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

Proteomics01:33

Proteomics

7.3K
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...
7.3K
Protein Networks02:26

Protein Networks

3.9K
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,...
3.9K

You might also read

Related Articles

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

Sort by
Same author

Mitochondrial respiratory capacity in kidney podocytes is high, age-dependent, and sexually dimorphic.

Kidney international·2026
Same author

Site Confidence Scores among All Available Structures to Help Infer Conformational Origins of Identified Cross-Links.

Journal of proteome research·2026
Same author

On the Feasibility of Clinical Studies with Cross-Linking Mass Spectrometry.

Journal of proteome research·2026
Same author

Long AKAP18 isoforms anchor ubiquitin specific proteinases and coordinate calcium reuptake at the sarcoplasmic reticulum.

The Journal of biological chemistry·2025
Same author

Contemporary insights into elamipretide's mitochondrial mechanism of action and therapeutic effects.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2025
Same author

Large-Scale Quantitative Cross-Linking and Mass Spectrometry Provide New Insight into Protein Conformational Plasticity within Organelles, Cells, and Tissues.

Journal of proteome research·2025

Related Experiment Video

Updated: Jun 23, 2025

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

11.9K

Combining quantitative proteomics and interactomics for a deeper insight into molecular differences between human

Anna A Bakhtina1, Helisa H Wippel1, Juan D Chavez1

  • 1Department of Genome Sciences, University of Washington, Seattle, WA, USA.

Biorxiv : the Preprint Server for Biology
|June 25, 2024
PubMed
Summary
This summary is machine-generated.

Researchers used quantitative cross-linking and mass spectrometry to analyze protein interactions in three human cell lines. This reveals cell-specific interactome changes beyond protein levels, highlighting cytoskeletal and RNA-binding proteins.

Keywords:
cellular quantitative interactomehuman cell linemass spectrometryquantitative cross-linking

More Related Videos

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

31.5K
Quantitative Mass Spectrometric Profiling of Cancer-cell Proteomes Derived From Liquid and Solid Tumors
08:08

Quantitative Mass Spectrometric Profiling of Cancer-cell Proteomes Derived From Liquid and Solid Tumors

Published on: February 27, 2015

16.2K

Related Experiment Videos

Last Updated: Jun 23, 2025

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

11.9K
Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

31.5K
Quantitative Mass Spectrometric Profiling of Cancer-cell Proteomes Derived From Liquid and Solid Tumors
08:08

Quantitative Mass Spectrometric Profiling of Cancer-cell Proteomes Derived From Liquid and Solid Tumors

Published on: February 27, 2015

16.2K

Area of Science:

  • Cellular biology and proteomics
  • Biomedical research

Background:

  • Cellular function relies on the protein interactome, influenced by protein levels and post-translational modifications.
  • Understanding cell-type specific functional differences requires insights beyond protein abundance, focusing on conformational and interaction changes.

Purpose of the Study:

  • To investigate large-scale protein conformational and interaction changes across different human cell lines.
  • To compare quantitative interactome data with proteome abundance levels.

Main Methods:

  • Quantitative in vivo protein cross-linking coupled with mass spectrometry.
  • Isobaric quantitative Protein Interaction Reporter (iqPIR) technologies for quantitative cross-linked peptides.
  • Data-independent acquisition quantitative proteomics for protein abundance measurements.

Main Results:

  • Highly reproducible quantitative interactome levels (R² > 0.8) were observed across biological replicates.
  • Identified cell type-specific interactome alterations, independent of proteome level changes.
  • Significant changes were detected in cytoskeletal proteins, RNA-binding proteins, chromatin remodeling complexes, and mitochondrial proteins.

Conclusions:

  • Quantitative cross-linking is a reproducible method for studying systems-level interactome variations.
  • Combining quantitative interactomics and proteomics provides unique insights into cellular functional landscapes.
  • Cell-specific interactome dynamics contribute significantly to cellular functional differences.