TY  - JOUR
A1  - Prestel, Andreas
A1  - Möller, Heiko Michael
T1  - Spatio-temporal control of cellular uptake achieved by photoswitchable cell-penetrating peptides
JF  - Chemical communications
N2  - The selective uptake of compounds into specific cells of interest is a major objective in cell biology and drug delivery. By incorporation of a novel, thermostable azobenzene moiety we generated peptides that can be switched optically between an inactive state and an active, cell-penetrating state with excellent spatio-temporal control.
Y1  - 2016
U6  - https://doi.org/10.1039/c5cc06848g
SN  - 1359-7345
SN  - 1364-548X
VL  - 52
SP  - 701
EP  - 704
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - JOUR
A1  - Prestel, Andreas
A1  - Möller, Heiko Michael
T1  - Spatio-temporal control of cellular uptake achieved by photoswitchable cell-penetrating peptides
JF  - Chemical communications : ChemComm
N2  - The selective uptake of compounds into specific cells of interest is a major objective in cell biology and drug delivery. By incorporation of a novel, thermostable azobenzene moiety we generated peptides that can be switched optically between an inactive state and an active, cell-penetrating state with excellent spatio-temporal control.
Y1  - 2015
U6  - https://doi.org/10.1039/C5CC06848G
SN  - 1364-548X
IS  - 52
SP  - 701
EP  - 704
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - JOUR
A1  - Kastl, Johanna
A1  - Braun, Joachim
A1  - Prestel, Andreas
A1  - Möller, Heiko Michael
A1  - Huhn, Thomas
A1  - Mayer, Thomas U.
T1  - Mad2 Inhibitor-1 (M2I-1): A Small Molecule Protein-Protein Interaction Inhibitor Targeting the Mitotic Spindle Assembly Checkpoint
JF  - ACS chemical biology
N2  - The genetic integrity of each organism depends on the faithful segregation of its genome during mitosis. To meet this challenge, a cellular surveillance mechanism, termed the spindle assembly checkpoint (SAC), evolved that monitors the correct attachment of chromosomes and blocks progression through mitosis if corrections are needed. While the central role of the SAC for genome integrity is well established, its functional dissection has been hampered by the limited availability of appropriate small molecule inhibitors. Using a fluorescence polarization-based screen, we identify Mad2 inhibitor-1 (M2I-1), the first small molecule inhibitor targeting the binding of Mad2 to Cdc20, an essential protein-protein interaction (PPI) within the SAC. Based on computational and biochemical analyses, we propose that M2I-1 disturbs conformational dynamics of Mad2 critical for complex formation with Cdc20. Cellular studies revealed that M2I-1 weakens the SAC response, indicating that the compound might be active in cells. Thus, our study identifies the SAC specific complex formation between Mad2 and Cdc20 as a protein-protein interaction that can be targeted by small molecules.
Y1  - 2015
U6  - https://doi.org/10.1021/acschembio.5b00121
SN  - 1554-8929
SN  - 1554-8937
VL  - 10
IS  - 7
SP  - 1661
EP  - 1666
PB  - American Chemical Society
CY  - Washington
ER  - 
TY  - JOUR
A1  - Holert, Johannes
A1  - Yücel, Onur
A1  - Jagmann, Nina
A1  - Prestel, Andreas
A1  - Möller, Heiko Michael
A1  - Philipp, Bodo
T1  - Identification of bypass reactions leading to the formation of one central steroid degradation intermediate in metabolism of different bile salts in Pseudomonas sp strain Chol1
JF  - Environmental microbiology
Y1  - 2016
U6  - https://doi.org/10.1111/1462-2920.13192
SN  - 1462-2912
SN  - 1462-2920
VL  - 18
SP  - 3373
EP  - 3389
PB  - Wiley-Blackwell
CY  - Hoboken
ER  -