AIMC Topic: Protein Processing, Post-Translational

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MDD-SOH: exploiting maximal dependence decomposition to identify S-sulfenylation sites with substrate motifs.

Bioinformatics (Oxford, England)
UNLABELLED: S-sulfenylation (S-sulphenylation, or sulfenic acid), the covalent attachment of S-hydroxyl (-SOH) to cysteine thiol, plays a significant role in redox regulation of protein functions. Although sulfenic acid is transient and labile, most ...

jEcho: an Evolved weight vector to CHaracterize the protein's posttranslational modification mOtifs.

Interdisciplinary sciences, computational life sciences
Protein's posttranslational modification (PTM) represents a major dynamic regulation of protein functions after the translation of polypeptide chains from mRNA molecule. Compared with the costly and labor-intensive wet laboratory characterization of ...

Accurate in silico identification of protein succinylation sites using an iterative semi-supervised learning technique.

Journal of theoretical biology
As a widespread type of protein post-translational modifications (PTMs), succinylation plays an important role in regulating protein conformation, function and physicochemical properties. Compared with the labor-intensive and time-consuming experimen...

Types and effects of protein variations.

Human genetics
Variations in proteins have very large number of diverse effects affecting sequence, structure, stability, interactions, activity, abundance and other properties. Although protein-coding exons cover just over 1 % of the human genome they harbor an di...

GlycoMine: a machine learning-based approach for predicting N-, C- and O-linked glycosylation in the human proteome.

Bioinformatics (Oxford, England)
MOTIVATION: Glycosylation is a ubiquitous type of protein post-translational modification (PTM) in eukaryotic cells, which plays vital roles in various biological processes (BPs) such as cellular communication, ligand recognition and subcellular reco...

A deep learning model for prediction of lysine crotonylation sites by fusing multi-features based on multi-head self-attention mechanism.

Scientific reports
Lysine crotonylation (Kcr) is an important post-translational modification, which is present in both histone and non-histone proteins, and plays a key role in a variety of biological processes such as metabolism and cell differentiation. Therefore, r...

MlyPredCSED: based on extreme point deviation compensated clustering combined with cross-scale convolutional neural networks to predict multiple lysine sites in human.

Briefings in bioinformatics
In post-translational modification, covalent bonds on lysine and attached chemical groups significantly change proteins' physical and chemical properties. They shape protein structures, enhance function and stability, and are vital for physiological ...

Sul-BertGRU: an ensemble deep learning method integrating information entropy-enhanced BERT and directional multi-GRU for S-sulfhydration sites prediction.

Bioinformatics (Oxford, England)
MOTIVATION: S-sulfhydration, a crucial post-translational protein modification, is pivotal in cellular recognition, signaling processes, and the development and progression of cardiovascular and neurological disorders, so identifying S-sulfhydration ...

Enhanced O-glycosylation site prediction using explainable machine learning technique with spatial local environment.

Bioinformatics (Oxford, England)
MOTIVATION: The accurate prediction of O-GlcNAcylation sites is crucial for understanding disease mechanisms and developing effective treatments. Previous machine learning (ML) models primarily relied on primary or secondary protein structural and re...

Personalized treatment decision-making using a machine learning-derived lactylation signature for breast cancer prognosis.

Frontiers in immunology
BACKGROUND: Breast cancer is a heterogeneous malignancy with complex molecular characteristics, making accurate prognostication and treatment stratification particularly challenging. Emerging evidence suggests that lactylation, a novel post-translati...