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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

Electron crystallography reveals that substrate release from the PTS IIC glucose transporter is coupled to a subtle conformational change

Autor: Kalbermatter, David, Chiu, Po-Lin, Jeckelmann, Jean-Marc, Ucurum, Zöhre, Walz, Thomas, Fotiadis, Dimitrios

Publikováno v: In Journal of Structural Biology July 2017 199(1):39-45

Engineering and functional characterization of a proton-driven β-lactam antibiotic translocation module for bionanotechnological applications.

Autor: Stauffer, Mirko¹, Ucurum, Zöhre¹, Harder, Daniel¹, Fotiadis, Dimitrios¹ dimitrios.fotiadis@ibmm.unibe.ch

Publikováno v: Scientific Reports. 8/26/2021, Vol. 11 Issue 1, p1-10. 10p.

Peptide transporter structure reveals binding and action mechanism of a potent PEPT1 and PEPT2 inhibitor

Autor: Stauffer, Mirko, Jeckelmann, Jean-Marc, Ilgü, Hüseyin, Ucurum, Zöhre, Boggavarapu, Rajendra, Fotiadis, Dimitrios

Publikováno v: Stauffer, Mirko; Jeckelmann, Jean-Marc; Ilgü, Hüseyin; Ucurum, Zöhre; Boggavarapu, Rajendra; Fotiadis, Dimitrios (2022). Peptide transporter structure reveals binding and action mechanism of a potent PEPT1 and PEPT2 inhibitor. Communications chemistry, 5(1) Springer Nature 10.1038/s42004-022-00636-0

Inhibitors for membrane transporters have been shown to be indispensable as drugs and tool compounds. The proton-dependent oligopeptide transporters PEPT1 and PEPT2 from the SLC15 family play important roles in human and mammalian physiology. With Ly

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