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Therefore, identification of mitochondrial proteins in cancer could provide a global view of tumorigenesis and progression. Mass spectrometry\u2010based quantitative mitochondrial proteomics fulfils this task by enabling systems\u2010wide, accurate, and quantitative analysis of mitochondrial protein abundance, and mitochondrial protein posttranslational modifications (PTMs). Multiple quantitative proteomics techniques, including isotope\u2010coded affinity tag, stable isotope labeling with amino acids in cell culture, isobaric tags for relative and absolute quantification, tandem mass tags, and label\u2010free quantification, in combination with different PTM\u2010peptide enrichment methods such as TiO<jats:sub>2<\/jats:sub> enrichment of tryptic phosphopeptides and antibody enrichment of other PTM\u2010peptides, increase flexibility for researchers to study mitochondrial proteomes. 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