Lars Björck
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- 2004
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Mark
Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG
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- Contribution to journal › Article
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Mark
Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin
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- Contribution to journal › Article
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Mark
alpha 2-macroglobulin-proteinase complexes protect Streptococcus pyogenes from killing by the antimicrobial peptide LL-37.
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- Contribution to journal › Article
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Mark
Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for igg cleavage due to exosite binding.
(
- Contribution to journal › Article
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Mark
SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1.
(
- Contribution to journal › Article
- 2003
-
Mark
Immunoglobulin Superantigen Protein L Induces IL-4 and IL-13 Secretion from Human Fc varepsilon RI(+) Cells Through Interaction with the kappa Light Chains of IgE.
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- Contribution to journal › Article
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Mark
Contact activation by pathogenic bacteria: a virulence mechanism contributing to the pathophysiology of sepsis.
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- Contribution to journal › Article
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Mark
Elastase-producing Pseudomonas aeruginosa degrade plasma proteins and extracellular products of human skin and fibroblasts, and inhibit fibroblast growth.
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- Contribution to journal › Article
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Mark
Interactions between surface proteins of Streptococcus pyogenes and coagulation factors modulate clotting of human plasma.
(
- Contribution to journal › Article
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Mark
IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes.
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- Contribution to journal › Scientific review