@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{SchellerSchubertBier1995,
  author    = {Scheller, Frieder W. and Schubert, Florian and Bier, Frank Fabian},
  title     = {Vom Biosensor zur Nanobiotechnologie},
  year      = {1995},
  language  = {de}
}
@article{JetzschmannJagerszkiDechtriratetal.2015,
  author    = {Jetzschmann, Katharina J. and Jagerszki, Gyula and Dechtrirat, Decha and Yarman, Aysu and Gajovic-Eichelmann, Nenad and Gilsing, Hans-Detlev and Schulz, Burkhard and Gyurcsanyi, Robert E. and Scheller, Frieder W.},
  title     = {Vectorially Imprinted Hybrid Nanofilm for Acetylcholinesterase Recognition},
  series = {Advanced functional materials},
  volume    = {25},
  journal   = {Advanced functional materials},
  number    = {32},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-301X},
  doi       = {10.1002/adfm.201501900},
  pages     = {5178 -- 5183},
  year      = {2015},
  abstract  = {Effective recognition of enzymatically active tetrameric acetylcholinesterase (AChE) is accomplished by a hybrid nanofilm composed of a propidium-terminated self-assembled monolayer (Prop-SAM) which binds AChE via its peripheral anionic site (PAS) and an ultrathin electrosynthesized molecularly imprinted polymer (MIP) cover layer of a novel carboxylate-modified derivative of 3,4-propylenedioxythiophene. The rebinding of the AChE to the MIP/Prop-SAM nanofilm covered electrode is detected by measuring in situ the enzymatic activity. The oxidative current of the released thiocholine is dependent on the AChE concentration from approximate to 0.04 x 10(-6) to 0.4 x 10(-6)m. An imprinting factor of 9.9 is obtained for the hybrid MIP, which is among the best values reported for protein imprinting. The dissociation constant characterizing the strength of the MIP-AChE binding is 4.2 x 10(-7)m indicating the dominant role of the PAS-Prop-SAM interaction, while the benefit of the MIP nanofilm covering the Prop-SAM layer is the effective suppression of the cross-reactivity toward competing proteins as compared with the Prop-SAM. The threefold selectivity gain provided by i) the shape-specific MIP filter, ii) the propidium-SAM, iii) signal generation only by the AChE bound to the nanofilm shows promise for assessing AChE activity levels in cerebrospinal fluid.},
  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{SzeponikMoellerPfeifferetal.1997,
  author    = {Szeponik, Jan and M{\"o}ller, B. and Pfeiffer, Dorothea and Lisdat, Fred and Wollenberger, Ursula and Makower, Alexander and Scheller, Frieder W.},
  title     = {Ultrasensitive bienzyme sensor for adrenaline},
  year      = {1997},
  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{Scheller2009,
  author    = {Scheller, Frieder W.},
  title     = {Tribute to Guenter Gauglitz (Editorial)},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-008-2548-0},
  year      = {2009},
  language  = {en}
}
@article{SchellerBier2002,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Trends in der Bioanalytik},
  year      = {2002},
  language  = {de}
}
@article{NiessnerBroekaertEinaxetal.2002,
  author    = {Nießner, Reinhard and Broekaert, J. and Einax, J. W. and Scheller, Frieder W. and St{\"o}cklein, Walter F. M.},
  title     = {Trendbericht analytische Biochemie 2000/2001},
  year      = {2002},
  language  = {de}
}
@article{SchellerBistolasLiuetal.2005,
  author    = {Scheller, Frieder W. and Bistolas, Nikitas and Liu, Songqin and J{\"a}nchen, Michael and Katterle, Martin and Wollenberger, Ursula},
  title     = {Thirty years of haemoglobin electrochemistry},
  year      = {2005},
  abstract  = {Electrochemical investigations of the blood oxygen carrier protein include both mediated and direct electron transfer. The reaction of haemoglobin (Hb) with typical mediators, e.g., ferricyanide, can be quantified by measuring the produced ferrocyanide which is equivalent to the Hb concentration. Immobilization of the mediator within the electrode body allows reagentless electrochemical measuring of Hb. On the other hand, entrapment of the protein within layers of polyclectrolytes, lipids, nanoparticles of clay or gold leads to a fast heterogeneous electron exchange of the partially denatured Hb. (c) 2005 Elsevier B.V. All rights reserved},
  language  = {en}
}
@article{YarmanSchulzSygmundetal.2014,
  author    = {Yarman, Aysu and Schulz, Christopher and Sygmund, Cristoph and Ludwig, Roland and Gorton, Lo and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Third generation ATP sensor with enzymatic analyte recycling},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {26},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201400231},
  pages     = {2043 -- 2048},
  year      = {2014},
  abstract  = {For the first time the direct electron transfer of an enzyme - cellobiose dehydrogenase, CDH - has been coupled with the hexokinase catalyzed competition for glucose in a sensor for ATP. To enhance the signal output for ATP, pyruvate kinase was coimmobilized to recycle ADP by the phosphoenolpyruvate driven reaction. The new sensor overcomes the limit of 1:1 stoichiometry of the sequential or competitive conversion of ATP by effective enzymatic recycling of the analyte. The anodic oxidation of the glucose converting CDH proceeds at electrode potentials below 0 mV vs. Ag vertical bar AgCl thus potentially interfering substances like ascorbic acid or catecholamines do not influence the measuring signal. The combination of direct electron transfer of CDH with the enzymatic recycling results in an interference-free and oxygen-independent measurement of ATP in the lower mu molar concentration range with a lower limit of detection of 63.3 nM (S/N=3).},
  language  = {en}
}
@article{KrylovBeissenhirtzAdamzigetal.2004,
  author    = {Krylov, Andrey V. and Beissenhirtz, Moritz Karl and Adamzig, Holger and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Thick-film electrodes for measurement of superoxide and hydrogen peroxide based on direct protein-electrode contacts},
  year      = {2004},
  abstract  = {Cytochrome c was immobilized on screen-printed thick-film gold electrodes by a self-assembly approach using mixed monolayers of mercaptoundecanoic acid and mercaptoundecanol. Cyclic voltammetry revealed quasi-reversible electrochemical behavior of the covalently fixed protein with a formal potential of +10 mV vs. Ag/AgCl. Polarized at +150 mV vs. Ag/AgCl the electrode was found to be sensitive to superoxide radicals in the range 300-1200 nmol L-1. Compared with metal needle electrodes sensitivity and reproducibility could be improved and combined with the easiness of preparation. This allows the fabrication of disposable sensors for nanomolar superoxide concentrations. By changing the electrode potential the sensor can be switched from response to superoxide radicals to hydrogen peroxide-another reactive oxygen species. H2O2 sensitivity can be provided in the range 10-1000 mumol L-1 which makes the electrode suitable for oxidative stress studies},
