Evidence map›Paper›PMID 32878321›Full record

ArticleGenes2020

Accurately Predicting Glutarylation Sites Using Sequential Bi-Peptide-Based Evolutionary Features.

Md Easin Arafat, Md Wakil Ahmad, S M Shovan, Abdollah Dehzangi, Shubhashis Roy Dipta, Md Al Mehedi Hasan, Ghazaleh Taherzadeh, Swakkhar Shatabda, Alok Sharma

Open access · goldAbstract read
In one paragraph

Article in Genes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. A chemical field guide to histone nonenzymatic modifications.Current opinion in chemical biology · 2021
    Review
  10. Functions and Mechanisms of Lysine Glutarylation in Eukaryotes.Frontiers in cell and developmental biology · 2021
    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 5 institutions in 5 countries.

Md Easin ArafatDepartment of Computer Science and Engineering, United International University, Dhaka 1212, Bangladesh.ORCID 0000-0003-4014-9144
Md Wakil AhmadDepartment of Computer Science and Engineering, United International University, Dhaka 1212, Bangladesh.
S M ShovanDepartment of Computer Science and Engineering, Rajshahi University of Engineering and Technology, Rajshahi 6204, Bangladesh.
Abdollah DehzangiDepartment of Computer Science, Rutgers University, Camden, NJ 08102, USA.
Shubhashis Roy DiptaDepartment of Computer Science and Engineering, United International University, Dhaka 1212, Bangladesh.ORCID 0000-0002-9176-1782
Md Al Mehedi HasanDepartment of Computer Science and Engineering, Rajshahi University of Engineering and Technology, Rajshahi 6204, Bangladesh.
Ghazaleh TaherzadehInstitute for Bioscience and Biotechnology Research, University of Maryland, College Park, MD 20742, USA.
Swakkhar ShatabdaDepartment of Computer Science and Engineering, United International University, Dhaka 1212, Bangladesh.ORCID 0000-0003-0669-072X
Alok SharmaInstitute for Integrated and Intelligent Systems, Griffith University, Brisbane, QLD 4111, Australia.
United International University · BDRajshahi University of Engineering and Technology · BDGriffith University · AURutgers, The State University of New Jersey · USUniversity of Maryland, College Park · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post Translational Modification (PTM) is defined as the alteration of protein sequence upon interaction with different macromolecules after the translation process. Glutarylation is considered one of the most important PTMs, which is associated with a wide range of cellular functioning, including metabolism, translation, and specified separate subcellular localizations. During the past few years, a wide range of computational approaches has been proposed to predict Glutarylation sites. However, despite all the efforts that have been made so far, the prediction performance of the Glutarylation sites has remained limited. One of the main challenges to tackle this problem is to extract features with significant discriminatory information. To address this issue, we propose a new machine learning method called BiPepGlut using the concept of a bi-peptide-based evolutionary method for feature extraction. To build this model, we also use the Extra-Trees (ET) classifier for the classification purpose, which, to the best of our knowledge, has never been used for this task. Our results demonstrate BiPepGlut is able to significantly outperform previously proposed models to tackle this problem. BiPepGlut achieves 92.0%, 84.8%, 95.6%, 0.82, and 0.88 in accuracy, sensitivity, specificity, Matthew's Correlation Coefficient, and F1-score, respectively. BiPepGlut is implemented as a publicly available online predictor.

Indexed as

Evolution, MolecularProtein Processing, Post-TranslationalAlgorithmsAmino Acid SequenceAnimalsComputational BiologyGlutaratesLysineMachine LearningMiceMycobacterium tuberculosisPeptide FragmentsProteinsSupport Vector MachineGlutaratesglutaric acidLysinePeptide FragmentsProteinsbi-peptide evolutionary featuresextra-trees classifierlysine Glutarylationmachine learningpost-translational modification

Identifiers

PMID32878321
PMCPMC7565944
OpenAlexW3082862577

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.