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

Phosphorylation

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...

Phosphorylation

Phosphorylation

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

You might also read

Related Articles

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

Sort by

Same author

Fred Wittinghofer and the GTP/GDP-binding proteins.

Biological chemistry·2026

Same author

Advances on the large-scale bacterial production and stable phosphorylation of Hsc70.

Protein expression and purification·2026

Same author

Lessons from Structural Biology for Understanding Drug Resistance in Gastrointestinal Stromal Tumors (GIST).

Journal of medicinal chemistry·2026

Same author

Targeting KRAS<sup>G13C</sup> with cyclic linker based inhibitors to explore warhead orientation.

Scientific reports·2025

Same author

The functional dynamics of FicD's TPR domain are modulated by the interaction with ATP and BiP.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

Computational Design of Lysine Targeting Covalent Binders Using Rosetta.

Journal of chemical information and modeling·2025

Search research articles

Related Experiment Video

Updated: May 6, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Exploring adenylylation and phosphocholination as post-translational modifications.

Matthias P Müller¹, Michael F Albers, Aymelt Itzen

¹Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund (Germany).

Chembiochem : a European Journal of Chemical Biology

|November 1, 2013

Summary

Pathogenic bacteria use adenylylation and phosphocholination for infections. This review explores using chemical tags and antibodies to find new targets of these modifications in host cells.

Keywords:

adenylylation antibodies bioorganic chemistry mass spectrometry phosphocholination post-translational modifications

More Related Videos

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Related Experiment Videos

Last Updated: May 6, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Area of Science:

Microbiology
Biochemistry
Molecular Biology

Background:

Adenylylation and phosphocholination are key bacterial post-translational modifications during infection.
Understanding these modifications is crucial for developing new anti-infective strategies.

Purpose of the Study:

To review methods for identifying novel substrates of adenylylation and phosphocholination.
To highlight the combined use of chemical handles and antibodies for this purpose.

Main Methods:

Utilizing chemical handles to tag modified proteins.
Employing specific antibodies for immunoprecipitation and detection.
Analyzing modified substrates within infected host cells.

Main Results:

Successful identification of previously unknown substrates for adenylylation and phosphocholination.
Demonstration of the efficacy of combined chemical and antibody approaches.
Insights into bacterial manipulation of host cell processes.

Conclusions:

The combined chemical handle and antibody strategy is effective for discovering new post-translational modification substrates.
This approach advances our understanding of bacterial pathogenesis.
Further research can leverage these methods to target bacterial infections.