  language  = {en}
}
@misc{YarmanScheller2014,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {The first electrochemical MIP sensor for tamoxifen},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1046},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47617},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-476173},
  pages     = {10},
  year      = {2014},
  abstract  = {We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.},
  language  = {en}
}
@article{YarmanScheller2014,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {The first electrochemical MIP sensor for tamoxifen},
  series = {Sensors},
  volume    = {14},
  journal   = {Sensors},
  number    = {5},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s140507647},
  pages     = {7647 -- 7654},
  year      = {2014},
  abstract  = {We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.},
  language  = {en}
}
@article{SpricigoLeimkuehlerGortonetal.2015,
  author    = {Spricigo, Roberto and Leimk{\"u}hler, Silke and Gorton, Lo and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active},
  series = {European journal of inorganic chemistry : a journal of ChemPubSoc Europe},
  journal   = {European journal of inorganic chemistry : a journal of ChemPubSoc Europe},
  number    = {21},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1434-1948},
  doi       = {10.1002/ejic.201500034},
  pages     = {3526 -- 3531},
  year      = {2015},
  abstract  = {We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25\% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices.},
  language  = {en}
}
@article{EremenkoBauerMakoweretal.1998,
  author    = {Eremenko, Arkadi V. and Bauer, Christian G. and Makower, Alexander and Kanne, Beate and Baumgarten, Horst and Scheller, Frieder W.},
  title     = {The development of a non-competitive immunoenzymometric Assay (IEMA) of cocaine},
  year      = {1998},
  language  = {en}
}
@article{HuangWarsinkeKuwanaetal.1998,
  author    = {Huang, T. and Warsinke, Axel and Kuwana, T. and Scheller, Frieder W.},
  title     = {The determination of L-phenylalanine based on a novel NADH-detecting biosensor},
  year      = {1998},
  language  = {en}
}
@article{YarmanGroebeNeumannetal.2012,
  author    = {Yarman, Aysu and Gr{\"o}be, Glenn and Neumann, Bettina and Kinne, Mathias and Gajovic-Eichelmann, Nenad and Wollenberger, Ursula and Hofrichter, Martin and Ullrich, Rene and Scheibner, Katrin and Scheller, Frieder W.},
  title     = {The aromatic peroxygenase from Marasmius rutola-a new enzyme for biosensor applications},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {402},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {1},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-011-5497-y},
  pages     = {405 -- 412},
  year      = {2012},
  abstract  = {The aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of -278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe(2+)/Fe(3+) redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensors and their further development are discussed.},
  language  = {en}
}
@article{LisdatScheller2000,
  author    = {Lisdat, Fred and Scheller, Frieder W.},
  title     = {Technical principles. Electrodes},
  isbn      = {90-5702-447-7},
  year      = {2000},
  language  = {en}
}
@article{PengUteschYarmanetal.2015,
  author    = {Peng, Lei and Utesch, Tillmann and Yarman, Aysu and Jeoung, Jae-Hun and Steinborn, Silke and Dobbek, Holger and Mroginski, Maria Andrea and Tanne, Johannes and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Surface-Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine-Coordinated Heme Protein},
  series = {Chemistry - a European journal},
  volume    = {21},
  journal   = {Chemistry - a European journal},
  number    = {20},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0947-6539},
  doi       = {10.1002/chem.201405932},
  pages     = {7596 -- 7602},
  year      = {2015},
  abstract  = {Molecular modeling, electrochemical methods, and quartz crystal microbalance were used to characterize immobilized hexameric tyrosine-coordinated heme protein (HTHP) on bare carbon or on gold electrodes modified with positively and negatively charged self-assembled monolayers (SAMs), respectively. HTHP binds to the positively charged surface but no direct electron transfer (DET) is found due to the long distance of the active sites from the electrode surfaces. At carboxyl-terminated surfaces, the neutrally charged bottom of HTHP can bind to the SAM. For this "disc" orientation all six hemes are close to the electrode and their direct electron transfer should be efficient. HTHP on all negatively charged SAMs showed a quasi-reversible redox behavior with rate constant k(s) values between 0.93 and 2.86 s(-1) and apparent formal potentials E-app(0)' between -131.1 and -249.1 mV. On the MUA/MU-modified electrode, the maximum surface concentration corresponds to a complete monolayer of the hexameric HTHP in the disc orientation. HTHP electrostatically immobilized on negatively charged SAMs shows electrocatalysis of peroxide reduction and enzymatic oxidation of NADH.},
  language  = {en}
}
@article{ChenWollenbergerLisdatetal.2000,
  author    = {Chen, Jian and Wollenberger, Ursula and Lisdat, Fred and Ge, Bixia and Scheller, Frieder W.},
  title     = {Superoxide sensor based on hemin modified electrode},
  year      = {2000},
  language  = {en}
}
@article{SpricigoRichterLeimkuehleretal.2010,
  author    = {Spricigo, Roberto and Richter, Claudia and Leimk{\"u}hler, Silke and Gorton, Lo and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Sulfite biosensor based on osmium redox polymer wired sulfite oxidase},
  issn      = {0927-7757},
  doi       = {10.1016/j.colsurfa.2009.09.001},
  year      = {2010},
