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Related Concept Videos

Protein Networks02:26

Protein Networks

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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.
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,...
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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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...
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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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A Knowledge Graph Approach to Elucidate the Role of Organellar Pathways in Disease via Biomedical Reports
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Annotated protein network analysis linking oral diseases.

Mukesh Kumar Sharma1,2, Vivek Kumar Srivastav1, Chetan Kumar Joshi3

  • 1Department of Biotechnology, Maharaj Vinayak Global University, Jaipur Rajasthan, India.

Bioinformation
|June 16, 2023
PubMed
Summary
This summary is machine-generated.

Oral cancer is a growing global health concern. This study maps protein interactions in oral bacteria, identifying potential therapeutic targets for oral disease drug discovery.

Keywords:
NetworkingSTRINGbacteriacystoscopeoral cancer

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Area of Science:

  • Molecular biology
  • Bioinformatics
  • Oral microbiology

Background:

  • Oral cancer is a significant and increasing global health issue.
  • Understanding molecular interactions is crucial for identifying therapeutic targets.
  • Elucidating protein networks and signaling pathways in oral bacteria is key.

Purpose of the Study:

  • To construct a protein-protein interaction network for oral bacterial proteins.
  • To identify potential therapeutic drug candidates for oral diseases.
  • To analyze functional annotations and cell signaling pathways.

Main Methods:

  • Utilized the STRING online software to build a molecular genetics interaction network.
  • Employed Cystoscope software for network analysis, identifying nodes and edges.
  • Analyzed network topology, including average node order.

Main Results:

  • Developed the AZURIN molecular genetics interaction network for oral bacterial proteins.
  • Identified 11 nodes and 16 edges within the constructed network.
  • Characterized network properties, such as an average node order of 2.91.

Conclusions:

  • The study provides valuable data on protein-protein interactions in oral bacteria.
  • The identified network serves as a foundation for discovering novel therapeutic drug candidates.
  • This research contributes to understanding oral disease mechanisms and potential interventions.