U. von Pawel-Rammingen

发表

Identification and Characterization of IgdE, a Novel IgG-degrading Protease of Streptococcus suis with Unique Specificity for Porcine IgG*

P. Valentin-Weigand, C. Baums, Jana Seele, 2016, The Journal of Biological Chemistry.

Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to enzyme dimerization

Christian Spoerry, U. von Pawel-Rammingen, Reine Vindebro, 2013, FEBS letters.

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

Patrik Engström, U. von Pawel-Rammingen, Jenny Johansson Söderberg, 2008, Infection and Immunity.

IdeS, a Highly Specific Immunoglobulin G (IgG)-Cleaving Enzyme from Streptococcus pyogenes, Is Inhibited by Specific IgG Antibodies Generated during Infection

P. Åkesson, B. Christensson, U. von Pawel-Rammingen, 2006, Infection and Immunity.

Low antibody levels against cell wall-attached proteins of Streptococcus pyogenes predispose for severe invasive disease.

A. Olsén, M. Rasmussen, P. Åkesson, 2004, The Journal of infectious diseases.

SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1.

L. Björck, M. Rasmussen, U. von Pawel-Rammingen, 2004, Microbiology.

The Streptococcal Cysteine Protease SpeB Is Not a Natural Immunoglobulin-Cleaving Enzyme

H. Persson, U. von Pawel-Rammingen, Reine Vindebro, 2013, Infection and Immunity.

IgG Protease Mac/IdeS Is Not Essential for Phagocyte Resistance or Mouse Virulence of M1T1 Group A Streptococcus

V. Nizet, Ericka L. Anderson, Joshua Olson, 2013, mBio.

The Membrane Bound LRR Lipoprotein Slr, and the Cell Wall-Anchored M1 Protein from Streptococcus pyogenes Both Interact with Type I Collagen

M. Mörgelin, M. Collin, A. Olin, 2011, PloS one.

Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae

A. Byström, S. Åström, U. von Pawel-Rammingen, 1992, Molecular and cellular biology.

Identification of a novel host-specific IgG protease in Streptococcus phocae subsp. phocae.

U. Siebert, P. Valentin-Weigand, J. Stott, 2017, Veterinary microbiology.

Identification of a Novel Host-Specific IgM Protease in Streptococcus suis

P. Valentin-Weigand, C. Baums, Alena Singpiel, 2012, Journal of bacteriology.

The human protease inhibitor cystatin C is an activating cofactor for the streptococcal cysteine protease IdeS.

M. Abrahamson, B. Vincents, U. von Pawel-Rammingen, 2008, Chemistry & biology.

Identification of the TRM2 gene encoding the tRNA(m5U54)methyltransferase of Saccharomyces cerevisiae.

A. Byström, J. Johansson, M E Nordlund, 2000, RNA.

3-Aminopiperidine-Based Peptide Analogues as the First Selective Noncovalent Inhibitors of the Bacterial Cysteine Protease IdeS

K. Luthman, J. Kihlberg, T. Fex, 2012, Journal of medicinal chemistry.

The immunoglobulin M-degrading enzyme of Streptococcus suis, IdeSsuis, is a highly protective antigen against serotype 2.

A. Beineke, P. Valentin-Weigand, C. Baums, 2015, Vaccine.

IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G

L. Björck, B. Johansson, U. von Pawel-Rammingen, 2002, The EMBO journal.

Multiple molecular determinants for retrotransposition in a primer tRNA

D. Voytas, J. Boeke, A. Byström, 1995, Molecular and cellular biology.

The yeast initiator tRNAMet can act as an elongator tRNA(Met) in vivo.

A. Byström, S. Åström, U. von Pawel-Rammingen, 1993, Journal of molecular biology.

Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.

R. Huber, L. Björck, P. Sondermann, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding.

L. Björck, M. Abrahamson, B. Vincents, 2004, Biochemistry.

Naturally Occurring IgG Antibodies Provide Innate Protection against Vibrio cholerae Bacteremia by Recognition of the Outer Membrane Protein U

Kyaw Min Aung, K. Riesbeck, S. Wai, 2016, Journal of Innate Immunity.

Proteolytic processing of the streptococcal IgG endopeptidase IdeS modulates the functional properties of the enzyme and results in reduced immunorecognition.

B. Johansson, H. Persson, U. von Pawel-Rammingen, 2015, Molecular immunology.

Streptococcal IdeS and Its Impact on Immune Response and Inflammation

U. von Pawel-Rammingen, 2012, Journal of Innate Immunity.

Novel IgG-Degrading Enzymes of the IgdE Protease Family Link Substrate Specificity to Host Tropism of Streptococcus Species

J. Woof, Melanie J. Lewis, Christian Spoerry, 2016, PloS one.

GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure

M. Telepnev, K. Aktories, H. Wolf‐Watz, 2000, Molecular microbiology.

IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes.

L. Björck, U. von Pawel-Rammingen, 2003, Current opinion in microbiology.

The immunoglobulin M-degrading enzyme of Streptococcus suis, IdeSsuis, is involved in complement evasion

A. Beineke, P. Valentin-Weigand, C. Baums, 2015, Veterinary Research.

The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytes.

U. von Pawel-Rammingen, Jenny Johansson Söderberg, 2008, Molecular immunology.

The protein expression of Streptococcus pyogenes is significantly influenced by human plasma.

L. Björck, B. Johansson, F. Levander, 2005, Journal of proteome research.

The immunoglobulin M-degrading enzyme of Streptococcus suis, IdeSsuis, is a highly protective antigen against serotype 2.

A. Beineke, P. Valentin-Weigand, C. Baums, 2015, Vaccine.

Proteolytic processing of the streptococcal IgG endopeptidase IdeS modulates the functional properties of the enzyme and results in reduced immunorecognition.

B. Johansson, H. Persson, U. von Pawel-Rammingen, 2015, Molecular immunology.