TY  - JOUR
A1  - Plum, Leona
A1  - Ma, Xiaosong
A1  - Hampel, Brigitte
A1  - Balthasar, Nina
A1  - Coppari, Roberto
A1  - Münzberg, Heike
A1  - Shanabrough, Marya
A1  - Burdakov, Denis
A1  - Rother, Eva
A1  - Janoschek, Ruth
A1  - Alber, Jens
A1  - Belgardt, Bengt F.
A1  - Koch, Linda
A1  - Seibler, Jost
A1  - Schenk, Frieder
A1  - Fekete, Csaba
A1  - Suzuki, Akira
A1  - Mak, Tak W.
A1  - Krone, Wilhelm
A1  - Horvath, Tamas L.
A1  - Ashcroft, Frances M.
A1  - Brüning, Jens C.
T1  - Enhanced PIP3 signaling in POMC neurons causes KATP channel activation and leads to diet-sensitive obesity
JF  - The Journal of Clinical Investigation (JCI)
Y1  - 2006
U6  - http://dx.doi.org/10.1172/JCI27123
SN  - 1558-8238
VL  - 116
IS  - 7
SP  - 1886
EP  - 1901
ER  - 
TY  - JOUR
A1  - Öhlschläger, Peter
A1  - Quetting, Michael
A1  - Alvarez, Gerardo
A1  - Dürst, Matthias
A1  - Gissmann, Lutz
A1  - Kaufmann, Andreas M.
T1  - Enhancement of immunogenicity of a therapeutic cervical cancer DNA-based vaccine by co-application of sequence-optimized genetic adjuvants
JF  - International Journal of Cancer
Y1  - 2009
SN  - 1097-0215
VL  - 125
IS  - 1
SP  - 189
EP  - 198
PB  - Wiley
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Deppe, Veronika Maria
A1  - Bongaerts, Johannes
A1  - O'Connell, Timothy
A1  - Maurer, Karl-Heinz
A1  - Meinhardt, Friedhelm
T1  - Enzymatic deglycation of Amadori products in bacteria
JF  - Applied microbiology and biotechnology
Y1  - 2011
SN  - 1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)
VL  - Vol. 90
IS  - Iss. 2
SP  - 399
EP  - 406
PB  - Springer
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Tippkötter, Nils
A1  - Duwe, Anna-Maria
A1  - Wiesen, Sebastian
A1  - Sieker, Tim
A1  - Ulber, Roland
T1  - Enzymatic hydrolysis of beech wood lignocellulose at high solid contents and its utilization as substrate for the production of biobutanol and dicarboxylic acids
JF  - Bioresource Technology
N2  - The development of a cost-effective hydrolysis for crude cellulose is an essential part of biorefinery developments. To establish such high solid hydrolysis, a new solid state reactor with static mixing is used. However, concentrations >10% (w/w) cause a rate and yield reduction of enzymatic hydrolysis. By optimizing the synergetic activity of cellulolytic enzymes at solid concentrations of 9%, 17% and 23% (w/w) of crude Organosolv cellulose, glucose concentrations of 57, 113 and 152 g L⁻¹ are reached. However, the glucose yield decreases from 0.81 to 0.72gg⁻¹ at 17% (w/w). Optimal conditions for hydrolysis scale-up under minimal enzyme addition are identified. As result, at 23% (w/w) crude cellulose the glucose yield increases from 0.29 to 0.49gg⁻¹. As proof of its applicability, biobutanol, succinic and itaconic acid are produced with the crude hydrolysate. The potential of the substrate is proven e.g. by a high butanol yield of 0.33gg⁻¹.
Y1  - 2014
U6  - http://dx.doi.org/10.1016/j.biortech.2014.06.052
VL  - 167
SP  - 447
EP  - 455
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Niehaus, F.
A1  - Gabor, E.
A1  - Wieland, S.
A1  - Siegert, Petra
A1  - Maurer, Karl-Heinz
A1  - Eck, J.
T1  - Enzymes for the laundry industries: tapping the vast metagenomic pool of alkaline proteases
JF  - Microbial biotechnology
Y1  - 2011
SN  - 1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)
VL  - Vol. 4
IS  - Iss. 6
SP  - 767
EP  - 776
PB  - Springer
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Elbers, Gereon
A1  - Remme, S.
A1  - Lehmann, G.
T1  - EPR and Optical Absorption of Cr3+ in CsCl and CsBr
JF  - Physica Status Solidi (B). 142 (1987), H. 2
Y1  - 1987
SN  - 0031-8957
SP  - 367
EP  - 377
ER  - 
TY  - JOUR
A1  - Elbers, Gereon
A1  - Remme, S.
A1  - Lehmann, G.
