Detection and Quantification of ADP-Ribosylated RhoA/B by Monoclonal Antibody
Clostridium botulinum exoenzyme C3 is the prototype of C3-like ADP-ribosyltransferases that modify the GTPases RhoA, B, and C. C3 catalyzes the transfer of an ADP-ribose moiety from the co-substrate nicotinamide adenine dinucleotide (NAD) to asparagine-41 of Rho-GTPases. Although C3 does not possess...
Main Authors: | Astrid Rohrbeck, Viola Fühner, Anke Schröder, Sandra Hagemann, Xuan-Khang Vu, Sarah Berndt, Michael Hust, Andreas Pich, Ingo Just |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2016-04-01
|
Series: | Toxins |
Subjects: | |
Online Access: | http://www.mdpi.com/2072-6651/8/4/100 |
Similar Items
-
General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes
by: Hideaki Tsuge, et al.
Published: (2024-07-01) -
The ADP-Ribosyl-Transferases Diphtheria Toxin-Like (ARTDs) Family: An Overview
by: Maria Di Girolamo, et al.
Published: (2018-05-01) -
Research Progress on Mono-ADP-Ribosyltransferases in Human Cell Biology
by: Yujie Gan, et al.
Published: (2022-05-01) -
Poly(ADP-ribosyl)ation /
by: Burkle, Alexander
Published: (2006) -
PARPs and ADP-Ribosylation in Chronic Inflammation: A Focus on Macrophages
by: Diego V. Santinelli-Pestana, et al.
Published: (2023-07-01)