TY  - GEN
A1  - Poth, S.
A1  - Monzon, M.
A1  - Tippkötter, Nils
A1  - Ulber, Roland
T1  - Fermentation von Hydrolysaten aus Lignocellulose
T2  - Chemie Ingenieur Technik
N2  - Die ökonomische Abhängigkeit von fossilen Brennstoffen und der klimatische Wandel durch die Nutzung dieser haben zu einer intensiven Suche nach erneuerbaren Rohstoffen für die Produktion von Chemikalien und Treibstoffen geführt. Ein viel versprechender Rohstoff in diesem Zusammenhang sind Zucker, die mittels enzymatischer Hydrolyse aus Lignocellulose gewonnen werden können. Die Fermentation erfolgt mit Cellulose- bzw. Hemicellulose-Fraktionen, welche durch thermo-chemische Vorbehandlung von Holz gewonnen und anschließend enzymatisch hydrolysiert werden. Die in den Hydrolysaten enthaltenen Zuckermonomere dienen als Kohlenstoffquelle für die Produktion von Ethanol. Da sowohl Glucose als auch Xylose in den unterschiedlichen Fraktionen enthalten sind, wird zur Umsetzung dieser eine Co-Fermentation zweier Hefen durchgeführt. Im Rahmen der Optimierung dieser Fermentationen werden neben der Ergänzung der Hydrolysate durch notwendige Salze auch Verfahrenweisen wie Fed-Batch-Fermentationen untersucht. Ein weiterer interessanter Ansatz, welcher in diesem Rahmen geprüft wird, ist die enzymatische Hydrolyse der Lignocellulose-Fraktionen und die simultane Fermentation der dabei entstehenden Zucker in einem Schritt. Des Weiteren wurde die Eignung der Hydrolysate für die Biomasseproduktion anderer Mikroorganismen wie Escherichia coli getestet.
Y1  - 2009
U6  - https://doi.org/10.1002/cite.200950243
SN  - 0009-286X
SN  - 1522-2640 (eISSN)
N1  - ProcessNet‐Jahrestagung 2009 und 27. DECHEMA-Jahrestagung der Biotechnologen, 8.- 10. September 2009, Mannheim
N1  - Das hier vorgestellte Vorhaben wird durch die Fachagentur für Nachwachsende Rohstoffe(FNR) gefördert: „Verbundvorhaben: Pilotprojekt Lignocellulose-Bioraffinerie, Teilvorhaben 1: Extraktverarbeitung, Enzymtechnologie, verfahrenstechnische Untersuchungen, Ökobilanzierung, Wirtschaftlichkeitsberechnungen“ (Förderkennzeichen: FNR 22027405).
VL  - 81
IS  - 8
SP  - 1220
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - GEN
A1  - Poth, S.
A1  - Monzon, M.
A1  - Tippkötter, Nils
A1  - Ulber, Roland
T1  - Lignocellulose-Bioraffinerie: Simultane Verzuckerung und Fermentation
T2  - Chemie Ingenieur Technik
N2  - Die am häufigsten genutzten Rohstoffe für die Produktion von Treibstoffen und Chemikalien sind fossilen Ursprungs. Da diese limitiert sind, werden im Hinblick auf die Nachhaltigkeit alternative, erneuerbare Rohstoffquellen intensiv untersucht. Vielversprechend in diesem Kontext sind die in Lignocellulose enthaltenen Zucker, die beispielsweise zur Produktion von Ethanol genutzt werden können. In der Regel sind für eine Lig-nocellulose-Bioraffinerie mehrere Prozessschritte notwendig: Vorbehandlung, Verzuckerung und Fermentation. Um diesen Prozess einfacher zu gestalten, ist es möglich, die Verzuckerung und die Fermentation in einem Schritt durchzuführen (SSF). Als Substrat wird hier Cellulose-Faserstoff verwendet, der durch das Organosolv-Verfahren aufgeschlossen wurde. Die Hydrolyse erfolgt mit kommerziell erhältlichen Enzymen und für die Fermentation zu Ethanol werden zwei Hefen verwendet. Beim SSF-Verfahren konnte, im Vergleich zur entkoppelten Verfahrensweise, trotz bestehender Unterschiede in den Temperatur-Optima von Enzymen und Hefen eine Steigerung in der Ethanol-Ausbeute von 0,15 auf 0,2 gg⁻¹ beobachtet werden. Um wirtschaftliche Ausbeuten und Konzentrationen des Produkts erzielen zu können, ist es notwendig den Prozess weiter zu optimieren. Im Einzelfall muss überprüft werden, ob diese Verfahrensweise auch für die Produktion anderer interessanter Stoffe (wie Itaconsäure, Bernsteinsäure) geeignet ist.