  abstract  = {A biosensor, based on a redoxactive osmium polymer and sulfite oxidase on screen-printed electrodes, is presented here as a promising method for the detection of sulfite. A catalytic oxidative current was generated when a sample containing sulfite was pumped over the carbon screen-printed electrode modified with osmium redox polymer wired sulfite oxidase. A stationary value was reached after approximately 50 s and a complete measurement lasted no more than 3 min. The electrode polarized at -0.1 V (vs. Ag vertical bar AgCl 1M KCl) permits minimizing the influence of interfering substances, since these compounds can be unspecific oxidized at higher potentials. Because of the good stability of the protein film on the electrode surface, a well functioning biosensor-flow system was possible to construct. The working stability and reproducibility were further enhanced by the addition of bovine serum albumin generating a more long-term stable and biocompatible protein environment. The optimized biosensor showed a stable signal for more than a week of operation and a coefficient of variation of 4.8\% for 12 successive measurements. The lower limit of detection of the sensor was 0.5 mu M sulfite and the response was linear until 100 mu M. The high sensitivity permitted a 1:500 dilution of wine samples. The immobilization procedure and the operational conditions granted minimized interferences. Additionally, repeating the immobilization procedure to form several layers of wired SO further increased the sensitivity of such a sensor. Finally. the applicability of the developed sulfite biosensor was tested on real samples, such as white and red wines.},
  language  = {en}
}
@article{EhrentreichFoersterShishniashviliSongetal.1998,
  author    = {Ehrentreich-F{\"o}rster, Eva and Shishniashvili, D. and Song, Min Ik and Scheller, Frieder W.},
  title     = {Study of antioxidative substances by means of a ssuperoxide sensor},
  year      = {1998},
  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{LisdatGeEhrentreichFoersteretal.1999,
  author    = {Lisdat, Fred and Ge, Bixia and Ehrentreich-F{\"o}rster, Eva and Reszka, R. and Scheller, Frieder W.},
  title     = {SOD activity measurement using cytochrome c modified electrode},
  year      = {1999},
  language  = {en}
}
@phdthesis{BenkertSchellerSchoessleretal.2000,
  author    = {Benkert, Alexander and Scheller, Frieder W. and Sch{\"o}ssler, W. and Micheel, Burkhard and Warsinke, Axel},
  title     = {Size exclusion redox-labeled immunoassay (SERI) : a new format for homogeneous amperometric creatinine determination},
  year      = {2000},
  language  = {en}
}
@article{YarmanKurbanoğluZebgeretal.2021,
  author    = {Yarman, Aysu and Kurbanoğlu, Sevin{\c{c}} and Zebger, Ingo and Scheller, Frieder W.},
  title     = {Simple and robust},
  series = {Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers},
  volume    = {330},
  journal   = {Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers},
  publisher = {Elsevier Science},
  address   = {Amsterdam [u.a.]},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2020.129369},
  pages     = {12},
  year      = {2021},
  abstract  = {A spectrum of 7562 publications on Molecularly Imprinted Polymers (MIPs) has been presented in literature within the last ten years (Scopus, September 7, 2020). Around 10 \% of the papers published on MIPs describe the recognition of proteins. The straightforward synthesis of MIPs is a significant advantage as compared with the preparation of enzymes or antibodies. MIPs have been synthesized from only one up to six functional monomers while proteins are made up of 20 natural amino acids. Furthermore, they can be synthesized against structures of low immunogenicity and allow multi-analyte measurements via multi-target synthesis. Electrochemical methods allow simple polymer synthesis, removal of the template and readout. Among the different sensor configurations electrochemical MIP-sensors provide the broadest spectrum of protein analytes. The sensitivity of MIP-sensors is sufficiently high for biomarkers in the sub-nanomolar region, nevertheless the cross-reactivity of highly abundant proteins in human serum is still a challenge. MIPs for proteins offer innovative tools not only for clinical and environmental analysis, but also for bioimaging, therapy and protein engineering.},
  language  = {en}
}
@article{LisdatGeMeyerhoffetal.2001,
  author    = {Lisdat, Fred and Ge, Bixia and Meyerhoff, M. E. and Scheller, Frieder W.},
  title     = {Signal chains with cytochromes at SAM modified gold electrodes},
  year      = {2001},
  language  = {en}
}
@article{HalamekWollenbergerStoeckleinetal.2007,
  author    = {Hal{\´a}mek, Jan and Wollenberger, Ursula and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Signal amplification in immunoassays using labeling via boronic acid binding to the sugar moiety of immunoglobulin G : proof of concept for glycated hemoglobin},
  issn      = {0003-2719},
  doi       = {10.1080/00032710701327096},
  year      = {2007},
  abstract  = {A novel electrochemical immunoassay based on the multiple affinity labeling of the indicator antibody with an electro-active tag is presented. The concept is illustrated for the determination of the glycated hemoglobin HbA1c in hemoglobin samples. Hemoglobin is adsorbed to the surfactant-modified surface of a piezoelectric quartz crystal. Whereas the quartz crystal nanobalance is used to validate the total Hb binding, the HbA1c on the sensor surface is recognized by an antibody and quantified electrochemically after the sugar moieties of the antibody have been labeled in-situ with ferroceneboronic acid. The sensitivity of this sensor is about threefold higher than the sensitivity of a hemoglobin sensor, where the ferroceneboronic acid is bound directly to HbA1c.},
  language  = {en}
}
@article{StoeckleinRohdeScharteetal.2000,
  author    = {St{\"o}cklein, Walter F. M. and Rohde, M. and Scharte, Gudrun and Behrsing, Olaf and Warsinke, Axel and Micheel, Burkhard and Scheller, Frieder W.},
  title     = {Sensitive detection of triazine and phenylurea pesticides in pure organic solvent by enzyme linked immunsorbent assay (ELISA): stabilities, solubilities and sensitives},
  year      = {2000},
  language  = {en}
}
@article{LisdatWollenbergerPaeschkeetal.1998,
  author    = {Lisdat, Fred and Wollenberger, Ursula and Paeschke, Manfred and Scheller, Frieder W.},
  title     = {Sensitive catecholamine measurement using a monoenzymatic recycling system},
  year      = {1998},
  language  = {en}
}
@article{LisdatDronovMoehwaldetal.2009,
  author    = {Lisdat, Fred and Dronov, Roman and M{\"o}hwald, Helmuth and Scheller, Frieder W. and Kurth, Dirk G.},
  title     = {Self-assembly of electro-active protein architectures on electrodes for the construction of biomimetic signal chains},
  issn      = {1359-7345},
  doi       = {10.1039/B813559b},
  year      = {2009},
