A draft map of the mouse pluripotent stem cell spatial proteome. Christoforou, A., Mulvey, C. M., Breckels, L. M., Geladaki, A., Hurrell, T., Hayward, P. C., Naake, T., Gatto, L., Viner, R., Arias, A. M., & Lilley, K. S. Nature Communications, 7:9992, January, 2016.
A draft map of the mouse pluripotent stem cell spatial proteome [link]Paper  doi  abstract   bibtex   
Knowledge of the subcellular distribution of proteins is vital for understanding cellular mechanisms. Capturing the subcellular proteome in a single experiment has proven challenging, with studies focusing on specific compartments or assigning proteins to subcellular niches with low resolution and/or accuracy. Here we introduce hyperLOPIT, a method that couples extensive fractionation, quantitative high-resolution accurate mass spectrometry with multivariate data analysis. We apply hyperLOPIT to a pluripotent stem cell population whose subcellular proteome has not been extensively studied. We provide localization data on over 5,000 proteins with unprecedented spatial resolution to reveal the organization of organelles, sub-organellar compartments, protein complexes, functional networks and steady-state dynamics of proteins and unexpected subcellular locations. The method paves the way for characterizing the impact of post-transcriptional and post-translational modification on protein location and studies involving proteome-level locational changes on cellular perturbation. An interactive open-source resource is presented that enables exploration of these data.
@article{christoforou_draft_2016,
	title = {A draft map of the mouse pluripotent stem cell spatial proteome},
	volume = {7},
	copyright = {© 2016 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.},
	url = {http://www.nature.com/ncomms/2016/160112/ncomms9992/full/ncomms9992.html},
	doi = {10.1038/ncomms9992},
	abstract = {Knowledge of the subcellular distribution of proteins is vital for understanding cellular mechanisms. Capturing the subcellular proteome in a single experiment has proven challenging, with studies focusing on specific compartments or assigning proteins to subcellular niches with low resolution and/or accuracy. Here we introduce hyperLOPIT, a method that couples extensive fractionation, quantitative high-resolution accurate mass spectrometry with multivariate data analysis. We apply hyperLOPIT to a pluripotent stem cell population whose subcellular proteome has not been extensively studied. We provide localization data on over 5,000 proteins with unprecedented spatial resolution to reveal the organization of organelles, sub-organellar compartments, protein complexes, functional networks and steady-state dynamics of proteins and unexpected subcellular locations. The method paves the way for characterizing the impact of post-transcriptional and post-translational modification on protein location and studies involving proteome-level locational changes on cellular perturbation. An interactive open-source resource is presented that enables exploration of these data.},
	language = {en},
	urldate = {2016-04-11},
	journal = {Nature Communications},
	author = {Christoforou, Andy and Mulvey, Claire M. and Breckels, Lisa M. and Geladaki, Aikaterini and Hurrell, Tracey and Hayward, Penelope C. and Naake, Thomas and Gatto, Laurent and Viner, Rosa and Arias, Alfonso Martinez and Lilley, Kathryn S.},
	month = jan,
	year = {2016},
	keywords = {Biochemistry, Biological sciences, Cell biology},
	pages = {9992},
}

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