Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Imke Wiedemann"'
Autor:
Brigitte Berger-Bächi, Susanne Rohrer, Hans-Georg Sahl, Mariana G. Pinho, Imke Wiedemann, Tanja Schneider, Daniela Alborn, Esther Holdener, Agnieszka Luczak-Kadlubowska, Chantal Quiblier, Maria Magdalena Senn
Publikováno v:
Antibiotics, Vol 2, Iss 1, Pp 11-27 (2013)
The yet uncharacterized membrane protein SA2056 belongs to the ubiquitous RND (Resistance-Nodulation-cell Division) family of transmembrane efflux transporters. The sa2056 gene is located downstream of femX, the gene encoding the essential, non-ribos
Externí odkaz:
https://doaj.org/article/5b00da0f0f234c8eb67e875e9dc3801e
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828:2628-2636
Many lantibiotics use the membrane bound cell wall precursor Lipid II as a specific target for killing Gram-positive bacteria. Binding of Lipid II usually impedes cell wall biosynthesis, however, some elongated lantibiotics such as nisin, use Lipid I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4e20100764a25219d9e62726a27ebb4
https://doi.org/10.1016/j.bbamem.2013.07.014
https://doi.org/10.1016/j.bbamem.2013.07.014
Autor:
Tanja Schneider, Hans-Georg Sahl, Maria M. Senn, Brigitte Berger-Bächi, Imke Wiedemann, Agnieszka Luczak-Kadlubowska, Esther Holdener, Chantal Quiblier, Mariana G. Pinho, Susanne Rohrer, Daniela Alborn
Publikováno v:
Antibiotics
Volume 2
Issue 1
Pages 11-27
Antibiotics, Vol 2, Iss 1, Pp 11-27 (2013)
Volume 2
Issue 1
Pages 11-27
Antibiotics, Vol 2, Iss 1, Pp 11-27 (2013)
The yet uncharacterized membrane protein SA2056 belongs to the ubiquitous RND (Resistance-Nodulation-cell Division) family of transmembrane efflux transporters. The sa2056 gene is located downstream of femX, the gene encoding the essential, non-ribos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee3a776b93e18305cc2161cf557fa9a5
https://doi.org/10.3390/antibiotics2010011
https://doi.org/10.3390/antibiotics2010011
Autor:
Imke Wiedemann, Saad Al-Kaddah, Manuela Brunschweiger, Katrin Reder-Christ, Gerd Bendas, Gabriela Klocek
Publikováno v:
Biophysical Chemistry. 152:145-152
The interaction of the lantibiotic gallidermin and the glycopeptide antibiotic vancomycin with bacterial membranes was simulated using mass sensitive biosensors and isothermal titration calorimetry (ITC). Both peptides interfere with cell wall biosyn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f7401ed3bb2711a3e181a63ad4e3be6
https://doi.org/10.1016/j.bpc.2010.09.002
https://doi.org/10.1016/j.bpc.2010.09.002
Autor:
Hans-Georg Sahl, Theo-Julian Hoffmann, Andrea Schiefer, Achim Hoerauf, Edith Nzukou, Katja Moelleken, Christina Poellinger, Beate Henrichfreise, Kenneth Pfarr, Imke Wiedemann, Tanja Schneider, Kelly L. Johnston
Publikováno v:
Molecular Microbiology. 73:913-923
Cell division and cell wall biosynthesis in prokaryotes are driven by partially overlapping multiprotein machineries whose activities are tightly controlled and co-ordinated. So far, a number of protein components have been identified and acknowledge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d0ec3e606581e69e33537a3456cd6af
https://doi.org/10.1111/j.1365-2958.2009.06815.x
https://doi.org/10.1111/j.1365-2958.2009.06815.x
Autor:
Michaele Josten, K. Gries, Tanja Schneider, S. Pelzer, Hans-Georg Sahl, Harald Labischinski, Imke Wiedemann
Publikováno v:
Antimicrobial Agents and Chemotherapy. 53:1610-1618
Friulimicin B is a naturally occurring cyclic lipopeptide, produced by the actinomycete Actinoplanes friuliensis , with excellent activity against gram-positive pathogens, including multidrug-resistant strains. It consists of a macrocyclic decapeptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a446edc83a96deb1578028208438fcb
https://doi.org/10.1128/aac.01040-08
https://doi.org/10.1128/aac.01040-08
Autor:
Ana Rodríguez, Hans-Georg Sahl, Beatriz Martínez, Imke Wiedemann, Tim Böttiger, Tanja Schneider
Publikováno v:
Applied and Environmental Microbiology. 74:4666-4670
Lactococcin 972 (Lcn972) is a nonlantibiotic bacteriocin that inhibits septum biosynthesis in Lactococcus lactis rather than forming pores in the cytoplasmic membrane. In this study, a deeper analysis of the molecular basis of the mode of action of L
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b38592d03578735081cd43523839eb08
https://doi.org/10.1128/aem.00092-08
https://doi.org/10.1128/aem.00092-08
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768(3):694-704
Nisin, a peptide antibiotic, efficiently kills bacteria through a unique mechanism which includes inhibition of cell wall biosynthesis and pore formation in cytoplasmic membranes. Both mechanisms are based on interaction with the cell wall precursor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5f7c07bd3720f841da3de3f2efbfd41
Autor:
Claus Garbe, Hans-Georg Sahl, Hubert Kalbacher, S. Rieg, Imke Wiedemann, Martin Deeg, Heiko Steffen, Andreas Peschel, Birgit Schittek, Friedrich Götz
Publikováno v:
Antimicrobial Agents and Chemotherapy. 50:2608-2620
Dermcidin (DCD) is a recently described antimicrobial peptide, which is constitutively expressed in eccrine sweat glands and transported via sweat to the epidermal surface. By postsecretory proteolytic processing in sweat the dermcidin protein gives
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abd92e7c5f2769d475f78e7e04a8b426
https://doi.org/10.1128/aac.00181-06
https://doi.org/10.1128/aac.00181-06
Publikováno v:
Antimicrobial Agents and Chemotherapy. 50:1449-1457
The activity of lanthionine-containing peptide antibiotics (lantibiotics) is based on different killing mechanisms which may be combined in one molecule. The prototype lantibiotic nisin inhibits peptidoglycan synthesis and forms pores through specifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e08cb9a8b768c5b85cf9c63a164d349
https://doi.org/10.1128/aac.50.4.1449-1457.2006
https://doi.org/10.1128/aac.50.4.1449-1457.2006