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Issue 2, 2016
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Systematic study of the dynamics and half-lives of newly synthesized proteins in human cells

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Abstract

Protein dynamics are essential in regulating nearly every cellular event, and aberrant proteostasis is the source of many diseases. It is extraordinarily difficult to globally study protein dynamics and accurately measure their half-lives. Here we have developed a chemical proteomics method integrating protein labeling, click chemistry and multiplexed proteomics, which overcomes current challenges with existing methods. Labeling with both azidohomoalanine (AHA) and heavy lysine allows us to selectively enrich newly synthesized proteins, clearly distinguish them from existing proteins, and reduce the impact of heavy amino acid recycling. Moreover, multiplexed proteomics enables us to quantify proteins at multiple time points simultaneously, thus increasing the accuracy of measuring protein abundance changes and their half-lives. Systematic investigation of newly synthesized protein dynamics will provide insight into proteostasis and the molecular mechanisms of disease.

Graphical abstract: Systematic study of the dynamics and half-lives of newly synthesized proteins in human cells

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Publication details

The article was received on 08 Oct 2015, accepted on 15 Nov 2015 and first published on 16 Nov 2015


Article type: Edge Article
DOI: 10.1039/C5SC03826J
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Chem. Sci., 2016,7, 1393-1400
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    All publication charges for this article have been paid for by the Royal Society of Chemistry

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    Systematic study of the dynamics and half-lives of newly synthesized proteins in human cells

    W. Chen, J. M. Smeekens and R. Wu, Chem. Sci., 2016, 7, 1393
    DOI: 10.1039/C5SC03826J

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