  abstract  = {The layer-by-layer adsorption technique based on the consecutive deposition of oppositely charged species is for the preparation of protein multilayers with fully electro-active protein molecules. The methodology was established with cytochrome c and the polyelectrolyte sulfonated polyaniline (PASA). The technique is also useful for the construction of bi-protein architectures confining protein-protein communication to an electrode. Following natural examples of protein complexes with defined signal transfer, cytochrome c was arranged with enzymes such as xanthine oxidase, bilirubin oxidase, laccase, and sulfite oxidase in self-assembled multilayer architectures. Thus, biomimetic signal chains from the enzyme substrate via the enzyme and cytochrome c towards the electrode can be established. Communication between proteins immobilised in multiple layers on the electrode can be achieved by in situ generation of small shuttle molecules or more advantageously by direct interprotein electron transfer. This allows the construction of new sensing electrodes, the properties of which can be tuned by the number of deposited protein layers. The mechanism of electron transfer within such protein assemblies on gold electrodes will be discussed.},
  language  = {en}
}
@misc{SchellerSakarDasdan2016,
  author    = {Scheller, Frieder W. and Sakar Dasdan, Dolunay},
  title     = {Selected papers presented on the 2nd International Conference on the New Trends in Chemistry, Zagreb, Croatia, April 19-22, 2016 Preface},
  series = {Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija},
  volume    = {48},
  journal   = {Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija},
  publisher = {Bulgarian Academy of Sciences},
  address   = {Sofia},
  issn      = {0324-1130},
  pages     = {4 -- 4},
  year      = {2016},
  language  = {en}
}
@article{SchellerWollenbergerWarsinkeetal.2001,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Warsinke, Axel and Lisdat, Fred},
  title     = {Research and development in biosensors},
  year      = {2001},
  language  = {en}
}
@article{LisdatHoWollenbergeretal.1998,
  author    = {Lisdat, Fred and Ho, Wah O. and Wollenberger, Ursula and Scheller, Frieder W. and Richter, Torsten and Bilitewski, Ursula},
  title     = {Recycling systems based on screen-printed electrodes},
  year      = {1998},
  language  = {en}
}
@article{WollenbergerSchubertPfeifferetal.1996,
  author    = {Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Recycling sensors based on kinases : proceedings of Mosbach Symposion on Biochemical Technology},
  year      = {1996},
  language  = {en}
}
@article{BierKleinjungScheller1997,
  author    = {Bier, Frank Fabian and Kleinjung, Frank and Scheller, Frieder W.},
  title     = {Real time measurement of nucleic acid hybridization using evanescent wave sensors - step towards the genosensor},
  year      = {1997},
  language  = {en}
}
@article{WelzelKossmehlEngelmannetal.1996,
  author    = {Welzel, H.-P. and Kossmehl, G. and Engelmann, G. and Neumann, B. and Wollenberger, Ursula and Scheller, Frieder W. and Schr{\"o}der, W.},
  title     = {Reactive groups on polymer covered electrodes, 4. Lactate-oxidase-biosensor based on electrodes modifies by polyphiophene},
  year      = {1996},
  language  = {en}
}
@article{RosePfeifferSchelleretal.2001,
  author    = {Rose, Andreas and Pfeiffer, Dorothea and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Quinoprotein glucose dehydrogenasemodified thick-film electrodes for the amperometric detection of phenolic compounds in flow injection analysis},
  year      = {2001},
  language  = {en}
}
@article{LisdatScheller2000,
  author    = {Lisdat, Fred and Scheller, Frieder W.},
  title     = {Principles of sensorial radical detection - a minireview},
  year      = {2000},
  language  = {en}
}
@article{SchellerSchubertFederowitz1997,
  author    = {Scheller, Frieder W. and Schubert, Frank and Federowitz, J.},
  title     = {Present state and frontiers in biosensorics},
  year      = {1997},
  language  = {en}
}
@article{SchellerHeiduschka1994,
  author    = {Scheller, Frieder W. and Heiduschka, P.},
  title     = {Preparation of an electrode surface with a high density of binding sites by an electrochemical reduction of a poly (nitrophenol) film},
  year      = {1994},
  language  = {en}
}
@article{JinWollenbergerScheller1998,
  author    = {Jin, Wen and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {PQQ as redox shuttle for quinoprotein glucose dehydrogenase},
  year      = {1998},
  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{HalamekMakowerKnoescheetal.2005,
  author    = {Halamek, Jan and Makower, Alexander and Kn{\"o}sche, Kristina and Skladal, Petr and Scheller, Frieder W.},
  title     = {Piezoelectric affinity sensors for cocaine and cholinesterase inhibitors},
  year      = {2005},
  abstract  = {We report here the development of piezoelectric affinity sensors for cocaine and cholinesterase inhibitors based on the formation of affinity complexes between an immobilized cocaine derivative and an anti-cocaine antibody or cholinesterase. For both binding reactions benzoylecgonine-1,8-diamino-3,4-dioxaoctane (BZE-DADOO) was immobilized on the surface of the sensor. For immobilization. pre-conjugated BZE-DADOO with 11-mercaptomonoundecanoic acid (MUA) via 2- (5-norbornen-2,3-dicarboximide)-1,1,3,3-tetramethyluronium-tetrafluoro borate (TNTU) allowed the formation of a chemisorbed monolayer on the piezosensor surface. The detection of cocaine was based oil a competitive assay. The change of frequency measured after 300 s of the binding reaction was used as the signal. The maximum binding of the antibody resulted in a frequency decrease of 35 Hz (with an imprecision 3\%, n = 3) while the presence of 100 pmol I-1 cocaine decreased the binding by 11\%. The limit of detection was consequently below 100 pmol I-1 for cocaine. The total time of one analysis was 15 min. This BZE-DADOO-modified sensor was adapted for the detection of organophosphates. BZE-DADOO - a competitive inhibitor - served as binding element for cholinesterase in a competitive assay. (C) 2004 Elsevier B.V. All rights reserved},
  language  = {en}
}
@article{BognarSupalaYarmanetal.2022,
  author    = {Bogn{\´a}r, Zs{\´o}fia and Supala, Eszter and Yarman, Aysu and Zhang, Xiaorong and Bier, Frank Fabian and Scheller, Frieder W. and Gyurcsanyi, R{\´o}bert E.},
  title     = {Peptide epitope-imprinted polymer microarrays for selective protein recognition},
  series = {Chemical science / RSC, Royal Society of Chemistry},
  volume    = {13},
  journal   = {Chemical science / RSC, Royal Society of Chemistry},
  number    = {5},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2041-6539},
