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
Conserved Binding Sites01:49

Conserved Binding Sites

4.1K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

1.0K
1.0K

You might also read

Related Articles

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

Sort by
Same author

Boundary constraints can determine pattern emergence.

Development (Cambridge, England)·2026
Same author

The notochord: development, disease and stem cell-based modelling.

Development (Cambridge, England)·2026
Same author

Analysis of monoclonal antibodies against the malaria invasion complex protein RIPR reveals the structural basis for synergistic antibody protection.

Immunity·2026
Same author

ANARCII enables alignment-free antigen receptor numbering using a generalised language model.

Communications biology·2026
Same author

iNOS modulates inflammatory responses in an NO-independent manner through direct interaction with IRG1 in mitochondria.

Nature metabolism·2026
Same author

Lethal conflict after group fission in wild chimpanzees.

Science (New York, N.Y.)·2026
Same journal

conMItion: an R package adjusting confounding factors for associations in multi-omics.

Bioinformatics (Oxford, England)·2026
Same journal

SpaMFG: a Spatial Multi-omics Integration Method based on Feature Grouping.

Bioinformatics (Oxford, England)·2026
Same journal

CSCN: Inference of Cell-Specific Causal Networks Using Single-Cell RNA-Seq Data.

Bioinformatics (Oxford, England)·2026
Same journal

Sparse CCA-Based Mediation Analysis with High-Dimensional Exposures and Mediators.

Bioinformatics (Oxford, England)·2026
Same journal

Enhancing Cross-Context Generalization in Drug Perturbation Prediction with a Multimodal Conditional Diffusion Framework.

Bioinformatics (Oxford, England)·2026
Same journal

Primer Design through Submodular Function Estimation.

Bioinformatics (Oxford, England)·2026
See all related articles

Related Experiment Video

Updated: Apr 25, 2026

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

Alignment-free protein interaction network comparison.

Waqar Ali1, Tiago Rito1, Gesine Reinert1

  • 1Department of Statistics, University of Oxford, Oxford OX1 3TG, UK and Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, CA 90089-2910, USA.

Bioinformatics (Oxford, England)
|August 28, 2014
PubMed
Summary
This summary is machine-generated.

Netdis, a novel topology-based distance measure, enables accurate phylogenetic reconstruction from biological networks. This method overcomes limitations of traditional network alignment, revealing evolutionary insights from network topology.

More Related Videos

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

2.7K
Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

1.1K

Related Experiment Videos

Last Updated: Apr 25, 2026

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
JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

2.7K
Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

1.1K

Area of Science:

  • Computational Biology
  • Bioinformatics
  • Systems Biology

Background:

  • Current biological network comparison methods, primarily network alignment, struggle with incomplete and error-prone data.
  • Network alignment results are often unsuitable for distance-based evolutionary analyses.
  • Existing approaches fail to fully leverage network topology for evolutionary insights.

Purpose of the Study:

  • To introduce Netdis, a topology-based distance measure for biological networks.
  • To enable network phylogeny reconstruction and distance-based evolutionary analysis.
  • To demonstrate the utility of network topology in understanding evolutionary processes.

Main Methods:

  • Developed Netdis, a novel algorithm measuring distances between networks based on topology.
  • Validated Netdis on random graph models to assess its independence from network size and density.
  • Applied Netdis to protein-interaction networks for phylogenetic tree reconstruction.

Main Results:

  • Netdis successfully distinguishes between different random graph models.
  • Phylogenetic trees of species were accurately reconstructed using only protein interaction network topology.
  • Netdis demonstrated speed and simplicity, clustering diverse biological and non-biological networks by type.

Conclusions:

  • Protein interaction network topology contains significant evolutionary information, independent of individual interaction conservation.
  • Netdis provides a robust and efficient tool for network comparison and phylogenetic analysis.
  • The method's applicability extends beyond biological networks, facilitating broader network classification.