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

Feedback Inhibition

Feedback Inhibition

Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!

Molecules and Compounds

Molecules and Compounds

Atoms and Molecules

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

Enzyme Inhibition

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

Negative Regulator Molecules

Negative Regulator Molecules

Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

You might also read

Related Articles

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

Sort by

Same author

Peptide Thioester and Triazole Derivatives Through On-Resin Dual-Modification of Peptide Thiosulfonates.

Angewandte Chemie (International ed. in English)·2026

Same author

The evolving role of cytokines for CAR-T cell manufacturing and beyond.

Nature biomedical engineering·2026

Same author

Impact of ASO conjugation and receptor binding affinity on intracellular transport of mono- and bispecific TfR- and CD98-Brainshuttle<sup>TM</sup> variants.

mAbs·2026

Same author

First-in-human study of lomvastomig, a PD-1-TIM-3 bispecific antibody, in patients with advanced and/or metastatic solid tumors.

Journal for immunotherapy of cancer·2026

Same author

Target receptor expression dictates the selective intra-tumoral targeting of CD8<sup>+</sup> T cells by eciskafusp alfa in matched PBMCs and TILs from CPI-naïve patients.

Frontiers in immunology·2026

Same author

Tobemstomig, a Novel Bispecific Antibody, Preferentially Blocks PD-1 and LAG-3 on CD8 TILs to Expand Stem-like T Cells for Sustained Tumor Control.

Cancer research communications·2026

Search research articles

Related Experiment Video

Updated: Jan 26, 2026

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

Small-Molecule Inhibition of the UNC-Src Interaction Impairs Dynamic Src Localization in Cells.

Guillaume Garivet¹, Walter Hofer¹, Antonios Konitsiotis²

¹Department of Chemical Biology, Max-Planck-Institute of Molecular Physiology, Dortmund, North Rhine-Westphalia 44227, Germany; Faculty of Chemistry and Chemical Biology, TU Dortmund, Dortmund, North Rhine-Westphalia 44227, Germany.

Cell Chemical Biology

|April 9, 2019

Summary

Researchers discovered a novel small molecule that disrupts the UNC119-Src interaction, a key pathway in cancer. This inhibitor shows promise for anti-cancer drug development by targeting Src spatial cycles and reducing tumor cell growth.

Keywords:

N-myristoylation Src family kinases UNC119 inhibitors protein-protein interactions target engagement

More Related Videos

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 15, 2013

Related Experiment Videos

Last Updated: Jan 26, 2026

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 15, 2013

Area of Science:

Oncology
Molecular Biology
Drug Discovery

Background:

Src signaling is crucial for cancer progression, but ATP-competitive inhibitors face clinical challenges.
UNC119 proteins regulate Src localization and activity at the plasma membrane, representing an alternative therapeutic target.
Targeting the UNC119-Src interaction offers a novel strategy for anti-cancer drug development.

Purpose of the Study:

To discover and characterize a novel inhibitor of the UNC119-Src interaction.
To investigate the effects of UNC119 inhibition on Src localization and activity.
To evaluate the anti-cancer potential of UNC119 inhibition in colorectal cancer models.

Main Methods:

Discovery of a small molecule inhibitor targeting the UNC119-Src protein-protein interaction.
Cellular assays to assess inhibitor binding to UNC119 and Src redistribution.
Measurement of Src autophosphorylation at Y419.
Assessment of cell growth and clonogenic potential in colorectal cancer cells.

Main Results:

A potent and specific inhibitor of the UNC119-Src interaction with a novel chemotype was identified.
The inhibitor binds UNC119 in cells, leading to Src redistribution to endomembranes.
Inhibition of UNC119 reduced activating Src autophosphorylation on Y419.
UNC119 inhibition specifically decreased cell growth and clonogenic potential in Src-dependent colorectal cancer cells.

Conclusions:

Small-molecule inhibition of the UNC119-Src interaction is a viable strategy to impair oncogenic Src signaling.
Interfering with Src spatial cycle dynamics offers a promising avenue for anti-cancer drug discovery.
This approach provides an alternative to traditional ATP-competitive Src inhibitors.