Related Experiment Video
Updated: Jun 30, 2025
10:08
Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
Published on: August 28, 2012
11.8K
Insights into amyloid precursor protein target through PPI network analysis.
Annu Grewal1, Deepak Sheokand1, Raveena Chauhan1
1Toxicology and Computational Biology Group, Centre for Bioinformatics, Maharshi Dayanand University, Rohtak, Haryana, India, 124001.
Bioinformation
|March 18, 2024
Summary
Alzheimer's disease (AD) research identified key proteins involved in its development. The Amyloid precursor protein (APP) emerged as a significant hub, suggesting its potential for future AD therapies.
Area of Science:
- Neuroscience
- Biochemistry
- Computational Biology
Background:
- Alzheimer's disease (AD) is a leading cause of dementia with limited effective treatments.
- Beta-amyloid (Aβ) accumulation is implicated in AD, but targeting it has yielded limited success, indicating other factors are crucial.
- Identifying novel therapeutic targets requires understanding complex protein interactions in AD pathogenesis.
Purpose of the Study:
- To identify key hub proteins involved in Alzheimer's disease etiology using a network-based approach.
- To explore the potential of these hub proteins as targets for AD drug design.
- To analyze protein-protein interaction networks associated with AD.
Main Methods:
- Literature mining to identify AD-implicated proteins.
- Retrieval of protein-protein interactions (PPIs) from the STRING database.
- Network construction and analysis using Cytoscape 3.10.1 and CytoHubba for hub protein prediction.
Main Results:
- Six major proteins (APP, BACE1, PSEN1, MAPT, APOE4, TREM2) were identified as central to AD pathogenesis.
- The merged PPI network comprised 51 nodes and 211 edges.
- Amyloid precursor protein (APP) was identified as the highest-scoring hub protein based on multiple centrality measures.
Conclusions:
- The study highlights the critical role of specific proteins, particularly APP, in Alzheimer's disease.
- APP presents a promising target for further investigation and potential therapeutic development for AD.
- Network-based approaches are valuable for identifying novel therapeutic targets in complex diseases like AD.
Related Concept Videos
02:26Protein Networks
3.9K
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,...
3.9K
02:04Protein-protein Interfaces
12.5K
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...
12.5K
03:03Amyloid Fibrils
9.5K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.5K