Semra Ince
Ruhr University Bochum
21 Papers
9 Citations
Semra Ince is an academic researcher from Ruhr University Bochum. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 6, co-authored 10 publications.
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Papers
Bisphenol A binds to Ras proteins and competes with guanine nucleotide exchange: implications for GTPase-selective antagonists.
Miriam Schöpel,Katharina F. G. Jockers,Peter M. Düppe,Jasmin Autzen,Veena Nambiar Potheraveedu,Semra Ince,King Tuo Yip,Rolf Heumann,Christian Herrmann,Jürgen Scherkenbeck,Raphael Stoll +10 more
TL;DR: The results propose a new mode of action for bisphenol A (10) that advocates a reduced exposure to this compound in the authors' environment and may lay the foundation for the future design of GTPase-selective antagonists with higher affinity to benefit of the treatment of cancer.
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ATP-binding and hydrolysis of human NLRP3
Rebecca Brinkschulte,David M. Fußhöller,Florian Hoss,Juan F. Rodriguez-Alcazar,Mario A. Lauterbach,Carl-Christian Kolbe,Melanie Rauen,Semra Ince,Christian Herrmann,Eicke Latz,Matthias Geyer +10 more
TL;DR: In this paper , the intrinsic ATP hydrolysis activity of recombinant NLRP3 was analyzed by reverse phase HPLC and the impact of canonical residues in the nucleotide binding site as the Walker A and B motifs was analyzed.
Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices
Adrian Syguda,Michael Bauer,Utz Benscheid,Nicole Ostler,Elisabeth Naschberger,Semra Ince,Michael Stürzl,Christian Herrmann +7 more
TL;DR: GTP hydrolysis‐driven release of the α12/13 subdomain is suggested, making it available for coiled‐coil formation, and the biological relevance of hGBP1 tetramer formation in living cells is demonstrated by chemical cross‐link experiments.
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Interaction of isolated cross-linked short actin oligomers with the skeletal muscle myosin motor domain
Zheng Qu,Setsuko Fujita-Becker,Edda Ballweber,Semra Ince,Christian Herrmann,Rasmus R. Schröder,Hans Georg Mannherz +6 more
TL;DR: To generate stable actin oligomer:myosin‐S1 complexes, actin polymerization inhibition was blocked with gelsolin and Clostridium botulinum iota toxin‐mediated ADP‐ribosylation and the stoichiometry and binding affinity of myosin •S1 to actIn oligomers were analysed.
11
Farnesylation of human guanylate-binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization.
Charlotte Lorenz,Charlotte Lorenz,Semra Ince,Tao Zhang,Anneliese Cousin,Renu Batra-Safferling,Luitgard Nagel-Steger,Christian Herrmann,Andreas M. Stadler,Andreas M. Stadler +9 more
TL;DR: Nonmodified hGBP1 is structurally perturbed as compared to farn‐hGBP, and GppNHp binding leads to large structural rearrangements and higher conformational flexibility of the monomer and the dimer.
10