Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Networks

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,...

Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

You might also read

Related Articles

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

Sort by

Same author

Peptides as multifunctional linchpins in targeted drug conjugates.

RSC medicinal chemistry·2026

Same author

Discovery of Potent and Orally bioavailable Benzoazepinamine-Based SHP2 Allosteric Inhibitors for the Treatment of Inflammatory Diseases.

Journal of medicinal chemistry·2025

Same author

Influence of Macrocyclization Strategies on DNA-Encoded Cyclic Peptide Libraries.

JACS Au·2025

Same author

Robust Chemical Cross-linking of Proteins and Protein Complexes via SuFEx Click Chemistry.

Analytical chemistry·2025

Same author

Fast and Selective Cysteine Conjugation Using <i>para</i>-Quinone Methides.

Organic letters·2024

Same author

Atroposelective Synthesis of Axially Chiral Diaryl Ethers by <i>N</i>-Heterocyclic-Carbene-Catalyzed Sequentially Desymmetric/Kinetic Resolution Process.

The Journal of organic chemistry·2024

Search research articles

Related Experiment Video

Updated: Jun 12, 2026

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

Organelle-Specific Interactome Mapping via Enzyme-Responsive Cross-Linking and Proximity Labeling.

Xuechun Yuan¹, Kai Li¹, Zifan Wang¹

¹Department of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University, Nanjing 211198, China.

Analytical Chemistry

|June 10, 2026

Summary

This study introduces an enzyme-responsive cross-linking method for mapping protein interactions within specific organelles. The technique enhances spatial resolution for studying dynamic protein networks and cellular organization.

More Related Videos

Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells

Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells

Published on: December 10, 2016

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

Related Experiment Videos

Last Updated: Jun 12, 2026

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells

Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells

Published on: December 10, 2016

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Chemical cross-linking mass spectrometry (CXMS) is vital for protein structure and interaction analysis.
Current CXMS limitations include restricted amino acid reactivity and lack of organelle specificity.
Advancing CXMS requires novel cross-linking strategies for deeper biological insights.

Purpose of the Study:

To develop an enzyme-responsive cross-linking strategy for organelle-specific interactome mapping.
To integrate lysine- and tyrosine-targeting cross-linking with proximity labeling.
To enhance spatiotemporal resolution in studying protein interactions and subcellular organization.

Main Methods:

Utilized an organelle-localized APEX2 peroxidase for enzyme-responsive cross-linking.
Activated phenol moieties for in situ protein cross-linking and biotinylation.
Employed proximity labeling for protein enrichment and mass spectrometry analysis.

Main Results:

Successfully validated the method using in vitro model proteins and live mammalian cells.
Achieved nucleus-specific cross-linking with high subcellular precision.
Established a robust platform for spatially resolved interactome mapping.

Conclusions:

The enzyme-responsive cross-linking strategy offers a powerful new tool for biological research.
This approach enables precise investigation of dynamic protein interactions within specific cellular compartments.
The method significantly advances the potential of CXMS for understanding subcellular organization.