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Related Concept Videos

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Ribosome Profiling

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Related Experiment Video

Updated: Jun 16, 2026

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Rapid interactome profiling by massive sequencing.

Roberto Di Niro1, Ana-Marija Sulic, Flavio Mignone

  • 1Department of Life Sciences, University of Trieste, Trieste, Italy.

Nucleic Acids Research
|February 11, 2010
PubMed
Summary
This summary is machine-generated.

Researchers developed a high-throughput platform combining phage display and gene sequencing to analyze protein interactions. This method rapidly identifies novel protein interaction partners, like those for transglutaminase 2 (TG2), accelerating biological discovery.

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Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genomics

Background:

  • Transglutaminase 2 (TG2) is a key enzyme in cell regulation, implicated in various diseases.
  • Understanding TG2's interaction network is crucial for disease research.
  • Existing methods for protein interaction analysis can be slow and limited in scope.

Purpose of the Study:

  • To develop and validate a high-throughput platform for protein expression and interaction analysis.
  • To identify novel interaction partners of transglutaminase 2 (TG2).
  • To characterize the protein interaction network of TG2.

Main Methods:

  • Construction of a cDNA phage display library from diverse tissue mRNA.
  • Selection of open reading frame (ORF) fragments interacting with TG2 via panning.
  • Massive gene sequencing (454 platform) to analyze ORF frequencies in selected phage populations.
  • Functional assays to confirm identified protein interactions.

Main Results:

  • Over 120,000 sequences were analyzed, revealing multiple TG2 interaction candidates.
  • Identified three known interacting proteins (fibronectin, SMOC1, GSTO2) and numerous novel interactors.
  • Confirmed specific interaction domains, exemplified by fibronectin.

Conclusions:

  • The developed platform significantly accelerates protein interaction discovery compared to traditional methods.
  • This high-throughput approach provides deeper insights into complex biological systems and protein networks.
  • The platform is effective for identifying novel protein interactors and characterizing interaction interfaces.