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Related Concept Videos

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,...
Proteomics01:33

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...
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...

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Related Experiment Video

Updated: May 28, 2026

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

A secreted protein microarray platform for extracellular protein interaction discovery.

Sree R Ramani1, Irene Tom, Nicholas Lewin-Koh

  • 1Department of Protein Chemistry, Genentech, South San Francisco, CA 94080, USA.

Analytical Biochemistry
|October 11, 2011
PubMed
Summary
This summary is machine-generated.

Functional protein microarrays effectively screen extracellular protein interactions, including low-affinity binding events. This method enhances the study of cell signaling and communication by improving the identification of specific receptor-ligand interactions.

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Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
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Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

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Last Updated: May 28, 2026

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
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Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

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Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
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Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
12:30

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

Area of Science:

  • Proteomics
  • Molecular Biology
  • Cell Biology

Background:

  • Characterizing extracellular protein interactions is crucial for understanding cell signaling and communication.
  • Existing methods like mass spectrometry and yeast two-hybrid excel at intracellular protein analysis but are less effective for extracellular interactions.
  • Identifying low-affinity binding events between membrane-bound coreceptors and extracellular matrix proteins is a significant challenge.

Purpose of the Study:

  • To develop and validate a high-throughput method for screening extracellular protein interactions.
  • To enhance the detection of low-affinity binding events crucial for cell-cell and cell-extracellular matrix communication.
  • To establish a robust statistical framework for analyzing protein microarray data and identifying specific interactions.

Main Methods:

  • Utilized functional protein microarrays for high-throughput screening of extracellular protein interactions.
  • Screened 89 immunoglobulin (Ig)-type receptors against a microarray of 686 extracellular proteins.
  • Developed a novel method using protein A microbeads to create multivalent complexes of bait Fc fusion proteins for enhanced low-affinity interaction detection.

Main Results:

  • The functional protein microarray platform demonstrated high specificity and minimal off-target binding for Ig receptor interactions.
  • A statistical methodology was developed for accurate hit calling and identification of nonspecific interactions.
  • Achieved a 70% true-positive to false-positive hit ratio, indicating high confidence in identified interactions.

Conclusions:

  • Functional protein microarrays, coupled with multivalent complex formation and robust statistical analysis, are a powerful tool for high-throughput screening of extracellular protein interactions.
  • This approach significantly advances the ability to study cell signaling and communication by accurately identifying specific, including low-affinity, protein interactions.
  • The developed methods are broadly applicable to users of functional protein microarrays for diverse biological discovery applications.