Evidence map›Paper›PMID 23173045›Full record

ArticlePloS one2012

Position-specific analysis and prediction for protein lysine acetylation based on multiple features.

Sheng-Bao Suo, Jian-Ding Qiu, Shao-Ping Shi, Xing-Yu Sun, Shu-Yun Huang, Xiang Chen, Ru-Ping Liang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 18% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
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  5. Review
  6. Article
  7. Article
  8. CREB1ACS omega · 2021
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  12. Review
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  15. Article
  16. LAIPT: Lysine Acetylation Site Identification with Polynomial Tree.International journal of molecular sciences · 2018
    Article
  17. Article
  18. Article
  19. Article
  20. Protein post-translational modifications:Computational and structural biotechnology journal · 2017
    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

7 authors at 1 institution in 1 country.

Sheng-Bao SuoDepartment of Chemistry, Nanchang University, Nanchang, China.
Jian-Ding Qiu
Shao-Ping Shi
Xing-Yu Sun
Shu-Yun Huang
Xiang Chen
Ru-Ping Liang
Nanchang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein lysine acetylation is a type of reversible post-translational modification that plays a vital role in many cellular processes, such as transcriptional regulation, apoptosis and cytokine signaling. To fully decipher the molecular mechanisms of acetylation-related biological processes, an initial but crucial step is the recognition of acetylated substrates and the corresponding acetylation sites. In this study, we developed a position-specific method named PSKAcePred for lysine acetylation prediction based on support vector machines. The residues around the acetylation sites were selected or excluded based on their entropy values. We incorporated features of amino acid composition information, evolutionary similarity and physicochemical properties to predict lysine acetylation sites. The prediction model achieved an accuracy of 79.84% and a Matthews correlation coefficient of 59.72% using the 10-fold cross-validation on balanced positive and negative samples. A feature analysis showed that all features applied in this method contributed to the acetylation process. A position-specific analysis showed that the features derived from the critical neighboring residues contributed profoundly to the acetylation site determination. The detailed analysis in this paper can help us to understand more of the acetylation mechanism and can provide guidance for the related experimental validation.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceBinding SitesChemical PhenomenaComputational BiologyConserved SequenceEvolution, MolecularLysineProteinsUser-Computer InterfaceLysineProteins

Identifiers

PMID23173045
PMCPMC3500252
OpenAlexW1999118478

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.