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Journal of Innate Immunity
|
January 18, 2012
Streptococcal IdeS and its impact on immune response and inflammation
Ulrich von Pawel-Rammingen
Current Opinion in Microbiology
|
March 5, 2003
IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes
Ulrich 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 leucocytes
Jenny Johansson Söderberg, Ulrich von Pawel-Rammingen
Infection and Immunity
|
April 10, 2013
The streptococcal cysteine protease SpeB is not a natural immunoglobulin-cleaving enzyme
Helena 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 dimerization
Reine 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 strains
Jenny 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 G
Ulrich 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 F1
Patrik 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 binding
Bjarne 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 IdeS
Bjarne Vincents, Reine Vindebro, Magnus Abrahamson, et al.
Page
of 3
Search research articles
Search
Showing results (1-10 of 28) with videos related to
Sort By:
Page
of 3
Journal of Innate Immunity
|
January 18, 2012
Streptococcal IdeS and its impact on immune response and inflammation
Ulrich von Pawel-Rammingen
Current Opinion in Microbiology
|
March 5, 2003
IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes
Ulrich 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 leucocytes
Jenny Johansson Söderberg, Ulrich von Pawel-Rammingen
Infection and Immunity
|
April 10, 2013
The streptococcal cysteine protease SpeB is not a natural immunoglobulin-cleaving enzyme
Helena 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 dimerization
Reine 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 strains
Jenny 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 G
Ulrich 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 F1
Patrik 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 binding
Bjarne 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 IdeS
Bjarne Vincents, Reine Vindebro, Magnus Abrahamson, et al.
Page
of 3