Zobrazeno 1 - 10
of 295
pro vyhledávání: '"Dirk Schneider"'
Autor:
Jan Sieder-Katzmann, Martin Propst, Ralf H. Stark, Dirk Schneider, Stephan General, Martin Tajmar, Christian Bach
Publikováno v:
Aerospace, Vol 11, Iss 7, p 507 (2024)
A cold-gas test campaign has been conducted at the DLR’s P6.2 test bench in Lampoldshausen, with the objective of investigating the linear aerospike nozzle flow in interaction with secondary injection thrust vector control (SITVC). In this campaign
Externí odkaz:
https://doaj.org/article/247ed885979145fba4704bc4ccf292af
Autor:
Lucas Gewehr, Benedikt Junglas, Ruven Jilly, Johannes Franz, Wenyu Eva Zhu, Tobias Weidner, Mischa Bonn, Carsten Sachse, Dirk Schneider
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Abstract Dynamin-like proteins are membrane remodeling GTPases with well-understood functions in eukaryotic cells. However, bacterial dynamin-like proteins are still poorly investigated. SynDLP, the dynamin-like protein of the cyanobacterium Synechoc
Externí odkaz:
https://doaj.org/article/6620f236a7994b4e9ceb79427a9499db
Autor:
Nadja Hellmann, Dirk Schneider
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
Genetic assays capable of measuring the propensity of transmembrane helices to oligomerize within the cytoplasmic membrane of the bacterium E. coli are frequently used when sequence-specificity in transmembrane helix-helix interactions is investigate
Externí odkaz:
https://doaj.org/article/91da12ce71a044e28bb231fe59a189e9
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Human Claudin-7 (Cldn7) is a member of the Claudin (Cldn) superfamily. In vivo, these proteins form tight junctions, which establish constricted connections between cells. Cldns oligomerize within the membrane plane (= cis-interaction), and also inte
Externí odkaz:
https://doaj.org/article/e67cf0ac4d754baaa6cb864cc9476ba8
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 6, p 5239 (2023)
The folding and stability of proteins are often studied via unfolding (and refolding) a protein with urea. Yet, in the case of membrane integral protein domains, which are shielded by a membrane or a membrane mimetic, urea generally does not induce u
Externí odkaz:
https://doaj.org/article/3b4eb5eed65b4ffaa2f13a2908c2fed9
Autor:
Eva Düppre, Dirk Schneider
Publikováno v:
FEBS Open Bio, Vol 10, Iss 11, Pp 2343-2349 (2020)
Hsp70 proteins and their Hsp40 co‐chaperones are essential components of cellular chaperone networks in both prokaryotes and eukaryotes. Here, we performed a genetic analysis to define the protein domains required for the key functions of the major
Externí odkaz:
https://doaj.org/article/d9948c35ea254ddc8fd2a4cdcc65ebd7
Autor:
Kristin Oepen, Hüseyin Özbek, Anja Schüffler, Johannes C. Liermann, Eckhard Thines, Dirk Schneider
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 24, p 13565 (2021)
ATP-binding cassette (ABC) transporters are conserved in all kingdoms of life, where they transport substrates against a concentration gradient across membranes. Some ABC transporters are known to cause multidrug resistances in humans and are able to
Externí odkaz:
https://doaj.org/article/1723998c87354982987cb686a9fc47ac
Publikováno v:
Frontiers in Plant Science, Vol 10 (2019)
The inner membrane-associated protein of 30 kDa (IM30), also known as the vesicle-inducing protein in plastids 1 (Vipp1), is essential for photo-autotrophic growth of cyanobacteria, algae and higher plants. While its exact function still remains larg
Externí odkaz:
https://doaj.org/article/4bcf442383e84e03acda648f6691a243
Autor:
Florian Cymer, Dirk Schneider
Publikováno v:
Membranes, Vol 11, Iss 7, p 512 (2021)
Amino acids with small side chains and motifs of small residues in a distance of four are rather abundant in human single-span transmembrane helices. While interaction of such helices appears to be common, the role of the small residues in mediating
Externí odkaz:
https://doaj.org/article/fad9b743307e4451a4ba48a15d8ddc97
The Bacteriostatic Activity of 2-Phenylethanol Derivatives Correlates with Membrane Binding Affinity
Autor:
Isabel S. Kleinwächter, Stefanie Pannwitt, Alessia Centi, Nadja Hellmann, Eckhard Thines, Tristan Bereau, Dirk Schneider
Publikováno v:
Membranes, Vol 11, Iss 4, p 254 (2021)
The hydrophobic tails of aliphatic primary alcohols do insert into the hydrophobic core of a lipid bilayer. Thereby, they disrupt hydrophobic interactions between the lipid molecules, resulting in a decreased lipid order, i.e., an increased membrane
Externí odkaz:
https://doaj.org/article/25d9d09325cd42f69cda206deb986fb9