KW  - Lignocellulose-Bioraffinerie
KW  - Prozessintegration
Y1  - 2010
U6  - https://doi.org/10.1002/cite.201050360
N1  - ProcessNet-Jahrestagung 2010 und 28. DECHEMA-Jahrestagung der Biotechnologen, 21. - 23. September 2010, Eurogress Aachen
VL  - 82
IS  - 9
SP  - 1568
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - GEN
A1  - Poth, S.
A1  - Monzon, M.
A1  - Tippkötter, Nils
A1  - Ulber, Roland
T1  - Enzymatische Hydrolyse von vorbehandelter Lignocellulose
T2  - Chemie Ingenieur Technik
N2  - Die ökonomische Abhängigkeit von fossilen Brennstoffen und der klimatische Wandel durch die Nutzung dieser haben zu einer intensiven Suche nach erneuerbaren Rohstoffen für die Produktion von Chemikalien und Treibstoffen geführt. Ein viel versprechender Rohstoff in diesem Zusammenhang sind Zucker, die mittels enzymatischer Hydrolyse aus Lignocellulose gewonnen und beispielsweise zu Ethanol umgesetzt werden können. Dabei ist es notwendig die Hydrolyse in Hinsicht auf das verwendete Substrat und die Verwendung der entstehenden Hydrolysate für die Fermentation von Alkohol zu optimieren. Als Substrat dienen Cellulose- und Hemicellulose-Fraktionen, die durch thermo-chemische Vorbehandlung von Holz gewonnen werden. Die Vorbehandlung erfolgt bei unserem Projektpartner am Johann Heinrich von Thünen Institut in Hamburg. Verschiedene kommerziell erhältliche Enzyme, thermostabile eingeschlossen, wurden auf ihre Fähigkeit hin untersucht, diese Fraktionen zu den entsprechenden Zuckern umsetzen zu können. Um die Konzentration an fermentierbaren Zuckern zu steigern werden verschiedene Optimierungen durchgeführt, z. B. die Erhöhung der Substrat- bzw. Enzymkonzentrationen. Ein weiterer interessanter Ansatz, welcher ebenfalls verfolgt wird, ist es die Hydrolyse und die Fermentation in einem Schritt durchzuführen.
Y1  - 2009
U6  - https://doi.org/10.1002/cite.200950244
SN  - 0009-286X
SN  - 1522-2640 (eISSN)
N1  - ProcessNet‐Jahrestagung 2009 und 27. DECHEMA-Jahrestagung der Biotechnologen, 8.- 10. September 2009, Mannheim
N1  - Das hier vorgestellte Vorhaben wird durch die Fachagentur für Nachwachsende Rohstoffe (FNR) gefördert: „Verbundvorhaben: Pilotprojekt Lignocellulose-Bioraffinerie, Teilvorhaben 1: Extraktverarbeitung, Enzymtechnologie, verfahrenstechnische Untersuchungen, Ökobilanzierung, Wirtschaftlichkeitsberechnungen“ (Förderkennzeichen: FNR 22027405)
VL  - 81
IS  - 8
SP  - 1049
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Poth, Sebastian
A1  - Monzon, Magaly
A1  - Tippkötter, Nils
A1  - Ulber, Roland
T1  - Lignocellulosic biorefinery: Process integration of hydrolysis and fermentation (SSF process)
JF  - Holzforschung
N2  - The aim of the present work is the process integration and the optimization of the enzymatic hydrolysis of wood and the following fermentation of the products to ethanol. The substrate is a fiber fraction obtained by organosolv pre-treatment of beech wood. For the ethanol production, a co-fermentation by two different yeasts (Saccharomyces cerevisiae and Pachysolen tannophilus) was carried out to convert glucose as well as xylose. Two approaches has been followed: 1. A two step process, in which the hydrolysis of the fiber fraction and the fermentation to product are separated from each other. 2. A process, in which the hydrolysis and the fermentation are carried out in one single process step as simultaneous saccharification and fermentation (SSF). Following the first approach, a yield of about 0.15 g ethanol per gram substrate can be reached. Based on the SSF, one process step can be saved, and additionally, the gained yield can be raised up to 0.3 g ethanol per gram substrate.
