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Journal Abstract Search
329 related items for PubMed ID: 10336419
1. Protein GRAB of streptococcus pyogenes regulates proteolysis at the bacterial surface by binding alpha2-macroglobulin. Rasmussen M, Müller HP, Björck L. J Biol Chem; 1999 May 28; 274(22):15336-44. PubMed ID: 10336419 [Abstract] [Full Text] [Related]
2. Binding of alpha2-macroglobulin to GRAB (Protein G-related alpha2-macroglobulin-binding protein), an important virulence factor of group A streptococci, is mediated by two charged motifs in the DeltaA region. Godehardt AW, Hammerschmidt S, Frank R, Chhatwal GS. Biochem J; 2004 Aug 01; 381(Pt 3):877-85. PubMed ID: 15113281 [Abstract] [Full Text] [Related]
3. Upregulation of capsule enables Streptococcus pyogenes to evade immune recognition by antigen-specific antibodies directed to the G-related alpha2-macroglobulin-binding protein GRAB located on the bacterial surface. Dinkla K, Sastalla I, Godehardt AW, Janze N, Chhatwal GS, Rohde M, Medina E. Microbes Infect; 2007 Jul 01; 9(8):922-31. PubMed ID: 17544803 [Abstract] [Full Text] [Related]
4. Contribution of protein G-related alpha2-macroglobulin-binding protein to bacterial virulence in a mouse skin model of group A streptococcal infection. Toppel AW, Rasmussen M, Rohde M, Medina E, Chhatwal GS. J Infect Dis; 2003 Jun 01; 187(11):1694-703. PubMed ID: 12751026 [Abstract] [Full Text] [Related]
5. Identification and characterization of a novel fibronectin-binding protein on the surface of group A streptococci. Rocha CL, Fischetti VA. Infect Immun; 1999 Jun 01; 67(6):2720-8. PubMed ID: 10338474 [Abstract] [Full Text] [Related]
12. Application of immunoproteomics to analysis of post-translational processing of the antiphagocytic M protein of Streptococcus. Romer TG, Boyle MD. Proteomics; 2003 Jan 15; 3(1):29-35. PubMed ID: 12548631 [Abstract] [Full Text] [Related]
13. Virulent aggregates of Streptococcus pyogenes are generated by homophilic protein-protein interactions. Frick IM, Mörgelin M, Björck L. Mol Microbiol; 2000 Sep 15; 37(5):1232-47. PubMed ID: 10972839 [Abstract] [Full Text] [Related]