminal peptides in a single run, the "],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["A Combined N-terminomics and Shotgun Proteomics Approach to Investigate the Responses of Human Cells to Rapamycin and Zinc at the Mitochondrial Level."],"pmcid":["PMC6553941"],"funding_grant_id":["energiome"],"pubmed_authors":["Carapito C","Bons J","Macron C","Rompais M","Aude-Garcia C","Cianferani S","Vaca-Jacome SA","Rabilloud T"],"additional_accession":[]},"is_claimable":false,"name":"A Combined N-terminomics and Shotgun Proteomics Approach to Investigate the Responses of Human Cells to Rapamycin and Zinc at the Mitochondrial Level.","description":"All but thirteen mammalian mitochondrial proteins are encoded by the nuclear genome, translated in the cytosol and then imported into the mitochondria. For a significant proportion of the mitochondrial proteins, import is coupled with the cleavage of a presequence called the transit peptide, and the formation of a new N-terminus. Determination of the neo N-termini has been investigated by proteomic approaches in several systems, but generally in a static way to compile as many N-termini as possible. In the present study, we have investigated how the mitochondrial proteome and N-terminome react to chemical stimuli that alter mitochondrial metabolism, namely zinc ions and rapamycin. To this end, we have used a strategy that analyzes both internal and N-terminal peptides in a single run, the ","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jun","modification":"2026-04-07T17:07:04.471Z","creation":"2020-06-04T07:07:49Z"},"accession":"S-EPMC6553941","cross_references":{"pubmed":["31154437"],"doi":["10.1074/mcp.ra118.001269","10.1074/mcp.RA118.001269"]}}