@article{SchellerScheller1996,
  author    = {Scheller, Frieder W. and Scheller, A.},
  title     = {Bi-Enzymelektrode zur Messung von Sorbitol in pharmazeutischen Produkten},
  year      = {1996},
  language  = {de}
}
@article{BanksNishiyamaHasebeetal.2011,
  author    = {Banks, Jo Ann and Nishiyama, Tomoaki and Hasebe, Mitsuyasu and Bowman, John L. and Gribskov, Michael and dePamphilis, Claude and Albert, Victor A. and Aono, Naoki and Aoyama, Tsuyoshi and Ambrose, Barbara A. and Ashton, Neil W. and Axtell, Michael J. and Barker, Elizabeth and Barker, Michael S. and Bennetzen, Jeffrey L. and Bonawitz, Nicholas D. and Chapple, Clint and Cheng, Chaoyang and Correa, Luiz Gustavo Guedes and Dacre, Michael and DeBarry, Jeremy and Dreyer, Ingo and Elias, Marek and Engstrom, Eric M. and Estelle, Mark and Feng, Liang and Finet, Cedric and Floyd, Sandra K. and Frommer, Wolf B. and Fujita, Tomomichi and Gramzow, Lydia and Gutensohn, Michael and Harholt, Jesper and Hattori, Mitsuru and Heyl, Alexander and Hirai, Tadayoshi and Hiwatashi, Yuji and Ishikawa, Masaki and Iwata, Mineko and Karol, Kenneth G. and Koehler, Barbara and Kolukisaoglu, Uener and Kubo, Minoru and Kurata, Tetsuya and Lalonde, Sylvie and Li, Kejie and Li, Ying and Litt, Amy and Lyons, Eric and Manning, Gerard and Maruyama, Takeshi and Michael, Todd P. and Mikami, Koji and Miyazaki, Saori and Morinaga, Shin-ichi and Murata, Takashi and M{\"u}ller-R{\"o}ber, Bernd and Nelson, David R. and Obara, Mari and Oguri, Yasuko and Olmstead, Richard G. and Onodera, Naoko and Petersen, Bent Larsen and Pils, Birgit and Prigge, Michael and Rensing, Stefan A. and Mauricio Riano-Pachon, Diego and Roberts, Alison W. and Sato, Yoshikatsu and Scheller, Henrik Vibe and Schulz, Burkhard and Schulz, Christian and Shakirov, Eugene V. and Shibagaki, Nakako and Shinohara, Naoki and Shippen, Dorothy E. and Sorensen, Iben and Sotooka, Ryo and Sugimoto, Nagisa and Sugita, Mamoru and Sumikawa, Naomi and Tanurdzic, Milos and Theissen, Guenter and Ulvskov, Peter and Wakazuki, Sachiko and Weng, Jing-Ke and Willats, William W. G. T. and Wipf, Daniel and Wolf, Paul G. and Yang, Lixing and Zimmer, Andreas D. and Zhu, Qihui and Mitros, Therese and Hellsten, Uffe and Loque, Dominique and Otillar, Robert and Salamov, Asaf and Schmutz, Jeremy and Shapiro, Harris and Lindquist, Erika and Lucas, Susan and Rokhsar, Daniel and Grigoriev, Igor V.},
  title     = {The selaginella genome identifies genetic changes associated with the evolution of vascular plants},
  series = {Science},
  volume    = {332},
  journal   = {Science},
  number    = {6032},
  publisher = {American Assoc. for the Advancement of Science},
  address   = {Washington},
  issn      = {0036-8075},
  doi       = {10.1126/science.1203810},
  pages     = {960 -- 963},
  year      = {2011},
  abstract  = {Vascular plants appeared similar to 410 million years ago, then diverged into several lineages of which only two survive: the euphyllophytes (ferns and seed plants) and the lycophytes. We report here the genome sequence of the lycophyte Selaginella moellendorffii (Selaginella), the first nonseed vascular plant genome reported. By comparing gene content in evolutionarily diverse taxa, we found that the transition from a gametophyte- to a sporophyte-dominated life cycle required far fewer new genes than the transition from a nonseed vascular to a flowering plant, whereas secondary metabolic genes expanded extensively and in parallel in the lycophyte and angiosperm lineages. Selaginella differs in posttranscriptional gene regulation, including small RNA regulation of repetitive elements, an absence of the trans-acting small interfering RNA pathway, and extensive RNA editing of organellar genes.},
  language  = {en}
}
@article{SchellerMakowerBieretal.1995,
  author    = {Scheller, Frieder W. and Makower, Alexander and Bier, Frank Fabian and Wollenberger, Ursula and Ghindilis, A. L. and Eremenko, A. V. and Pfeiffer, Dorothea},
