Analysis of Expression of a Cytosolic Enzyme on the Surface of Streptococcus pyogenes
- 30 November 2000
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 278 (3) , 826-832
- https://doi.org/10.1006/bbrc.2000.3884
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Interaction of Group A Streptococci with Human Plasmin(ogen) under Physiological ConditionsMethods, 2000
- Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of the plr gene does not reduce plasmin binding to group A streptococciMicrobiology, 1998
- α-Enolase, a Novel Strong Plasmin(ogen) Binding Protein on the Surface of Pathogenic StreptococciJournal of Biological Chemistry, 1998
- The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenaseMicrobiology, 1996
- Cloning and molecular characterization of two genes encoding adhesion proteins involved in Trichomonas vaginalis cytoadherenceMolecular Microbiology, 1995
- The Role of an Enolase‐Related Molecule in Plasminogen Binding to CellsEuropean Journal of Biochemistry, 1995
- Capturing host plasmin(ogen): a common mechanism for invasive pathogens?Trends in Microbiology, 1994
- A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity.The Journal of Experimental Medicine, 1992
- Conservation of a hexapeptide sequence in the anchor region of surface proteins from Gram‐positive cocciMolecular Microbiology, 1990
- The major parasite surface antigen associated with human resistance to schistosomiasis is a 37-kD glyceraldehyde-3P-dehydrogenase.The Journal of Experimental Medicine, 1989