Compositional complexity of the mitochondrial proteome of a unicellular eukaryote (Acanthamoeba castellanii, supergroup Amoebozoa) rivals that of animals, fungi, and plants

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DOIResolve DOI: http://doi.org/10.1016/j.jprot.2014.07.005
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TypeArticle
Journal titleJournal of Proteomics
ISSN1874-3919
Volume109
Pages400416; # of pages: 17
Subjectglyoxylic acid; hybrid protein; iron; isocitrate lyase; malate synthase; mitochondrial protein; pyruvic acid; sulfur; tricarboxylic acid; ferrous sulfide; isocitrate lyase; malate synthase; mitochondrial DNA; proteome; ribosome protein; amino acid metabolism; amino acid sequence; bioinformatics; biosynthesis; cell nucleus; cell respiration; chemical composition; computer model; data mining; DNA metabolism; DNA replication; DNA transcription; mass spectrometry; mitochondrial targeting signal; molecular evolution; phylogeny; protein analysis; protein degradation; protein domain; protein metabolism; protein targeting; protein transport; RNA metabolism; citric acid cycle; nucleotide metabolism; protist; tandem mass spectrometry; Acanthamoeba castellanii; Amoebozoa; Fungi
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PublisherElsevier
LanguageEnglish
AffiliationNational Research Council Canada; Human Health Therapeutics
Peer reviewedYes
NPARC number21275451
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Record identifierd47df9aa-60b7-4050-827e-0313554dc565
Record created2015-07-14
Record modified2017-03-23
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