  title     = {Enzymsensoren zur Bestimmung subnanomolarer Konzentrationen},
  year      = {1995},
  language  = {de}
}
@article{FreaneyMacShaneKeavenyetal.1997,
  author    = {Freaney, R. and MacShane, A. and Keaveny, T. V. and MacKenna, M. and Rabenstein, K. and Scheller, Frieder W. and Pfeiffer, Dorothea and Urban, G. and Moser, I. and Jobst, G. and Manz, A. and Verpoorte, E. and Widmer, M. W. and Diamond, D. and Dempsey, E. and deViteri, F. J. S. and Smyth, M.},
  title     = {Novel instrumentation for real-time monitoring using miniaturized flow systems with integrated biosensors},
  year      = {1997},
  language  = {en}
}
@article{BauerEremenkoKuehnetal.1998,
  author    = {Bauer, Christian G. and Eremenko, A. V. and K{\"u}hn, A. and K{\"u}rzinger, K. and Markower, Alexander and Scheller, Frieder W.},
  title     = {Automated amplifield flow immunoassay for cocaine},
  year      = {1998},
  language  = {en}
}
@article{FridmanWollenbergerBogdanovskayaetal.2000,
  author    = {Fridman, Vadim and Wollenberger, Ursula and Bogdanovskaya, V. A. and Lisdat, Fred and Ruzgas, T. and Lindgren, A. and Gorton, Lo and Scheller, Frieder W.},
  title     = {Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator},
  year      = {2000},
  language  = {en}
}
@article{KappBeissenhirtzGeyeretal.2006,
  author    = {Kapp, A. and Beissenhirtz, Moritz Karl and Geyer, F. and Scheller, F. and Viezzoli, Maria Silvia and Lisdat, Fred},
  title     = {Electrochemical and sensorial behavior of SOD mutants immobilized on gold electrodes in aqueous/organic solvent mixtures},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {18},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.200603620},
  pages     = {1909 -- 1915},
  year      = {2006},
  abstract  = {A cysteine mutant of a monomeric human Cu, Zn-SOD (Glycine 61, Serine 142) has been immobilized directly on gold electrodes using the thiol groups introduced. The electrochemical behavior of the surface confined protein was studied in mixtures of aqueous buffer and DMSO up to an organic solvent content of 60\%. The formal potential was found to be rather independent of the DMSO content. However, half peak width increased and the redoxactive amount clearly decreased with raising DMSO content. In addition, the kinetics of the heterogeneous electron transfer became slower; but still a quasireversible electrochemical conversion of the mutant SOD was feasible. Thus, the electrodes were applied for sensorial superoxide detection. At a potential of +220 mV vs. Ag/AgCl advantage was taken of the partial oxidation reaction of the enzyme. A defined superoxide signal was obtained in solutions up to 40\% DMSO. The sensitivity of the mutant electrodes decreased linearly with the organic solvent content in solution but was still higher compared to conventional cyt.c based sensors. At DMSO concentrations higher than 40\% no sensor response was detected.},
  language  = {en}
}
@article{OzcelikayKurbanogluZhangetal.2019,
  author    = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Zhang, Xiaorong and S{\"o}z, {\c{C}}ağla Kosak and Wollenberger, Ulla and Ozkan, Sibel A. and Yarman, Aysu and Scheller, Frieder W.},
  title     = {Electrochemical MIP Sensor for Butyrylcholinesterase},
  series = {Polymers},
  volume    = {11},
  journal   = {Polymers},
  number    = {12},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2073-4360},
  doi       = {10.3390/polym11121970},
  pages     = {11},
  year      = {2019},
