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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-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 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...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Updated: May 27, 2026

A Data Integration Workflow to Identify Drug Combinations Targeting Synthetic Lethal Interactions
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A Data Integration Workflow to Identify Drug Combinations Targeting Synthetic Lethal Interactions

Published on: May 27, 2021

The IntAct molecular interaction database in 2012.

Samuel Kerrien1, Bruno Aranda, Lionel Breuza

  • 1EMBL Outstation, European Bioinformatics Institute, Wellcome Trust Genome Campus Hinxton, Cambridge CB10 1SD, UK.

Nucleic Acids Research
|November 29, 2011
PubMed
Summary
This summary is machine-generated.

IntAct is a molecular interaction database offering open-source, open data with enhanced search and graphical display features. It supports two curation levels and facilitates Semantic Web integration.

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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Last Updated: May 27, 2026

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Published on: May 27, 2021

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

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Area of Science:

  • Biochemistry
  • Bioinformatics
  • Molecular Biology

Background:

  • IntAct is a widely used open-source database for molecular interactions.
  • It relies on curated data from scientific literature and direct depositions.
  • Existing data access and visualization methods require enhancement.

Purpose of the Study:

  • To improve the IntAct database's functionality and data accessibility.
  • To enhance the user experience for searching and visualizing molecular interaction data.
  • To facilitate the integration of IntAct data into the Semantic Web.

Main Methods:

  • Continued curation of molecular interaction data from literature.
  • Implementation of two distinct data curation levels: IMEx and MIMIx.
  • Enhancements to the IntAct website for improved search and graphical result display.
  • Development of new data download formats.

Main Results:

  • As of September 2011, IntAct contains approximately 275,000 curated binary interaction evidences from over 5000 publications.
  • The IntAct website now offers improved search capabilities and graphical result visualization.
  • New data download formats are available, supporting Semantic Web integration.

Conclusions:

  • IntAct provides a valuable and expanding resource for molecular interaction data.
  • Website enhancements improve data retrieval and analysis for researchers.
  • The database actively contributes to the IMEx consortium and promotes open data sharing.