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

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 proteomics...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

You might also read

Related Articles

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

Sort by
Same author

Paracrine signals from HIV-1-infected immune cells reprogram cervical cancer pathways.

iScience·2026
Same author

A multi-omics study reveals pathway-level insights and predictive biomarkers in pediatric TB.

Clinical proteomics·2026
Same author

Rapid Peptide Mapping of Monoclonal Antibodies with Direct Infusion Mass Spectrometry.

bioRxiv : the preprint server for biology·2026
Same author

Coronavirus protein interaction mapping in bat and human cells reveals network rewiring governing immune evasion and zoonotic potential.

Cell host & microbe·2026
Same author

Translation-dependent degradation of cas12 mRNA triggered by an anti-CRISPR.

Nature·2026
Same author

Multi-omic phenotyping of MAPT V337M neurons reveals early changes in axonogenesis and tau phosphorylation.

NPJ dementia·2026
Same journal

Lipid Metabolic Labeling to Study Site- and Lipid-Specific Long-Chain <i>S</i>-Acylation Dynamics.

ACS chemical biology·2026
Same journal

Inositol Thiophosphates as Inhibitors of Mammalian, Plant, and Fungal Phytases.

ACS chemical biology·2026
Same journal

Synthesis and Characterization of the Spectroscopic and Imaging Utilities of Two Indole-Based Cyan Fluorescent Nucleoside Analogues.

ACS chemical biology·2026
Same journal

Indole Ring Expansion and Rearrangement-Enabled Quinoline Scaffold Formation in the Biosynthesis of the Antitumor Monoterpene Indole Alkaloid Camptothecin.

ACS chemical biology·2026
Same journal

Intracellular Delivery of Peptides and Proteins with an Engineered Membrane Translocation Domain.

ACS chemical biology·2026
Same journal

Development of Next-Generation Fluoroacetamidine-Containing Activity-Based Probes for the Selective Labeling of the Protein Arginine Deiminases (PADs).

ACS chemical biology·2026
See all related articles

Related Experiment Video

Updated: Jun 17, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
12:23

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

Phosphoproteomics for the masses.

Paul A Grimsrud1, Danielle L Swaney, Craig D Wenger

  • 1Department of Chemistry,University of Wisconsin-Madison, Madison, WI 53706, USA.

ACS Chemical Biology
|January 6, 2010
PubMed
Summary
This summary is machine-generated.

Advancements in mass spectrometry enable large-scale identification of protein phosphorylation sites. Translating this data into biological insights remains a key challenge for researchers.

More Related Videos

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Related Experiment Videos

Last Updated: Jun 17, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
12:23

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

  • Biochemistry
  • Cellular Biology
  • Proteomics

Background:

  • Protein phosphorylation is a critical cellular signaling mechanism.
  • Mass spectrometry technology has rapidly advanced for biological research.
  • High-throughput analysis of phosphorylation is now feasible.

Purpose of the Study:

  • To provide an overview of advancements in mass spectrometry for studying protein phosphorylation.
  • To discuss current applications of this technology.
  • To highlight future challenges in the field.

Main Methods:

  • Large-scale identification and quantitation of in vivo phosphorylation sites.
  • Improvements in sample preparation, instrumentation, and quantitative methodology.
  • Application of informatics for data analysis.

Main Results:

  • Identification and quantification of 10,000-20,000 phosphorylation sites within weeks.
  • Unprecedented levels of detail in mapping cellular signaling pathways.
  • Demonstration of the technology's capacity for comprehensive phosphoproteomic analysis.

Conclusions:

  • Mass spectrometry has revolutionized the study of protein phosphorylation.
  • The challenge lies in effectively translating vast datasets into biological knowledge.
  • Future efforts should focus on developing robust analytical frameworks for phosphoproteomic data.