  abstract  = {Molecularly imprinted polymers (MIPs) mimic the binding sites of antibodies by substituting the amino acid-scaffold of proteins by synthetic polymers. In this work, the first MIP for the recognition of the diagnostically relevant enzyme butyrylcholinesterase (BuChE) is presented. The MIP was prepared using electropolymerization of the functional monomer o-phenylenediamine and was deposited as a thin film on a glassy carbon electrode by oxidative potentiodynamic polymerization. Rebinding and removal of the template were detected by cyclic voltammetry using ferricyanide as a redox marker. Furthermore, the enzymatic activity of BuChE rebound to the MIP was measured via the anodic oxidation of thiocholine, the reaction product of butyrylthiocholine. The response was linear between 50 pM and 2 nM concentrations of BuChE with a detection limit of 14.7 pM. In addition to the high sensitivity for BuChE, the sensor responded towards pseudo-irreversible inhibitors in the lower mM range.},
  language  = {en}
}
@article{BistolasChristensonRuzgasetal.2004,
  author    = {Bistolas, Nikitas and Christenson, A. and Ruzgas, T. and Jung, Christiane and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Spectroelectrochemistry of cytochrome P450cam},
  year      = {2004},
  abstract  = {The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4'-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4'-dithiodipyridin and dithionite modified electrodes. A formal potential (E-0') of -373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis. (C) 2003 Elsevier Inc. All rights reserved},
  language  = {en}
}
@article{LeiWollenbergerBistolasetal.2002,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Bistolas, Nikitas and Guiseppi-Eli, A. and Scheller, Frieder W.},
  title     = {Electron transfer of hemoglobin at electrodes modified with colloidal clay nanoparticles},
  year      = {2002},
  language  = {en}
}
@article{ButtermeyerPhilippMalletal.2002,
  author    = {Buttermeyer, R. and Philipp, A. W. and Mall, J. W. and Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred},
  title     = {In vivo measurement of oxygen derived free radicals during reperfusion injury},
  year      = {2002},
  language  = {en}
}
@article{OzcelikayKurbanogluYarmanetal.2020,
  author    = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Yarman, Aysu and Scheller, Frieder W. and Ozkan, Sibel A.},
  title     = {Au-Pt nanoparticles based molecularly imprinted nanosensor for electrochemical detection of the lipopeptide antibiotic drug Daptomycin},
  series = {Sensors and actuators : B, Chemical},
  volume    = {320},
  journal   = {Sensors and actuators : B, Chemical},
  publisher = {Elsevier Science},
  address   = {Amsterdam},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2020.128285},
  pages     = {7},
  year      = {2020},
  abstract  = {In this work, a novel electrochemical molecularly imprinted polymer (MIP) sensor for the detection of the lipopeptide antibiotic Daptomycin (DAP) is presented which integrates gold decorated platinum nanoparticles (Au-Pt NPs) into the nanocomposite film. The sensor was prepared by electropolymerization of o-phenylenediamine (o-PD) in the presence of DAP using cyclic voltammetry. Cyclic voltammetry and differential pulse voltammetry were applied to follow the changes in the MIP-layer related to rebinding and removal of the target DAP by using the redox marker [Fe(CN)(6)](3-/4-). Under optimized operational conditions, the MIP/Au-Pt NPs/ GCE nanosensor exhibits a linear response in the range of 1-20 pM towards DAP. The limit of detection and limit of quantification were determined to be 0.161pM +/- 0.012 and 0.489pM +/- 0.012, respectively. The sensitivity towards the antibiotics Vancomycin and Erythromycin and the amino acids glycine and tryptophan was below 7 percent as compared with DAP. Moreover, the nanosensor was also successfully used for the detection of DAP in deproteinated human serum samples.},
  language  = {en}
}
@article{JetzschmannYarmanRustametal.2018,
  author    = {Jetzschmann, Katharina J. and Yarman, Aysu and Rustam, L. and Kielb, P. and Urlacher, V. B. and Fischer, A. and Weidinger, I. M. and Wollenberger, Ulla and Scheller, Frieder W.},
