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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

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 polypeptide...
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,...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...

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Updated: Jun 23, 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

Protein-protein interaction databases: keeping up with growing interactomes.

Benjamin Lehne1, Thomas Schlitt

  • 1Department of Medical and Molecular Genetics, Kings College London, Guy's Campus, London, UK.

Human Genomics
|May 1, 2009
PubMed
Summary
This summary is machine-generated.

Protein-protein interaction data from six major databases were integrated to improve accessibility. Combining datasets is complex due to annotation differences, but essential for comprehensive protein interaction information.

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
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Area of Science:

  • Bioinformatics
  • Molecular Biology
  • Systems Biology

Background:

  • The exponential growth of protein-protein interaction (PPI) data necessitates efficient storage and retrieval.
  • Publicly available databases are crucial for curating and disseminating PPI information.
  • Challenges exist in integrating data from diverse sources due to varying annotation standards.

Purpose of the Study:

  • To compare and integrate protein-protein interaction data from six major public databases.
  • To assess the comprehensiveness of individual databases for human PPI data.
  • To highlight the need for integrated resources for accessing PPI information.

Main Methods:

  • Retrieval of PPI data from BioGRID, MINT, BIND, DIP, IntAct, and HPRD.
  • Integration of datasets from the six selected protein interaction databases.
  • Comparative analysis of the scope and content of the integrated datasets.

Main Results:

  • Significant variations in scope and content were observed among the six databases.
  • The Human Protein Reference Database (HPRD) appears most comprehensive for human PPI data.
  • Complete PPI datasets require combining information from all six sources, presenting integration challenges.

Conclusions:

  • Integrating PPI data from multiple databases is vital for a comprehensive view.
  • Differences in data annotation present non-trivial challenges for dataset integration.
  • Meta-databases like APID offer solutions but currently have limitations.