  doi       = {10.1039/d1sc04502d},
  pages     = {1263 -- 1269},
  year      = {2022},
  abstract  = {We introduce a practically generic approach for the generation of epitope-imprinted polymer-based microarrays for protein recognition on surface plasmon resonance imaging (SPRi) chips. The SPRi platform allows the subsequent rapid screening of target binding kinetics in a multiplexed and label-free manner. The versatility of such microarrays, both as synthetic and screening platform, is demonstrated through developing highly affine molecularly imprinted polymers (MIPs) for the recognition of the receptor binding domain (RBD) of SARS-CoV-2 spike protein. A characteristic nonapeptide GFNCYFPLQ from the RBD and other control peptides were microspotted onto gold SPRi chips followed by the electrosynthesis of a polyscopoletin nanofilm to generate in one step MIP arrays. A single chip screening of essential synthesis parameters, including the surface density of the template peptide and its sequence led to MIPs with dissociation constants (K-D) in the lower nanomolar range for RBD, which exceeds the affinity of RBD for its natural target, angiotensin-convertase 2 enzyme. Remarkably, the same MIPs bound SARS-CoV-2 virus like particles with even higher affinity along with excellent discrimination of influenza A (H3N2) virus. While MIPs prepared with a truncated heptapeptide template GFNCYFP showed only a slightly decreased affinity for RBD, a single mismatch in the amino acid sequence of the template, i.e. the substitution of the central cysteine with a serine, fully suppressed the RBD binding.},
  language  = {en}
}
@article{KleuserStoeckleinPieperFuerstetal.2004,
  author    = {Kleuser, U. and St{\"o}cklein, Walter F. M. and Pieper-F{\"u}rst, U. and Scheller, Frieder W.},
  title     = {Partikelverst{\"a}rkte Oberfl{\"a}chenplasmonresonanz f{\"u}r die Quantifizierung von Matrix Metalloproteinase-2},
  year      = {2004},
  language  = {de}
}
@article{SchellerWollenbergerPfeifferetal.1996,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Pfeiffer, Dorothea and Schubert, Florian},
  title     = {Overview of biosensor technology : proceedings of Mosbach Symposion on Biochemical Technology},
  year      = {1996},
  language  = {en}
}
@article{StoeckleinWarsinkeScheller1997,
  author    = {St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Organic solvent modified enzyme-liked immunoassay for the detection of triazine herbicides},
  year      = {1997},
  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{NitscheKurthDunkhorstetal.2007,
  author    = {Nitsche, Andreas and Kurth, Andreas and Dunkhorst, Anna and P{\"a}nke, Oliver and Sielaff, Hendrik and Junge, Wolfgang and Muth, Doreen and Scheller, Frieder W. and St{\"o}cklein, Walter F. M. and Pauli, Georg and Kage, Andreas},
  title     = {One-step selection of vaccinia virus binding DNA-aptamers by MonoLEX},
  doi       = {10.1186/1472-6750-7-48},
  year      = {2007},
  language  = {en}
}
@article{LisdatGeScheller1999,
  author    = {Lisdat, Fred and Ge, Bixia and Scheller, Frieder W.},
  title     = {Oligonucleotide-modified electrodes for fast electron transfer to cytochrome c},
  year      = {1999},
  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{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{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{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{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}
}
@article{Scheller1996,
  author    = {Scheller, Frieder W.},
  title     = {New recognition elements for bioanalytics},
  year      = {1996},
  language  = {en}
}
@article{MakowerHalamekSkladaletal.2003,
  author    = {Makower, Alexander and Hal{\´a}mek, Jan and Skl{\´a}dal, Petr and Kernchen, Frank and Scheller, Frieder W.},
  title     = {New principle of direct real-time monitoring of the interaction of cholinesterase and its inhibitors by piezoelectric biosensor},
  year      = {2003},
  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{Scheller1998,
  author    = {Scheller, Frieder W.},
  title     = {Neue Dimensionen der Biosensorik},
  year      = {1998},
  language  = {de}
}
@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{SchmidtMatthesSchelleretal.2001,
  author    = {Schmidt, Peter Michael and Matthes, E. and Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Nachweis der Telomeraseaktivit{\"a}t in Zellkulturen mittels eines faseroptischen Sensors},
  year      = {2001},
  language  = {de}
}
@article{KroeningSchellerWollenbergeretal.2004,
  author    = {Kr{\"o}ning, Steffen and Scheller, Frieder W. and Wollenberger, Ursula and Lisdat, Fred},
  title     = {Myoglobin-Clay Electrode for Nitric Oxide (NO) Detection in Solution},
  year      = {2004},
  language  = {en}
}
@article{SchellerWollenbergerSchubertetal.1993,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Markower, Alexander and McNeil, C. J.},
  title     = {Multienzyme biosensors : coupled enzyme reactions and enzyme activation},
  year      = {1993},
  language  = {en}
}
@misc{SchellerZhangYarmanetal.2019,
  author    = {Scheller, Frieder W. and Zhang, Xiaorong and Yarman, Aysu and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E.},
  title     = {Molecularly imprinted polymer-based electrochemical sensors for biopolymers},
  series = {Current opinion in electrochemistry},
  volume    = {14},
  journal   = {Current opinion in electrochemistry},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {2451-9103},
  doi       = {10.1016/j.coelec.2018.12.005},
  pages     = {53 -- 59},
  year      = {2019},
  abstract  = {Electrochemical synthesis and signal generation dominate among the almost 1200 articles published annually on protein-imprinted polymers. Such polymers can be easily prepared directly on the electrode surface, and the polymer thickness can be precisely adjusted to the size of the target to enable its free exchange. In this architecture, the molecularly imprinted polymer (MIP) layer represents only one 'separation plate'; thus, the selectivity does not reach the values of 'bulk' measurements. The binding of target proteins can be detected straightforwardly by their modulating effect on the diffusional permeability of a redox marker through the thin MIP films. However, this generates an 'overall apparent' signal, which may include nonspecific interactions in the polymer layer and at the electrode surface. Certain targets, such as enzymes or redox active proteins, enables a more specific direct quantification of their binding to MIPs by in situ determination of the enzyme activity or direct electron transfer, respectively.},
