Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Networks02:26

Protein Networks

4.1K
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,...
4.1K
Protein-protein Interfaces02:04

Protein-protein Interfaces

13.8K
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...
13.8K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.6K
Proteomics01:33

Proteomics

8.0K
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...
8.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Artificial intelligence in periodontal disease research: a bibliometric and visualized analysis of global research trends (2007-2025).

The Saudi dental journal·2026
Same author

Proteostasis sustains T cell differentiation potential and tumor-infiltrating lymphocyte function.

Cell·2026
Same author

Machine learning driven discovery of low modulus biomedical titanium alloys for additive manufacturing.

Nature communications·2026
Same author

Microstructural Characteristics and Mechanical Properties of Al-5Cu-0.4Mg-0.1Zr (-0.4Ag) Alloys Processed by Continuous Cast and Conform Processes.

Materials (Basel, Switzerland)·2026
Same author

Proteostasis sustains T cell differentiation potential and tumor-infiltrating lymphocyte function.

bioRxiv : the preprint server for biology·2026
Same author

CRISPR-mediated conditional mutagenesis of <i>Smad1/5/8</i> reveals BMP/GDF signaling restricts postnatal bone overgrowth.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Sep 20, 2025

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
11:19

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

16.4K

Employing Expression-Matched Controls Enables High-Confidence Proximity-Based Interactome Classification.

Fulin Jiang1, Xuezhen Ge1, Eric J Bennett1

  • 1School of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, California, USA.

Molecular & Cellular Proteomics : MCP
|May 29, 2025
PubMed
Summary
This summary is machine-generated.

Controlling TurboID protein expression is crucial for accurate proximity labeling interactome mapping. Matched expression controls significantly reduce background noise and improve the reliability of protein interaction studies.

More Related Videos

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

8.6K
A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

11.3K

Related Experiment Videos

Last Updated: Sep 20, 2025

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
11:19

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

16.4K
Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

8.6K
A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

11.3K

Area of Science:

  • Proteomics
  • Molecular Biology
  • Biochemistry

Background:

  • Proximity labeling is widely used to identify protein interactomes.
  • TurboID-based methods can suffer from promiscuity, necessitating effective controls.
  • Accurate interactome mapping relies on mitigating background interference.

Purpose of the Study:

  • To evaluate expression controls and data normalization for high-confidence interactome maps.
  • To assess the impact of TurboID protein expression levels on interactome assignment.
  • To demonstrate the benefits of matched expression controls in proximity labeling.

Main Methods:

  • Evaluation of expression controls and data normalization strategies.
  • Utilizing TurboID proximity labeling with ubiquitin ligases RNF10 and HUWE1 as bait.
  • Comparison of matched versus mismatched TurboID expression levels between bait and control samples.

Main Results:

  • TurboID expression levels directly correlate with signal intensity and identified proteins.
  • Discordant expression leads to false-negative and false-positive identifications.
  • Matched expression controls reduce background interference and enhance interactome accuracy.

Conclusions:

  • Matched TurboID expression controls are essential for robust proximity labeling proteomics.
  • Experimental workflows should incorporate matched expression controls for improved interactome mapping.
  • This strategy enhances the robustness and reproducibility of proximity labeling studies.