Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Noah Ritzmann"'
Publikováno v:
Advanced Science, Vol 11, Iss 15, Pp n/a-n/a (2024)
Abstract Controlling the pH at the microliter scale can be useful for applications in research, medicine, and industry, and therefore represents a valuable application for synthetic biology and microfluidics. The presented vesicular system translates
Externí odkaz:
https://doaj.org/article/35689160b8d74aaf9cf18dec9f56eaa5
Autor:
Selen Manioglu, Seyed Majed Modaresi, Noah Ritzmann, Johannes Thoma, Sarah A. Overall, Alexander Harms, Gregory Upert, Anatol Luther, Alexander B. Barnes, Daniel Obrecht, Daniel J. Müller, Sebastian Hiller
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Abstract Polymyxins are last-resort antibiotics with potent activity against multi-drug resistant pathogens. They interact with lipopolysaccharide (LPS) in bacterial membranes, but mechanistic details at the molecular level remain unclear. Here, we c
Externí odkaz:
https://doaj.org/article/0539de9771d743a08fee0604262fc708
Autor:
Kevin Jahnke, Noah Ritzmann, Julius Fichtler, Anna Nitschke, Yannik Dreher, Tobias Abele, Götz Hofhaus, Ilia Platzman, Rasmus R. Schröder, Daniel J. Müller, Joachim P. Spatz, Kerstin Göpfrich
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Controlled actuation is an important aspect of synthetic cellular systems. Here, the authors combine pH responsive DNA origami structures with light triggered proton pump engineered E. coli to trigger a change in pH and control the deformation of gia
Externí odkaz:
https://doaj.org/article/7aa84b3740d243739cbffb55d2194277
Autor:
Anna Nitschke, Noah Ritzmann, Julius Fichtler, Kerstin Göpfrich, Ilia Platzman, Joachim P. Spatz, Daniel J. Müller, Rasmus R. Schröder, Tobias Abele, Kevin Jahnke, Götz Hofhaus, Yannik Dreher
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Nature Communications, 12 (1)
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Nature Communications, 12 (1)
Bottom-up and top-down approaches to synthetic biology each employ distinct methodologies with the common aim to harness living systems. Here, we realize a strategic merger of both approaches to convert light into proton gradients for the actuation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df4e0707b9bcd907f7814a1811893234
https://hdl.handle.net/21.11116/0000-0008-C54A-721.11116/0000-0008-C54B-621.11116/0000-0008-C54C-521.11116/0000-0008-C54D-421.11116/0000-0008-C54E-321.11116/0000-0008-C54F-221.11116/0000-0008-C550-F21.11116/0000-0008-C551-E21.11116/0000-0008-C552-D21.11116/0000-0008-C553-C21.11116/0000-0008-C554-B21.11116/0000-0008-C555-A21.11116/0000-0008-C548-9
https://hdl.handle.net/21.11116/0000-0008-C54A-721.11116/0000-0008-C54B-621.11116/0000-0008-C54C-521.11116/0000-0008-C54D-421.11116/0000-0008-C54E-321.11116/0000-0008-C54F-221.11116/0000-0008-C550-F21.11116/0000-0008-C551-E21.11116/0000-0008-C552-D21.11116/0000-0008-C553-C21.11116/0000-0008-C554-B21.11116/0000-0008-C555-A21.11116/0000-0008-C548-9
Publikováno v:
Nano Letters, 19 (9)
Maltoporins are a family of membrane proteins that facilitate the diffusion of hydrophilic molecules and maltosaccharides across the outer membrane of Gram-negative bacteria. Two contradicting models propose the sugar binding, uptake, and transport b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c54545069cfba087d2d6b029dd1905b7
https://doi.org/10.1021/acs.nanolett.9b02674
https://doi.org/10.1021/acs.nanolett.9b02674
Autor:
Anna Nitschke, Kevin Jahnke, Kerstin Göpfrich, Joachim P. Spatz, Ilia Platzman, Daniel J. Müller, Noah Ritzmann, Julius Fichtler, Yannik Dreher, Tobias Abele, Rasmus R. Schröder, Götz Hofhaus
Publikováno v:
In Review
Bottom-up and top-down approaches to synthetic biology each employ distinct methodologies with the common aim to harness new types of living systems. Both approaches, however, face their own challenges towards biotechnological and biomedical applicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbcd63f478b81c8317ce8d7f8c0c5285
https://doi.org/10.21203/rs.3.rs-82114/v1
https://doi.org/10.21203/rs.3.rs-82114/v1
Autor:
Noah, Ritzmann, Johannes, Thoma
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2127
Atomic force microscopy (AFM)-based single-molecule force spectroscopy allows direct physical manipulation of single membrane proteins under near-physiological conditions. It can be applied to study mechanical properties and molecular interactions as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bae05fc596738270510d28991f1c0daa
https://pubmed.ncbi.nlm.nih.gov/32112333
https://pubmed.ncbi.nlm.nih.gov/32112333
Autor:
Johannes Thoma, Noah Ritzmann
Publikováno v:
Methods in Molecular Biology ISBN: 9781071603727
Atomic force microscopy (AFM)-based single-molecule force spectroscopy allows direct physical manipulation of single membrane proteins under near-physiological conditions. It can be applied to study mechanical properties and molecular interactions as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df3f6e9488f743ffdbbad69fafaf2ad9
https://doi.org/10.1007/978-1-0716-0373-4_23
https://doi.org/10.1007/978-1-0716-0373-4_23
Autor:
Johannes Thoma, David Kalbermatter, Noah Ritzmann, Stephan Hirschi, Daniel J. Müller, Dimitrios Fotiadis
Publikováno v:
Biophysical Journal, 113 (6)
One major objective of synthetic biology is the bottom-up assembly of minimalistic nanocells consisting of lipid or polymer vesicles as architectural scaffolds and of membrane and soluble proteins as functional elements. However, there is no reliable
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f460e360fc9f51da07ab467e9bb7d38
https://doi.org/10.1016/j.bpj.2017.06.022
https://doi.org/10.1016/j.bpj.2017.06.022
Publikováno v:
Structure, 26 (7)
The core component BamA of the β barrel assembly machinery (BAM) adopts several conformations, which are thought to facilitate the insertion and folding of β barrel proteins into the bacterial outer membrane. Which factors alter the stability of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7148f6bd67bfe20b5386d51dcab6a395
https://pubmed.ncbi.nlm.nih.gov/29861346
https://pubmed.ncbi.nlm.nih.gov/29861346