ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility
- 31 October 1991
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 180 (2), 615-622
- https://doi.org/10.1016/s0006-291x(05)81110-6
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Isoprenylation of the low molecular mass GTP-binding proteins rac 1 and rac 2: Possible role in membrane localizationBiochemical and Biophysical Research Communications, 1990
- Activation of superoxide radical anion generating oxidase of bovine neutrophils in a cell-free system. Interaction of a cytosolic factor with the plasma membrane and control by G nucleotidesBiochemistry, 1989
- Multiple chromatographic forms of the formylpeptide chemoattractant receptor and their relationship to GTP-binding proteinsBiochemical and Biophysical Research Communications, 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 productFEBS Letters, 1989
- The rho gene product expressed in E. Coli is a substrate of botulinum ADP-ribosyltransferase C3Biochemical and Biophysical Research Communications, 1989
- The respiratory burst of bovine neutrophilisEuropean Journal of Biochemistry, 1985
- A novel ras-related gene familyCell, 1985
- Examination of the oxidase function of the b-type cytochrome in human polymorphonuclear leucocytesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1984
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973