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

Rho-modifying C3-like ADP-ribosyltransferases.

K Aktories1, C Wilde, M Vogelsgesang

  • 1Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University Freiburg, Otto-Krayer-Haus, Albertstr. 25, Freiburg, Germany. Klaus.Aktories@pharmakol.uni-freiburg.de.

Reviews of Physiology, Biochemistry and Pharmacology
|September 17, 2004
PubMed
Summary

C3-like exoenzymes are bacterial enzymes that modify Rho GTPases. New research reveals the functional consequences of this modification are more complex than previously understood.

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

Effect on compression of lowering the design adiabat in the SQ-n campaign.

Physical review. E·2025
Same author

First Demonstration of Improved Fusion Yield with Increased Compression through Reduced Adiabat in Inertial Confinement Fusion Experiments at the National Ignition Facility.

Physical review letters·2025
Same author

Optically multiplexed neutron time-of-flight technique for inertial confinement fusion.

The Review of scientific instruments·2024
Same author

Spot size measurement of a deuterium-tritium dense plasma focus using neutron radiography.

The Review of scientific instruments·2024
Same author

Observations and properties of the first laboratory fusion experiment to exceed a target gain of unity.

Physical review. E·2024
Same author

Dynamics and Power Balance of Near Unity Target Gain Inertial Confinement Fusion Implosions.

Physical review letters·2023

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • C3-like exoenzymes are a family of bacterial ADP-ribosyltransferases.
  • These enzymes selectively modify RhoA, B, and C GTPases at asparagine-41.
  • Available crystal structures offer insights into exoenzyme structure-function relationships.

Purpose of the Study:

  • To review the fundamental properties of C3 exoenzymes.
  • To present and discuss recent findings on the functional consequences of C3-induced ADP-ribosylation.
  • To explore the complexity of Rho GTPase inhibition by C3 exoenzymes.

Main Methods:

  • Review of existing literature and structural data.
  • Analysis of recent experimental findings on C3 exoenzyme activity.

Related Experiment Videos

  • Synthesis of information regarding Rho GTPase function and inhibition.

    • Main Results:

    • C3 exoenzymes inhibit Rho GTPase functions via ADP-ribosylation.
    • The functional outcomes of C3-induced ADP-ribosylation are more intricate than initially presumed.
    • Structural information aids in understanding enzyme-substrate interactions.

    Conclusions:

    • C3 exoenzymes are valuable pharmacological tools for studying Rho GTPase biology.
    • Emerging evidence highlights a more nuanced understanding of C3 exoenzyme mechanisms and effects.
    • Further research is warranted to fully elucidate the complex functional consequences.