The Rho ADP-ribosylating C3 exoenzyme (C3bot) is a bacterial protein toxin devoid of a cell-
binding or-translocation domain. Nevertheless, C3 can efficiently enter intact cells, including …

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 …

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 …

Clostridium botulinum C3 exoenzyme inactivates the small GTP-binding protein family Rho
by ADP-ribosylating asparagine 41, which depolymerizes the actin cytoskeleton. C3 thus …

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 …

C3 exoenzyme from Clostridium limosum, specifically ADP‐ribosylates and inactivates Rho
GTPases, but not or much less than Rac and Cdc42. To bypass the poor cell accessibility of …

The Clostridium botulinum C3 exoenzyme selectively ADP-ribosylates low molecular weight
GTP-binding proteins RhoA, B and C. This covalent modification inhibits Rho signaling …

C3-like ADP-ribosyltransferases represent an expanding family of related exoenzymes,
which are produced by Clostridia and various Staphylococcus aureus strains. Here we …

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 …

The family of C3-like exoenzymes comprises seven bacterial ADP-ribosyltransferases of
different origin. The common hallmark of these exoenzymes is the selective N-ADP …