2026-08-29T06:31:01Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/65762024-10-31T11:41:20Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605col_20.500.12105_19607

00925njm 22002777a 4500 dc Bagwan, Navratan author Bonzon-Kulichenko, Elena author Calvo, Enrique author Lechuga-Vieco, Ana V. author Michalakopoulos, Spiros author Trevisan-Herraz, Marco author Ezkurdia, Iakes author Rodriguez, Jose Manuel author Magni, Ricardo author Latorre-Pellicer, Ana author Enriquez, Jose Antonio author Vazquez, Jesus author 2018 Post-translational modifications hugely increase the functional diversity of proteomes. Recent algorithms based on ultratolerant database searching are forging a path to unbiased analysis of peptide modifications by shotgun mass spectrometry. However, these approaches identify only one-half of the modified forms potentially detectable and do not map the modified residue. Moreover, tools for the quantitative analysis of peptide modifications are currently lacking. Here, we present a suite of algorithms that allows comprehensive identification of detectable modifications, pinpoints the modified residues, and enables their quantitative analysis through an integrated statistical model. These developments were used to characterize the impact of mitochondrial heteroplasmy on the proteome and on the modified peptidome in several tissues from 12-week-old mice. Our results reveal that heteroplasmy mainly affects cardiac tissue, inducing oxidative damage to proteins of the oxidative phosphorylation system, and provide a molecular mechanism explaining the structural and functional alterations produced in heart mitochondria. Cell Rep. 2018; 23(12):3685-3697 10.1016/j.celrep.2018.05.080 2211-1247 Cell Reports 29925008 http://hdl.handle.net/20.500.12105/6576 SPECTROMETRY-BASED PROTEOMICS TANDEM MASS-SPECTROMETRY DATABASE SEARCH TOOL POSTTRANSLATIONAL MODIFICATIONS PEPTIDE IDENTIFICATION SHOTGUN PROTEOMICS QUANTITATIVE PROTEOMICS PHOSPHORYLATION PHOSPHOPROTEOME EXPRESSION Comprehensive Quantification of the Modified Proteome Reveals Oxidative Heart Damage in Mitochondrial Heteroplasmy