  title     = {Molecular LEGO by domain-imprinting of cytochrome P450 BM3},
  series = {Colloids and surfaces : an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin ; B, Biointerfaces},
  volume    = {164},
  journal   = {Colloids and surfaces : an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin ; B, Biointerfaces},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0927-7765},
  doi       = {10.1016/j.colsurfb.2018.01.047},
  pages     = {240 -- 246},
  year      = {2018},
  abstract  = {Hypothesis: Electrosynthesis of the MIP nano-film after binding of the separated domains or holocytochrome BM3 via an engineered anchor should result in domain-specific cavities in the polymer layer. Experiments: Both the two domains and the holo P450 BM3 have been bound prior polymer deposition via a N-terminal engineered his6-anchor to the electrode surface. Each step of MIP preparation was characterized by cyclic voltammetry of the redox-marker ferricyanide. Rebinding after template removal was evaluated by quantifying the suppression of the diffusive permeability of the signal for ferricyanide and by the NADH-dependent reduction of cytochrome c by the reductase domain (BMR). Findings: The working hypothesis is verified by the discrimination of the two domains by the respective MIPs: The holoenzyme P450 BM3 was ca. 5.5 times more effectively recognized by the film imprinted with the oxidase domain (BMO) as compared to the BMR-MIP or the non-imprinted polymer (NIP). Obviously, a cavity is formed during the imprinting process around the hiss-tag-anchored BMR which cannot accommodate the broader BMO or the P450 BM3. The affinity of the MIP towards P450 BM3 is comparable with that to the monomer in solution. The hiss-tagged P450 BM3 binds (30 percent) stronger which shows the additive effect of the interaction with the MIP and the binding to the electrode.},
  language  = {en}
}
@article{AltintasTakidenUteschetal.2019,
  author    = {Altintas, Zeynep and Takiden, Aref and Utesch, Tillmann and Mroginski, Maria A. and Schmid, Bianca and Scheller, Frieder W. and S{\"u}ssmuth, Roderich D.},
  title     = {Integrated approaches toward high-affinity artificial protein binders obtained via computationally simulated epitopes for protein recognition},
  series = {Advanced functional materials},
  volume    = {29},
  journal   = {Advanced functional materials},
  number    = {15},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-301X},
  doi       = {10.1002/adfm.201807332},
  pages     = {11},
  year      = {2019},
  abstract  = {Widely used diagnostic tools make use of antibodies recognizing targeted molecules, but additional techniques are required in order to alleviate the disadvantages of antibodies. Herein, molecular dynamic calculations are performed for the design of high affinity artificial protein binding surfaces for the recognition of neuron specific enolase (NSE), a known cancer biomarker. Computational simulations are employed to identify particularly stabile secondary structure elements. These epitopes are used for the subsequent molecular imprinting, where surface imprinting approach is applied. The molecular imprints generated with the calculated epitopes of greater stability (Cys-Ep1) show better binding properties than those of lower stability (Cys-Ep5). The average binding strength of imprints created with stabile epitopes is found to be around twofold and fourfold higher for the NSE derived peptide and NSE protein, respectively. The recognition of NSE is investigated in a wide concentration range, where high sensitivity (limit of detection (LOD) = 0.5 ng mL(-1)) and affinity (dissociation constant (K-d) = 5.3 x 10(-11)m) are achieved using Cys-Ep1 imprints reflecting the stable structure of the template molecules. This integrated approach employing stability calculations for the identification of stabile epitopes is expected to have a major impact on the future development of high affinity protein capturing binders.},
