Characterization of the human heart mitochondrial proteome. Export

@article{citeulike:3438773, abstract = {To gain a better understanding of the critical role of mitochondria in cell function, we have compiled an extensive catalogue of the mitochondrial proteome using highly purified mitochondria from normal human heart tissue. Sucrose gradient centrifugation was employed to partially resolve protein complexes whose individual protein components were separated by one-dimensional PAGE. Total in-gel processing and subsequent detection by mass spectrometry and rigorous bioinformatic analysis yielded a total of 615 distinct protein identifications. All protein pI values, molecular weight ranges, and hydrophobicities were represented. The coverage of the known subunits of the oxidative phosphorylation machinery within the inner mitochondrial membrane was >90\%. A significant proportion of identified proteins are involved in signaling, RNA, DNA, and protein synthesis, ion transport, and lipid metabolism. The biochemical roles of 19\% of the identified proteins have not been defined. This database of proteins provides a comprehensive resource for the discovery of novel mitochondrial functions and pathways.}, author = {Taylor, S. W. and Fahy, E. and Zhang, B. and Glenn, G. M. and Warnock, D. E. and Wiley, S. and Murphy, A. N. and Gaucher, S. P. and Capaldi, R. A. and Gibson, B. W. and Ghosh, S. S.}, citeulike-article-id = {3438773}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nbt793}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/12592411}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=12592411}, doi = {10.1038/nbt793}, issn = {1087-0156}, journal = {Nature biotechnology}, keywords = {analysis, db, human, methodspaper, mitochondria, parts-list, proteomics}, month = {March}, number = {3}, pages = {281--286}, posted-at = {2008-10-22 09:21:51}, priority = {2}, title = {Characterization of the human heart mitochondrial proteome.}, url = {http://dx.doi.org/10.1038/nbt793}, volume = {21}, year = {2003} }

TY - JOUR ID - citeulike:3438773 L3 - citeulike-article-id:3438773 N2 - To gain a better understanding of the critical role of mitochondria in cell function, we have compiled an extensive catalogue of the mitochondrial proteome using highly purified mitochondria from normal human heart tissue. Sucrose gradient centrifugation was employed to partially resolve protein complexes whose individual protein components were separated by one-dimensional PAGE. Total in-gel processing and subsequent detection by mass spectrometry and rigorous bioinformatic analysis yielded a total of 615 distinct protein identifications. All protein pI values, molecular weight ranges, and hydrophobicities were represented. The coverage of the known subunits of the oxidative phosphorylation machinery within the inner mitochondrial membrane was >90%. A significant proportion of identified proteins are involved in signaling, RNA, DNA, and protein synthesis, ion transport, and lipid metabolism. The biochemical roles of 19% of the identified proteins have not been defined. This database of proteins provides a comprehensive resource for the discovery of novel mitochondrial functions and pathways. IS - 3 JF - Nature biotechnology SN - 1087-0156 EP - 286 TI - Characterization of the human heart mitochondrial proteome. VL - 21 SP - 281 KW - analysis KW - db KW - human KW - methodspaper KW - mitochondria KW - parts-list KW - proteomics AU - Taylor, SW AU - Fahy, E AU - Zhang, B AU - Glenn, GM AU - Warnock, DE AU - Wiley, S AU - Murphy, AN AU - Gaucher, SP AU - Capaldi, RA AU - Gibson, BW AU - Ghosh, SS PY - 2003/03// UR - http://dx.doi.org/10.1038/nbt793 ER -