Evidence map›Paper›PMID 31844018›Full record

ArticleThe Journal of biological chemistry2020

Development of a yeast model to study the contribution of vacuolar polyphosphate metabolism to lysine polyphosphorylation.

Cristina Azevedo, Yann Desfougères, Yannasittha Jiramongkol, Hamish Partington, Sasanan Trakansuebkul, Jyoti Singh, Nicole Steck, Henning J Jessen, Adolfo Saiardi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
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

19 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Ppn2 Polyphosphatase Improves the Ability ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  5. Review
  6. Article
  7. Review
  8. Article
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Biology · 2021
    Article
  16. Article
  17. Article
  18. Catching protein polyphosphorylation in the act.The Journal of biological chemistry · 2020
    Article
  19. 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

9 authors at 2 institutions in 2 countries.

Cristina AzevedoMedical Research Council, Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom. Electronic address: c.azevedo@ucl.ac.uk.
Yann DesfougèresMedical Research Council, Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom.
Yannasittha JiramongkolMedical Research Council, Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom.
Hamish PartingtonMedical Research Council, Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom.
Sasanan TrakansuebkulMedical Research Council, Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom.
Jyoti SinghInstitute of Organic Chemistry, University of Freiburg, 79104 Freiburg, Germany.
Nicole SteckInstitute of Organic Chemistry, University of Freiburg, 79104 Freiburg, Germany.
Henning J JessenInstitute of Organic Chemistry, University of Freiburg, 79104 Freiburg, Germany; CIBSS-Centre for Integrative Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany.
Adolfo SaiardiMedical Research Council, Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom. Electronic address: a.saiardi@ucl.ac.uk.
MRC Laboratory for Molecular Cell Biology · GBUniversity of Freiburg · DE

Funding

Medical Research Council MC_UU_00012/4Medical Research Council MC_UU_12018/4
6 · The paper itself

Abstract

A recently-discovered protein post-translational modification, lysine polyphosphorylation (K-PPn), consists of the covalent attachment of inorganic polyphosphate (polyP) to lysine residues. The nonenzymatic nature of K-PPn means that the degree of this modification depends on both polyP abundance and the amino acids surrounding the modified lysine. K-PPn was originally discovered in budding yeast (

Indexed as

DNA Topoisomerases, Type ILysineNuclear ProteinsPhosphorylationPolyphosphatesProtein Processing, Post-TranslationalRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesDNA Topoisomerases, Type ILysineNSR1 protein, S cerevisiaeNuclear ProteinsPolyphosphatesRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTOP1 protein, S cerevisiaecell signalinginorganic polyphosphatelysine modificationslysine polyphosphorylation (K-PPn)molecular cell biologyphosphorylationpolyphosphatasespost-translational modification (PTM)protein phosphorylationTop1

Identifiers

PMID31844018
PMCPMC7008358
OpenAlexW2996150229

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.