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 Networks02:26

Protein Networks

3.7K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
3.7K
Protein Networks02:26

Protein Networks

1.8K
1.8K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

3.4K
3.4K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

1.0K
1.0K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.1K

You might also read

Related Articles

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

Sort by
Same author

Development and validation of an online dynamic nomogram for nonobese metabolic dysfunction-associated steatotic liver disease based on body composition analysis.

BMC gastroenterology·2026
Same author

Entropy for Prediction of MACEs in Myocarditis: A Cardiac MRI-based Biomarker of Myocardial Tissue Heterogeneity.

Radiology·2026
Same author

A predictive model for high-quality blastocyst formation using Day 3 morphological scores in women of advanced maternal age.

BMC pregnancy and childbirth·2026
Same author

Transparent EMI shielding and a thermal insulating optical window based on a randomized metallic mesh and ITO-based coating.

Applied optics·2026
Same author

A preclinical investigation into the potential associations of geraniin with ulcerative colitis alleviation through integrated multi-omics and <i>in vivo</i> analysis.

Frontiers in medicine·2026
Same author

Dynamics and optimal control of a weighted-network dengue model with seasonal transmission.

Infectious Disease Modelling·2026

Related Experiment Video

Updated: Apr 26, 2026

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

2.8K

A novel feature extraction scheme with ensemble coding for protein-protein interaction prediction.

Xiuquan Du1, Jiaxing Cheng2, Tingting Zheng3

  • 1Key Laboratory of Intelligent Computing and Signal Processing of Ministry of Education, Anhui University, Hefei 230601, China. dxqllp@163.com.

International Journal of Molecular Sciences
|July 22, 2014
PubMed
Summary

A new method called DXEC-RF accurately predicts protein-protein interactions (PPIs) using Random Forest and ensemble coding. This approach enhances computational efficiency and achieves high accuracy on yeast and human datasets, aiding functional genomics research.

More Related Videos

Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation
07:16

Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation

Published on: January 5, 2024

1.6K
Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Published on: March 3, 2015

17.8K

Related Experiment Videos

Last Updated: Apr 26, 2026

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

2.8K
Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation
07:16

Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation

Published on: January 5, 2024

1.6K
Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Published on: March 3, 2015

17.8K

Area of Science:

  • Genomics
  • Bioinformatics
  • Computational Biology

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions including metabolism, immune response, and gene regulation.
  • Predicting PPIs is a significant challenge in functional genomics despite advances in high-throughput technologies.
  • Existing computational methods for PPI prediction require improvement in accuracy and efficiency.

Purpose of the Study:

  • To develop a novel and efficient computational method for predicting protein-protein interactions.
  • To enhance the accuracy and reduce the computational time of PPI prediction.
  • To integrate diverse features and physicochemical properties for robust PPI prediction.

Main Methods:

  • A Random Forest (RF) algorithm was employed with an ensemble coding (EC) method.
  • A feature selection method (DX) was utilized to optimize feature combinations and reduce computational cost.
  • The DXEC method was developed by integrating multiple features and biochemical properties.

Main Results:

  • The DXEC method achieved 67.2% precision, 80.74% recall, and 70.67% accuracy on the Gold Yeast dataset.
  • On the Silver Yeast dataset, DXEC yielded 76.93% precision, 77.98% recall, and 77.27% accuracy.
  • The DXEC-RF method reached 80% prediction accuracy on a human dataset and maintained 50-80% recall on larger datasets.

Conclusions:

  • The DXEC method, combined with RF, demonstrates significant suitability and effectiveness for protein-protein interaction prediction.
  • The developed approach offers improved accuracy and efficiency for PPI prediction in functional genomics.
  • The prediction service is publicly available, facilitating further research in the field.