2026-06-16T15:00:03Zhttps://repisalud.isciii.es/rest/oai/requestoai: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
Repisalud
author
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
funder
Ministerio de Economía y Competitividad (España)
funder
Fundación La Marató TV3
funder
Unión Europea. Comisión Europea
funder
Instituto de Salud Carlos III
funder
Fundación ProCNIC
2018-11-05T11:58:21Z
2018-11-05T11:58:21Z
2018
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
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.
eng
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
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