Evidence map›Paper›PMID 34556767›Full record

ArticleScientific reports2021

Computational identification of multiple lysine PTM sites by analyzing the instance hardness and feature importance.

Sabit Ahmed, Afrida Rahman, Md Al Mehedi Hasan, Shamim Ahmad, S M Shovan

Abstract readValidation Study
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed, 1 pooled it
–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

7 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Impact of Lysine Succinylation on the Biology of Fungi.Current issues in molecular biology · 2024
    Review
  6. Article
  7. 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

5 authors.

Sabit AhmedComputer Science and Engineering, Rajshahi University of Engineering and Technology, Rajshahi, 6204, Bangladesh. sabit.a.sirat@gmail.com.
Afrida RahmanComputer Science and Engineering, Rajshahi University of Engineering and Technology, Rajshahi, 6204, Bangladesh.
Md Al Mehedi HasanComputer Science and Engineering, Rajshahi University of Engineering and Technology, Rajshahi, 6204, Bangladesh.
Shamim AhmadComputer Science and Engineering, University of Rajshahi, Rajshahi, 6205, Bangladesh.
S M ShovanComputer Science and Engineering, Rajshahi University of Engineering and Technology, Rajshahi, 6204, Bangladesh.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identification of post-translational modifications (PTM) is significant in the study of computational proteomics, cell biology, pathogenesis, and drug development due to its role in many bio-molecular mechanisms. Though there are several computational tools to identify individual PTMs, only three predictors have been established to predict multiple PTMs at the same lysine residue. Furthermore, detailed analysis and assessment on dataset balancing and the significance of different feature encoding techniques for a suitable multi-PTM prediction model are still lacking. This study introduces a computational method named 'iMul-kSite' for predicting acetylation, crotonylation, methylation, succinylation, and glutarylation, from an unrecognized peptide sample with one, multiple, or no modifications. After successfully eliminating the redundant data samples from the majority class by analyzing the hardness of the sequence-coupling information, feature representation has been optimized by adopting the combination of ANOVA F-Test and incremental feature selection approach. The proposed predictor predicts multi-label PTM sites with 92.83% accuracy using the top 100 features. It has also achieved a 93.36% aiming rate and 96.23% coverage rate, which are much better than the existing state-of-the-art predictors on the validation test. This performance indicates that 'iMul-kSite' can be used as a supportive tool for further K-PTM study. For the convenience of the experimental scientists, 'iMul-kSite' has been deployed as a user-friendly web-server at http://103.99.176.239/iMul-kSite .

Indexed as

AlgorithmsComputational BiologyDatasets as TopicHumansLysineProtein Processing, Post-TranslationalLysine

Identifiers

PMID34556767
PMCPMC8460736

What OpenQuestion holds

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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.