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

4.7K
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,...
4.7K
Protein Networks02:26

Protein Networks

2.9K
2.9K
Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
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...
15.0K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.6K
4.6K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
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...
3.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.2K
2.2K

You might also read

Related Articles

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

Sort by
Same author

Drosophila melanogaster miPEP8 Regulates Cell Size Through its Interaction With ref(2)P/p62.

Molecular & cellular proteomics : MCP·2026
Same author

Effector-host interactome map links type III secretion systems in healthy gut microbiomes to immune modulation.

Nature microbiology·2026
Same author

Characterization of the immune landscape in healthy mouse prostate and during prostate cancer progression.

Oncoimmunology·2025
Same author

Prevalence and predictors of uncommon features in FSHD1 patients: insights from the French FSHD registry.

Orphanet journal of rare diseases·2025
Same author

SciGeneX: enhancing transcriptional analysis through gene module detection in single-cell and spatial transcriptomics data.

NAR genomics and bioinformatics·2025
Same author

mimicINT: A workflow for microbe-host protein interaction inference.

F1000Research·2025

Related Experiment Video

Updated: Apr 11, 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

14.0K

Extreme multifunctional proteins identified from a human protein interaction network.

Charles E Chapple1, Benoit Robisson1, Lionel Spinelli2

  • 11] Aix-Marseille University, TAGC, Marseille F-13009, France [2] INSERM UMR_S1090, Marseille F-13009, France.

Nature Communications
|June 10, 2015
PubMed
Summary

Researchers developed a new method to identify

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

3.7K
Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

9.4K

Related Experiment Videos

Last Updated: Apr 11, 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

14.0K
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

3.7K
Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

9.4K

Area of Science:

  • Proteomics and Bioinformatics
  • Molecular and Cellular Biology

Background:

  • Moonlighting proteins possess multiple, unrelated functions, crucial for cellular processes.
  • Identifying and characterizing these multifunctional proteins on a large scale remains challenging.

Purpose of the Study:

  • To introduce the first large-scale method for identifying 'extreme multifunctional' proteins.
  • To characterize these proteins as a distinct group within the human interactome.

Main Methods:

  • Combined network topological information with protein annotations.
  • Analyzed the human interactome to identify candidate proteins.

Main Results:

  • Identified 430 extreme multifunctional proteins, representing 3% of the human interactome.
  • These proteins exhibit unique features, distinguishing them from network hubs.
  • Extreme multifunctional proteins are enriched in linear motifs and less intrinsically disordered.

Conclusions:

  • The developed method successfully identifies a distinct class of extreme multifunctional proteins.
  • These proteins have specific characteristics that define their unique functional roles.
  • MoonDB database provides a valuable resource for studying moonlighting proteins.