Y1  - 2011
N1  - 11th EWLP, Hamburg, Germany, August 16–19, 2010
VL  - 65
IS  - 5
SP  - 633
EP  - 637
PB  - De Gruyter
CY  - Berlin
ER  - 
TY  - CHAP
A1  - Poth, Sebastian
A1  - Monzon, Magaly
A1  - Tippkötter, Nils
A1  - Ulber, Roland
T1  - Lignocellulosic biorefinery : process integration of hydrolysis and fermentation
T2  - Proceedings / 11th European Workshop on Lignocellulosics and Pulp : August 16 - 19, 2010, Hamburg, Germany
Y1  - 2010
SP  - 65
EP  - 68
PB  - vTi
CY  - Hamburg
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Hörstermann, D.
A1  - Gyngell, M. L.
A1  - Merboldt, K.-D.
T1  - Localized Proton MRS of Acute and Chronic Gyperglycemia in Rat Brain in vivo / D. Hörstermann, F. Prielmeier , M. L. Gyngell, K.-D. Merboldt, W. Hänicke, J. Frahm
JF  - Book of Abstracts, SMRM, 11th Annual Meeting Berlin
Y1  - 1992
N1  - Society of Magnetic Resonance in Medicine
SP  - 2740
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Lang, E. W.
T1  - Multinuclear Spin-Lattice Relaxation Time Studies of Supercooled Aqueous LiCl-Solutions / E .W. Lang, F. X. Prielmeier
JF  - Berichte der Bunsen-Gesellschaft für Physikalische Chemie. 92 (1988)
Y1  - 1988
SN  - 0005-9021
SP  - 717
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Lang, E. W.
A1  - Lüdemann, H.-D.
T1  - Pressure dependence of the self-diffusion in liquid trifluoromethane / F. X. Prielmeier; E. W. Lang; H.-D. Lüdemann
JF  - Molecular Physics. 52 (1984), H. 5
Y1  - 1984
SN  - 0026-8976
SP  - 1105
EP  - 1113
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Lang, E. W.
A1  - Radkowitsch, H.
A1  - Lüdemann, H. D.
T1  - High Pressure NMR Study of the Molecular Dynamics of Liquid fluoroform and deutero-fluoroform / Lang, E. W. ; Prielmeier, F. X. ; Radkowitsch, H. ; Lüdemann, H. D.
JF  - Berichte der Bunsen-Gesellschaft für Physikalische Chemie. 91 (1987), H. 10
Y1  - 1987
SN  - 0005-9021
SP  - 1025
EP  - 1033
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Lang, E. W.
A1  - Radkowitsch, H.
A1  - Lüdemann, H.-D.
T1  - High Pressure NMR Study of the Molecular Dynamics of Liquid methyl fluoride and deutero-methyl fluoride / Lang, E. W. ; Prielmeier, F. X. ; Radkowitsch, H. ; Lüdemann, H. D.
JF  - Berichte der Bunsen-Gesellschaft für Physikalische Chemie. 91 (1987), H. 10
Y1  - 1987
SN  - 0005-9021
SP  - 1017
EP  - 1025
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Lang, E. W.
A1  - Speedy, R. J.
A1  - Lüdemann, H.-D.
T1  - The pressure Dependence of Self Diffusion in Supercooled Light and Heavy Water / F.X. Prielmeier, E .W. Lang, R. J. Speedy, H.-D. Lüdemann
JF  - Berichte der Bunsen-Gesellschaft für Physikalische Chemie. 92 (1988)
Y1  - 1988
SN  - 0005-9021
SP  - 1111
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Lang, E. W.
A1  - Speedy, R. J.
A1  - Lüdemann, H.-D.
