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I Just

Showing results (51-60 of 114) with videos related to

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The Journal of Physiology|October 15, 1996
Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscleB Otto, A Steusloff, I Just, et al.
The Journal of Clinical Investigation|March 1, 1995
The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficileI Just, J Selzer, C von Eichel-Streiber, et al.
FEBS Letters|January 16, 1989
Purification of the 22 kDa protein substrate of botulinum ADP-ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP-binding protein highly homologous to the rho gene productU Braun, B Habermann, I Just, et al.
Infection and Immunity|April 7, 1998
The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxinH Barth, F Hofmann, C Olenik, et al.
European Journal of Biochemistry|November 26, 1990
ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxinS Mauss, C Chaponnier, I Just, et al.
European Journal of Pharmacology|May 12, 1992
ADP-ribosylation of rho proteins is inhibited by melittin, mast cell degranulating peptide and compound 48/80G Koch, B Habermann, C Mohr, et al.
FEBS Letters|October 21, 1991
Interaction of mastoparan with the low molecular mass GTP-binding proteins rho/racG Koch, B Haberman, C Mohr, et al.
European Journal of Biochemistry|January 15, 1989
ADP-ribosylation of actin causes increase in the rate of ATP exchange and inhibition of ATP hydrolysisU Geipel, I Just, B Schering, et al.
Biochemical Pharmacology|April 6, 1993
Enhancement of Clostridium botulinum C3-catalysed ADP-ribosylation of recombinant rhoA by sodium dodecyl sulfateI Just, C Mohr, B Habermann, et al.
The Journal of Biological Chemistry|April 25, 1997
Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxinF Hofmann, C Busch, U Prepens, et al.
Pageof 12

Showing results (51-60 of 114) with videos related to

Sort By:
Pageof 12
The Journal of Physiology|October 15, 1996
Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscleB Otto, A Steusloff, I Just, et al.
The Journal of Clinical Investigation|March 1, 1995
The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficileI Just, J Selzer, C von Eichel-Streiber, et al.
FEBS Letters|January 16, 1989
Purification of the 22 kDa protein substrate of botulinum ADP-ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP-binding protein highly homologous to the rho gene productU Braun, B Habermann, I Just, et al.
Infection and Immunity|April 7, 1998
The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxinH Barth, F Hofmann, C Olenik, et al.
European Journal of Biochemistry|November 26, 1990
ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxinS Mauss, C Chaponnier, I Just, et al.
European Journal of Pharmacology|May 12, 1992
ADP-ribosylation of rho proteins is inhibited by melittin, mast cell degranulating peptide and compound 48/80G Koch, B Habermann, C Mohr, et al.
FEBS Letters|October 21, 1991
Interaction of mastoparan with the low molecular mass GTP-binding proteins rho/racG Koch, B Haberman, C Mohr, et al.
European Journal of Biochemistry|January 15, 1989
ADP-ribosylation of actin causes increase in the rate of ATP exchange and inhibition of ATP hydrolysisU Geipel, I Just, B Schering, et al.
Biochemical Pharmacology|April 6, 1993
Enhancement of Clostridium botulinum C3-catalysed ADP-ribosylation of recombinant rhoA by sodium dodecyl sulfateI Just, C Mohr, B Habermann, et al.
The Journal of Biological Chemistry|April 25, 1997
Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxinF Hofmann, C Busch, U Prepens, et al.
Pageof 12