Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Margot Koster"'
Publikováno v:
Microbiology. 154:3025-3032
The subcellular localization of the major type II secretion system of Pseudomonas aeruginosa, the Xcp system, was studied microscopically using a biarsenical ligand that becomes fluorescent upon binding to a tetracysteine motif (Lumio tag), which was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::977c2283bb7e1d9a81c3a23125e4dfd0
https://doi.org/10.1099/mic.0.2008/018069-0
https://doi.org/10.1099/mic.0.2008/018069-0
Autor:
Michael Breuer, Jan Tommassen, Karl-Erich Jaeger, Margot Koster, Frank Rosenau, Bernhard Hauer, Anke Beselin, Bouke K. H. L. Boekema
Publikováno v:
Applied and Environmental Microbiology. 73:3838-3844
Burkholderia glumae strain PG1 produces a lipase of biotechnological relevance. Lipase production by this strain and its derivative LU8093, which was obtained through classical strain improvement, was investigated under different conditions. When 10%
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb742bc47f539534e3f35282c8b9bbd9
https://doi.org/10.1128/aem.00097-07
https://doi.org/10.1128/aem.00097-07
Autor:
Mohammed El Khattabi, Margot Koster, Geneviève Ball, Alain Filloux, Jan Tommassen, Jorik Arts, Arjan de Groot, Eric Durand
Publikováno v:
Microbiology. 153:1582-1592
Pseudomonas aeruginosa is an opportunistic pathogen, which secretes a wide variety of enzymes and toxins into the extracellular medium. Most exoproteins are exported by the type II secretion machinery, the Xcp system, which encompasses 12 different p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddc79722cae9431e42a318d3f143e5ff
https://doi.org/10.1099/mic.0.2006/002840-0
https://doi.org/10.1099/mic.0.2006/002840-0
Autor:
Mathijs Groeneweg, Wilbert Bitter, Jan Tommassen, Margot Koster, Patricia M. Sánchez Carballo, Ulrich Zähringer, Ria van Boxtel
Publikováno v:
Journal of Bacteriology. 189:2967-2975
Secretins are oligomeric proteins that mediate the export of macromolecules across the bacterial outer membrane. The members of the secretin superfamily possess a C-terminal homology domain that is important for oligomerization and channel formation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::362530a5cb2b2937f5f3e4adec9b9595
https://doi.org/10.1128/jb.01583-06
https://doi.org/10.1128/jb.01583-06
Autor:
Margot Koster, Peter Burghout, Ria van Boxtel, Philippe Ringler, Patrick Van Gelder, Jan Tommassen, Shirley A. Müller
Publikováno v:
Journal of Bacteriology. 186:4645-4654
YscC is the integral outer membrane component of the type III protein secretion machinery of Yersinia enterocolitica and belongs to the family of secretins. This group of proteins forms stable ring-like oligomers in the outer membrane, which are thou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5c23f4d5179ade72222a9a8977c7e10
https://doi.org/10.1128/jb.186.14.4645-4654.2004
https://doi.org/10.1128/jb.186.14.4645-4654.2004
Autor:
Emmie de Wit, Frank Beckers, Jan Tommassen, Ria van Boxtel, Margot Koster, Peter Burghout, Guy R. Cornelis
Publikováno v:
Journal of Bacteriology. 186(16):5366-5375
The YscC secretin is a major component of the type III protein secretion system of Yersinia enterocolitica and forms an oligomeric structure in the outer membrane. In a mutant lacking the outer membrane lipoprotein YscW, secretion is strongly reduced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dad94b8f4536029121d8ad52a78f776
https://researchportal.unamur.be/en/publications/3202bb91-dd09-44c5-a864-fb38f05e4056
https://researchportal.unamur.be/en/publications/3202bb91-dd09-44c5-a864-fb38f05e4056
Autor:
Holger Braunschweig, Margot Koster
Publikováno v:
Scopus-Elsevier
Reaction of various 1,2-dihalodiboranes(4) with Na[(η5-C5H4R)M(CO)3] yielded the diborane(4)yl complexes [X(Me2N)B-B(NMe2){ η5-(C5H4R)M(CO)3}] (5, X = Cl, R = H, M = Mo; 6, X = Br, R = Me, M = Mo; 7, X = Br, R = H, M = W ;8, X = Br, R = Me, M = W )
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f8da4d2bf71590ffaf7d68635e5f975
https://doi.org/10.1515/znb-2002-0502
https://doi.org/10.1515/znb-2002-0502
Autor:
Margot Koster, Jan Tommassen, Corrine Ockhuijsen, Peter Braun, Elaine F Eppens, Wilbert Bitter
Publikováno v:
Journal of Biological Chemistry. 276:26030-26035
Elastase of Pseudomonas aeruginosa is synthesized as a preproenzyme. After propeptide-mediated folding in the periplasm, the proenzyme is autoproteolytically processed, prior to translocation of both the mature enzyme and the propeptide across the ou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::438dfa69ec30fde0cf8253d59fb7ba18
https://doi.org/10.1074/jbc.m007122200
https://doi.org/10.1074/jbc.m007122200
Autor:
Jan Tommassen, Alain Filloux, Andrée Lazdunski, Margot Koster, Manon Gérard-Vincent, Arjan de Groot, Gijs Gerritse
Publikováno v:
Journal of Bacteriology. 183:959-967
Pseudomonas aeruginosa and Pseudomonas alcaligenes are gram-negative bacteria that secrete proteins using the type II or general secretory pathway, which requires at least 12 xcp gene products (XcpA and XcpP to -Z). Despite strong conservation of thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9308197eaa26671b0bdf208a6aef578
https://doi.org/10.1128/jb.183.3.959-967.2001
https://doi.org/10.1128/jb.183.3.959-967.2001
Publikováno v:
International Journal of Medical Microbiology. 290:325-331
Gram-negative bacteria have developed a variety of secretion pathways to secrete toxins and enzymes into the extracellular medium. These pathways are very different with respect to their functional mechanism and complexity, and each system has its ow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66b10d9e98f9af50f71359ee792d3eb0
https://doi.org/10.1016/s1438-4221(00)80033-8
https://doi.org/10.1016/s1438-4221(00)80033-8