T1  - Diffusion in supercooled water to 300 MPa
JF  - Physical Review Letters. 59 (1987), H. 10
Y1  - 1987
SN  - 0031-9007
SP  - 1128
EP  - 1131
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Lüdemann, H.-D.
T1  - Self diffusion in compressed liquid chloromethane, dichloromethane and trichloromethane / F. X. Prielmeier; H.-D. Lüdemann
JF  - Molecular Physics. 58 (1986), H. 3
Y1  - 1986
SN  - 0026-8976
SP  - 593
EP  - 604
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Merboldt, K. D.
A1  - Hanicke, W.
A1  - Frahm, J.
T1  - Dynamic high-resolution MR imaging of brain deoxygenation during transient anoxia in the anesthetized rat
JF  - Journal of cerebral blood flow and metabolism. 13 (1993), H. 5
Y1  - 1993
SN  - 0271-678X
SP  - 889
EP  - 894
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Nagatomo, Yasushi
A1  - Frahm, Jens
T1  - Cerebral blood oxygenation in rat brain during hypoxic hypoxia. Quantitative MRI of effective transverse relaxation rates
JF  - Magnetic Resonance in Medicine. 31 (1994), H. 6
Y1  - 1994
SN  - 0740-3194
SP  - 678
EP  - 681
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Nagatomo, Yasushi
A1  - Wick, Markus
A1  - Frahm, Jens
T1  - Dynamic monitoring of cerebral metabolites during and after transient global ischemia in rats by quantitative proton NMR spectroscopy in vivo / Yasushi Nagatomo, Markus Wick, Franz Prielmeier, Jens Frahm
JF  - NMR in Biomedicine. 8 (1995), H. 6
Y1  - 1995
SN  - 1099-1492
SP  - 265
EP  - 270
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Radkowitsch, H.
A1  - Lang, E. W.
A1  - Lüdemann, H.-D.
T1  - Density dependence of the molecular dynamics of fluid CH3F and CF3H studied by NMR / H. Radkowitsch, F. X.  Prielmeier, E. W. Lang and H.-D. Lüdemann
JF  - Physica B+C. 139-140 (1986)
Y1  - 1986
SN  - 0921-4526
SP  - 96
EP  - 99
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Speedy, R. J.
A1  - Lüdemann, H.-D.
T1  - High Pressure NMR Self-Diffusion Studies on Supercooled Water
JF  - High Pressure Science and Technology Proceeding XI AIRAPT, Kiew. 1
Y1  - 1987
N1  - AIRAPT Conference / International Association for the Advancement of High Pressure Science and Technology
SP  - 75
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Speedy, R. J.
A1  - Vardag, T.
A1  - Lang, E. W.
T1  - Diffusion in simple fluids / R. J. Speedy;  F. X. Prielmeier;  T. Vardag;  E. W. Lang; H.-D. Lüdemann
JF  - Molecular Physics. 66 (1989), H. 3
Y1  - 1989
SN  - 0026-8976
SP  - 577
EP  - 590
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Wick, Markus
A1  - Nagatomo, Yasushi
A1  - Frahm, Jens
T1  - Alteration of Intracellular Metabolite Diffusion in Rat Brain In Vivo During Ischemia and Reperfusion / Markus Wick,  Yasushi Nagatomo,  Franz Prielmeier,  Jens Frahm
JF  - Stroke. 26 (1995), H. 10
Y1  - 1995
SN  - 0039-2499
SP  - 1930
EP  - 1934
ER  - 
TY  - JOUR
A1  - Prielmeier, Franz
A1  - Woznyj, M.
A1  - Lüdemann, H.-D.
T1  - Pressure Dependence of the Melting and Self Diffusion in 2,2-Dimethylpropane, 2,2-Dimethylpropionitrile, and 2-Methylpropanol-2 / M. Woznyj, F. X. Prielmeier, H.-D. Lüdemann
JF  - Zeitschrift für Naturforschung A, Journal of Physical Sciences. 39 (1984)
Y1  - 1984
SN  - 0932-0784
SP  - 800
ER  - 
TY  - JOUR
A1  - Raab, Monika
A1  - Kappel, Sven
A1  - Krämer, Andrea
A1  - Sanhaji, Mourad
A1  - Matthess, Yves
A1  - Kurunci-Csacsko, Elisabeth
A1  - Calzada-Wack, Julia
A1  - Rathkolb, Birgit
A1  - Rosman, Jan
A1  - Adler, Thure
A1  - Busch, Dirk H.
