Ausgewählte Publikationen

Im Folgenden finden Sie die ausgewählten Publikationen der letzten fünf Jahre.
Weitere essenzielle Publikationen entnehmen Sie bitte den jeweiligen Principals Investigators.

2022

Endres, Kristina, Bufe, Bernd and Tarasov, Alexey. "The “MultiSensE” consortium" Neuroforum, vol. , no. , 2022. doi: doi.org/10.1515/nf-2022-0012.

2021

Valeri F, Endres K. How biological sex of the host shapes its gut microbiota Front Neuroendocrinol. 2021 Mar 10;61:100912. doi: dx.doi.org/10.1016/j.yfrne.2021.100912. IF 9,06

Nguyen,VTT, Sallbach, J, dos Santos Guilherme,M, Endres, K. Influence of Acetylcholine Esterase Inhibitors and Memantine, Clinically Approved for Alzheimer’s Dementia Treatment, on Intestinal Properties of the Mouse. Int. J. Mol. Sci. 2021, 22(3), 1015; doi: doi.org/10.25358/openscience-5926 - 20 Jan 2021. IF 4,56

A. Welker, C. Kersten, C. Müller, R. Madhugiri, C. Zimmer, P. Müller, R. Zimmermann, S. Hammerschmidt, H. Maus, J. Ziebuhr, C. Sotriffer, T. Schirmeister, SAR of novel benzamides and isoindolines, designed as SARS-CoV protease inhibitors – effective against SARS-CoV-2. ChemMedChem 2021, 16, 340-354, Cover page, doi: doi.org/10.1002/cmdc.202000548; IF: 3.124.

P. Johe, S. Jung, E. Endres, C. Kersten, C. Zimmer, W. Xe, C. Sönnichsen, U. A. Hellmich, C. Sotriffer, T. Schirmeister*, H. Neuweiler*, Warhead reactivity limits the speed of covalent inhibition of the cysteine protease rhodesain. ACS Chemical Biology 2021, 16, 661-670, doi: doi.org/10.1021/acschembio.0c00911 . IF: 4.434.

P. Johe, E. Jaenicke, H. Neuweiler, T. Schirmeister, C. Kersten*, U. A. Hellmich*; Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes. J. Biol. Chem. 2021, 296, 100565, doi: doi.org/10.1016/j.jbc.2021.100565. IF: 4.238

2020

García-Chamé, M. Á.; Gutiérrez-Sanz, Ó.; Ercan-Herbst, E.; Haustein, N.; Filipiak, M. S.; Ehrnhöfer, D. E.; Tarasov, A. A Transistor-Based Label-Free Immunosensor for Rapid Detection of Tau Protein. Biosens. Bioelectron. 2020, 159, 112129. IF: 10,257; doi: doi.org/10.1016/j.bios.2020.112129

Perniss A.; Liu S.; Boonen B.; Keshavarz M.; Ruppert . A. L.; Timm T., Pfeil U.; Soultanova A.; Kusumakshi S.; Delventhal L.; Aydin Ö.; Pyrski M.; Deckmann K.; Hain T.; Schmidt N.; Ewers C.; Günther A.; Lochnit G.; Chubanov V.; Gudermann T.; Oberwinkler J.; Klein J.; Mikoshiba K.; Leinders-Zufall T.; Offermanns S.; Schütz B.; Boehm U.; Zufall F.; Bufe B.; Kummer W. Chemosensory Cell-Derived Acetylcholine Drives Tracheal Mucociliary Clearance in Response to Virulence-Associated Formyl Peptides. Immunity. 2020 14;52(4):683-699.e11. doi: doi.org/10.1016/j.immuni.2020.03.005. IF: 22,6.

B. Nowduri, S. Schulte, D. Decker, K.-H. Schäfer, M. Saumer: Biomimetic nanostructures fabricated by Nanoimprint Lithography for improved cell-coupling, Adv. Funct. Mater., 2020, 30, 2004227; doi: doi.org/10.1002/adfm.202004227

Stoye N.M., dos Santos Guilherme M., Endres K. Alzheimer’s disease in the gut – major changes in the gut of 5xFAD model mice with ApoA1 as potential key player. FASEB J 2020. IF 4,97; doi: openscience.ub.uni-mainz.de/bitstream/20.500.12030/6176/1/stoye_nicolai_m.-alzheimer%27s_di-20210705102703146.pdf

