iProtGly-SS: A Tool to Accurately Predict Protein Glycation Site Using Structural-Based Features
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Sharma, A
Shatabda, S
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Dukka, BKC
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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/.
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Computational Methods for Predicting Post-Translational Modification Sites
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2499
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© 2022 Springer. This is the author-manuscript version of this paper. It is reproduced here in accordance with the copyright policy of the publisher. Please refer to the publisher’s website for further information.
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Subject
Biochemistry and cell biology
Evolutionary features
Feature selection
Posttranslational modification
Protein glycation
Structural features
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Dehzangi, I; Sharma, A; Shatabda, S, iProtGly-SS: A Tool to Accurately Predict Protein Glycation Site Using Structural-Based Features, Computational Methods for Predicting Post-Translational Modification Sites, 2022, 2499, pp. 125-134