Literature DB >> 35696077

iProtGly-SS: A Tool to Accurately Predict Protein Glycation Site Using Structural-Based Features.

Iman Dehzangi1,2, Alok Sharma3,4,5, Swakkhar Shatabda6.   

Abstract

Posttranslational modification (PTM) is an important biological mechanism to promote functional diversity among the proteins. So far, a wide range of PTMs has been identified. Among them, glycation is considered as one of the most important PTMs. Glycation is associated with different neurological disorders including Parkinson and Alzheimer. It is also shown to be responsible for different diseases, including vascular complications of diabetes mellitus. Despite all the efforts have been made so far, the prediction performance of glycation sites using computational methods remains limited. Here we present a newly developed machine learning tool called iProtGly-SS that utilizes sequential and structural information as well as Support Vector Machine (SVM) classifier to enhance lysine glycation site prediction accuracy. The performance of iProtGly-SS was investigated using the three most popular benchmarks used for this task. Our results demonstrate that iProtGly-SS is able to achieve 81.61%, 93.62%, and 92.95% prediction accuracies on these benchmarks, which are significantly better than those results reported in the previous studies. iProtGly-SS is implemented as a web-based tool which is publicly available at http://brl.uiu.ac.bd/iprotgly-ss/ .
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Evolutionary features; Feature selection; Posttranslational modification; Protein glycation; Structural features; Support vector machine

Mesh:

Substances:

Year:  2022        PMID: 35696077     DOI: 10.1007/978-1-0716-2317-6_5

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  26 in total

1.  Active glycation in neurofibrillary pathology of Alzheimer disease: N(epsilon)-(carboxymethyl) lysine and hexitol-lysine.

Authors:  R J Castellani; P L Harris; L M Sayre; J Fujii; N Taniguchi; M P Vitek; H Founds; C S Atwood; G Perry; M A Smith
Journal:  Free Radic Biol Med       Date:  2001-07-15       Impact factor: 7.376

2.  MusiteDeep: a deep-learning based webserver for protein post-translational modification site prediction and visualization.

Authors:  Duolin Wang; Dongpeng Liu; Jiakang Yuchi; Fei He; Yuexu Jiang; Siteng Cai; Jingyi Li; Dong Xu
Journal:  Nucleic Acids Res       Date:  2020-07-02       Impact factor: 16.971

Review 3.  Prediction of posttranslational modification of proteins from their amino acid sequence.

Authors:  Birgit Eisenhaber; Frank Eisenhaber
Journal:  Methods Mol Biol       Date:  2010

4.  Predicting Post-Translational Modifications from Local Sequence Fragments Using Machine Learning Algorithms: Overview and Best Practices.

Authors:  Marcin Tatjewski; Marcin Kierczak; Dariusz Plewczynski
Journal:  Methods Mol Biol       Date:  2017

Review 5.  Protein glycation, diabetes, and aging.

Authors:  P Ulrich; A Cerami
Journal:  Recent Prog Horm Res       Date:  2001

6.  Lysine acetylation targets protein complexes and co-regulates major cellular functions.

Authors:  Chunaram Choudhary; Chanchal Kumar; Florian Gnad; Michael L Nielsen; Michael Rehman; Tobias C Walther; Jesper V Olsen; Matthias Mann
Journal:  Science       Date:  2009-07-16       Impact factor: 47.728

7.  Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry.

Authors:  Paul J Thornalley; Sinan Battah; Naila Ahmed; Nikolaos Karachalias; Stamatina Agalou; Roya Babaei-Jadidi; Anne Dawnay
Journal:  Biochem J       Date:  2003-11-01       Impact factor: 3.857

Review 8.  A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic disease.

Authors:  Qibin Zhang; Jennifer M Ames; Richard D Smith; John W Baynes; Thomas O Metz
Journal:  J Proteome Res       Date:  2009-02       Impact factor: 4.466

9.  PTM-ssMP: A Web Server for Predicting Different Types of Post-translational Modification Sites Using Novel Site-specific Modification Profile.

Authors:  Yu Liu; Minghui Wang; Jianing Xi; Fenglin Luo; Ao Li
Journal:  Int J Biol Sci       Date:  2018-05-22       Impact factor: 6.580

10.  CPLM: a database of protein lysine modifications.

Authors:  Zexian Liu; Yongbo Wang; Tianshun Gao; Zhicheng Pan; Han Cheng; Qing Yang; Zhongyi Cheng; Anyuan Guo; Jian Ren; Yu Xue
Journal:  Nucleic Acids Res       Date:  2013-11-08       Impact factor: 16.971

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