A1  - Esposito, Irene
A1  - Fuchs, Helmut
A1  - Gailus-Durner, Valérie
A1  - Klingenspor, Martin
A1  - Wolf, Eckhard
A1  - Sänger, Nicole
A1  - Prinz, Florian
A1  - Hrabe de Angelis, Martin
A1  - Seibler, Jost
A1  - Yuan, Juping
A1  - Bergmann, Martin
A1  - Knecht, Rainald
A1  - Kreft, Bertolt
A1  - Strebhardt, Klaus
T1  - Toxicity modelling of Plk1-targeted therapies in genetically engineered mice and cultured primary mammalian cells
JF  - Nature Communications
Y1  - 2011
U6  - https://doi.org/10.1038/ncomms1395
SN  - 2041-1723
VL  - 2
IS  - 395
SP  - 1
EP  - 11
PB  - Nature
CY  - London
ER  - 
TY  - JOUR
A1  - Rachinger, Michael
A1  - Bauch, Melanie
A1  - Strittmatter, Axel
A1  - Bongaerts, Johannes
A1  - Evers, Stefan
A1  - Maurer, Karl-Heinz
A1  - Daniel, Rolf
A1  - Liebl, Wolfgang
A1  - Liesegang, Heiko
A1  - Ehrenreich, Armin
T1  - Size unlimited markerless deletions by a transconjugative plasmid-system in Bacillus licheniformis
JF  - Journal of biotechnology
Y1  - 2013
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
VL  - Vol. 164
IS  - Iss. 4
SP  - 365
EP  - 369
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - BOOK
A1  - Rath, Walter
T1  - Umsetzung [alpha,beta]-ungesaettigter Ketone und ihrer Vorprodukte mit Urotropin
Y1  - 1984
N1  - Stuttgart, Univ., Diss., 1984
ER  - 
TY  - BOOK
A1  - Rath, Walter
A1  - Dzierzynski, Elmar
T1  - Solvent-free contact adhesive = Lösungsmittelfreier Kontaktklebstoff / Rath, Walter ; Dzierzynski, Elmar [Erfinder]
Y1  - 1995
N1  - EP0436347 06.04.1995 Veröffentlichungstag im Patentblatt ; Volltext recherchierbar über:
PB  - Europäisches Patentamt
CY  - München
ER  - 
TY  - BOOK
A1  - Rath, Walter
A1  - Koch, Markus
A1  - Reichardt, Rüdiger
T1  - Composition de polyurethanne et joint d’etancheite pour vitrage = Polyurethanzusammensetzung und Verglasungsdichtungs-Profil / Rath, Walter, Koch, Markus ; Reichardt, Rüdiger [Erfinder]
Y1  - 2002
N1  - EP0789719 24.01.2002 Veröffentlichungstag im Patentblatt  ; Volltext recherchierbar über
PB  - Europäisches Patentamt
CY  - München
ER  - 
TY  - PAT
A1  - Rath, Walter
A1  - Seitz, Karsten
T1  - Frühregenfeste Dichtmasse auf Basis wässriger Acrylatdispersionen und Verfahren zu ihrer Herstellung
Y1  - 1993
N1  - DE000004205358A1 Veröffentlichungstag im Patentblatt 26.08.1993 ; Volltext recherchierbar über
PB  - Deutsches Patent- und Markenamt
CY  - München
ER  - 
TY  - PAT
A1  - Rath, Walter
A1  - Seitz, Karsten
T1  - Frühregenfeste Dichtmasse auf Basis wässriger Acrylatdispersionen und Verfahren zu ihrer Herstellung
Y1  - 1993
N1  - DE000004224044A1 Veröffentlichungstag im Patentblatt 27.01.1994 ; Volltext recherchierbar über
PB  - Deutsches Patent- und Markenamt
CY  - München
ER  - 
TY  - JOUR
A1  - Ratke, Lorenz
A1  - Milow, Barbara
A1  - Lisinski, Susanne
A1  - Hoepfner, Sandra
T1  - On an effect of fine ceramic particles on the structure of aerogels
JF  - Microgravity science and technology
Y1  - 2014
U6  - https://doi.org/10.1007/s12217-014-9380-2
SN  - 0938-0108 ; 1875-0494
VL  - 26
SP  - 103
EP  - 110
PB  - Springer Nature
CY  - Heidelberg
ER  - 
TY  - JOUR
A1  - Raue, Markus
A1  - Wambach, M.