  language  = {en}
}
@misc{YarmanKurbanogluJetzschmannetal.2018,
  author    = {Yarman, Aysu and Kurbanoglu, Sevinc and Jetzschmann, Katharina J. and Ozkan, Sibel A. and Wollenberger, Ulla and Scheller, Frieder W.},
  title     = {Electrochemical MIP-Sensors for Drugs},
  series = {Current Medicinal Chemistry},
  volume    = {25},
  journal   = {Current Medicinal Chemistry},
  number    = {33},
  publisher = {Bentham Science Publishers LTD},
  address   = {Sharjah},
  issn      = {0929-8673},
  doi       = {10.2174/0929867324666171005103712},
  pages     = {4007 -- 4019},
  year      = {2018},
  abstract  = {In order to replace bio-macromolecules by stable synthetic materials in separation techniques and bioanalysis biomimetic receptors and catalysts have been developed: Functional monomers are polymerized together with the target analyte and after template removal cavities are formed in the "molecularly imprinted polymer" (MIP) which resemble the active sites of antibodies and enzymes. Starting almost 80 years ago, around 1,100 papers on MIPs were published in 2016. Electropolymerization allows to deposit MIPs directly on voltammetric electrodes or chips for quartz crystal microbalance (QCM) and surface plasmon resonance (SPR). For the readout of MIPs for drugs amperometry, differential pulse voltammetry (DPV) and impedance spectroscopy (EIS) offer higher sensitivity as compared with QCM or SPR. Application of simple electrochemical devices allows both the reproducible preparation of MIP sensors, but also the sensitive signal generation. Electrochemical MIP-sensors for the whole arsenal of drugs, e.g. the most frequently used analgesics, antibiotics and anticancer drugs have been presented in literature and tested under laboratory conditions. These biomimetic sensors typically have measuring ranges covering the lower nano-up to millimolar concentration range and they are stable under extreme pH and in organic solvents like nonaqueous extracts.},
  language  = {en}
}
@misc{OzcelikayKurbanogluZhangetal.2019,
  author    = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Zhang, Xiaorong and S{\"o}z, {\c{C}}ağla Kosak and Wollenberger, Ulla and Ozkan, Sibel A. and Yarman, Aysu and Scheller, Frieder W.},
  title     = {Electrochemical MIP Sensor for Butyrylcholinesterase},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1138},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-50185},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-501854},
  pages     = {13},
  year      = {2019},
  abstract  = {Molecularly imprinted polymers (MIPs) mimic the binding sites of antibodies by substituting the amino acid-scaffold of proteins by synthetic polymers. In this work, the first MIP for the recognition of the diagnostically relevant enzyme butyrylcholinesterase (BuChE) is presented. The MIP was prepared using electropolymerization of the functional monomer o-phenylenediamine and was deposited as a thin film on a glassy carbon electrode by oxidative potentiodynamic polymerization. Rebinding and removal of the template were detected by cyclic voltammetry using ferricyanide as a redox marker. Furthermore, the enzymatic activity of BuChE rebound to the MIP was measured via the anodic oxidation of thiocholine, the reaction product of butyrylthiocholine. The response was linear between 50 pM and 2 nM concentrations of BuChE with a detection limit of 14.7 pM. In addition to the high sensitivity for BuChE, the sensor responded towards pseudo-irreversible inhibitors in the lower mM range.},
  language  = {en}
}
@article{KleinjungKlussmannErdmannetal.1998,
  author    = {Kleinjung, Frank and Klußmann, S. and Erdmann, V. A. and Scheller, Frieder W. and F{\"u}rste, J. P. and Bier, Frank Fabian},
  title     = {Novel binders in biosensorics : hight affinity RNA for smal analytes},
