TY  - JOUR
A1  - Bandodkar, Amay J.
A1  - Molinnus, Denise
A1  - Mirza, Omar
A1  - Guinovart, Tomas
A1  - Windmiller, Joshua R.
A1  - Valdes-Ramirez, Gabriela
A1  - Andrade, Francisco J.
A1  - Schöning, Michael Josef
A1  - Wang, Joseph
T1  - Epidermal tattoo potentiometric sodium sensors with wireless signal transduction for continuous non-invasive sweat monitoring
JF  - Biosensors and bioelectronics
N2  - This article describes the fabrication, characterization and application of an epidermal temporary-transfer tattoo-based potentiometric sensor, coupled with a miniaturized wearable wireless transceiver, for real-time monitoring of sodium in the human perspiration. Sodium excreted during perspiration is an excellent marker for electrolyte imbalance and provides valuable information regarding an individual's physical and mental wellbeing. The realization of the new skin-worn non-invasive tattoo-like sensing device has been realized by amalgamating several state-of-the-art thick film, laser printing, solid-state potentiometry, fluidics and wireless technologies. The resulting tattoo-based potentiometric sodium sensor displays a rapid near-Nernstian response with negligible carryover effects, and good resiliency against various mechanical deformations experienced by the human epidermis. On-body testing of the tattoo sensor coupled to a wireless transceiver during exercise activity demonstrated its ability to continuously monitor sweat sodium dynamics. The real-time sweat sodium concentration was transmitted wirelessly via a body-worn transceiver from the sodium tattoo sensor to a notebook while the subjects perspired on a stationary cycle. The favorable analytical performance along with the wearable nature of the wireless transceiver makes the new epidermal potentiometric sensing system attractive for continuous monitoring the sodium dynamics in human perspiration during diverse activities relevant to the healthcare, fitness, military, healthcare and skin-care domains.
Y1  - 2014
U6  - https://doi.org/10.1016/j.bios.2013.11.039
SN  - 1873-4235 (E-Journal); 0956-5663 (Print)
VL  - 54
SP  - 603
EP  - 609
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Reisert, Steffen
A1  - Geissler, Hanno
A1  - Flörke, Rudolf
A1  - Weiler, Christian
A1  - Wagner, Patrick
A1  - Schöning, Michael Josef
T1  - Characterisation of aseptic sterilisation processes using an electronic nose
JF  - International journal of nanotechnology
Y1  - 2013
SN  - 1475-7435 (Print) 7141-8151 (Online)
VL  - Vol. 10
IS  - No. 5-7
SP  - 470
EP  - 484
PB  - Inderscience Enterprises
CY  - Genève
ER  - 
TY  - JOUR
A1  - Miyamoto, Ko-ichiro
A1  - Hirayama, Yuji
A1  - Wagner, Torsten
A1  - Schöning, Michael Josef
A1  - Yoshinobu, Tatsuo
T1  - Visualization of enzymatic reaction in a microfluidic channel using chemical imaging sensor
JF  - Electrochimica acta
Y1  - 2013
SN  - 1873-3859 (E-Journal); 0013-4686 (Print)
SP  - Publ. online
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - GEN
A1  - Ingebrandt, Sven
A1  - Wagner, Patrick
A1  - Schöning, Michael Josef
T1  - Engineering of functional interfaces / guest eds. Sven Ingebrandt ; Patrick Wagner ; Michael J. Schöning
T2  - Physica Status Solidi (A)
Y1  - 2013
SN  - 1521-396X (E-Journal); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)
VL  - Vol. 210
IS  - Iss. 5
SP  - 845
ER  - 
TY  - GEN
A1  - Abdelghani, Adnane
A1  - Menaa, Bouzid
A1  - Obare, Sherine O.
A1  - Schöning, Michael Josef
T1  - Special issue on nanoscale science and technology / guest eds.: Adnane Abdelghani, Bouzid Menaa, Sherine O. Obare, Michael J. Schöning
T2  - International journal of nanotechnology
Y1  - 2013
SN  - 1741-8151 (E-Journal), 1475-7435 (Print)
VL  - Vol. 10
IS  - No. 5-7
SP  - 373
EP  - 619
ER  - 
TY  - JOUR
A1  - Sabitova, A.
