Evidence map›Paper›PMID 29881919›Full record

ReviewCurrent genetics2019

From underlying chemistry to therapeutic potential: open questions in the new field of lysine polyphosphorylation.

Amanda Bentley-DeSousa, Michael Downey

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Pyro(phospho)mania.Nature chemical biology · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Effect of Polyphosphorylation on Behavior of Protein Disordered Regions.International journal of molecular sciences · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Amanda Bentley-DeSousaDepartment of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON, K1H 8M5, Canada.
Michael DowneyDepartment of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON, K1H 8M5, Canada. mdowne2@uottawa.ca.

Funding

Canadian Institutes of Health Research PJT-148722
6 · The paper itself

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.

Indexed as

DNA Topoisomerases, Type ILysineNuclear ProteinsPhosphorylationProtein Processing, Post-TranslationalRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionDNA Topoisomerases, Type ILysineNSR1 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTOP1 protein, S cerevisiaeEcPPK1Lysine polyphosphorylationPolyPPpn1Ppn2Ppx1Vtc4

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.