Evidence map›Paper›PMID 22164248›Full record

ArticlePloS one2011

Bioinformatic analysis and post-translational modification crosstalk prediction of lysine acetylation.

Zhike Lu, Zhongyi Cheng, Yingming Zhao, Samuel L Volchenboum

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 53 citations in OpenAlex.

  1. Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  2. Review
  3. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. A Molecular Perspective on Sirtuin Activity.International journal of molecular sciences · 2020
    Review
  8. Article
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  18. Review
  19. Article
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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

4 authors at 1 institution in 1 country.

Zhike LuBen May Department for Cancer Research, University of Chicago, Chicago, Illinois, United States of America.
Zhongyi Cheng
Yingming Zhao
Samuel L Volchenboum
University of Chicago · US

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Global characterization of lysine acetylation in cancer by a proteomics approachR01CA126832 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI ZHAO, YINGMING · 2008 to 2012
$1.6M
NCI NIH HHS CA126832NCI NIH HHS R01 CA126832NCRR NIH HHS RR020839NCRR NIH HHS U54 RR020839
6 · The paper itself

Abstract

Recent proteomics studies suggest high abundance and a much wider role for lysine acetylation (K-Ac) in cellular functions. Nevertheless, cross influence between K-Ac and other post-translational modifications (PTMs) has not been carefully examined. Here, we used a variety of bioinformatics tools to analyze several available K-Ac datasets. Using gene ontology databases, we demonstrate that K-Ac sites are found in all cellular compartments. KEGG analysis indicates that the K-Ac sites are found on proteins responsible for a diverse and wide array of vital cellular functions. Domain structure prediction shows that K-Ac sites are found throughout a wide variety of protein domains, including those in heat shock proteins and those involved in cell cycle functions and DNA repair. Secondary structure prediction proves that K-Ac sites are preferentially found in ordered structures such as alpha helices and beta sheets. Finally, by mutating K-Ac sites in silico and predicting the effect on nearby phosphorylation sites, we demonstrate that the majority of lysine acetylation sites have the potential to impact protein phosphorylation, methylation, and ubiquitination status. Our work validates earlier smaller-scale studies on the acetylome and demonstrates the importance of PTM crosstalk for regulation of cellular function.

Indexed as

Gene Expression RegulationProtein Processing, Post-TranslationalAcetylationAnimalsCell CycleComputational BiologyDNA RepairHumansLysineMethylationMiceModels, BiologicalPhosphorylationProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryLysineUbiquitin

Identifiers

PMID22164248
PMCPMC3229533
OpenAlexW2041408621

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.