  year      = {1998},
  language  = {en}
}
@article{BierEhrentreichFoersterDoellingetal.1997,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and D{\"o}lling, R. and Eremenko, A. V. and Scheller, Frieder W.},
  title     = {A redox-label immunosensor on basis of a bi-enzyme electrode},
  year      = {1997},
  language  = {en}
}
@article{BierFuersteKleinjungetal.1997,
  author    = {Bier, Frank Fabian and F{\"u}rste, J. P. and Kleinjung, Frank and Erdmann, V. A. and Scheller, Frieder W.},
  title     = {Nukleins{\"a}uren als Basis f{\"u}r Biosensoren},
  year      = {1997},
  language  = {de}
}
@article{BauerEremenkoEhrentreichFoersteretal.1996,
  author    = {Bauer, Christian G. and Eremenko, A. V. and Ehrentreich-F{\"o}rster, Eva and Bier, Frank Fabian and Makower, Alexander and Halsall, H. B. and Heineman, W. R. and Scheller, Frieder W.},
  title     = {Zeptomole-detecting biosensor for alkaline phosphatase in an electroche mical immunoassay for 2,4- dichlorophenoacetic acid},
  year      = {1996},
  language  = {en}
}
@article{BierEhrentreichFoersterSchelleretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W. and Makower, Alexander and Eremenko, A. V. and Wollenberger, Ursula and Bauer, Christian G. and Pfeiffer, Dorothea and Micheel, Burkhard},
  title     = {Ultrasensitive biosensors},
  year      = {1996},
  language  = {en}
}
@article{GhindilisMakowerBaueretal.1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Bauer, Christian G. and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Determination of p-aminophenol and catecholamines at picomolar concentrations based on recycling enzyme amplification},
  year      = {1995},
  language  = {en}
}
@article{SchellerMakowerGhindilisetal.1995,
  author    = {Scheller, Frieder W. and Makower, Alexander and Ghindilis, A. L. and Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Wollenberger, Ursula and Bauer, Christian G. and Micheel, Burkhard and Pfeiffer, Dorothea and Szeponik, Jan and Michael, N. and Kaden, H.},
  title     = {Enzyme sensors for subnanomolar concentrations},
  year      = {1995},
  language  = {en}
}
@article{EremenkoMakowerBaueretal.1997,
  author    = {Eremenko, A. V. and Makower, Alexander and Bauer, Christian G. and Kurochkin, I. N. and Scheller, Frieder W.},
  title     = {A bienzyme electrode for tyrosine containing peptides determination},
  year      = {1997},
  language  = {en}
}
@article{KulysDrungilieneWollenbergeretal.1997,
  author    = {Kulys, J. and Drungiliene, A. and Wollenberger, Ursula and Krikstopaitis, K. and Scheller, Frieder W.},
  title     = {Electroanalytical determination of peroxidases and laccases on carbon paste electrodes},
  year      = {1997},
  language  = {en}
}
@article{WollenbergerDrungilieneStoeckleinetal.1996,
  author    = {Wollenberger, Ursula and Drungiliene, A. and St{\"o}cklein, Walter F. M. and Kulys, J. and Scheller, Frieder W.},
  title     = {Direct electrocatalytic determination of dissolved peroxidases},
  year      = {1996},
  language  = {en}
}
@article{KaishevaIlievKazarevaetal.1996,
  author    = {Kaisheva, A. and Iliev, I. and Kazareva, R. and Christov, S. and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Enzyme/gas diffusion electrodes for determination of phenol},
  year      = {1996},
  language  = {en}
}
@article{MakowerEremenkoStrefferetal.1996,
  author    = {Makower, Alexander and Eremenko, A. V. and Streffer, Katrin and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Tyrosinase-glucose dehydrogenase substrate-recycling biosensor : a highly sensitive measurement of phenolic compounds},
  year      = {1996},
  language  = {en}
}
@article{EremenkoMakowerScheller1995,
