Related Experiment Video
Updated: Jun 2, 2026

10:17
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
MinePhos: a literature mining system for protein phoshphorylation information extraction
1University of Science and Technology of China, Hefei and Anhui Province Key Laboratory of High Performance Computing, Hefei.
Summary
MinePhos, an SVM-based system, improves protein phosphorylation data extraction from scientific literature. It surpasses rule-based methods like RLIMS-P in precision and recall for biological research.
Area of Science:
- Biochemistry and Bioinformatics
- Molecular Biology
- Computational Biology
Background:
- The exponential growth of scientific literature necessitates automated methods for extracting critical experimental data.
- Protein phosphorylation is a key post-translational modification vital for understanding cellular signaling, cancer, and diabetes.
- Current data extraction tools, such as RLIMS-P, rely heavily on rule-based systems with limitations in performance.
Purpose of the Study:
- To develop and evaluate an automated system for extracting protein phosphorylation information from scientific texts.
- To improve the precision and recall of experimental data extraction compared to existing methods.
Main Methods:
- A Support Vector Machine (SVM) based system, named MinePhos, was developed for information extraction.
- The system was trained and tested on a dataset of research articles randomly selected from PubMed.
Main Results:
- MinePhos demonstrated superior performance over the rule-based RLIMS-P system.
- The proposed SVM-based approach achieved higher precision and recall in extracting protein phosphorylation data.
Conclusions:
- MinePhos offers a more effective and efficient solution for mining protein phosphorylation data from the scientific literature.
- This advancement can significantly aid biologists in their research on cellular processes and diseases.
Related Concept Videos
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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...
Proteomics
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
