Evidence map›Paper›PMID 35323738›Full record

ArticleMembranes2022

iAcety-SmRF: Identification of Acetylation Protein by Using Statistical Moments and Random Forest.

Sharaf Malebary, Shaista Rahman, Omar Barukab, Rehab Ash'ari, Sher Afzal Khan

Abstract read
In one paragraph

Article in Membranes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Identify Bitter Peptides by Using Deep Representation Learning Features.International journal of molecular sciences · 2022
    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.

Sharaf MalebaryFaculty of Computing and Information Technology, King Abdulaziz University, Jeddah 21911, Saudi Arabia.ORCID 0000-0003-4339-3791
Shaista RahmanDepartment of Computer Science, Abdul Wali Khan University Mardan, Mardan 23200, Pakistan.ORCID 0000-0002-7054-4957
Omar BarukabFaculty of Computing and Information Technology, King Abdulaziz University, Jeddah 21911, Saudi Arabia.ORCID 0000-0002-5725-9430
Rehab Ash'ariFaculty of Computing and Information Technology, King Abdulaziz University, Jeddah 21911, Saudi Arabia.
Sher Afzal KhanDepartment of Computer Science, Abdul Wali Khan University Mardan, Mardan 23200, Pakistan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylation is the most important post-translation modification (PTM) in eukaryotes; it has manifold effects on the level of protein that transform an acetyl group from an acetyl coenzyme to a specific site on a polypeptide chain. Acetylation sites play many important roles, including regulating membrane protein functions and strongly affecting the membrane interaction of proteins and membrane remodeling. Because of these properties, its correct identification is essential to understand its mechanism in biological systems. As such, some traditional methods, such as mass spectrometry and site-directed mutagenesis, are used, but they are tedious and time-consuming. To overcome such limitations, many computer models are being developed to correctly identify their sequences from non-acetyl sequences, but they have poor efficiency in terms of accuracy, sensitivity, and specificity. This work proposes an efficient and accurate computational model for predicting Acetylation using machine learning approaches. The proposed model achieved an accuracy of 100 percent with the 10-fold cross-validation test based on the Random Forest classifier, along with a feature extraction approach using statistical moments. The model is also validated by the jackknife, self-consistency, and independent test, which achieved an accuracy of 100, 100, and 97, respectively, results far better as compared to the already existing models available in the literature.

Indexed as

acetylationmachine learningmembrane proteinspost-translational modificationprobabilistic neural networkrandom foreststatistical movement

Identifiers

PMID35323738
PMCPMC8955084

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.