A1  - Glöggler, S.
A1  - Grefen, Dana
A1  - Kaufmann, R.
A1  - Abetz, C.
A1  - Georgopanos, P.
A1  - Handge, U. A.
A1  - Mang, Thomas
A1  - Blümich, B.
A1  - Abetz, V.
T1  - Investigation of historical hard rubber ornaments of Charles Goodyear
JF  - Macromolecular chemistry and physics
Y1  - 2014
SN  - 1022-1352
VL  - Vol. 215
IS  - No. 3
SP  - 245
EP  - 254
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Raupp, Sebastian M.
A1  - Schmitt, Marcel
A1  - Walz, Anna-Lena
A1  - Diehm, Ralf
A1  - Hummel, Helga
A1  - Scharfer, Philip
A1  - Schabel, Wilhelm
T1  - Slot die stripe coating of low viscous fluids
JF  - Journal of Coatings Technology and Research
N2  - Slot die coating is applied to deposit thin and homogenous films in roll-to-roll and sheet-to-sheet applications. The critical step in operation is to choose suitable process parameters within the process window. In this work, we investigate an upper limit for stripe coatings. This maximum film thickness is characterized by stripe merging which needs to be avoided in a stable process. It is shown that the upper limit reduces the process window for stripe coatings to a major extent. As a result, stripe coatings at large coating gaps and low viscosities are only possible for relatively thick films. Explaining the upper limit, a theory of balancing the side pressure in the gap region in the cross-web direction has been developed.
Y1  - 2018
U6  - https://doi.org/10.1007/s11998-017-0039-y
SN  - 1935-3804
VL  - 15
IS  - 5
SP  - 899
EP  - 911
PB  - Springer
ER  - 
TY  - JOUR
A1  - Reugels, Alexander M.
A1  - Boggetti, Barbara
A1  - Scheer, Nico
A1  - Campos-Ortega, José A.
T1  - Asymmetric localization of Numb:EGFP in dividing neuroepithelial cells during neurulation in Danio rerio
JF  - Developmental Dynamics
Y1  - 2006
U6  - https://doi.org/10.1002/dvdy.20699
SN  - 1097-0177
VL  - 235
IS  - 4
SP  - 934
EP  - 948
ER  - 
TY  - JOUR
A1  - Ribitsch, D.
A1  - Heumann, S.
A1  - Karl, W.
A1  - Gerlach, J.
A1  - Leber, R.
A1  - Birner-Gruenberger, R.
A1  - Gruber, K.
A1  - Eiteljoerg, I.
A1  - Remler, P.
A1  - Siegert, Petra
A1  - Lange, J.
A1  - Maurer, Karl-Heinz
A1  - Berg, G.
A1  - Guebitz, G. M.
A1  - Schwab, H.
T1  - Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli
JF  - Journal of biotechnology
N2  - A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3.

From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.
KW  - Alginate beads
KW  - Stenotrophomonas maltophilia
KW  - Detergent protease
Y1  - 2012
U6  - https://doi.org/10.1016/j.jbiotec.2011.09.025
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
VL  - 157
IS  - 1
SP  - 140
EP  - 147
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Ribitsch, D.
A1  - Karl, W.
A1  - Birner-Gruenberger, R.
A1  - Gruber, K.
A1  - Eiteljoerg, I.
A1  - Remler, P.
A1  - Wieland, S.
A1  - Siegert, Petra
A1  - Maurer, Karl-Heinz
A1  - Schwab, H.
T1  - C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli
JF  - Journal of biotechnology
N2  - Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477.

This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7–11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.