A1  - Ebert, Ph.
A1  - Lenz, A.
A1  - Schaafhausen, S.
A1  - Ivanova, L.
A1  - Dähne, M.
A1  - Hoffmann, A.
A1  - Dunin-Borkowski, R. E.
A1  - Förster, Arnold
A1  - Grandidier, B.
A1  - Eisele, H.
T1  - Intrinsic bandgap of cleaved ZnO(112¯0) surfaces
JF  - Applied physics letters
Y1  - 2013
SN  - 1077-3118 (E-Journal); 0003-6951 (Print)
VL  - Vol. 102
SP  - 021608
ER  - 
TY  - CHAP
A1  - Takenaga, Shoko
A1  - Herrera, Cony F.
A1  - Werner, Frederik
A1  - Biselli, Manfred
A1  - Schnitzler, Thomas
A1  - Schöning, Michael Josef
A1  - Öhlschläger, Peter
A1  - Wagner, Torsten
T1  - Detection of the metabolic activity of cells by differential measurements based on a single light-addressable potentiometric sensor chip
T2  - 11. Dresdner Sensor-Symposium : 9.-11.12.2013
Y1  - 2013
SN  - 978-3-9813484-5-3
SP  - 63
EP  - 67
ER  - 
TY  - CHAP
A1  - Oberländer, Jan
A1  - Reisert, Steffen
A1  - Kirchner, Patrick
A1  - Wagner, Patrick
A1  - Schöning, Michael Josef
T1  - Kalorimetrische Gassensoren zur H2O2-Detektion in aseptischen Sterilisationsprozessen
T2  - 11. Dresdner Sensor-Symposium : 9.-11.12.2013
Y1  - 2013
SN  - 978-3-9813484-5-3
SP  - 234
EP  - 238
ER  - 
TY  - JOUR
A1  - Heine, A.
A1  - Herrmann, G.
A1  - Selmer, Thorsten
A1  - Terwesten, F.
A1  - Buckel, W.
A1  - Reuter, K.
T1  - High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily
JF  - Proteins
N2  - Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 Å as well as in complex with CoA at a resolution of 1.59 Å. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called “hot dog fold” which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all “hot dog fold” proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041–2053. © 2014 Wiley Periodicals, Inc.
Y1  - 2014
U6  - https://doi.org/10.1002/prot.24557
SN  - 1097-0134 (E-Journal); 0887-3585 (Print)
VL  - 82
IS  - 9
SP  - 2041
EP  - 2053
PB  - Wiley-Liss
CY  - New York
ER  - 
TY  - JOUR
A1  - Takenaga, Shoko
A1  - Biselli, Manfred
A1  - Schnitzler, Thomas
A1  - Öhlschläger, Peter
A1  - Wagner, Torsten
A1  - Schöning, Michael Josef
T1  - Toward multi-analyte bioarray sensors: LAPS-based on-chip determination of a Michaelis–Menten-like kinetics for cell culturing
JF  - Physica status solidi A : Applications and materials science
N2  - The metabolic activity of Chinese hamster ovary (CHO) cells was observed using a light-addressable potentiometric sensor (LAPS). The dependency toward different glucose concentrations (17–200 mM) follows a Michaelis–Menten kinetics trajectory with Kₘ = 32.8 mM, and the obtained Kₘ value in this experiment was compared with that found in literature. In addition, the pH shift induced by glucose metabolism of tumor cells transfected with the HPV-16 genome (C3 cells) was successfully observed. These results indicate the possibility to determine the tumor cells metabolism with a LAPS-based measurement device.
Y1  - 2014
U6  - https://doi.org/10.1002/pssa.201330464
SN  - 1521-396X (E); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)
VL  - 211
IS  - 6
SP  - 1410
EP  - 1415
PB  - Wiley-VCH
CY  - Weinheim
ER  -