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pro vyhledávání: '"Horst Funken"'
Autor:
Horst Funken, Kai-Malte Bartels, Susanne Wilhelm, Melanie Brocker, Michael Bott, Manjeet Bains, Robert E W Hancock, Frank Rosenau, Karl-Erich Jaeger
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46857 (2012)
The fucose binding lectin LecB affects biofilm formation and is involved in pathogenicity of Pseudomonas aeruginosa. LecB resides in the outer membrane and can be released specifically by treatment of an outer membrane fraction with fucose suggesting
Externí odkaz:
https://doaj.org/article/3a674b52b31241e9858a1cd911018280
Autor:
Sander H. J. Smits, Susanne Wilhelm, Astrid Wirtz, Karl-Erich Jaeger, Andreas Knapp, Alexander Pelzer, Lutz Schmitt, Horst Funken, Christian Schwarz
Publikováno v:
MicrobiologyOpen
The Pseudomonas aeruginosa genome encodes a variety of different proteolytic enzymes several of which play an important role as virulence factors. Interestingly, only two of these proteases are predicted to belong to the subtilase family and we have
Autor:
Susanne Wilhelm, Alexander Pelzer, Karl-Erich Jaeger, Michael Bott, Tino Polen, Horst Funken, Frank Rosenau
Publikováno v:
MicrobiologyOpen
MicrobiologyOpen 3(1), 89-103 (2014). doi:10.1002/mbo3.150
MicrobiologyOpen 3(1), 89-103 (2014). doi:10.1002/mbo3.150
The open reading frame PA1242 in the genome of Pseudomonas aeruginosa PAO1 encodes a putative protease belonging to the peptidase S8 family of subtilases. The respective enzyme termed SprP consists of an N-terminal signal peptide and a so-called S8 d
Autor:
Javier Rojo, Tamis Darbre, Alessandro Casnati, W. Bruce Turnbull, Cristina Nativi, Francesco Peri, Stéphane P. Vincent, Paul V. Murphy, Han Zuilhof, Anna Bernardi, Trinidad Velasco-Torrijos, Franck Fieschi, Anne Imberty, Christina De Castro, Paul Messner, Martina Lahmann, Jean-Reymond Reymond, Sébastien Vidal, Marco Marradi, Jukka Finne, Barbara Richichi, Jesús Jiménez-Barbero, Antonio Molinaro, Olivier Renaudet, Thisbe K. Lindhorst, Horst Funken, Christina Schäffer, Soledad Penadés, Stefan Oscarson, Karl-Erich Jaeger, Roland J. Pieters, Tom Wennekes, Francesco Sansone
Publikováno v:
Bernardi, A, Jiménez-Barbero, J, Casnati, A, De Castro, C, Darbre, T, Fieschi, F, Finne, J, Funken, H, Jaeger, K E, Lahmann, M, Lindhorst, T K, Marradi, M, Messner, P, Molinaro, A, Murphy, P V, Nativi, C, Oscarson, S, Penadés, S, Peri, F, Pieters, R J, Renaudet, O, Reymond, J L, Richichi, B, Rojo, J, Sansone, F, Schäffer, C, Turnbull, W B, Velasco-Torrijos, T, Vidal, S, Vincent, S, Wennekes, T, Zuilhof, H & Imberty, A 2013, ' Multivalent glycoconjugates as anti-pathogenic agents ', Chemical Society Reviews, vol. 42, no. 11, pp. 4709-4727 . https://doi.org/10.1039/c2cs35408j
Chemical Society Reviews
Chemical Society Reviews, 2013, 42 (11), pp.4709-27. ⟨10.1039/c2cs35408j⟩
Digital.CSIC. Repositorio Institucional del CSIC
instname
Chemical Society Reviews, 42, 4709-4727
Chemical Society reviews
Chemical Society Reviews 42 (2013)
