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Journal Abstract Search


213 related items for PubMed ID: 12615219

  • 1. IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes.
    von Pawel-Rammingen U, Björck L.
    Curr Opin Microbiol; 2003 Feb; 6(1):50-5. PubMed ID: 12615219
    [Abstract] [Full Text] [Related]

  • 2. IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G.
    von Pawel-Rammingen U, Johansson BP, Björck L.
    EMBO J; 2002 Apr 02; 21(7):1607-15. PubMed ID: 11927545
    [Abstract] [Full Text] [Related]

  • 3. Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins.
    Collin M, Olsén A.
    Infect Immun; 2001 Nov 02; 69(11):7187-9. PubMed ID: 11598100
    [Abstract] [Full Text] [Related]

  • 4. Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.
    Wenig K, Chatwell L, von Pawel-Rammingen U, Björck L, Huber R, Sondermann P.
    Proc Natl Acad Sci U S A; 2004 Dec 14; 101(50):17371-6. PubMed ID: 15574492
    [Abstract] [Full Text] [Related]

  • 5. IdeS, a secreted proteinase of Streptococcus pyogenes, is bound to a nuclease at the bacterial surface where it inactivates opsonizing IgG antibodies.
    Frick IM, Happonen L, Wrighton S, Nordenfelt P, Björck L.
    J Biol Chem; 2023 Nov 14; 299(11):105345. PubMed ID: 37838172
    [Abstract] [Full Text] [Related]

  • 6. EndoS and SpeB from Streptococcus pyogenes inhibit immunoglobulin-mediated opsonophagocytosis.
    Collin M, Svensson MD, Sjöholm AG, Jensenius JC, Sjöbring U, Olsén A.
    Infect Immun; 2002 Dec 14; 70(12):6646-51. PubMed ID: 12438337
    [Abstract] [Full Text] [Related]

  • 7. Cysteine proteinase from Streptococcus pyogenes enables evasion of innate immunity via degradation of complement factors.
    Honda-Ogawa M, Ogawa T, Terao Y, Sumitomo T, Nakata M, Ikebe K, Maeda Y, Kawabata S.
    J Biol Chem; 2013 May 31; 288(22):15854-64. PubMed ID: 23589297
    [Abstract] [Full Text] [Related]

  • 8. EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity.
    Allhorn M, Olsén A, Collin M.
    BMC Microbiol; 2008 Jan 08; 8():3. PubMed ID: 18182097
    [Abstract] [Full Text] [Related]

  • 9. Endopeptidase PepO Regulates the SpeB Cysteine Protease and Is Essential for the Virulence of Invasive M1T1 Streptococcus pyogenes.
    Brouwer S, Cork AJ, Ong CY, Barnett TC, West NP, McIver KS, Walker MJ.
    J Bacteriol; 2018 Apr 15; 200(8):. PubMed ID: 29378883
    [Abstract] [Full Text] [Related]

  • 10. The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytes.
    Söderberg JJ, von Pawel-Rammingen U.
    Mol Immunol; 2008 Jul 15; 45(12):3347-53. PubMed ID: 18533265
    [Abstract] [Full Text] [Related]

  • 11. Proteolytic processing of the streptococcal IgG endopeptidase IdeS modulates the functional properties of the enzyme and results in reduced immunorecognition.
    Persson H, Söderberg JJ, Vindebro R, Johansson BP, von Pawel-Rammingen U.
    Mol Immunol; 2015 Dec 15; 68(2 Pt A):176-84. PubMed ID: 26343448
    [Abstract] [Full Text] [Related]

  • 12. The streptococcal cysteine protease SpeB is not a natural immunoglobulin-cleaving enzyme.
    Persson H, Vindebro R, von Pawel-Rammingen U.
    Infect Immun; 2013 Jun 15; 81(6):2236-41. PubMed ID: 23569114
    [Abstract] [Full Text] [Related]

  • 13. Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding.
    Vincents B, von Pawel-Rammingen U, Björck L, Abrahamson M.
    Biochemistry; 2004 Dec 14; 43(49):15540-9. PubMed ID: 15581366
    [Abstract] [Full Text] [Related]

  • 14. Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins.
    Berge A, Björck L.
    J Biol Chem; 1995 Apr 28; 270(17):9862-7. PubMed ID: 7730368
    [Abstract] [Full Text] [Related]

  • 15. The deficient cleavage of M protein-bound IgG by IdeS: insight into the escape of Streptococcus pyogenes from antibody-mediated immunity.
    Su YF, Chuang WJ, Wang SM, Chen WY, Chiang-Ni C, Lin YS, Wu JJ, Liu CC.
    Mol Immunol; 2011 Oct 28; 49(1-2):134-42. PubMed ID: 21925735
    [Abstract] [Full Text] [Related]

  • 16. SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1.
    Nyberg P, Rasmussen M, von Pawel-Rammingen U, Björck L.
    Microbiology (Reading); 2004 May 28; 150(Pt 5):1559-1569. PubMed ID: 15133117
    [Abstract] [Full Text] [Related]

  • 17. IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection.
    Akesson P, Moritz L, Truedsson M, Christensson B, von Pawel-Rammingen U.
    Infect Immun; 2006 Jan 28; 74(1):497-503. PubMed ID: 16369006
    [Abstract] [Full Text] [Related]

  • 18. Immunoglobulin cleavage by the streptococcal cysteine protease IdeS can be detected using protein G capture and mass spectrometry.
    Hess JL, Porsch EA, Shertz CA, Boyle MD.
    J Microbiol Methods; 2007 Aug 28; 70(2):284-91. PubMed ID: 17543400
    [Abstract] [Full Text] [Related]

  • 19. An Irreversible Inhibitor to Probe the Role of Streptococcus pyogenes Cysteine Protease SpeB in Evasion of Host Complement Defenses.
    Woehl JL, Kitamura S, Dillon N, Han Z, Edgar LJ, Nizet V, Wolan DW.
    ACS Chem Biol; 2020 Aug 21; 15(8):2060-2069. PubMed ID: 32662975
    [Abstract] [Full Text] [Related]

  • 20. The SpeB virulence factor of Streptococcus pyogenes, a multifunctional secreted and cell surface molecule with strepadhesin, laminin-binding and cysteine protease activity.
    Hytönen J, Haataja S, Gerlach D, Podbielski A, Finne J.
    Mol Microbiol; 2001 Jan 21; 39(2):512-9. PubMed ID: 11136470
    [Abstract] [Full Text] [Related]


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