Linking entries in protein interaction database to structured text: the FEBS Letters experiment.
Arnaud Ceol1, Andrew Chatr-Aryamontri, Luana Licata
1Department of Biology, University of Rome, Tor Vergata, Rome, Italy.
FEBS Letters
|March 11, 2008
Summary
Scientists are developing structured summaries to capture protein interactions from research articles, improving data retrieval. This aims to enhance biological databases and aid automatic analysis of scientific literature.
Area of Science:
- Biomedical Informatics
- Molecular Biology
- Scientific Publishing
Background:
- The vast scientific literature contains valuable biological data that is difficult to access due to unstructured text.
- Current manual curation of databases is unsustainable for comprehensive coverage of published information.
- Efficient automatic retrieval of entity relationships (e.g., protein interactions) from text is a significant challenge.
Purpose of the Study:
- To test a novel method for integrating structured summaries of protein interactions into scientific manuscripts.
- To enhance the discoverability and usability of biological data within published research.
- To explore a more sustainable and accurate approach to scientific data curation.
Main Methods:
- An experiment was conducted by FEBS Letters involving authors providing structured summaries of protein interactions.
- These summaries include database identifiers and controlled vocabularies.
- The structured information is appended as human-readable paragraphs to traditional abstracts.
Main Results:
- The experiment demonstrated the feasibility of authors contributing structured data on protein interactions.
- This approach facilitates the integration of machine-readable information directly into scientific publications.
- The structured text is intended to become part of Medline abstracts for improved data retrieval.
Conclusions:
- Integrating structured summaries is a promising strategy to overcome data retrieval challenges in the biological domain.
- Author-provided structured information can enhance the value of scientific literature for database curation and analysis.
- Further community discussion is planned to establish a widely accepted strategy for scientific information storage and retrieval.
Related Concept Videos
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,...
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 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,...
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 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 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 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...
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 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...
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...

