Cell Entry of C3 Exoenzyme from Clostridium botulinum
A Rohrbeck, I Just - Uptake and Trafficking of Protein Toxins, 2017 - Springer
Clostridium botulinum C3 is the prototype of C3-like ADP-ribosyltransferases that selectively
ADP-ribosylate the small GTP-binding proteins RhoA/B/C and inhibit their downstream …
ADP-ribosylate the small GTP-binding proteins RhoA/B/C and inhibit their downstream …
Clostridium Botulinum C3 Exoenzyme and C3-Like Transferases
K Aktories, H Barth, I Just - Bacterial Protein Toxins, 2000 - Springer
Clostridium botulinum adenosine diphosphate (ADP)—ribosyltransferase C3 was the first
bacterial exoenzyme/toxin found to act on small guanosine triphosphate (GTP) ases of the …
bacterial exoenzyme/toxin found to act on small guanosine triphosphate (GTP) ases of the …
Clostridium botulinum C3 exoenzyme: Rho-inactivating tool in cell biology and a neurotrophic agent
I Just, SC Huelsenbeck, H Genth - The Open Toxinology …, 2010 - benthamopen.com
C3 exoenzyme from Clostridium botulinum is the prototype of bacterial ADP-
ribosyltransferases, which selectively modifies the Rho isoforms RhoA, RhoB and RhoC by …
ribosyltransferases, which selectively modifies the Rho isoforms RhoA, RhoB and RhoC by …
The Rho-ADP-ribosylating C3 exoenzyme from Clostridium botulinum and related C3-like transferases
C Wilde, K Aktories - Toxicon, 2001 - Elsevier
Various bacterial protein toxins and exoenzymes interfere with target cell functions by
catalyzing posttranslational modification of eukaryoticmaster regulators'. Studies from recent …
catalyzing posttranslational modification of eukaryoticmaster regulators'. Studies from recent …
[HTML][HTML] Uptake of Clostridium botulinum C3 exoenzyme into intact HT22 and J774A. 1 cells
A Rohrbeck, L Von Elsner, S Hagemann, I Just - Toxins, 2015 - mdpi.com
The Clostridium botulinum C3 exoenzyme selectively ADP-ribosylates low molecular weight
GTP-binding proteins RhoA, B and C. This covalent modification inhibits Rho signaling …
GTP-binding proteins RhoA, B and C. This covalent modification inhibits Rho signaling …
[HTML][HTML] Vimentin mediates uptake of C3 exoenzyme
A Rohrbeck, A Schröder, S Hagemann, A Pich… - PLoS …, 2014 - journals.plos.org
Clostridium botulinum C3 exoenzyme (C3) selectively inactivates RhoA/B/C GTPases by
ADP-ribosylation. Based on this substrate specificity C3 is a well-established tool in cell …
ADP-ribosylation. Based on this substrate specificity C3 is a well-established tool in cell …
[HTML][HTML] Detection and quantification of ADP-ribosylated RhoA/B by monoclonal antibody
A Rohrbeck, V Fühner, A Schröder, S Hagemann… - Toxins, 2016 - mdpi.com
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 …
that modify the GTPases RhoA, B, and C. C3 catalyzes the transfer of an ADP-ribose moiety …
[图书][B] Clostridium botulinum C3 exoenzyme and studies on Rho proteins
CD Nobes, A Hall - 1997 - books.google.com
The Rho family of small GTP-binding proteins functions to regulate the assembly of distinct
actin structures in cells; Rho regulates stress fiber assembly, Rac regulates lamellipodia …
actin structures in cells; Rho regulates stress fiber assembly, Rac regulates lamellipodia …
Binding of Clostridium botulinum C3 exoenzyme to intact cells
A Rohrbeck, L von Elsner, S Hagemann… - … Schmiedeberg's archives of …, 2014 - Springer
C3 from Clostridium botulinum (C3) specifically modifies Rho GTPases RhoA, RhoB, and
RhoC by mono-ADP-ribosylation. The confined substrate profile of C3 is the basis for its use …
RhoC by mono-ADP-ribosylation. The confined substrate profile of C3 is the basis for its use …
[HTML][HTML] Recognition of RhoA by Clostridium botulinum C3 exoenzyme
C Wilde, H Genth, K Aktories, I Just - Journal of Biological Chemistry, 2000 - ASBMB
The C3-like ADP-ribosyltransferases exhibit a very confined substrate specificity compared
with other Rho-modifying bacterial toxins; they selectively modify the RhoA,-B, and-C …
with other Rho-modifying bacterial toxins; they selectively modify the RhoA,-B, and-C …