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Ulrich von Pawel-Rammingen

Showing results (1-10 of 28) with videos related to

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Journal of Innate Immunity|January 18, 2012
Streptococcal IdeS and its impact on immune response and inflammationUlrich von Pawel-Rammingen
Current Opinion in Microbiology|March 5, 2003
IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenesUlrich von Pawel-Rammingen, Lars Björck
Molecular Immunology|June 6, 2008
The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytesJenny Johansson Söderberg, Ulrich von Pawel-Rammingen
Infection and Immunity|April 10, 2013
The streptococcal cysteine protease SpeB is not a natural immunoglobulin-cleaving enzymeHelena Persson, Reine Vindebro, Ulrich von Pawel-Rammingen
FEBS Letters|May 14, 2013
Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to enzyme dimerizationReine Vindebro, Christian Spoerry, Ulrich von Pawel-Rammingen
Infection and Immunity|March 12, 2008
The intrinsic immunoglobulin g endopeptidase activity of streptococcal Mac-2 proteins implies a unique role for the enzymatically impaired Mac-2 protein of M28 serotype strainsJenny Johansson Söderberg, Patrik Engström, Ulrich von Pawel-Rammingen
The EMBO Journal|April 3, 2002
IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin GUlrich von Pawel-Rammingen, Björn P Johansson, Lars Björck
Microbiology (Reading, England)|May 11, 2004
SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1Patrik Nyberg, Magnus Rasmussen, Ulrich von Pawel-Rammingen, et al.
Biochemistry|December 8, 2004
Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite bindingBjarne Vincents, Ulrich von Pawel-Rammingen, Lars Björck, et al.
Chemistry & Biology|September 23, 2008
The human protease inhibitor cystatin C is an activating cofactor for the streptococcal cysteine protease IdeSBjarne Vincents, Reine Vindebro, Magnus Abrahamson, et al.
Pageof 3

Showing results (1-10 of 28) with videos related to

Sort By:
Pageof 3
Journal of Innate Immunity|January 18, 2012
Streptococcal IdeS and its impact on immune response and inflammationUlrich von Pawel-Rammingen
Current Opinion in Microbiology|March 5, 2003
IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenesUlrich von Pawel-Rammingen, Lars Björck
Molecular Immunology|June 6, 2008
The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytesJenny Johansson Söderberg, Ulrich von Pawel-Rammingen
Infection and Immunity|April 10, 2013
The streptococcal cysteine protease SpeB is not a natural immunoglobulin-cleaving enzymeHelena Persson, Reine Vindebro, Ulrich von Pawel-Rammingen
FEBS Letters|May 14, 2013
Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to enzyme dimerizationReine Vindebro, Christian Spoerry, Ulrich von Pawel-Rammingen
Infection and Immunity|March 12, 2008
The intrinsic immunoglobulin g endopeptidase activity of streptococcal Mac-2 proteins implies a unique role for the enzymatically impaired Mac-2 protein of M28 serotype strainsJenny Johansson Söderberg, Patrik Engström, Ulrich von Pawel-Rammingen
The EMBO Journal|April 3, 2002
IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin GUlrich von Pawel-Rammingen, Björn P Johansson, Lars Björck
Microbiology (Reading, England)|May 11, 2004
SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1Patrik Nyberg, Magnus Rasmussen, Ulrich von Pawel-Rammingen, et al.
Biochemistry|December 8, 2004
Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite bindingBjarne Vincents, Ulrich von Pawel-Rammingen, Lars Björck, et al.
Chemistry & Biology|September 23, 2008
The human protease inhibitor cystatin C is an activating cofactor for the streptococcal cysteine protease IdeSBjarne Vincents, Reine Vindebro, Magnus Abrahamson, et al.
Pageof 3