A PROTEOLYTIC ENZYME PRODUCED BY GROUP A STREPTOCOCCI WITH SPECIAL REFERENCE TO ITS EFFECT ON THE TYPE-SPECIFIC M ANTIGEN.
about
Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine proteaseA New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain AEndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgGIdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G.Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes.alpha2-Macroglobulin-proteinase complexes protect Streptococcus pyogenes from killing by the antimicrobial peptide LL-37.Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities.Genetic inactivation of an extracellular cysteine protease (SpeB) expressed by Streptococcus pyogenes decreases resistance to phagocytosis and dissemination to organsEffect of group A streptococcal cysteine protease on invasion of epithelial cells.The M protein is dispensable for maturation of streptococcal cysteine protease SpeB.The rgg gene of Streptococcus pyogenes NZ131 positively influences extracellular SPE B production.Absence of SpeB production in virulent large capsular forms of group A streptococcal strain 64Streptococcal erythrogenic toxin B abrogates fibronectin-dependent internalization of Streptococcus pyogenes by cultured mammalian cellsReplacement of histidine 340 with alanine inactivates the group A Streptococcus extracellular cysteine protease virulence factorFrom transcription to activation: how group A streptococcus, the flesh-eating pathogen, regulates SpeB cysteine protease production.Cysteine proteinase SpeB from Streptococcus pyogenes - a potent modifier of immunologically important host and bacterial proteins.Antimicrobial Peptide Resistance Mechanisms of Gram-Positive Bacteria.Proteolysis and its regulation at the surface of Streptococcus pyogenes.Extracellular enzymes with immunomodulating activities: variations on a theme in Streptococcus pyogenesImmunoglobulin cleavage by the streptococcal cysteine protease IdeS can be detected using protein G capture and mass spectrometry.An M-associated protein antigen (MAP) of group A streptococci.The use of precipitin analysis in agar for the study of human streptococcal infections. III. The purification of some of the antigens detected by these methodsGroup A streptococcal bacteriocin. Production, purification, and mode of action.Biochemical and biological properties of the binding of human fibrinogen to M protein in group A streptococciHighly efficient recombinant production and purification of streptococcal cysteine protease streptopain with increased enzymatic activity.Synthesis of M protein by group A hemolytic streptococci in completely synthetic media during steady-state growth.Laboratory diagnosis of streptococcal infections.Antistreptolysin-O: its interaction with streptolysin-O, its titration and a comparison of some standard preparations.Protease production by clinical isolates of type III group B streptococci.Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.Streptococcal IdeS and its impact on immune response and inflammation.Streptococcal DNase B is immunologically identical to superantigen SpeF but involves separate domains.Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins.Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodesGenerating and Purifying Fab Fragments from Human and Mouse IgG Using the Bacterial Enzymes IdeS, SpeB and Kgp.Streptococcal cysteine proteinase releases kinins: a virulence mechanism.Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins.Sequence variability is correlated with weak immunogenicity in Streptococcus pyogenes M protein.Catalytic site cysteines of thiol enzyme: sulfurtransferases.Myocardial necrosis produced in animals by means of crystalline streptococcal proteinase.
P2860
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P2860
A PROTEOLYTIC ENZYME PRODUCED BY GROUP A STREPTOCOCCI WITH SPECIAL REFERENCE TO ITS EFFECT ON THE TYPE-SPECIFIC M ANTIGEN.
description
1945 nî lūn-bûn
@nan
1945 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1945 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1945年の論文
@ja
1945年論文
@yue
1945年論文
@zh-hant
1945年論文
@zh-hk
1945年論文
@zh-mo
1945年論文
@zh-tw
1945年论文
@wuu
name
A PROTEOLYTIC ENZYME PRODUCED ...... N THE TYPE-SPECIFIC M ANTIGEN.
@ast
A PROTEOLYTIC ENZYME PRODUCED ...... N THE TYPE-SPECIFIC M ANTIGEN.
@en
type
label
A PROTEOLYTIC ENZYME PRODUCED ...... N THE TYPE-SPECIFIC M ANTIGEN.
@ast
A PROTEOLYTIC ENZYME PRODUCED ...... N THE TYPE-SPECIFIC M ANTIGEN.
@en
prefLabel
A PROTEOLYTIC ENZYME PRODUCED ...... N THE TYPE-SPECIFIC M ANTIGEN.
@ast
A PROTEOLYTIC ENZYME PRODUCED ...... N THE TYPE-SPECIFIC M ANTIGEN.
@en
P2860
P356
P1476
A PROTEOLYTIC ENZYME PRODUCED ...... N THE TYPE-SPECIFIC M ANTIGEN.
@en
P2093
Elliott SD
P2860
P304
P356
10.1084/JEM.81.6.573
P407
P577
1945-06-01T00:00:00Z