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Cryo-electron microscopic and X-ray crystallographic analysis of the light-driven proton pump proteorhodopsin reveals a pentameric assembly

Autor: Hirschi, Stephan, Kalbermatter, David, Ucurum, Zöhre, Fotiadis, Dimitrios

Publikováno v: In Journal of Structural Biology: X 2020 4

Primary resistance mechanism of the canine distemper virus fusion protein against a small-molecule membrane fusion inhibitor

Autor: Kalbermatter, David, Shrestha, Neeta, Ader-Ebert, Nadine, Herren, Michael, Moll, Pascal, Plemper, Richard K., Altmann, Karl-Heinz, Langedijk, Johannes P., Gall, Flavio, Lindenmann, Urs, Riedl, Rainer, Fotiadis, Dimitrios, Plattet, Philippe

Publikováno v: In Virus Research 2 January 2019 259:28-37

The making of a potent L-lactate transport inhibitor.

Autor: Bosshart, Patrick D.^1,2, Kalbermatter, David¹, Bonetti, Sara¹, Fotiadis, Dimitrios¹ dimitrios.fotiadis@ibmm.unibe.ch

Publikováno v: Communications Chemistry. 9/6/2021, Vol. 4 Issue 1, p1-9. 9p.

High-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding

Autor: Ilgü, Hüseyin, Jeckelmann, Jean-Marc, Kalbermatter, David, Ucurum, Zöhre, Lemmin, Thomas, Fotiadis, Dimitrios

Publikováno v: Ilgü, Hüseyin; Jeckelmann, Jean-Marc; Kalbermatter, David; Ucurum, Zöhre; Lemmin, Thomas; Fotiadis, Dimitrios (2021). High-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding. BMC biology, 19(1), p. 179. BioMed Central 10.1186/s12915-021-01102-4
BMC Biology, Vol 19, Iss 1, Pp 1-13 (2021)
BMC Biology
BMC Biology, 19 (1)

Background: The L-arginine/agmatine transporter AdiC is part of the arginine-dependent extreme acid resistance system of the bacterium Escherichia coli and its pathogenic varieties such as strain E. coli O157:H7. At the present time, there is a lack

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https://boris.unibe.ch/161698/1/12915_2021_Article_1102.pdf