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

Phosphorylation01:02

Phosphorylation

55.1K
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...
55.1K
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

20.2K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
20.2K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

15.4K
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...
15.4K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.6K
4.6K

You might also read

Related Articles

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

Sort by
Same author

CMA-Nano: A DNA Methylation Detection Method for Nanopore Sequencing Data Based on a Cross-Modal Attention Mechanism.

ACS omega·2026
Same author

An Explainable Deep Learning Framework Integrating DNA Sequence and Transcription Initiation Signals for Gene Expression Prediction.

ACS synthetic biology·2026
Same author

LysePred: A Multiscale Convolutional Neural Network for Predicting Hemolytic Activity of Antimicrobial Peptides.

ACS synthetic biology·2026
Same author

An Interpretable Deep Learning Framework Leveraging RNA Foundation Model and Capsule Networks for Accurate Prediction of RNA 2'-O-Methylation Sites.

Journal of chemical information and modeling·2026
Same author

MPMFMol: Multitask Self-Supervised Pretraining with Multimodal Fine-Tuning for Molecular Property Prediction.

Journal of chemical information and modeling·2026
Same author

Quantum computing applications in drug discovery.

Briefings in bioinformatics·2026
Same journal

Investigating Effect of Dimensional Variance on Separation of Glomerular Ultrafiltrate in a Microfluidic Environment.

IEEE transactions on nanobioscience·2026
Same journal

Green synthesis of multifunctional ZnFe<sub>2</sub>O<sub>4</sub>-MWCNT-Cellulose acetate nanocomposite for peroxidase enzyme immobilization.

IEEE transactions on nanobioscience·2026
Same journal

IoT-Enabled SnOâ‚‚-Based Humidity Sensor for Real-Time Monitoring in Neonatal Incubators.

IEEE transactions on nanobioscience·2026
Same journal

Electrokinetic and Antibiofilm Effects of Silver Nanoparticles Combined with Imipenem Against multidrug-resistant of Klebsiella pneumoniae.

IEEE transactions on nanobioscience·2026
Same journal

Bio-inspired Optofluidic Molecular Communication with Photothermally Actuated Microrobot Swarms.

IEEE transactions on nanobioscience·2026
Same journal

Nanostructured ZnO Thin Film-Based Enzymatic Biosensor for Sensitive Acetylcholine Detection in Neurological Applications.

IEEE transactions on nanobioscience·2026
See all related articles

Related Experiment Video

Updated: Mar 7, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

9.0K

PhosPred-RF: A Novel Sequence-Based Predictor for Phosphorylation Sites Using Sequential Information Only.

Leyi Wei, Pengwei Xing, Jijun Tang

    IEEE Transactions on Nanobioscience
    |February 7, 2017
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces PhosPred-RF, a novel machine learning tool for predicting protein phosphorylation sites using only primary sequences. It offers a faster and more accurate alternative to complex methods, improving protein function analysis.

    More Related Videos

    A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
    11:44

    A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

    Published on: January 24, 2016

    12.6K
    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

    2.7K

    Related Experiment Videos

    Last Updated: Mar 7, 2026

    Oligopeptide Competition Assay for Phosphorylation Site Determination
    09:16

    Oligopeptide Competition Assay for Phosphorylation Site Determination

    Published on: May 18, 2017

    9.0K
    A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
    11:44

    A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

    Published on: January 24, 2016

    12.6K
    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

    2.7K

    Area of Science:

    • Bioinformatics
    • Computational Biology
    • Molecular Biology

    Background:

    • Protein phosphorylation is a critical post-translational modification regulating cellular processes.
    • Accurate prediction of phosphorylation sites is essential for understanding protein function and signaling pathways.
    • Existing machine learning methods often rely on complex features, limiting their applicability.

    Purpose of the Study:

    • To develop a fast, accurate, and simple machine learning method for predicting protein phosphorylation sites.
    • To overcome the limitations of homology-dependent and computationally intensive prediction approaches.
    • To provide a user-friendly tool for researchers in the field.

    Main Methods:

    • A novel feature representation algorithm exploring sequential information from primary protein sequences.
    • Development of a random forest-based predictor, PhosPred-RF.
    • Evaluation and comparison against state-of-the-art predictors on benchmark datasets.

    Main Results:

    • The proposed feature representation effectively captures differences between phosphorylation and non-phosphorylation sites.
    • PhosPred-RF demonstrated superior performance compared to existing predictors.
    • The tool is accessible via a public webserver.

    Conclusions:

    • PhosPred-RF offers a powerful and efficient solution for protein phosphorylation site prediction.
    • The method's reliance solely on primary sequences broadens its applicability.
    • PhosPred-RF has the potential to be a valuable tool in biological research.