T1  - EPR of Cr3+ in Tris(acetylacetonato)gallium(III) Single Crystals
JF  - Inorganic Chemistry. 25 (1986)
Y1  - 1986
SN  - 0020-1669
SP  - 896
EP  - 897
ER  - 
TY  - JOUR
A1  - Sieker, Tim
A1  - Neuner, Andreas
A1  - Dimitrova, Darina
A1  - Tippkötter, Nils
A1  - Muffler, Kai
A1  - Bart, Hans-Jörg
A1  - Heinzle, Elmar
A1  - Ulber, Roland
T1  - Ethanol production from grass silage by simultaneous pretreatment, saccharification and fermentation: First steps in the process development
JF  - Engineering in Life Sciences
N2  - Grass silage provides a great potential as renewable feedstock. Two fractions of the grass silage, a press juice and the fiber fraction, were evaluated for their possible use for bioethanol production. Direct production of ethanol from press juice is not possible due to high concentrations of organic acids. For the fiber fraction, alkaline peroxide or enzymatic pretreatment was used, which removes the phenolic acids in the cell wall. In this study, we demonstrate the possibility to integrate the enzymatic pretreatment with a simultaneous saccharification and fermentation to achieve ethanol production from grass silage in a one-process step. Achieved yields were about 53 g ethanol per kg silage with the alkaline peroxide pretreatment and 91 g/kg with the enzymatic pretreatment at concentrations of 8.5 and 14.6 g/L, respectively. Furthermore, it was shown that additional supplementation of the fermentation medium with vitamins, trace elements and nutrient salts is not necessary when the press juice is directly used in the fermentation step.
Y1  - 2011
U6  - http://dx.doi.org/10.1002/elsc.201000160
N1  - Special Issue "Bioprocess‐oriented plant design"
VL  - 11
IS  - 4
SP  - 436
EP  - 442
PB  - Wiley
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Roth, Jasmine
A1  - Tippkötter, Nils
T1  - Evaluation of lignocellulosic material for butanol production using enzymatic hydrolysate medium
JF  - Cellulose Chemistry and Technology
N2  - Butanol is a promising gasoline additive and platform chemical that can be readily produced via acetone-butanolethanol (ABE) fermentation from pretreated lignocellulosic materials. This article examines lignocellulosic material from beech wood for ABE fermentation, using Clostridium acetobutylicum. First, the utilization of both C₅₋ (xylose) and C₆₋ (glucose) sugars as sole carbon source was investigated in static cultivation, using serum bottles and synthetic medium. The utilization of pentose sugar resulted in a solvent yield of 0.231 g·g_sugar⁻¹, compared to 0.262 g·g_sugar⁻¹ using hexose. Then, the Organosolv pretreated crude cellulose fibers (CF) were enzymatically decomposed, and the resulting hydrolysate medium was analyzed for inhibiting compounds (furans, organic acids, phenolics) and treated with ionexchangers for detoxification. Batch fermentation in a bioreactor using CF hydrolysate medium resulted in a total solvent yield of 0.20 gABE·g_sugar⁻¹.
Y1  - 2016
VL  - 50
IS  - 3-4
SP  - 405
EP  - 410
PB  - Editura Academiei Romane
CY  - Bukarest
ER  - 
TY  - JOUR
A1  - Salpati, Laurent
A1  - Chu, Xiaoyan
A1  - Chen, Liangfu
A1  - Prasad, Bhagwat
A1  - Dallas, Shannon
A1  - Evers, Raymond
A1  - Mamaril-Fishman, Donna
A1  - Geier, Ethan G.
A1  - Kehler, Jonathan
A1  - Kunta, Jeevan
A1  - Mezler, Mario
A1  - Laplanche, Loic
A1  - Pang, Jodie
A1  - Soars, Matthew G.
A1  - Unadkat, Jashvant D.
A1  - van Waterschoot, Robert A.B.
A1  - Yabut, Jocelyn
A1  - Schinkel, Alfred H.
A1  - Scheer, Nico
A1  - Rode, Anja
T1  - Evaluation of organic anion transporting polypeptide 1B1 and 1B3 humanized mice as a translational model to study the pharmacokinetics of statins
JF  - Drug Metabolism and Disposition
N2  - Organic anion transporting polypeptide (Oatp) 1a/1b knockout and OATP1B1 and -1B3 humanized mouse models are promising tools for studying the roles of these transporters in drug disposition. Detailed characterization of these models will help to better understand their utility for predicting clinical outcomes. To advance this approach, we carried out a comprehensive analysis of these mouse lines by evaluating the compensatory changes in mRNA expression, quantifying the amounts of OATP1B1 and -1B3 protein by liquid chromatography–tandem mass spectrometry, and studying the active uptake in isolated hepatocytes and the pharmacokinetics of some prototypical substrates including statins. Major outcomes from these studies were 1) mostly moderate compensatory changes in only a few genes involved in drug metabolism and disposition, 2) a robust hepatic expression of OATP1B1 and -1B3 proteins in the respective humanized mouse models, and 3) functional activities of the human transporters in hepatocytes isolated from the humanized models with several substrates tested in vitro and with pravastatin in vivo. However, the expression of OATP1B1 and -1B3 in the humanized models did not significantly alter liver or plasma concentrations of rosuvastatin and pitavastatin compared with Oatp1a/1b knockout controls under the conditions used in our studies. Hence, although the humanized OATP1B1 and -1B3 mice showed in vitro and/or in vivo functional activity with some statins, further characterization of these models is required to define their potential use and limitations in the prediction of drug disposition and drug-drug interactions in humans.
Y1  - 2014
U6  - http://dx.doi.org/10.1124/dmd.114.057976
SN  - 1521-009X
VL  - 42
IS  - 8
SP  - 1301
EP  - 1313
PB  - ASPET
CY  - Bethesda, Md.
ER  -