Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kai-Malte Bartels"'
Publikováno v:
BioTechniques, Vol 41, Iss 3, Pp 327-332 (2006)
The production of pure protein is indispensable for many applications in life sciences, however, protein purification protocols are difficult to establish, and the experimental procedures are usually tedious and time-consuming. Therefore, a number of
Externí odkaz:
https://doaj.org/article/4088bf740c0b4ab09a75796206215dff
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:
Gabriele Loers, Udo Schumacher, Melitta Schachner, Nina Nehmann, Heike Gustke, Kai-Malte Bartels, Ralf Kleene, M. Jaehne, Karl-Erich Jaeger
Publikováno v:
European Journal of Clinical Microbiology & Infectious Diseases. 31:207-215
Pseudomonas aeruginosa (PA) can cause infections in compromised hosts by interacting with the glycocalyx of host epithelial cells. It binds to glycostructures on mucosal surfaces via two lectins, which are carbohydrate-binding proteins, named PA-IL a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ea0229ec6c80ae7b692364be696159e
https://doi.org/10.1007/s10096-011-1295-x
https://doi.org/10.1007/s10096-011-1295-x
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6177fee5d79f6b5e2a0c42181ceb15ef
https://doi.org/10.1128/jb.01507-10
https://doi.org/10.1128/jb.01507-10
Publikováno v:
BioTechniques. 41:327-332
The production of pure protein is indispensable for many applications in life sciences, however, protein purification protocols are difficult to establish, and the experimental procedures are usually tedious and time-consuming. Therefore, a number of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d34774f29199fcb4af1f61e3136e823
https://doi.org/10.2144/000112236
https://doi.org/10.2144/000112236
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3a216c227da62151aad72fd890be1f5
http://europepmc.org/articles/PMC3466170?pdf=render
http://europepmc.org/articles/PMC3466170?pdf=render
Autor:
Emma M. V. Johansson, Miguel Cámara, Cristina Nativi, Shanika A. Crusz, Kai-Malte Bartels, Karl-Erich Jaeger, Lieven Buts, Rameshwar U. Kadam, Frank Rosenau, Paul Williams, Tamis Darbre, Stephen P. Diggle, Martina Cacciarini, Remy Loris, Jean-Louis Reymond, Elena Kolomiets
Summary The human pathogenic bacterium Pseudomonas aeruginosa produces a fucose-specific lectin, LecB, implicated in tissue attachment and the formation of biofilms. To investigate if LecB inhibition disrupts these processes, high-affinity ligands we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19e6e166b04e851a6469c7034c97dfb9
https://biblio.vub.ac.be/vubir/inhibition-and-dispersion-of-pseudomonas-aeruginosa-biofilms-by-glycopeptide-dendrimers-targeting-the-fucosespecific-lectin-lecb(21a636bf-35bd-4b51-ad9a-b5a2df14a999).html
https://biblio.vub.ac.be/vubir/inhibition-and-dispersion-of-pseudomonas-aeruginosa-biofilms-by-glycopeptide-dendrimers-targeting-the-fucosespecific-lectin-lecb(21a636bf-35bd-4b51-ad9a-b5a2df14a999).html
Inhibition of Pseudomonas aeruginosa biofilms with a glycopeptide dendrimer containing D-amino acids
Autor:
Kai-Malte Bartels, Gabriele Rispoli, Paul Williams, Miguel Cámara, Jean-Louis Reymond, Shanika A. Crusz, Rameshwar U. Kadam, Tamis Darbre, Emma M. V. Johansson, Stephen P. Diggle, Karl-Erich Jaeger
Publikováno v:
MedChemComm. 2:418
The C-fucosyl peptide dendrimer D-FD2 (CFuc-lys-pro-leu)4(Lys-phe-lys-leu)2Lys-his-leu-NH2 was prepared as the D-amino acid containing stereoisomer of the Pseudomonas aeruginosa biofilm inhibitor FD2. D-FD2 showed lower affinity for the fucose specif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fe34618b9dd3221e2b1ae5abf67a0b1a
https://doi.org/10.1039/c0md00270d
https://doi.org/10.1039/c0md00270d