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

Amplifying Signals via Enzymatic Cascade

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...

You might also read

Related Articles

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

Sort by

Same author

Total Synthesis of Conjugation-Ready Sulfated Red Algae Carrageenan Oligosaccharides for Sensing Applications.

Journal of the American Chemical Society·2026

Same author

Methods for studying the effects of phosphorylation patterns in proteins.

Biochemical Society transactions·2026

Same author

MiProChip: A Scalable Microfluidic Platform for Multiplexed Single-Cell Proteomics via Isobaric Labeling.

Analytical chemistry·2026

Same author

Mechanistic Insights into Unary Peptide-Membrane Interactions Enable Stable Encapsulation and Trigger-Responsive Peptidyl Liposomes.

Journal of the American Chemical Society·2026

Same author

Integrative proteogenomics maps multifactorial aetiology, progression and therapeutic vulnerabilities in gastric cancer.

Gut·2026

Same author

IsoPS-DIA: Dual Functionality of Absolute Targeted Quantification and Global Proteome Profiling.

Analytical chemistry·2026

Same journal

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Biochemistry·2026

Same journal

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Biochemistry·2026

Same journal

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026

Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026

Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026

Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Aug 25, 2025

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Using a Single Peptide to Electrochemically Sense Multiple Kinases.

Ohad Solomon¹, Israel Alshanski¹, Ariel Shitrit¹

¹Institute of Chemistry and Center for Nanoscience and Nanotechnology, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem 91904, Israel.

|October 14, 2022

Summary

This summary is machine-generated.

This study introduces a novel electrochemical sensor for detecting multiple kinases, specifically ERK2 and PKCδ, using a single peptide. This advancement offers a new tool for disease biomarker discovery and enzyme sensing.

More Related Videos

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Related Experiment Videos

Last Updated: Aug 25, 2025

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Area of Science:

Biochemistry
Molecular Biology
Analytical Chemistry

Background:

Kinases regulate crucial cellular functions, and their dysregulation is linked to various diseases.
Current kinase detection methods typically target only one kinase, limiting comprehensive analysis.
Identifying multiple kinases involved in disease pathways is essential for accurate diagnosis and treatment.

Purpose of the Study:

To develop a novel electrochemical sensing tool for the simultaneous and selective detection of multiple kinases.
To demonstrate the capability of this tool for detecting specific kinases, ERK2 and PKCδ, using a single peptide substrate.
To establish a versatile platform for advanced enzyme sensing and disease biomarker identification.

Main Methods:

Designed a single peptide sensing element with distinct phosphorylation sites for ERK2 and PKCδ.
Utilized an electrochemical approach for kinase activity detection.
Employed alkaline phosphatase for reversibility experiments and ferrocene-labeled ATP to confirm phosphorylation detection.

Main Results:

Successfully demonstrated selective electrochemical sensing of two distinct kinases, ERK2 and PKCδ, using the same peptide.
Confirmed the sensing mechanism relies on enzymatic phosphorylation.
Established the reversibility of the sensing process.

Conclusions:

The developed electrochemical tool enables the selective detection of multiple kinases using a single peptide.
This approach provides a foundation for creating devices capable of detecting numerous kinases simultaneously.
The methodology can be extended to sense other disease-related enzymes.