Evidence map›Paper›PMID 30544729›Full record

ArticleMolecules (Basel, Switzerland)2018

SumSec: Accurate Prediction of Sumoylation Sites Using Predicted Secondary Structure.

Abdollah Dehzangi, Yosvany López, Ghazaleh Taherzadeh, Alok Sharma, Tatsuhiko Tsunoda

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

7 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

5 authors.

Abdollah DehzangiDepartment of Computer Science, Morgan State University, Baltimore, MD 21251, USA. abdollah.dehzangi@morgan.edu.
Yosvany LópezGenesis Institute of Genetic Research, Genesis Healthcare Co., Tokyo 150-6015, Japan. yosvany.lopez.alvarez@gmail.com.
Ghazaleh TaherzadehSchool of Information and Communication Technology, Griffith University, Gold Coast 4222, Australia. ghazaleh.taherzadeh@griffithuni.edu.au.
Alok SharmaInstitute for Integrated and Intelligent Systems, Griffith University, Brisbane 4111, Australia. alokanand.sharma@riken.jp.
Tatsuhiko TsunodaLaboratory for Medical Science Mathematics, RIKEN Center for Integrative Medical Sciences, Yokohama, Kanagawa 230-0045, Japan. tatsuhiko.tsunoda@riken.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post Translational Modification (PTM) is defined as the modification of amino acids along the protein sequences after the translation process. These modifications significantly impact on the functioning of proteins. Therefore, having a comprehensive understanding of the underlying mechanism of PTMs turns out to be critical in studying the biological roles of proteins. Among a wide range of PTMs, sumoylation is one of the most important modifications due to its known cellular functions which include transcriptional regulation, protein stability, and protein subcellular localization. Despite its importance, determining sumoylation sites via experimental methods is time-consuming and costly. This has led to a great demand for the development of fast computational methods able to accurately determine sumoylation sites in proteins. In this study, we present a new machine learning-based method for predicting sumoylation sites called SumSec. To do this, we employed the predicted secondary structure of amino acids to extract two types of structural features from neighboring amino acids along the protein sequence which has never been used for this task. As a result, our proposed method is able to enhance the sumoylation site prediction task, outperforming previously proposed methods in the literature. SumSec demonstrated high sensitivity (0.91), accuracy (0.94) and MCC (0.88). The prediction accuracy achieved in this study is 21% better than those reported in previous studies. The script and extracted features are publicly available at: https://github.com/YosvanyLopez/SumSec.

Indexed as

Amino Acid SequenceBinding SitesComputational BiologyInternetMachine LearningModels, MolecularProteinsProtein Structure, SecondarySumoylationProteinsbaggingensemble classifierpost translational modificationprofile-bigramsecondary structuresumoylation

Identifiers

PMID30544729
PMCPMC6320791

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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.