Evidence map›Paper›PMID 26813983›Full record

ArticleScientific reports2016

Proteome-wide analysis reveals widespread lysine acetylation of major protein complexes in the malaria parasite.

Simon A Cobbold, Joana M Santos, Alejandro Ochoa, David H Perlman, Manuel Llinás

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Article
  3. Unique Properties of Apicomplexan Mitochondria.Annual review of microbiology · 2023
    Review
  4. Article
  5. The mitochondrion ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. The Putative Bromodomain Protein PfBDP7 of the Human Malaria ParasiteFrontiers in cell and developmental biology · 2022
    Article
  11. Review
  12. Review
  13. Article
  14. Peculiarities ofInternational journal of molecular sciences · 2021
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

5 authors at 2 institutions in 1 country.

Simon A CobboldLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.
Joana M SantosLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.
Alejandro OchoaLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.
David H PerlmanLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.
Manuel LlinásLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.
Princeton University · USCenter for Disease Dynamics, Economics & Policy · US

Funding

Spatial Patterning During DevelopmentP50GM071508 · NIGMS · PRINCETON UNIVERSITY · PI POWELL, SUSAN M · 2004 to 2013
$30.6M
Novel antimalarial strategies using metabolomic network discoveryDP2OD001315 · OD · PRINCETON UNIVERSITY · PI LLINAS, MANUEL · 2007 to 2007
$2.4M
NIGMS NIH HHS P50 GM071508NIH HHS 1DP2OD001315-01NIH HHS DP2 OD001315
6 · The paper itself

Abstract

Lysine acetylation is a ubiquitous post-translational modification in many organisms including the malaria parasite Plasmodium falciparum, yet the full extent of acetylation across the parasite proteome remains unresolved. Moreover, the functional significance of acetylation or how specific acetyl-lysine sites are regulated is largely unknown. Here we report a seven-fold expansion of the known parasite 'acetylome', characterizing 2,876 acetylation sites on 1,146 proteins. We observe that lysine acetylation targets a diverse range of protein complexes and is particularly enriched within the Apicomplexan AP2 (ApiAP2) DNA-binding protein family. Using quantitative proteomics we determined that artificial perturbation of the acetate/acetyl-CoA balance alters the acetyl-lysine occupancy of several ApiAP2 DNA-binding proteins and related transcriptional proteins. This metabolic signaling could mediate significant downstream transcriptional responses, as we show that acetylation of an ApiAP2 DNA-binding domain ablates its DNA-binding propensity. Lastly, we investigated the acetyl-lysine targets of each class of lysine deacetylase in order to begin to explore how each class of enzyme contributes to regulating the P. falciparum acetylome.

Indexed as

ProteomeProteomicsAcetylationAmino Acid MotifsAmino Acid SequenceBinding SitesComputational BiologyDNA-Binding ProteinsGene OntologyLysinePlasmodiumPlasmodium falciparumPosition-Specific Scoring MatricesProtein BiosynthesisProtozoan ProteinsTranscription, GeneticDNA-Binding ProteinsLysineProteomeProtozoan Proteins

Identifiers

PMID26813983
PMCPMC4728587
OpenAlexW2414475319

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.