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

4.6K
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,...
4.6K
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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
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...
3.0K
Protein Complex Assembly02:41

Protein Complex Assembly

17.0K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
17.0K

You might also read

Related Articles

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

Sort by
Same author

SynergyGraph: predicting cell line specific drug combination synergy scores using knowledge graph representation and hypergraph modeling.

Scientific reports·2025
Same author

SynergyImage: image-based model for drug combinations synergy score prediction.

BMC bioinformatics·2025
Same author

Improving virtual try on clothes using image depth estimation.

Scientific reports·2025
Same author

Comparison of the Effects of Norepinephrine and Phenylephrine Infusion in Preventing Hypotension during Spinal Anesthesia for Cesarean Delivery: A Randomized, Double-Blind Clinical Trial.

Archives of Iranian medicine·2025
Same author

Disease candidate genes prediction using positive labeled and unlabeled instances.

BMC medical genomics·2025
Same author

Drug Repurposing Using Hypergraph Embedding Based on Common Therapeutic Targets of a Drug.

Journal of computational biology : a journal of computational molecular cell biology·2024
Same journal

Invaders taking over-Mollusc faunal change in volcanic barrier lakes of the Albertine Rift biodiversity hotspot.

PloS one·2026
Same journal

AI-driven molecular diversification and ligand-based optimization of macitentan derivatives targeting VEGFR1 and endothelin signaling pathways.

PloS one·2026
Same journal

Performance patterns and records in the world aquatics masters championships: Where do the most frequently represented nations among the top-ten masters swimmers come from?

PloS one·2026
Same journal

Modeling diurnal Temperature-Rainfall relationships under multicollinearity using PLS-SEM: A case study of Ghana.

PloS one·2026
Same journal

Organizational culture, social capital, and emergency capacity in primary healthcare institutions: A cross-sectional structural equation modeling study comparing ordinary and older communities.

PloS one·2026
Same journal

Impact of kidney function on the metabolome in the general population.

PloS one·2026
See all related articles

Related Experiment Video

Updated: Mar 17, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Published on: June 15, 2018

8.0K

BiCAMWI: A Genetic-Based Biclustering Algorithm for Detecting Dynamic Protein Complexes.

Amir Lakizadeh1, Saeed Jalili1

  • 1Computer Engineering Department, Tarbiat Modares University, Tehran, Iran.

Plos One
|July 28, 2016
PubMed
Summary
This summary is machine-generated.

This study introduces BiCAMWI, a novel method for detecting protein complexes by incorporating dynamic protein-protein interaction (PPI) networks. BiCAMWI effectively models cellular dynamicity, outperforming existing methods for more reliable protein complex identification.

More Related Videos

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
09:02

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

20.6K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

10.0K

Related Experiment Videos

Last Updated: Mar 17, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Published on: June 15, 2018

8.0K
Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
09:02

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

20.6K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

10.0K

Area of Science:

  • Computational Biology
  • Systems Biology
  • Bioinformatics

Background:

  • Protein complexes orchestrate vital cellular processes, making their detection crucial in the post-genomic era.
  • Existing computational methods often overlook the inherent dynamicity of protein-protein interactions (PPIs), focusing on static networks.
  • Dynamic PPI networks, represented by time-point specific subnetworks, offer a more realistic model but require methods to handle gene subsets and specific conditions.

Purpose of the Study:

  • To develop a novel computational method, BiCAMWI, for enhanced protein complex detection by leveraging the dynamicity of PPI networks.
  • To address the limitation of static PPI network analysis by integrating gene expression data to identify dynamic subnetworks.
  • To improve the accuracy and reliability of protein complex identification through a bicluster-based approach.

Main Methods:

  • BiCAMWI employs a genetic algorithm in its preprocessing phase to extract co-regulated gene sets (biclusters) from gene expression data.
  • Dynamic PPI subnetworks are subsequently extracted from a static PPI network, guided by the identified biclusters.
  • Protein complexes are detected within these dynamic subnetworks, with results aggregated for final identification.

Main Results:

  • BiCAMWI effectively captures and models the inherent dynamicity within static PPI networks.
  • Experimental results demonstrate that BiCAMWI significantly outperforms current state-of-the-art methods in protein complex detection.
  • The method's ability to identify biologically relevant subnetworks based on biclusters contributes to its improved performance.

Conclusions:

  • BiCAMWI offers a more reliable approach to protein complex detection by effectively incorporating network dynamicity.
  • The bicluster-driven extraction of dynamic PPI subnetworks is a key innovation enabling improved detection accuracy.
  • This method advances the field of computational biology by providing a robust tool for analyzing dynamic biological networks.