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 Experiment Videos

Phosphoproteomic analysis with a solid-phase capture-release-tag approach.

Huang-Chun Tseng1, Huib Ovaa, Nancy J C Wei

  • 1Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02155, USA. huang-chun_tseng@hms.harvard.edu

Chemistry & Biology
|July 26, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Modulation of Ube2R1 activity by a nanobody that binds near its N-terminus.

The Biochemical journal·2026
Same author

Leveraging Targeted Protein Degradation for G Protein-Coupled Receptors: The Development of CCR2 Molecular Degraders.

Journal of medicinal chemistry·2025
Same author

Growth inhibition of Saccharomyces cerevisiae by SUMO-specific nanobodies.

Scientific reports·2025
Same author

A nanobody that binds to the backside of the ubiquitin conjugating enzyme Ube2G2 differentially affects interactions with its partner E3 Ligases.

Communications biology·2025
Same author

Site-directed multivalent conjugation of antibodies to ubiquitinated payloads.

Nature biomedical engineering·2025
Same author

Bi-specific antibody engagers for cancer immunotherapy.

Research square·2024
Same journal

The Hedgehog Pathway Effector Smoothened Exhibits Signaling Competency in the Absence of Ciliary Accumulation.

Chemistry & biology·2017
Same journal

DIVERSE System: De Novo Creation of Peptide Tags for Non-enzymatic Covalent Labeling by In Vitro Evolution for Protein Imaging Inside Living Cells.

Chemistry & biology·2015
Same journal

Differential Regulation of Specific Sphingolipids in Colon Cancer Cells during Staurosporine-Induced Apoptosis.

Chemistry & biology·2015
Same journal

Synthetic Peptides as cGMP-Independent Activators of cGMP-Dependent Protein Kinase Iα.

Chemistry & biology·2015
Same journal

Unraveling the B. pseudomallei Heptokinase WcbL: From Structure to Drug Discovery.

Chemistry & biology·2015
Same journal

Vitamin C as Cancer Destroyer, Investigating Sulfhydration, and the Variability in CFTR Interactome.

Chemistry & biology·2015
See all related articles

Researchers developed a novel chemical method to isolate and tag phosphorylated peptides. This technique confirmed that microtubule-associated protein 2 (MAP2) has phosphorylation sites similar to Tau, suggesting a shared CDK5 phosphorylation motif.

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Proteomics

Background:

  • Global phosphorylation analysis is crucial for understanding biological systems.
  • Existing methods for isolating phosphorylated peptides can be complex.

Purpose of the Study:

  • To develop and apply a novel chemistry-based method for capturing and tagging phosphoserine/threonine peptides.
  • To analyze the phosphorylation status of microtubule-associated proteins.

Main Methods:

  • A capture-release-tag strategy utilizing liquid beta-elimination and solid-phase Michael addition.
  • Immobilized Michael donors on functionalized resin captured dehydro-peptides.
  • Acid-mediated release and labeling of phosphopeptides with a thiol-reactive tag.

Related Experiment Videos

Main Results:

  • Successfully isolated and tagged complex phospho-Ser/Thr-containing peptides.
  • Analyzed phosphorylation of microtubule-associated proteins, including MAP2.
  • Identified phosphorylation on MAP2 residues homologous to Tau, within a potential CDK5 phosphorylation motif.

Conclusions:

  • The developed chemical method is effective for analyzing phosphorylation events.
  • Findings suggest a conserved CDK5 phosphorylation motif in Tau and MAP2.
  • Corroborates previous findings and provides new insights into protein phosphorylation.