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Related Concept Videos

Protein-protein Interfaces02:04

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 Interfaces02:04

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 Networks02:26

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,...
Quantitative Aspects of Drug-Receptor Interaction01:30

Quantitative Aspects of Drug-Receptor Interaction

The receptor occupancy theory connects a drug's response to the number of occupied receptors. With higher drug concentrations, more receptors are occupied, leading to increased responses. The formation of drug-receptor complexes involves association and dissociation rates, which reach equilibrium when the forward and backward reactions are equal. The equilibrium association constant (Ka) and its inverse, the equilibrium dissociation constant (Kd), indicate drug affinity. Higher Ka and lower Kd...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Ligand Binding Sites02:40

Ligand Binding Sites

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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Related Experiment Video

Updated: Jul 17, 2026

Comparing Bibliometric Analysis Using PubMed, Scopus, and Web of Science Databases
05:02

Comparing Bibliometric Analysis Using PubMed, Scopus, and Web of Science Databases

Published on: October 24, 2019

PubMed Interact: an interactive search application for MEDLINE/PubMed.

Michael Muin1, Paul Fontelo, Michael Ackerman

  • 1Office of High Performance Computing and Communications, National Library of Medicine, Bethesda, Maryland, USA.

AMIA ... Annual Symposium Proceedings. AMIA Symposium
|January 24, 2007
PubMed
Summary

PubMed Interact enhances medical literature searches using Web 2.0 technologies. This system improves user experience by allowing easy refinement of search parameters and interaction with results.

Related Experiment Videos

Last Updated: Jul 17, 2026

Comparing Bibliometric Analysis Using PubMed, Scopus, and Web of Science Databases
05:02

Comparing Bibliometric Analysis Using PubMed, Scopus, and Web of Science Databases

Published on: October 24, 2019

Area of Science:

  • Medical Informatics
  • Information Retrieval
  • Web Technologies

Background:

  • Online search systems are crucial for accessing medical literature.
  • Advancements in Web 2.0 technologies offer potential improvements for search strategies and user interaction.
  • Existing systems may lack dynamic refinement and result interaction capabilities.

Purpose of the Study:

  • To introduce PubMed Interact, a system designed to enhance the PubMed search experience.
  • To leverage Web 2.0 technologies for improved medical literature retrieval and analysis.
  • To provide users with intuitive tools for refining search parameters and interacting with results.

Main Methods:

  • Development of PubMed Interact utilizing PHP, Document Object Model (DOM) manipulation, and Asynchronous JavaScript and XML (Ajax).
  • Implementation of dynamic search parameter refinement features.
  • Integration of interactive elements for result exploration and display of related articles.

Main Results:

  • PubMed Interact offers enhanced functionality for refining search parameters.
  • Users can easily interact with search results for better information retrieval.
  • The system facilitates the display of relevant and related articles efficiently.

Conclusions:

  • PubMed Interact represents a significant improvement in online medical literature search systems.
  • The application of Web 2.0 technologies enhances user experience and search efficiency.
  • This system empowers researchers to interact more effectively with medical literature databases.