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Gly-LysPred: Identification of Lysine Glycation Sites in Protein Using Position Relative Features and Statistical Moments via Chou's 5 Step Rule

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dc.contributor.authorKhanum, S.-
dc.contributor.authorAshraf, M.A.-
dc.contributor.authorKarim, A.-
dc.contributor.authorShoaib, B.-
dc.contributor.authorKhan, M.A.-
dc.contributor.authorNaqvi, R.A.-
dc.contributor.authorSiddique, K.-
dc.contributor.authorAlswaitti, M.-
dc.date.accessioned2022-06-19T02:40:15Z-
dc.date.available2022-06-19T02:40:15Z-
dc.date.created2021-06-14-
dc.date.issued2021-02-
dc.identifier.issn1546-2218-
dc.identifier.urihttps://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/84656-
dc.description.abstractGlycation is a non-enzymatic post-translational modification which assigns sugar molecule and residues to a peptide. It is a clinically important attribute to numerous age-related, metabolic, and chronic diseases such as diabetes, Alzheimer's, renal failure, etc. Identification of a non-enzymatic reaction are quite challenging in research. Manual identification in labs is a very costly and timeconsuming process. In this research, we developed an accurate, valid, and a robust model named as Gly-LysPred to differentiate the glycated sites from non-glycated sites. Comprehensive techniques using position relative features are used for feature extraction. An algorithm named as a random forest with some preprocessing techniques and feature engineering techniques was developed to train a computational model. Various types of testing techniques such as self-consistency testing, jackknife testing, and cross-validation testing are used to evaluate the model. The overall model's accuracy was accomplished through self-consistency, jackknife, and cross-validation testing 100%, 99.92%, and 99.88% with MCC 1.00, 0.99, and 0.997 respectively. In this regard, a user-friendly webserver is also urbanized to accumulate the whole procedure. These features vectorization methods suggest that they can play a critical role in other web servers which are developed to classify lysine glycation. © 2021 Tech Science Press. All rights reserved.-
dc.language영어-
dc.language.isoen-
dc.publisherTECH SCIENCE PRESS-
dc.relation.isPartOfCMC-COMPUTERS MATERIALS & CONTINUA-
dc.titleGly-LysPred: Identification of Lysine Glycation Sites in Protein Using Position Relative Features and Statistical Moments via Chou's 5 Step Rule-
dc.typeArticle-
dc.type.rimsART-
dc.description.journalClass1-
dc.identifier.wosid000811518100001-
dc.identifier.doi10.32604/cmc.2020.013646-
dc.identifier.bibliographicCitationCMC-COMPUTERS MATERIALS & CONTINUA, v.66, no.2, pp.2165 - 2181-
dc.description.isOpenAccessN-
dc.identifier.scopusid2-s2.0-85097199313-
dc.citation.endPage2181-
dc.citation.startPage2165-
dc.citation.titleCMC-COMPUTERS MATERIALS & CONTINUA-
dc.citation.volume66-
dc.citation.number2-
dc.contributor.affiliatedAuthorKhan, M.A.-
dc.type.docTypeArticle-
dc.subject.keywordAuthorChou&apos-
dc.subject.keywordAuthors 5 step rule-
dc.subject.keywordAuthorGly-LysPred-
dc.subject.keywordAuthorLysine glycation-
dc.subject.keywordAuthorPosition relative features-
dc.subject.keywordAuthorPost-translational modification-
dc.subject.keywordAuthorPseAAC-
dc.subject.keywordPlusAmino acids-
dc.subject.keywordPlusDecision trees-
dc.subject.keywordPlusTesting-
dc.subject.keywordPlusComputational model-
dc.subject.keywordPlusFeature engineerings-
dc.subject.keywordPlusManual identification-
dc.subject.keywordPlusPost-translational modifications-
dc.subject.keywordPlusPreprocessing techniques-
dc.subject.keywordPlusSelf-consistency-
dc.subject.keywordPlusStatistical moments-
dc.subject.keywordPlusTesting technique-
dc.subject.keywordPlusGlycosylation-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
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