  author    = {Eremenko, A. V. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Measurement of nanomolar diphenols by substrate recycling coupled to a pH- sensitive electrode},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Laccase - glucose dehydrogenase recycling enzyme electrode based on potentiometric mediatorless electrocatalytic detection},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Nanomolar determination of the ferrocene derivatives using a recycling enzyme electrode : development of the redox label immunoassay},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Potentiometric enzyme electrodes based on substrate recycling and mediatorless bioelectrocatalysis},
  year      = {1995},
  language  = {en}
}
@article{EremenkoMakowerJinetal.1995,
  author    = {Eremenko, A. V. and Makower, Alexander and Jin, Wen and R{\"u}ger, P. and Scheller, Frieder W.},
  title     = {Biosensor based on an enzyme modified electrode for highly - sensitive measurement of polyphenols},
  year      = {1995},
  language  = {en}
}
@article{IlievKaishevaSchelleretal.1995,
  author    = {Iliev, I. and Kaisheva, A. and Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Amperometric gas-diffusion / enzyme electrode},
  year      = {1995},
  language  = {en}
}
@article{KulysDrungilieneWollenbergeretal.1998,
  author    = {Kulys, J. and Drungiliene, A. and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Membrane covered carbon paste electrode for the electrochemical determination of perioxidase and microperoxidase in a flow system},
  year      = {1998},
  language  = {en}
}
@article{BogdanovskayaFridmanTarasevichetal.1994,
  author    = {Bogdanovskaya, V. A. and Fridman, Vadim and Tarasevich, M. R. and Scheller, Frieder W.},
  title     = {Bioelectrocatalysis by immobilized peroxidase : the reaction mechanism and the possibility of electroanalytical detection of both inhibitors and activators of enzyme},
  year      = {1994},
  language  = {en}
}
@article{VijgenboomVijgenboomTeppneretal.2001,
  author    = {Vijgenboom, E. and Vijgenboom, E. and Teppner, A. W. J. W. and Makower, Alexander and Scheller, Frieder W. and Canters, Gerard W. and Wollenberger, Ursula},
  title     = {Determination of phenolic compounds using recombinant tyrosinanse from Streptomyces antibioticus},
  year      = {2001},
  language  = {en}
}
@article{SigolaevaMarkowerEremenkoetal.2001,
  author    = {Sigolaeva, L. V. and Markower, Alexander and Eremenko, A. V. and Makhaeva, G. F. and Malygin, V. V. and Kurochkin, I. N. and Scheller, Frieder W.},
  title     = {Bioelectrochemical anaysis of neuropathy targes esterase activity in blood},
  year      = {2001},
  language  = {en}
}
@article{LisdatGeKrauseetal.2001,
  author    = {Lisdat, Fred and Ge, Bixia and Krause, B. and Ehrlich, A. and Bienert, H. and Scheller, Frieder W.},
  title     = {Nucleic acid-promoted electron transfer to cytochrome c},
  year      = {2001},
  language  = {en}
}
@article{GajovicBinyaminWarsinkeetal.2000,
  author    = {Gajovic, Nenad and Binyamin, Gary and Warsinke, Axel and Scheller, Frieder W. and Heller, A.},
  title     = {Operation of a miniature redox hydrogel-based pyruvate sensor in undiluted deoxygenated calf serum},
  year      = {2000},
  language  = {en}
}
@article{BauerKuehnGajovicetal.1999,
  author    = {Bauer, Christian G. and K{\"u}hn, A. and Gajovic, Nenad and Skorobogatko, O. V. and Holt, P. J. and Bruce, N. C. and Makower, Alexander and Lowe, Ch. R. and Scheller, Frieder W.},
  title     = {New enzymen sensors for morphine and codeine based on morphine dehydrogenase and laccase},
  year      = {1999},
  language  = {en}
}
@article{SchellerKleinjungBieretal.1998,
  author    = {Scheller, Frieder W. and Kleinjung, Frank and Bier, Frank Fabian and Markower, Alexander and Neumann, Barbara and Wollenberger, Ursula and Kurochkin, Iliya N. and Eremenko, Arkadi V. and Barmin, Anatoli V. and Klußmann, Sven and F{\"u}rste, Jens-Peter and Erdmann, Volker A. and Mansuy, D.},
  title     = {New recognition elements in biosensing},
  year      = {1998},
  language  = {en}
}