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Related Concept Videos

Protein Networks02:26

Protein Networks

4.4K
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,...
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Protein Networks02:26

Protein Networks

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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Protein-Protein Interfaces

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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Updated: Dec 24, 2025

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

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A reference map of the human binary protein interactome.

Katja Luck1,2,3, Dae-Kyum Kim1,4,5,6, Luke Lambourne1,2,3

  • 1Center for Cancer Systems Biology (CCSB), Dana-Farber Cancer Institute, Boston, MA, USA.

Nature
|April 17, 2020
PubMed
Summary
This summary is machine-generated.

Researchers created the human protein-protein interaction network, HuRI, mapping 53,000 interactions. This comprehensive interactome map aids understanding of genotype-phenotype relationships and cellular functions.

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Area of Science:

  • Molecular Biology
  • Genomics
  • Systems Biology

Background:

  • Understanding cellular organization and genome function is crucial for linking genotype to phenotype.
  • Existing protein-protein interaction data is limited in scale and scope.

Purpose of the Study:

  • To present a comprehensive human 'all-by-all' reference interactome map, named HuRI.
  • To enable the study of cellular functions within various physiological and pathological contexts by integrating interactome data with genomic, transcriptomic, and proteomic data.

Main Methods:

  • Construction of an 'all-by-all' human binary protein-protein interaction map (HuRI).
  • Integration of the HuRI map with genome, transcriptome, and proteome datasets.
  • Inference of tissue-specific networks from the HuRI map.

Main Results:

  • HuRI contains approximately 53,000 human binary protein-protein interactions, significantly expanding existing curated datasets.
  • Demonstrated utility of HuRI in identifying specific subcellular roles of protein-protein interactions.
  • Inferred tissue-specific networks revealed principles of cellular context-specific functions and potential mechanisms for Mendelian diseases.

Conclusions:

  • HuRI serves as a systematic, proteome-wide reference map for human protein interactions.
  • The map facilitates the study of genotype-phenotype relationships and cellular functions.
  • HuRI aids in elucidating molecular mechanisms underlying tissue-specific phenotypes and diseases.