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Related Concept Videos

Protein Networks02:26

Protein Networks

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,...
Protein Networks02:26

Protein Networks

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,...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Conserved Binding Sites01:49

Conserved Binding Sites

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 analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

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 analyses the...
Microbial Interactions: Mutualism01:25

Microbial Interactions: Mutualism

Mutualism is a symbiotic interaction in which all participating organisms benefit. These relationships can be obligate or facultative and are fundamental to ecosystem functions across diverse biological systems.Plant–Fungi MutualismOne well-known example is the association between plant roots and mycorrhizal fungi, such as Rhizophagus species. The fungal hyphae penetrate the root hairs and the epidermis, forming an extensive hyphal network that establishes a symbiotic association. Through this...

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Related Experiment Video

Updated: May 30, 2026

Divergence of Root Microbiota in Different Habitats based on Weighted Correlation Networks
09:49

Divergence of Root Microbiota in Different Habitats based on Weighted Correlation Networks

Published on: September 25, 2021

Biological interaction networks are conserved at the module level.

Guy E Zinman1, Shan Zhong, Ziv Bar-Joseph

  • 1Lane Center for Computational Biology, School of Computer Science, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

BMC Systems Biology
|August 25, 2011
PubMed
Summary
This summary is machine-generated.

Protein interaction data is conserved at the module level, not just between species. Interactions within functional modules are conserved more than those connecting different modules, explaining conserved biological processes.

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Area of Science:

  • Systems Biology
  • Comparative Genomics
  • Network Biology

Background:

  • Orthologous genes are conserved across species, but protein interaction data shows lower conservation than expected, even for similar sequences.
  • Previous studies comparing high-throughput interaction data (expression, protein-protein, protein-DNA, genetic) between species indicate surprisingly low conservation rates.
  • Understanding the conservation of biological interactions is crucial for deciphering conserved biological processes.

Purpose of the Study:

  • To investigate and explain the lower-than-expected conservation rates of protein interaction data across closely related species.
  • To test existing hypotheses and propose a novel network-based explanation for interaction conservation patterns.

Main Methods:

  • Collected comprehensive high-throughput interaction datasets for four model organisms: S. cerevisiae, S. pombe, C. elegans, and D. melanogaster.
  • Integrated all interaction evidence into a single network for each species.
  • Identified functional modules within these integrated networks and analyzed conservation rates of intra-module versus inter-module interactions.

Main Results:

  • Previously proposed hypotheses offered only limited explanations for the observed low conservation of interaction data.
  • Interactions within identified functional modules were conserved at significantly higher rates than previously reported.
  • Interactions connecting distinct functional modules showed lower conservation rates.

Conclusions:

  • Conservation of biological networks is primarily maintained at the functional module level between species.
  • Interactions within modules are substantially more conserved than interactions linking different modules.
  • This module-level conservation provides a network-based explanation for conserved biological processes despite variable protein interaction conservation.