L. Hofherr, C. Müller-Renno, C. Ziegler: Fluid-FM as a Tool to study adhesion forces of bacteriaoptimization of parameters and comparison to conventional bacterial probe scanning force spectroscopy, PLoS ONE 15 (7) (2020) e0227395. doi: doi.org/10.1371/journal.pone.0227395. IF:2,7

F. Barthels, G. Marincola, T. Marciniak, M. Konhäuser, S. Hammerschmidt, J. Bierlmeier, U. Distler, P. R. Wich, S. Tenzer, D. Schwarzer, W. Ziebuhr, T. Schirmeister, Asymmetric disulfanylbenzamides as irreversible and selective inhibitors of Staphylococcus aureus Sortase A. ChemMedChem 2020, 15, 839-850, doi: doi.org/10.1002/cmdc.201900687. IF: 3.124.

Knaff, P. M.; Kersten, C.; Willbold, R.; Champanhac, C.; Crespy, D.; Wittig, R.; Landfester, K.; Mailänder, V. From In Silico to Experimental Validation: Tailoring Peptide Substrates for a Serine Protease. Biomacromolecules 2020, 21 (4), 1636–1643. doi: doi.org/10.1021/acs.biomac.0c00240

Kersten, C.; Fleischer, E.; Kehrein, J.; Borek, C.; Jaenicke, E.; Sotriffer, C.; Brenk, R. How to Design Selective Ligands for Highly Conserved Binding Sites: A Case Study Using N-Myristoyltransferases as a Model System. J. Med. Chem. 2020, 63 (5), 2095–2113. doi: doi.org/10.1021/acs.jmedchem.9b00586

Welker, A.; Kersten, C.; Müller, C.; Madhugiri, R.; Zimmer, C.; Müller, P.; Zimmermann, R. A.; Hammerschmidt, S.; Maus, H.; Ziebuhr, J.; Sotriffer, C.; Schirmeister, T. SAR of Novel Benzamides and Isoindolines, Designed as SARS-CoV Protease Inhibitors – Effective against SARS-CoV-2. ChemMedChem 2020, 1–16. doi: doi.org/10.1002/cmdc.202000548

Barthels, F.; Schirmeister, T.; Kersten, C.* BANΔIT: B’-Factor Analysis for Drug Design and Structural Biology. Mol. Inform. 2020, 2000144, 1–7. doi: doi.org/10.1002/minf.202000144

2019

Haustein,.; Gutiérrez-Sanz, Ó.; Tarasov, A. Analytical Model to Describe the Effect of Polyethylene Glycol on Ionic Screening of Analyte Charges in Transistor-Based Immunosensing. ACS Sensors 2019, 4 (4), 874–882. IF: 6,944; doi: dx.doi.org/10.1021/acssensors.8b01515

Bufe B.; Teuchert Y,: Schmid A.; Pyrski M.; Pérez-Gómez A.; Eisenbeis J.; Timm T.; Ishii T.; Lochnit G.; Bischoff M.; Mombaerts P.; Leinders-Zufall T.; Zufall F. Bacterial MgrB peptide activates chemoreceptor Fpr3 in mouse accessory olfactory system and drives avoidance behaviour. Nat Commun. 2019 25;10(1):4889. doi: www.nature.com/articles/s41467-019-12842-x. IF: 12,1.

Blum T.; Moreno-Pérez A.; Pyrski M.; Bufe B.; Arifovic A.; Weissgerber P.; Freichel M.; Zufall F.; Leinders-Zufall T. Trpc5 deficiency causes hypoprolactinemia and altered function of oscillatory dopamine neurons in the arcuate nucleus. Proc Natl Acad Sci U S A. 2019 116(30):15236-15243. doi: doi.org/10.1073/pnas.1905705116.IF: 9,4.