  language  = {en}
}
@misc{PengYarmanJetzschmannetal.2017,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly imprinted electropolymer for a hexameric heme protein with direct electron transfer and peroxide electrocatalysis},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400627},
  pages     = {11},
  year      = {2017},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 ± 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@article{PengYarmanJetzschmannetal.2016,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis},
  series = {SENSORS},
  volume    = {16},
  journal   = {SENSORS},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s16030272},
  pages     = {1343 -- 1364},
  year      = {2016},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 +/- 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@article{KnoescheHalamekMakoweretal.2003,
  author    = {Kn{\"o}sche, Kristina and Hal{\´a}mek, Jan and Makower, Alexander and Fournier, Didier and Scheller, Frieder W.},
  title     = {Molecular recognition of cocaine by acetylcholinesterases for affinity purification and bio-sensing},
  year      = {2003},
  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{BosserdtGajovicEichelmanScheller2013,
  author    = {Bosserdt, Maria and Gajovic-Eichelman, Nenad and Scheller, Frieder W.},
  title     = {Modulation of direct electron transfer of cytochrome c by use of a molecularly imprinted thin film},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {405},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {20},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-013-7009-8},
  pages     = {6437 -- 6444},
  year      = {2013},
  abstract  = {We describe the preparation of a molecularly imprinted polymer film (MIP) on top of a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold, where the template cytochrome c (cyt c) participates in direct electron transfer (DET) with the underlying electrode. To enable DET, a non-conductive polymer film is electrodeposited from an aqueous solution of scopoletin and cyt c on to the surface of a gold electrode previously modified with MUA. The electroactive surface concentration of cyt c was 0.5 pmol cm(-2). In the absence of the MUA layer, no cyt c DET was observed and the pseudo-peroxidatic activity of the scopoletin-entrapped protein, assessed via oxidation of Ampliflu red in the presence of hydrogen peroxide, was only 30 \% of that for the MIP on MUA. This result indicates that electrostatic adsorption of cyt c by the MUA-SAM substantially increases the surface concentration of cyt c during the electrodeposition step, and is a prerequisite for the productive orientation required for DET. After template removal by treatment with sulfuric acid, rebinding of cyt c to the MUA-MIP-modified electrode occurred with an affinity constant of 100,000 mol(-1) L, a value three times higher than that determined by use of fluorescence titration for the interaction between scopoletin and cyt c in solution. The DET of cyt c in the presence of myoglobin, lysozyme, and bovine serum albumin (BSA) reveals that the MIP layer suppresses the effect of competing proteins.},
  language  = {en}
}
@article{LehmannWollenbergerBrigeliusFloheetal.2001,
  author    = {Lehmann, Claudia and Wollenberger, Ursula and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide},
  year      = {2001},
  language  = {en}
}
@misc{MengerYarmanErdoessyetal.2016,
  author    = {Menger, Marcus and Yarman, Aysu and Erd{\"o}ssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing},
  series = {Biosensors : open access journal},
  volume    = {6},
  journal   = {Biosensors : open access journal},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2079-6374},
  doi       = {10.3390/bios6030035},
  pages     = {4399 -- 4413},
  year      = {2016},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}
@misc{MengerYarmanErdőssyetal.2017,
  author    = {Menger, Marcus and Yarman, Aysu and Erdőssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and aptamers for recognition of proteins in biomimetic sensing},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400496},
  pages     = {19},
  year      = {2017},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}
@article{YarmanScheller2016,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {MIP-esterase/Tyrosinase Combinations for Paracetamol and Phenacetin},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {28},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201600042},
  pages     = {2222 -- 2227},
  year      = {2016},
  abstract  = {A new electrochemical MIP sensor for the most frequently used drug paracetamol (PAR) was prepared by electropolymerization of mixtures containing the template molecule and the functional monomers ophenylenediamine, resorcinol and aniline. The imprinting factor of 12 reflects the effective target binding to the MIP as compared with the non-imprinted electropolymer. Combination of the MIP with a nonspecific esterase allows the measurement of phenacetin - another analgesic drug. In the second approach the PAR containing sample solution was pretreated with tyrosinase in order to prevent electrochemical interferences by ascorbic acid and uric acid. Interference-free indication at a very low electrode potential without fouling of the electrode surface was achieved with the o-phenylenediamine: resorcinol-based MIP.},
  language  = {en}
}
@article{RiedelBeyersdorfRadeckNeumannetal.1995,
  author    = {Riedel, K. and Beyersdorf-Radeck, Baerbel and Neumann, B. and Scheller, Frieder W. and Schmid, Rolf D.},
  title     = {Microbial sensors for determination of aromatics and their chloro derivatives. Part III: Determination of chlorinated phenols using a biosensor containing Trichosporon beigelii (cutaneum)},
  year      = {1995},
  language  = {en}
}
@article{FrascavonGrabergFengetal.2010,
  author    = {Frasca, Stefano and von Graberg, Till and Feng, Jiu-Ju and Thomas, Arne and Smarsly, Bernd M. and Weidinger, Inez M. and Scheller, Frieder W. and Hildebrandt, Peter and Wollenberger, Ursula},
  title     = {Mesoporous indium tin oxide as a novel platform for bioelectronics},
  issn      = {1867-3880},
  doi       = {10.1002/cctc.201000047},
  year      = {2010},
