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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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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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Protein Networks02:26

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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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Ligand Binding Sites02:40

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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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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.
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Targets for Drug Action: Overview01:26

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Drugs target macromolecules to modify ongoing cellular processes. Primary drug targets include receptors, ion channels, transporters, and enzymes.
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Updated: May 6, 2026

Author Spotlight: Streamlining Protein Target Prediction and Validation via Molecular Docking and CETSA
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Targeting protein-protein interaction by small molecules.

Lingyan Jin1, Weiru Wang, Guowei Fang

  • 1Discovery Oncology and.

Annual Review of Pharmacology and Toxicology
|October 29, 2013
PubMed
Summary
This summary is machine-generated.

Targeting protein-protein interactions (PPIs) with small molecules is challenging but advancing. This review covers recent progress in discovering small-molecule regulators for oncogenic proteins, focusing on inhibition, allosteric regulation, and stabilization mechanisms.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Pharmacology
  • Cancer Biology

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions and disease processes.
  • Targeting PPIs for drug development is difficult due to large interface areas and lack of binding pockets.
  • Despite challenges, small-molecule modulators of PPIs are increasingly successful.

Purpose of the Study:

  • To review recent advancements in small-molecule regulators of PPIs involving key oncogenic proteins.
  • To discuss the mechanisms of action for these small-molecule modulators.
  • To highlight opportunities and challenges in developing PPI-targeting drugs.

Main Methods:

  • Literature review of recent studies on small-molecule modulators of PPIs.
  • Focus on modulators targeting oncogenic proteins.
  • Categorization of modulators based on their mechanism of action.

Main Results:

  • Growing number of successful small-molecule modulators for PPIs.
  • Identification of three key modes of action: orthosteric inhibition, allosteric regulation, and interfacial binding/stabilization.
  • Examples of modulators targeting key oncogenic proteins are discussed.

Conclusions:

  • Small-molecule modulation of PPIs is a viable therapeutic strategy.
  • Understanding diverse mechanisms is key to future drug development.
  • Further research is needed to overcome challenges in targeting PPIs.