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Related Concept Videos

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...
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.
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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.
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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 polypeptide...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
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New Features in Visual Dynamics 3.0
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Published on: August 9, 2024

MINT, the molecular interaction database: 2012 update.

Luana Licata1, Leonardo Briganti, Daniele Peluso

  • 1Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome, Italy.

Nucleic Acids Research
|November 19, 2011
PubMed
Summary
This summary is machine-generated.

The Molecular INTeraction Database (MINT) provides a vast collection of protein-protein interactions (PPI) from scientific literature. A new algorithm now assigns confidence scores to these interactions, enhancing data usability.

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Published on: April 12, 2019

Area of Science:

  • Biochemistry
  • Bioinformatics
  • Proteomics

Background:

  • The Molecular INTeraction Database (MINT) is a public repository for protein-protein interactions (PPI).
  • It curates data from peer-reviewed journals, steadily growing over the years.
  • MINT is a member of the International Molecular Exchange (IMEx) consortium.

Purpose of the Study:

  • To report the growth and recent developments of the MINT database.
  • To describe changes in curation policy.
  • To introduce a new algorithm for assigning confidence scores to protein-protein interactions.

Main Methods:

  • Data collection from peer-reviewed publications.
  • Adoption of Proteomics Standards Initiative Molecular Interaction Ontology (PSI-MI) standards for curation and data exchange.
  • Development of a novel algorithm for confidence scoring of interactions.

Main Results:

  • As of September 2011, MINT contains approximately 235,000 binary interactions from over 4750 publications.
  • The database offers a web interface for searching, visualizing, and downloading interaction data.
  • A new algorithm has been implemented to assign confidence scores to each interaction.

Conclusions:

  • MINT continues to expand as a valuable resource for protein-protein interaction data.
  • Standardized curation and data exchange ensure data quality and interoperability.
  • The new confidence scoring algorithm enhances the utility of MINT data for researchers.