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Proteomes 2014, 2(2), 191-207; doi:10.3390/proteomes2020191

Developmentally-Dynamic Murine Brain Proteomes and Phosphoproteomes Revealed by Quantitative Proteomics

Department of Biology, University of Vermont, 109 Carrigan Drive, Burlington, VT 05405, USA
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Received: 31 December 2013 / Revised: 14 March 2014 / Accepted: 26 March 2014 / Published: 3 April 2014
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Abstract

Developmental processes are governed by a diverse suite of signaling pathways employing reversible phosphorylation. Recent advances in large-scale phosphoproteomic methodologies have made possible the identification and quantification of hundreds to thousands of phosphorylation sites from primary tissues. Towards a global characterization of proteomic changes across brain development, we present the results of a large-scale quantitative mass spectrometry study comparing embryonic, newborn and adult murine brain. Using anti-phosphotyrosine immuno-affinity chromatography and strong cation exchange (SCX) chromatography, coupled to immobilized metal affinity chromatography (IMAC), we identified and quantified over 1,750 phosphorylation sites and over 1,300 proteins between three developmental states. Bioinformatic analyses highlight functions associated with the identified proteins and phosphoproteins and their enrichment at distinct developmental stages. These results serve as a primary reference resource and reveal dynamic developmental profiles of proteins and phosphoproteins from the developing murine brain. View Full-Text
Keywords: brain development; phosphoproteomics; phosphorylation; quantitative mass spectrometry; reductive amination brain development; phosphoproteomics; phosphorylation; quantitative mass spectrometry; reductive amination
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Doubleday, P.F.; Ballif, B.A. Developmentally-Dynamic Murine Brain Proteomes and Phosphoproteomes Revealed by Quantitative Proteomics. Proteomes 2014, 2, 191-207.

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