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Protein Processing, Post-Translational

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Deep learning approaches for data-independent acquisition proteomics.

Expert review of proteomics
INTRODUCTION: Data-independent acquisition (DIA) is an emerging technology for large-scale proteomic studies. DIA data analysis methods are evolving rapidly, and deep learning has cut a conspicuous figure in this field.

Deep Learning-Based Advances In Protein Posttranslational Modification Site and Protein Cleavage Prediction.

Methods in molecular biology (Clifton, N.J.)
Posttranslational modification (PTM ) is a ubiquitous phenomenon in both eukaryotes and prokaryotes which gives rise to enormous proteomic diversity. PTM mostly comes in two flavors: covalent modification to polypeptide chain and proteolytic cleavage...

Enhancing the Discovery of Functional Post-Translational Modification Sites with Machine Learning Models - Development, Validation, and Interpretation.

Methods in molecular biology (Clifton, N.J.)
Protein posttranslational modifications (PTMs) are a rapidly expanding feature class of significant importance in cell biology. Due to a high burden of experimental proof, the number of functionals PTMs in the eukaryotic proteome is currently underes...

Computational Prediction of N- and O-Linked Glycosylation Sites for Human and Mouse Proteins.

Methods in molecular biology (Clifton, N.J.)
Protein glycosylation is one of the most complex posttranslational modifications (PTM) that play a fundamental role in protein function. Identification and annotation of these sites using experimental approaches are challenging and time consuming. He...

Glycosylation-Related Genes Predict the Prognosis and Immune Fraction of Ovarian Cancer Patients Based on Weighted Gene Coexpression Network Analysis (WGCNA) and Machine Learning.

Oxidative medicine and cellular longevity
BACKGROUND: Ovarian cancer (OC) is a malignancy exhibiting high mortality in female tumors. Glycosylation is a posttranslational modification of proteins but research has failed to demonstrate a systematic link between glycosylation-related signature...

Computational identification of 4-carboxyglutamate sites to supplement physiological studies using deep learning.

Scientific reports
In biological systems, Glutamic acid is a crucial amino acid which is used in protein biosynthesis. Carboxylation of glutamic acid is a significant post-translational modification which plays important role in blood coagulation by activating prothrom...

Adapt-Kcr: a novel deep learning framework for accurate prediction of lysine crotonylation sites based on learning embedding features and attention architecture.

Briefings in bioinformatics
Protein lysine crotonylation (Kcr) is an important type of posttranslational modification that is associated with a wide range of biological processes. The identification of Kcr sites is critical to better understanding their functional mechanisms. H...

TransPhos: A Deep-Learning Model for General Phosphorylation Site Prediction Based on Transformer-Encoder Architecture.

International journal of molecular sciences
Protein phosphorylation is one of the most critical post-translational modifications of proteins in eukaryotes, which is essential for a variety of biological processes. Plenty of attempts have been made to improve the performance of computational pr...

Mul-SNO: A Novel Prediction Tool for S-Nitrosylation Sites Based on Deep Learning Methods.

IEEE journal of biomedical and health informatics
Protein s-nitrosylation (SNO) is one of the most important post-translational modifications and is formed by the covalent modification of nitric oxide and cysteine residues. Extensive studies have shown that SNO plays a pivotal role in the plant immu...

A convolutional neural network based tool for predicting protein AMPylation sites from binary profile representation.

Scientific reports
AMPylation is an emerging post-translational modification that occurs on the hydroxyl group of threonine, serine, or tyrosine via a phosphodiester bond. AMPylators catalyze this process as covalent attachment of adenosine monophosphate to the amino a...