Research progress in protein posttranslational modification site prediction

W He, L Wei, Q Zou - Briefings in functional genomics, 2019 - academic.oup.com
Posttranslational modifications (PTMs) play an important role in regulating protein folding,
activity and function and are involved in almost all cellular processes. Identification of PTMs …

Using deep neural networks and biological subwords to detect protein S-sulfenylation sites

DT Do, TQT Le, NQK Le - Briefings in Bioinformatics, 2021 - academic.oup.com
Protein S-sulfenylation is one kind of crucial post-translational modifications (PTMs) in which
the hydroxyl group covalently binds to the thiol of cysteine. Some recent studies have shown …

A comprehensive review of in silico analysis for protein S-sulfenylation sites

MM Hasan, MS Khatun, H Kurata - Protein and peptide letters, 2018 - ingentaconnect.com
Background: Cysteine S-sulfenylation is a major type of dynamic post-translational
modification of the protein that plays an important role in regulating many biological …

Prediction of S-sulfenylation sites using statistical moments based features via CHOU'S 5-step rule

AH Butt, YD Khan - International Journal of Peptide Research and …, 2020 - Springer
Post-translation modification (PTM) of cysteine S-sulfenylation sites in protein is important in
cellular biology. S-sulfenylation plays a significant role in protein functioning, cell signaling …

Fu-SulfPred: identification of protein S-sulfenylation sites by fusing forests via Chou's general PseAAC

L Wang, R Zhang, Y Mu - Journal of theoretical biology, 2019 - Elsevier
Protein S-sulfenylation is an essential post-translational modification (PTM) that provides
critical information to understand molecular mechanisms of cell signaling transduction …

SulSite-GTB: identification of protein S-sulfenylation sites by fusing multiple feature information and gradient tree boosting

M Wang, X Cui, B Yu, C Chen, Q Ma, H Zhou - Neural Computing and …, 2020 - Springer
Protein cysteine S-sulfenylation is an essential and reversible post-translational modification
that plays a crucial role in transcriptional regulation, stress response, cell signaling and …

Computational identification of protein S-sulfenylation sites by incorporating the multiple sequence features information

MM Hasan, D Guo, H Kurata - Molecular BioSystems, 2017 - pubs.rsc.org
Cysteine S-sulfenylation is a major type of posttranslational modification that contributes to
protein structure and function regulation in many cellular processes. Experimental …

S-SulfPred: A sensitive predictor to capture S-sulfenylation sites based on a resampling one-sided selection undersampling-synthetic minority oversampling technique

C Jia, Y Zuo - Journal of theoretical biology, 2017 - Elsevier
Protein S-sulfenylation is a reversible post-translational modification involving covalent
attachment of hydroxide to the thiol group of cysteine residues, which is involved in various …

DeepCSO: a deep-learning network approach to predicting cysteine S-sulphenylation sites

X Lyu, S Li, C Jiang, N He, Z Chen, Y Zou… - Frontiers in Cell and …, 2020 - frontiersin.org
Cysteine S-sulphenylation (CSO), as a novel post-translational modification (PTM), has
emerged as a potential mechanism to regulate protein functions and affect signal networks …

BiGRUD-SA: Protein S-sulfenylation sites prediction based on BiGRU and self-attention

T Zhang, J Jia, C Chen, Y Zhang, B Yu - Computers in Biology and …, 2023 - Elsevier
S-sulfenylation is a vital post-translational modification (PTM) of proteins, which is an
intermediate in other redox reactions and has implications for signal transduction and …