  abstract  = {Stable immobilization and reversible electrochemistry of cytochrome c in a tranparent indium tin oxide film with a well-defined mesoporosity (mpITO) is demonstrated. the transparency and good conductivity, in combination with the large surface area of mpITO, allow the incorporation of a high amount of elelctroactive biomolecules and their electrochemical and spectroscopic investigation. UV/Vis and resonance Raman spectroscopy, in combination with direct protein voltammetry are employed for the characterization of cytochrome c immobilized in the mpITO and reveal no perturbant of the structural of the integrity of the redox protein. The potential of this modified material as a biosensor detection of superoxide anions is also demonstrated.},
  language  = {en}
}
@article{StoellnerStoeckleinSchelleretal.2002,
  author    = {St{\"o}llner, Daniela and St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Warsinke, Axel},
  title     = {Membrane-immobilized haptoglobin as affinity matrix for a hemoglobin-A1c-immunosensor},
  year      = {2002},
  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{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{SchulmeisterRoseScheller1997,
  author    = {Schulmeister, Thomas and Rose, J{\"u}rgen and Scheller, Frieder W.},
  title     = {Mathematical modelling of exponential amplification in membrane-based enzyme sensors},
  year      = {1997},
  language  = {en}
}
@article{StoeckleinScheller1996,
  author    = {St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Laccase : a marker enzyme for solvent modified immunoassays},
  year      = {1996},
  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{BierScheller1996,
  author    = {Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Label-free observation of DNA-hybridisation and endonuclease activity on a wave guide surface using a grating coupler},
  year      = {1996},
  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}
}
@article{CasertaZhangYarmanetal.2021,
  author    = {Caserta, Giorgio and Zhang, Xiaorong and Yarman, Aysu and Supala, Eszter and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E. and Zebger, Ingo and Scheller, Frieder W.},
  title     = {Insights in electrosynthesis, target binding, and stability of peptide-imprinted polymer nanofilms},
  series = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)},
  volume    = {381},
  journal   = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)},
  publisher = {Elsevier},
  address   = {New York, NY [u.a.]},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2021.138236},
  pages     = {8},
  year      = {2021},
  abstract  = {Molecularly imprinted polymer (MIP) nanofilms have been successfully implemented for the recognition of different target molecules: however, the underlying mechanistic details remained vague. This paper provides new insights in the preparation and binding mechanism of electrosynthesized peptide-imprinted polymer nanofilms for selective recognition of the terminal pentapeptides of the beta-chains of human adult hemoglobin, HbA, and its glycated form HbA1c. To differentiate between peptides differing solely in a glucose adduct MIP nanofilms were prepared by a two-step hierarchical electrosynthesis that involves first the chemisorption of a cysteinyl derivative of the pentapeptide followed by electropolymerization of scopoletin. This approach was compared with a random single-step electrosynthesis using scopo-letin/pentapeptide mixtures. Electrochemical monitoring of the peptide binding to the MIP nanofilms by means of redox probe gating revealed a superior affinity of the hierarchical approach with a Kd value of 64.6 nM towards the related target. Changes in the electrosynthesized non-imprinted polymer and MIP nanofilms during chemical, electrochemical template removal and rebinding were substantiated in situ by monitoring the characteristic bands of both target peptides and polymer with surface enhanced infrared absorption spectroscopy. This rational approach led to MIPs with excellent selectivity and provided key mechanistic insights with respect to electrosynthesis, rebinding and stability of the formed MIPs.},
  language  = {en}
}
@article{LoewBogdanoffHerrmannetal.2006,
  author    = {Loew, Noya and Bogdanoff, Peter and Herrmann, Iris and Wollenberger, Ursula and Scheller, Frieder W. and Katterle, Martin},
  title     = {Influence of modifications on the efficiency of pyrolysed CoTMPP as electrode material for horseradish peroxidase and the reduction of hydrogen peroxide},
  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},
  number    = {23},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.200603664},
  pages     = {2324 -- 2330},
  year      = {2006},
  abstract  = {A tailor-made horseradish peroxidase (HRP) bulk composite electrode was developed on the basis of pyrolyzed cobalt tetramethoxyphenylporphyrin (CoTMPP) by modifying pore size and surface area of the porous carbon material through varying amounts of iron oxalate and sulfur prior to pyrolyzation. The materials were used to immobilize horseradish peroxidase (HRP). These electrodes were characterized in terms of their efficiency to reduce hydrogen peroxide. The heterogeneous electron transfer rate constants of different materials were determined with the rotating disk electrode method and a k(S) (401 +/- 61 s(-1)) exceeding previously reported values for native HRP was found.},
  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{SchellerBauerMakoweretal.2002,
  author    = {Scheller, Frieder W. and Bauer, Christian G. and Makower, Alexander and Wollenberger, Ursula and Warsinke, Axel and Bier, Frank Fabian},
  title     = {Immunoassays using enzymatic amplification electrodes},
  isbn      = {0-7484-0791-X},
  year      = {2002},
  language  = {en}
}
@article{BeissenhirtzSchellerLisdat2003,
  author    = {Beissenhirtz, Moritz Karl and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Immobilized cytochrome c sensor in organic / aqueous media for the characterization of hydrophilic and hydrophobic antioxidants},
  year      = {2003},
  language  = {en}
}
@article{LettauGajovicEichelmannKwaketal.2004,
  author    = {Lettau, Kristian and Gajovic-Eichelmann, N. and Kwak, Young-Keun and Scheller, Frieder W. and Warsinke, Axel},
  title     = {Hydroxylasen und katalytische Polymere f{\"u}r Biochips},
  year      = {2004},
  language  = {de}
}
@article{XieTangWollenbergeretal.1997,
  author    = {Xie, B. and Tang, X. and Wollenberger, Ursula and Johansson, G. and Gorton, Lo and Scheller, Frieder W. and Danielsson, B.},
  title     = {Hybrid biosensor for simultaneous electrochemical and thermal detection},
  year      = {1997},
  language  = {en}
}
@misc{YarmanScheller2020,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {How reliable is the electrochemical readout of MIP sensors?},
  series = {Sensors},
  volume    = {20},
  journal   = {Sensors},