Ana M. R. Rebelo, Yang Liu, Changqing Liu*, Karl-Herbert Schäfer, Monika Saumer, and Guang Yang: Carbon Nanotube-Reinforced Poly(4-vinylaniline)/Polyaniline Bilayer-Grafted Bacterial Cellulose for Bioelectronic Applications, ACS Biomaterials Science & Engineering 2019, 5, 2160-2172 ; doi: doi.org/10.1021/acsbiomaterials.9b00039

Lallepak Lamboni, Cheng Xu, Jasmin Clasohm, Junchuan Yang, Monika Saumer, Karl-Herbert Schäfer, Guang Yang: Silk sericin-enhanced microstructured bacterial cellulose as tissue engineering scaffold towards prospective gut repair, Materials Science and Engineering: C, 2019, 102, 502-510; doi: doi.org/10.1016/j.msec.2019.04.043

Brummer T, Müller SA, Pan-Montojo F, Yoshida F, Fellgiebel A, Tomita T, Endres K, Lichtenthaler SF. NrCAM is a marker for substrate-selective activation of ADAM10 in Alzheimer's disease. EMBO Mol Med. 2019 Apr;11(4). pii: e9695. doi: doi.org/10.15252/emmm.201809695. IF 10,62

Reinhardt S, Schuck F, Stoye N, Hartmann T, Grimm MOW, Pflugfelder G, Endres K.Transcriptional repression of the ectodomain sheddase ADAM10 by TBX2 and potential implication for Alzheimer's disease. Cell Mol Life Sci. 2019 Mar;76(5):1005-1025. doi: doi.org/10.1007/s00018-018-2998-2. Epub 2019 Jan 1. IF 7,01

S. Lach, A. Altenhof, S. Shi, M. Fahlman, Ch. Ziegler: Electronic and Magnetic Properties of a Ferromagnetic Cobalt Surface by Adsorbing Ultrathin Films of Tetracyanoethylen, Phys. Chem. Chem. Phys. 21 (2019) 15833 - 15844. doi: pubs.rsc.org/en/content/articlelanding/2019/CP/C9CP02205H IF: 3,4

B. Millies, F. v. Hammerstein, A. Gellert, S. Hammerschmidt, F. Barthels, U. Göppel, M. Immerheiser, F. Elgner, N. Jung, M. Basic, C. Kersten, W. Kiefer, J. Bodem, E. Hildt, M. Windbergs, U. A. Hellmich, T. Schirmeister, Proline-based allosteric inhibitors of Zika and Dengue NS2B/NS3 proteases. J. Med. Chem. 2019, 62, 11359-11382, doi: doi.org/10.1021/acs.jmedchem.9b01697. IF: 6.205

Millies, B.; Von Hammerstein, F.; Gellert, A.; Hammerschmidt, S.; Barthels, F.; Göppel, U.; Immerheiser, M.; Elgner, F.; Jung, N.; Basic, M.; Kersten, C.; Kiefer, W.; Bodem, J.; Hildt, E.; Windbergs, M.; Hellmich, U. A.; Schirmeister, T. Proline-Based Allosteric Inhibitors of Zika and Dengue Virus NS2B/NS3 Proteases. J. Med. Chem. 2019, 62 (24), 11359–11382. doi: doi.org/10.1021/acs.jmedchem.9b01697.

2018

Fey, P.; Chartomatsidou, R.; Kiefer, W.; Mottram, J. C.; Kersten, C.; Schirmeister, T. New Aziridine- Based Inhibitors of Cathepsin L-like Cysteine Proteases with Selectivity for the Leishmania Cysteine Protease LmCPB2.8. Eur. J. Med. Chem. 2018, 156, 587–597. doi: doi.org/10.1016/j.ejmech.2018.07.012

M. Giroud, U. Dietzel, L. Anselm, D. Banner, J.-B. Blanc, D. Gaufreteau, H. Liu, A. Stich, B. Kuhn, F. Schuler, M. Kaiser, R. Brun, T. Schirmeister, C. Kisker, F. Diederich, W. Haap, Repurposing a human cathepsin L inhibitors library: Identification of macrocyclic lactams as potent rhodesain and Trypanosoma brucei inhibitors, J. Med. Chem. 2018, 61, 3350-3369. doi: doi.org/10.1021/acs.jmedchem.7b01869. IF: 6.205.

M. Giroud, B. Kuhn, S. Saint-Auret, C. Kuratli, R. E. Martin, F. Schuler, F. Diederich, M. Kaiser, R. Brun, T. Schirmeister,* W. Haap*, 2H-1,2,3-Triazole-based dipeptidyl nitriles: potent, selective and trypanocidal rhodesain inhibitors by structure-based design. J. Med. Chem. 2018, 61, 3370-3388. doi: pubs.acs.org/doi/10.1021/acs.jmedchem.7b01870 . IF: 6.205.

