Title |
From underlying chemistry to therapeutic potential: open questions in the new field of lysine polyphosphorylation
|
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Published in |
Current Genetics, June 2018
|
DOI | 10.1007/s00294-018-0854-4 |
Pubmed ID | |
Authors |
Amanda Bentley-DeSousa, Michael Downey |
Abstract |
Polyphosphorylation is a newly described non-enzymatic post-translational modification wherein long chains of inorganic phosphates are attached to lysine residues. The first targets of polyphosphorylation identified were S. cerevisiae proteins Nsr1 and Top1. Building on this theme, we recently exploited functional genomics tools in yeast to identify 15 new targets, including a conserved network of nucleolar proteins implicated in ribosome biogenesis. We also described the polyphosphorylation of six human proteins, suggesting that this unique post-translational modification could be conserved throughout eukaryotes. The study of polyphosphorylation seems poised to uncover novel modes of protein regulation in pathways spanning diverse biological processes. In this review, we establish a framework for future work by outlining critical questions related to the biochemistry of polyphosphorylation, its therapeutic potential, and everything in between. |
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Canada | 5 | 42% |
United Kingdom | 2 | 17% |
United States | 2 | 17% |
Unknown | 3 | 25% |
Demographic breakdown
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Members of the public | 4 | 33% |
Mendeley readers
Geographical breakdown
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Unknown | 16 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 4 | 25% |
Student > Bachelor | 3 | 19% |
Student > Master | 3 | 19% |
Professor | 1 | 6% |
Unspecified | 1 | 6% |
Other | 1 | 6% |
Unknown | 3 | 19% |
Readers by discipline | Count | As % |
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Unspecified | 1 | 6% |
Energy | 1 | 6% |
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Medicine and Dentistry | 1 | 6% |
Other | 0 | 0% |
Unknown | 2 | 13% |