Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.2K
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...
13.2K
Phosphorylation01:02

Phosphorylation

50.4K
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...
50.4K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

10.9K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.9K
Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

45
Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...
45
Protein and Protein Structure02:15

Protein and Protein Structure

79.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
79.6K
Conservation of Protein Domains02:26

Conservation of Protein Domains

3.1K
3.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Delivering artificial intelligence-ready genomics with the Maize Genetics and Genomics Database.

Genetics·2026
Same author

GrainGenes: genetics, genomes, and pangenomes.

Genetics·2025
Same author

Fishing for a reelGene: evaluating gene models with evolution and machine learning.

The Plant journal : for cell and molecular biology·2025
Same author

Structural Variability of Pfam Domains Based on Alphafold2 Predictions.

Proteins·2025
Same author

Assessing the performance of generative artificial intelligence in retrieving information against manually curated genetic and genomic data.

Database : the journal of biological databases and curation·2025
Same author

Extensive genome evolution distinguishes maize within a stable tribe of grasses.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Jul 7, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

1.9K

PhosBoost: Improved phosphorylation prediction recall using gradient boosting and protein language models.

Elly Poretsky1, Carson M Andorf2,3, Taner Z Sen1,4

  • 1Agricultural Research Service, Crop Improvement and Genetics Research Unit U.S. Department of Agriculture Albany CA United States.

Plant Direct
|December 21, 2023
PubMed
Summary
This summary is machine-generated.

PhosBoost, a new machine learning tool, accurately predicts plant protein phosphorylation sites. It outperforms existing methods, especially for tyrosine phosphorylation, and is scalable for genome-wide analysis.

More Related Videos

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

9.2K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.7K

Related Experiment Videos

Last Updated: Jul 7, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

1.9K
A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

9.2K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.7K

Area of Science:

  • Biochemistry
  • Computational Biology
  • Plant Science

Background:

  • Protein phosphorylation is a crucial post-translational modification regulating plant biological processes.
  • Current experimental data for plant phosphorylation is limited, hindering comprehensive analysis.
  • Accurate prediction of phosphorylation sites is essential for understanding cellular signaling and function.

Purpose of the Study:

  • To develop a scalable and accurate machine-learning method for predicting protein phosphorylation sites in plants.
  • To compare the performance of the new method against existing prediction tools.
  • To assess the cross-species transferability and scalability of the developed model.

Main Methods:

  • Developed PhosBoost, a machine-learning approach combining protein language models and gradient-boosting trees.
  • Trained PhosBoost on data from the qPTMplants database.
  • Compared PhosBoost with PhosphoLingo and DeepPhos, incorporating a sequence-based pairwise alignment step.

Main Results:

  • PhosBoost demonstrated superior recall for serine and threonine phosphorylation prediction compared to existing methods.
  • PhosBoost successfully predicted tyrosine phosphorylation sites, where other methods failed.
  • The inclusion of pairwise alignment improved prediction accuracy for all tested classifiers.
  • PhosBoost models showed cross-species transferability and scalability for genome-wide predictions.

Conclusions:

  • PhosBoost offers improved recall for protein phosphorylation site prediction in plants, particularly for tyrosine sites.
  • The method is scalable for large-scale genome-wide predictions and transferable across plant species.
  • PhosBoost provides a valuable tool for advancing plant phosphoproteomics research.