Evidence map›Paper›PMID 31555063›Full record

ArticleCurrent genomics2019

iHyd-PseAAC (EPSV): Identifying Hydroxylation Sites in Proteins by Extracting Enhanced Position and Sequence Variant Feature

Asma Ehsan, Muhammad K Mahmood, Yaser D Khan, Omar M Barukab, Sher A Khan, Kuo-Chen Chou

Abstract read
In one paragraph

Article in Current genomics, 2019. 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
–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

10 citing papers in PubMed.

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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

6 authors.

Asma Ehsan1Department of Mathematics, University of the Punjab, Lahore, Pakistan; 2Faculty of Information Technology, University of Management and Technology, Lahore, Pakistan; 3King Abdul Aziz University, Faculty of Computing and Information Technology in Rabigh, Jeddah, KSA; 4Gordon Life Science Institute, Boston, MA 02478, USA.
Muhammad K Mahmood1Department of Mathematics, University of the Punjab, Lahore, Pakistan; 2Faculty of Information Technology, University of Management and Technology, Lahore, Pakistan; 3King Abdul Aziz University, Faculty of Computing and Information Technology in Rabigh, Jeddah, KSA; 4Gordon Life Science Institute, Boston, MA 02478, USA.
Yaser D Khan1Department of Mathematics, University of the Punjab, Lahore, Pakistan; 2Faculty of Information Technology, University of Management and Technology, Lahore, Pakistan; 3King Abdul Aziz University, Faculty of Computing and Information Technology in Rabigh, Jeddah, KSA; 4Gordon Life Science Institute, Boston, MA 02478, USA.
Omar M Barukab1Department of Mathematics, University of the Punjab, Lahore, Pakistan; 2Faculty of Information Technology, University of Management and Technology, Lahore, Pakistan; 3King Abdul Aziz University, Faculty of Computing and Information Technology in Rabigh, Jeddah, KSA; 4Gordon Life Science Institute, Boston, MA 02478, USA.
Sher A Khan1Department of Mathematics, University of the Punjab, Lahore, Pakistan; 2Faculty of Information Technology, University of Management and Technology, Lahore, Pakistan; 3King Abdul Aziz University, Faculty of Computing and Information Technology in Rabigh, Jeddah, KSA; 4Gordon Life Science Institute, Boston, MA 02478, USA.
Kuo-Chen Chou1Department of Mathematics, University of the Punjab, Lahore, Pakistan; 2Faculty of Information Technology, University of Management and Technology, Lahore, Pakistan; 3King Abdul Aziz University, Faculty of Computing and Information Technology in Rabigh, Jeddah, KSA; 4Gordon Life Science Institute, Boston, MA 02478, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn various biological processes and cell functions, Post Translational Modifications (PTMs) bear critical significance. Hydroxylation of proline residue is one kind of PTM, which occurs following protein synthesis. The experimental determination of hydroxyproline sites in an uncharacterized protein sequence requires extensive, time-consuming and expensive tests.

methodsWith the torrential slide of protein sequences produced in the post-genomic age, certain remarkable computational strategies are desired to overwhelm the issue. Keeping in view the composition and sequence order effect within polypeptide chains, an innovative

resultsLater, it was stringently verified using self-consistency, cross-validation and jackknife tests on benchmark datasets. It was established after a rigorous jackknife test that the new predictor values are superior to the values predicted by previous methodologies.

conclusionThis new mathematical technique is the most appropriate and encouraging as compared with the existing models.

Indexed as

Hydroxylation of prolineHydroxyprolineMammalian proteinsPost Translational Modifications (PTMs)PseAACSequence-coupling model

Identifiers

PMID31555063
PMCPMC6728902

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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.