Bernardi, Anna; Jiménez-Barbero, Jesus; Casnati, Alessandro; De Castro, Cristina; Darbre, Tamis; Fieschi, Franck; Finne, Jukka; Funken, Horst; Jaeger, Karl-Erich; Lahmann, Martina; Lindhorst, Thisbe K.; Marradi, Marco; Messner, Paul; Molinaro, Antonio; Murphy, Paul V.; Nativi, Cristina; Oscarson, Stefan; Penadés, Soledad; Peri, Francesco; Pieters, Roland J.; ... (2013). Multivalent glycoconjugates as anti-pathogenic agents. Chemical Society reviews, 42(11), pp. 4709-4727. Royal Society of Chemistry 10.1039/C2CS35408J
Chemical Society Reviews, Royal Society of Chemistry, 2013, 42 (11), pp.4709-27. ⟨10.1039/c2cs35408j⟩
Chemical Society Reviews
Chemical Society Reviews, 2013, 42 (11), pp.4709-27. ⟨10.1039/c2cs35408j⟩
Digital.CSIC. Repositorio Institucional del CSIC
instname
Chemical Society Reviews, 42, 4709-4727
Chemical Society reviews
Chemical Society Reviews 42 (2013)
Bernardi, Anna; Jiménez-Barbero, Jesus; Casnati, Alessandro; De Castro, Cristina; Darbre, Tamis; Fieschi, Franck; Finne, Jukka; Funken, Horst; Jaeger, Karl-Erich; Lahmann, Martina; Lindhorst, Thisbe K.; Marradi, Marco; Messner, Paul; Molinaro, Antonio; Murphy, Paul V.; Nativi, Cristina; Oscarson, Stefan; Penadés, Soledad; Peri, Francesco; Pieters, Roland J.; ... (2013). Multivalent glycoconjugates as anti-pathogenic agents. Chemical Society reviews, 42(11), pp. 4709-4727. Royal Society of Chemistry 10.1039/C2CS35408J
Chemical Society Reviews, Royal Society of Chemistry, 2013, 42 (11), pp.4709-27. ⟨10.1039/c2cs35408j⟩
Multivalency plays a major role in biological processes and particularly in the relationship between pathogenic microorganisms and their host that involves protein–glycan recognition. These interactions occur during the first steps of infection, fo
Autor:
Horst Funken, Kai-Malte Bartels, Andreas Knapp, Susanne Wilhelm, Frank Rosenau, Michael Bott, Melanie Brocker, Karl-Erich Jaeger
Publikováno v:
Journal of Bacteriology. 193:1107-1113
The fucose-/mannose-specific lectin LecB from Pseudomonas aeruginosa is transported to the outer membrane; however, the mechanism used is not known so far. Here, we report that LecB is present in the periplasm of P. aeruginosa in two variants of diff
Publikováno v:
Journal of Biotechnology. 191:1-2
Autor:
Michael Bott, Kai-Malte Bartels, Melanie Brocker, Manjeet Bains, Susanne Wilhelm, Horst Funken, Robert E. W. Hancock, Frank Rosenau, Karl-Erich Jaeger
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46857 (2012)
PLoS one 7(10), e46857-(2012). doi:10.1371/journal.pone.0046857
PLoS ONE
PLoS one 7(10), e46857-(2012). doi:10.1371/journal.pone.0046857
PLoS ONE
The fucose binding lectin LecB affects biofilm formation and is involved in pathogenicity of Pseudomonas aeruginosa. LecB resides in the outer membrane and can be released specifically by treatment of an outer membrane fraction with fucose suggesting
Autor:
Karl-Erich Jaeger, Michael L. Vasil, Andreas Knapp, Horst Funken, Frank Rosenau, Susanne Wilhelm
Publikováno v:
Journal of bacteriology. 193(20)
A key element in iron-dependent regulation of iron metabolism and virulence-related functions for Pseudomonas aeruginosa is the sigma factor PvdS. PvdS expression itself is also influenced by iron-independent stimuli. We show that pyoverdine producti