[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 …

[引用][C] Recognition of RhoA by Clostridium botulinum C3 Exoenzyme

C Wilde, H Genth, K Aktories, I Just - Journal of Biological Chemistry, 2000 - cir.nii.ac.jp

[HTML][HTML] Recognition of RhoA by Clostridium botulinum C3 Exoenzyme

C Wilde, H Genth, K Aktories, I Just - Journal of Biological Chemistry, 2000 - Elsevier
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 …

Recognition of RhoA by Clostridium botulinum C3 exoenzyme.

C Wilde, H Genth, K Aktories, I Just - The Journal of Biological …, 2000 - europepmc.org
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 …

Recognition of RhoA by Clostridium botulinum C3 exoenzyme

C Wilde, H Genth, K Aktories… - The Journal of …, 2000 - pubmed.ncbi.nlm.nih.gov
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 …

[PDF][PDF] Recognition of RhoA by Clostridium botulinum C3 Exoenzyme

C Wilde, H Genth, K Aktories, I Just - 2000 - academia.edu
The C3-like ADP-ribosyltransferases exhibit a very confined substrate specificity compared
with other Rhomodifying bacterial toxins; they selectively modify the RhoA,-B, and-C …

[引用][C] Recognition of RhoA by Clostridium botulinum C3 exoenzyme

C WILDE - J. Biol. Chem., 2000 - cir.nii.ac.jp