  number    = {9},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s20092677},
  pages     = {23},
  year      = {2020},
  abstract  = {Electrochemical methods offer the simple characterization of the synthesis of molecularly imprinted polymers (MIPs) and the readouts of target binding. The binding of electroinactive analytes can be detected indirectly by their modulating effect on the diffusional permeability of a redox marker through thin MIP films. However, this process generates an overall signal, which may include nonspecific interactions with the nonimprinted surface and adsorption at the electrode surface in addition to (specific) binding to the cavities. Redox-active low-molecular-weight targets and metalloproteins enable a more specific direct quantification of their binding to MIPs by measuring the faradaic current. The in situ characterization of enzymes, MIP-based mimics of redox enzymes or enzyme-labeled targets, is based on the indication of an electroactive product. This approach allows the determination of both the activity of the bio(mimetic) catalyst and of the substrate concentration.},
  language  = {en}
}
@article{BierEhrentreichFoersterBaueretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Bauer, Christian G. and Scheller, Frieder W.},
  title     = {High sensitive competitive immunodetection of 2,4-dichlorophenoxyacetic acid using enzymatic amplification with electrochemical detection},
  year      = {1996},
  language  = {en}
}
@article{SchellerYarmanBachmannetal.2014,
  author    = {Scheller, Frieder W. and Yarman, Aysu and Bachmann, Till and Hirsch, Thomas and Kubick, Stefan and Renneberg, Reinhard and Schumacher, Soeren and Wollenberger, Ursula and Teller, Carsten and Bier, Frank Fabian},
  title     = {Future of biosensors: a personal view},
  series = {Advances in biochemical engineering, biotechnology},
  volume    = {140},
  journal   = {Advances in biochemical engineering, biotechnology},
  editor    = {Gu, MB and Kim, HS},
  publisher = {Springer},
  address   = {Berlin},
  isbn      = {978-3-642-54143-8; 978-3-642-54142-1},
  issn      = {0724-6145},
  doi       = {10.1007/10_2013_251},
  pages     = {1 -- 28},
  year      = {2014},
  abstract  = {Biosensors representing the technological counterpart of living senses have found routine application in amperometric enzyme electrodes for decentralized blood glucose measurement, interaction analysis by surface plasmon resonance in drug development, and to some extent DNA chips for expression analysis and enzyme polymorphisms. These technologies have already reached a highly advanced level and need minor improvement at most. The dream of the "100-dollar' personal genome may come true in the next few years provided that the technological hurdles of nanopore technology or of polymerase-based single molecule sequencing can be overcome. Tailor-made recognition elements for biosensors including membrane-bound enzymes and receptors will be prepared by cell-free protein synthesis. As alternatives for biological recognition elements, molecularly imprinted polymers (MIPs) have been created. They have the potential to substitute antibodies in biosensors and biochips for the measurement of low-molecular-weight substances, proteins, viruses, and living cells. They are more stable than proteins and can be produced in large amounts by chemical synthesis. Integration of nanomaterials, especially of graphene, could lead to new miniaturized biosensors with high sensitivity and ultrafast response. In the future individual therapy will include genetic profiling of isoenzymes and polymorphic forms of drug-metabolizing enzymes especially of the cytochrome P450 family. For defining the pharmacokinetics including the clearance of a given genotype enzyme electrodes will be a useful tool. For decentralized online patient control or the integration into everyday "consumables' such as drinking water, foods, hygienic articles, clothing, or for control of air conditioners in buildings and cars and swimming pools, a new generation of "autonomous' biosensors will emerge.},
  language  = {en}
}
@article{WollenbergerJinBernhardtetal.1998,
  author    = {Wollenberger, Ursula and Jin, Wen and Bernhardt, Rita and Lehmann, Claudia and St{\"o}cklein, Walter F. M. and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Funktionalisierung von Elektroden f{\"u}r den direkten heterogenen Elektrotransfer},
  year      = {1998},
  language  = {de}
}
@article{SchellerWagener2004,
  author    = {Scheller, Frieder W. and Wagener, C.},
  title     = {From gene to life},
  year      = {2004},
  language  = {en}
}
@article{BaeumnerGauglitzScheller2010,
  author    = {Baeumner, Antje J. and Gauglitz, Guenter and Scheller, Frieder W.},
  title     = {Focus on bioanalysis},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-010-4203-9},
  year      = {2010},
  abstract  = {Editoria},
  language  = {en}
}
@article{KleinjungBeierWarsinkeetal.1997,
  author    = {Kleinjung, Frank and Beier, Frank F. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Fibre-optic genosensor for specific determination of femtomolar DNA oligomers},
  year      = {1997},
  language  = {en}
}
@article{LiuWollenbergerKatterleetal.2006,
  author    = {Liu, Songqin and Wollenberger, Ursula and Katterle, Martin and Scheller, Frieder W.},
  title     = {Ferroceneboronic acid-based amperometric biosensor for glycated hemoglobin},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2005.07.011},
  year      = {2006},
  abstract  = {An amperometric biosensor for the determination of glycated hemoglobin in human whole blood is proposed. The principle is based on the electrochemical measurement of ferroceneboronic acid (FcBA) that has been specifically bound to the glycated N-terminus. Hemoglobin is immobilized on a zirconium dioxide nanoparticle modified pyrolytic graphite electrode (PGE) in the presence of didodecyldimethylammonium bromide (DDAB). The incubation of this sensor in FcBA solution leads to the formation of an FcBA-modified surface due to the affinity interaction between boronate and the glycated sites of the hemoglobin. The binding of FcBA results in well-defined redox peaks with an E-0' of 0.299 V versus Ag/AgCl (1 M KCl). The square wave voltammetric response of the bound FcBA reflects the amount of glycated hemoglobin at the surface. This signal increases linearily with the degree of glycated hemoglobin from 6.8 to 14.0\% of total immobilized hemoglobin. The scheme was applied to the determination of the fraction of glycated hemoglobin in whole blood samples.},
  language  = {en}
}