K. Huttenlochner, N. Davoudi, Ch. Schlegel, M. Bohley, Ch. Müller-Renno, J.C. Aurich, R. Ulber, Ch. Ziegler: Paracoccus seriniphilus adhered on surfaces: Resistance of a seawater bacterium against shear forces under the influence of roughness, surface energy, and zeta potential of the surfaces, Biointerphases 13 (2018) 051003. doi: doi.org/10.1116/1.5049226 IF: 2,0

Reinhardt S, Stoye N, Luderer M, Kiefer F, Schmitt U, Lieb K, Endres K. Identification of disulfiram as a secretase-modulating compound with beneficial effects on Alzheimer's disease hallmarks. Sci Rep. 2018. IF 4,01; doi: www.nature.com/articles/s41598-018-19577-7

D. Decker, H. Natter, M. Pirrung, K.-H. Schäfer, H. Rabe, M. Saumer: 3D nanostructured multielectrode arrays - fabrication, characterization and investigation of cell-electrode adhesion, Adv. Mater. Technol. Vol 4 (2018); doi: doi.org/10.1002/admt.201800436

Andoy, N. M.; Filipiak, M. S.; Vetter, D.; Gutiérrez-Sanz, Ó.; Tarasov, A. Graphene-Based Electronic Immunosensor with Femtomolar Detection Limit in Whole Serum. Adv. Mater. Technol. 2018, 3 (12), 1800186. IF: 5,969; doi: doi.org/10.1002/admt.201800186

Filipiak, M. S.; Rother, M.; Andoy, N. M.; Knudsen, A. C.; Grimm, S.; Bachran, C.; Swee, L. K.; Zaumseil, J.; Tarasov, A. Highly Sensitive, Selective and Label-Free Protein Detection in Physiological Solutions Using Carbon Nanotube Transistors with Nanobody Receptors. Sens. Actuators B Chem. 2018, 255, 1507. IF: 7,100; doi: doi.org/10.1016/j.snb.2017.08.164

2017

Gutiérrez-Sanz, Ó.; Andoy, N. M.; Filipiak, M. S.; Haustein, N.; Tarasov, A. Direct, Label-Free, and Rapid Transistor-Based Immunodetection in Whole Serum. ACS Sensors 2017, 2 (9), 1278–1286. IF: 6,944; doi: doi.org/10.1021/acssensors.7b00187

Endres, K, Deller, T. Regulation of Alpha-Secretase ADAM10 In vitro and In vivo: Genetic, Epigenetic, and Protein-Based Mechanisms. FRONTIERS IN MOLECULAR NEUROSCIENCE Volume: 10 Article Number: 56 Published: MAR 17 2017, IF 5,08; doi: doi.org/10.1016/j.biopha.2019.108661

V. Rink, C. Müller-Renno, Ch. Ziegler, M. Braun, K. Boonrod, G. Krczal: Electrostatic conditions define the 2D self-assembly of tomato bushy stunt viruses on solid surfaces, Biointerphases 12 (2017) 04E402. doi: dx.doi.org/10.1116/1.4986055 IF: 2,0

N. Davoudi, K. Huttenlochner, J. Chodorski, C. Schlegel, M. Bohley, C. Müller-Renno, J.C. Aurich, R. Ulber, Ch. Ziegler: Adhesion forces of the sea-water bacterium Paracoccus seriniphilus on titanium: Influence of microstructures and environmental conditions, Biointerphases 12 (2017) 05G606. doi: doi.org/10.1116/1.5002676 IF: 2,0

Ch. Rösch, F. Kratz, Th. Hering, S. Trautmann, N. Umanskaya, N. Tippkötter, Ch. Müller-Renno, R. Ulber, M. Hannig, Ch. Ziegler: Albumin-Lysozyme Interactions: Cooperative Adsorption on Titanium and Enzymatic Activity, Colloids Surf. B 149 (2017) 115–121. doi: dx.doi.org/10.1016/j.colsurfb.2016.09.048 IF: 3,1

B. Kuhn, M. Tichý, L. Wang, S. Robinson, R. Martin, A. Kuglstatter, J. Benz, M. Giroud, T. Schirmeister, R. Abel, F. Diederich, J. Hert, Prospective evaluation of free energy calculations for the prioritization of cathepsin L inhibitors. J. Med. Chem. 2017, 60, 2485-2497. doi: doi.org/10.1021/acs.jmedchem.6b01881. IF: 6.205.