Ulrich von Pawel-Rammingen

Contact

ulrich.von.pawel-rammingen@umu.se

+46 90 785 25 23

Works at

Affiliated as other position at Department of Molecular Biology Units: Research group Ulrich von Pawel-Rammingen

6K och 6L, Sjukhusområdet Umeå universitet, 901 87 Umeå

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

Veterinary Microbiology, Elsevier 2017, Vol. 201 : 42-48

Rungelrath, Viktoria; Wohlsein, Jan Christian; Siebert, Ursula; et al.

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

Journal of Innate Immunity, Vol. 8, (3) : 269-283

Aung, Kyaw Min; Sjöström, Annika E; von Pawel-Rammingen, Ulrich; et al.

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

PLOS ONE, Vol. 11, (10)

Spoerry, Christian; Hessle, Pontus; Lewis, Melanie J; et al.

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

Journal of Biological Chemistry, Vol. 291, (15) : 7915-7925

Spoerry, Christian; Seele, Jana; Valentin-Weigand, Peter; et al.

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

Molecular Immunology, Elsevier 2015, Vol. 68, (2) : 176-184

Persson, Helena; Johansson Söderberg, Jenny; Vindebro, Reine; et al.

The immunoglobulin M-degrading enzyme of Streptococcus suis, Ide(Ssuis), is involved in complement evasion

Veterinary research (Print), Vol. 46

Seele, Jana; Beineke, Andreas; Hillermann, Lena-Maria; et al.

The immunoglobulin M-degrading enzyme of Streptococcus suis, Ide(Ssuis), is a highly protective antigen against serotype 2

Vaccine, Vol. 33, (19) : 2207-2212

Seele, Jana; Hillermann, Lena-Maria; Beineke, Andreas; et al.

IgG protease Mac/IdeS is not essential for phagocyte resistance or mouse virulence of M1T1 group A Streptococcus

mBio, Vol. 4, (4) : e00499-e00513

Okumura, Cheryl; Anderson, Ericka L; Döhrmann, Simon; et al.

The streptococcal cysteine protease SpeB is not a natural immunoglobulin-cleaving enzyme

Infection and Immunity, Vol. 81, (6) : 2236-2241

Persson, Helena; Vindebro, Reine; von Pawel-Rammingen, Ulrich

Identification of a novel host-specific IgM protease in Streptococcus suis

International Journal of Medical Microbiology, Elsevier 2013, Vol. 303, (Suppl. 1, MPP35) : 58-58

Seele, J.; Singpiel, A.; Spoerry, Christian; et al.

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

Journal of Bacteriology, Washington: American society of microbiology 2013, Vol. 195, (5) : 930-940

Seele, Jana; Singpiel, Alena; Spoerry, Christian; et al.

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

FEBS Letters, Elsevier 2013, Vol. 587, (12) : 1818-1822

Vindebro, Reine; Spoerry, Christian; von Pawel-Rammingen, Ulrich

IdeS Peptidase

Handbook of proteolytic enzymes, Academic Press 2013 : 2175-2178

von Pawel-Rammingen, Ulrich

3-aminopiperidine-based peptide analogues as the first selective noncovalent inhibitors of the bacterial cysteine protease IdeS

Journal of Medicinal Chemistry, Vol. 55, (6) : 2549-2560

Berggren, Kristina; Vindebro, Reine; Bergström, Claes; et al.

Characterization of SPINK9, a KLK5-specific inhibitor expressed in palmo-plantar epidermis

Biological chemistry (Print), Walter de Gruyter 2012, Vol. 393, (5) : 369-377

Brännström, Kristoffer; Öhman, Anders; von Pawel-Rammingen, Ulrich; et al.

Streptococcal IdeS and Its Impact on Immune Response and Inflammation

JOURNAL OF INNATE IMMUNITY, Vol. 4, (2) : 132-140

von Pawel-Rammingen, Ulrich

The membrane bound LRR lipoprotein Slr, and the cell wall-anchored M1 protein from Streptococcus pyogenes both interact with type I collagen.

PloS one, Public Library of Science 2011, Vol. 6, (5) : e20345-

Bober, Marta; Mörgelin, Matthias; Olin, Anders I; et al.

Cleavage of IgG(1) and IgG(3) by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis

The FASEB Journal, Bethesda, Md.: Federation of American Societies for Experimental Biology 2011, Vol. 25, (10) : 3741-3750

Vincents, Bjarne; Guentsch, Arndt; Kostolowska, Dominika; et al.

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

Infection and Immunity, Vol. 76, (5) : 2183-2188

Söderberg, Jenny Johansson; Engström, Patrik; von Pawel-Rammingen, Ulrich

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

Molecular Immunology, Vol. 45, (12) : 3347-3353

Söderberg, Jenny Johansson; von Pawel-Rammingen, Ulrich

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

Chemistry and Biology, Vol. 15, (9) : 960-968

Vincents, Bjarne; Vindebro, Reine; Abrahamson, Magnus; et al.

IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection

Infection and Immunity, American Society for Microbiology 2006, Vol. 74, (1) : 497-503

Åkesson, Per; Moritz, Linnea; Truedsson, Mikael; et al.

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

Journal of Proteome Research, Washington: American Chemical Society (ACS) 2005, Vol. 4, (6) : 2302-2311

Johansson, Björn P; Levander, Fredrik; von Pawel-Rammingen, Ulrich; et al.

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

Biochemistry, Vol. 43, (49) : 15540-15549

Vincents, Bjarne; von Pawel-Rammingen, Ulrich; Björck, Lars; et al.

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

Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, (50) : 17371-17376

Wenig, Katja; Chatwell, Lorenz; von Pawel-Rammingen, Ulrich; et al.

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

Molecular Microbiology, Vol. 36, (3) : 737-748

Von Pawel-Rammingen, Ulrich; Telepnev, Maxim V; Schmidt, Gudula; et al.

Multiple molecular determinants for retrotransposition in a primer tRNA

Molecular and Cellular Biology, American Society for Microbiology 1995, Vol. 15, (1) : 217-226

Keeney, Jill B; Chapman, Karen B; Lauermann, Vit; et al.

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

Journal of Molecular Biology, Academic Press 1993, Vol. 233, (1) : 43-58

Åström, Stefan U.; von Pawel-Rammingen, Ulrich; Byström, Anders S

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

Molecular and Cellular Biology, American Society for Microbiology 1992, Vol. 12, (4) : 1432-1442

von Pawel-Rammingen, Ulrich; Åström, Stefan; Byström, Anders S

Proteolytic processing of the streptococcal IgG cleaving enzyme IdeS reduces immunorecognition without affecting the biological activity of the enzyme

Persson, Helena; Johansson Söderberg, Jenny; Vindebro, Reine; et al.

Insights into substrate recognition and biochemical properties of the streptococcal IgG endopeptidase IdeS

Vindebro, Reine; von Pawel-Rammingen, Ulrich

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Research groups

Head of research

Ulrich von Pawel-Rammingen Group