Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Kirstin Fritz"'
Autor:
Olga Lamprecht, Maryia Ratnikava, Paulina Jacek, Eugen Kaganovitch, Nina Buettner, Kirstin Fritz, Ina Biazruchka, Robin Köhler, Julian Pietsch, Victor Sourjik
Publikováno v:
PLoS Genetics, Vol 19, Iss 5, p e1010750 (2023)
Curli amyloid fibers are a major constituent of the extracellular biofilm matrix formed by bacteria of the Enterobacteriaceae family. Within Escherichia coli biofilms, curli gene expression is limited to a subpopulation of bacteria, leading to hetero
Externí odkaz:
https://doaj.org/article/97ba43a3e3084709b68765949c61cb4c
Autor:
Olga Lamprecht, Maryia Ratnikava, Paulina Jacek, Eugen Kaganovitch, Nina Buettner, Kirstin Fritz, Ina Biazruchka, Robin Köhler, Julian Pietsch, Victor Sourjik
Curli amyloid fibers are a major constituent of the extracellular biofilm matrix formed by bacteria of the Enterobacteriaceae family. Within Escherichia coli biofilms, curli gene expression is limited to a subpopulation of bacteria, leading to hetero
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::165a9e2fc64d00f7f0a2fd50052adf0c
https://doi.org/10.1101/2022.05.23.493020
https://doi.org/10.1101/2022.05.23.493020
Autor:
Remy Colin, Kirstin Fritz, Verena Maria Suchanek, Victor Sourjik, Olga Besharova, María Esteban-López
Publikováno v:
Molecular Microbiology. 113:728-739
Attachment to surfaces is an important early step during bacterial infection and during formation of submerged biofilms. Although flagella-mediated motility is known to be important for attachment of Escherichia coli and other bacteria, implications
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93f2d66e9418bd93988f8c5e721b6031
https://doi.org/10.1111/mmi.14438
https://doi.org/10.1111/mmi.14438
Autor:
Kirstin Fritz, M. Haese-Seiller, S. Stanglmaier, Jean-François Moulin, Bert Nickel, Joachim O. Rädler, Samira Hertrich
Publikováno v:
Langmuir. 28:10818-10821
Lipid bilayers with a controlled content of anionic lipids are a prerequisite for the quantitative study of hydrophobic-electrostatic interactions of proteins with lipid bilayers. Here, the asymmetric distribution of zwitterionic and anionic lipids i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1cb21280f766457fd47176a12d3dd06
https://doi.org/10.1021/la3019887
https://doi.org/10.1021/la3019887
Annexins are a family of proteins that bind to anionic phospholipid membranes in a Ca2+-dependent manner. Annexin A2 forms heterotetramers (Anx A2t) with the S100A10 (p11) protein dimer. The tetramer is capable of bridging phospholipid membranes and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5645eac6c1d5a829529cb4043310e86d
http://arxiv.org/abs/1009.3161
http://arxiv.org/abs/1009.3161