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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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DeepPhoPred: Accurate Deep Learning Model to Predict Microbial Phosphorylation.

Faisal Ahmed1,2, Alok Sharma3,4,5,6, Swakkhar Shatabda7

  • 1Digital Health Unit, NVISION Systems and Technologies SL, Barcelona, Spain.

Proteins
|September 6, 2024
PubMed
Summary
This summary is machine-generated.

DeepPhoPred is a new deep learning tool that accurately predicts microbial phosphorylation sites (pS, pT, pY). This computational approach offers a faster, low-cost alternative to experimental methods for understanding microbial functions and developing new drugs.

Keywords:
classificationconvolutional neural networkevolutionary informationimbalance learningmicrobial phosphorylationposttranslational modificationstructural information

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Area of Science:

  • Biochemistry
  • Computational Biology
  • Bioinformatics

Background:

  • Phosphorylation is a critical posttranslational protein modification regulating essential cellular processes.
  • Predicting microbial phosphorylation sites aids in understanding pathogenesis and developing antimicrobial agents.
  • Experimental prediction methods are time-consuming and expensive, necessitating computational solutions.

Purpose of the Study:

  • To introduce DeepPhoPred, a novel deep learning tool for predicting microbial phospho-serine (pS), phospho-threonine (pT), and phospho-tyrosine (pY) sites.
  • To provide a low-cost, high-speed computational alternative for phosphorylation site prediction in microbes.

Main Methods:

  • DeepPhoPred utilizes a two-headed convolutional neural network architecture.
  • The model incorporates squeeze and excitation blocks for feature learning.
  • It integrates peptide structural and evolutionary information for prediction.

Main Results:

  • DeepPhoPred demonstrates superior performance compared to existing microbial phosphorylation site predictors.
  • The deep-learning architecture effectively learns significant features for accurate prediction.
  • Empirical results validate the tool's high efficiency and accuracy.

Conclusions:

  • DeepPhoPred offers a significant advancement in computational prediction of microbial phosphorylation sites.
  • The tool's performance and efficiency make it valuable for research in microbial pathogenesis and drug development.
  • DeepPhoPred, its code, and datasets are publicly available for broader scientific use.