Y1  - 2010
U6  - https://doi.org/10.1016/j.jbiotec.2010.09.947
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
VL  - 150
IS  - 3
SP  - 408
EP  - 416
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Ross, Jillian
A1  - Plummer, Simon M.
A1  - Rode, Anja
A1  - Scheer, Nico
A1  - Bower, Conrad C.
A1  - Vogel, Ortwin
A1  - Henderson, Colin J.
A1  - Wolf, C. Roland
A1  - Elcombe, Clifford R.
T1  - Human constitutive androstane receptor (CAR) and pregnane X receptor (PXR) support the  hypertrophic but not the hyperplastic response to the murine nongenotoxic hepatocarcinogens phenobarbital and chlordane in vivo
JF  - Toxicological Sciences
N2  - Mouse nongenotoxic hepatocarcinogens phenobarbital (PB) and chlordane induce hepatomegaly characterized by hypertrophy and hyperplasia. Increased cell proliferation is implicated in the mechanism of tumor induction. The relevance of these tumors to human health is unclear. The xenoreceptors, constitutive androstane receptors (CARs), and pregnane X receptor (PXR) play key roles in these processes. Novel “humanized” and knockout models for both receptors were developed to investigate potential species differences in hepatomegaly. The effects of PB (80 mg/kg/4 days) and chlordane (10 mg/kg/4 days) were investigated in double humanized PXR and CAR (huPXR/huCAR), double knockout PXR and CAR (PXRKO/CARKO), and wild-type (WT) C57BL/6J mice. In WT mice, both compounds caused increased liver weight, hepatocellular hypertrophy, and cell proliferation. Both compounds caused alterations to a number of cell cycle genes consistent with induction of cell proliferation in WT mice. However, these gene expression changes did not occur in PXRKO/CARKO or huPXR/huCAR mice. Liver hypertrophy without hyperplasia was demonstrated in the huPXR/huCAR animals in response to both compounds. Induction of the CAR and PXR target genes, Cyp2b10 and Cyp3a11, was observed in both WT and huPXR/huCAR mouse lines following treatment with PB or chlordane. In the PXRKO/CARKO mice, neither liver growth nor induction of Cyp2b10 and Cyp3a11 was seen following PB or chlordane treatment, indicating that these effects are CAR/PXR dependent. These data suggest that the human receptors are able to support the chemically induced hypertrophic responses but not the hyperplastic (cell proliferation) responses. At this time, we cannot be certain that hCAR and hPXR when expressed in the mouse can function exactly as the genes do when they are expressed in human cells. However, all parameters investigated to date suggest that much of their functionality is maintained.
Y1  - 2010
U6  - https://doi.org/10.1093/toxsci/kfq118
SN  - 1096-0929
VL  - 116
IS  - 2
SP  - 452
EP  - 466
PB  - Oxford University Press
CY  - Oxford
ER  - 
TY  - GEN
A1  - Ross-Jones, J.
A1  - Teumer, T.
A1  - Capitain, C.
A1  - Tippkötter, Nils
A1  - Krause, M. J.
A1  - Methner, F.-J.
A1  - Rädle, M.
T1  - Analytical methods for in-line characterization of beer haze
T2  - Trends in Brewing
N2  - In most beers, producers strive to minimize haze to maximize visual appeal. To detect the formation of particulates, a measurement system for sub-micron particles is required. Beer haze is naturally occurring, composed of protein or polyphenol particles; in their early stage of growth their size is smaller than 2 µm. Microscopy analysis is time and resource intensive; alternatively, backscattering is an inexpensive option for detecting particle sizes of interest.
Y1  - 2018
N1  - Trends in Brewing, April 8 –12, 2018, Ghent, Belgium
ER  - 
TY  - CHAP
A1  - Roth, J.
A1  - Möhring, S.
A1  - Tippkötter, Nils
T1  - Characterization and evaluation of lignocellulosic biomass 130 hydrolysates for ABE fermentation
T2  - New frontiers of biotech-processes (Himmelfahrtstagung) : 02-04 May 2016, Rhein-Mosel-Halle, Koblenz/Germany
Y1  - 2016
SP  - 130
PB  - DECHEMA
CY  - Frankfurt am Main
ER  - 
TY  - GEN
A1  - Roth, J.
A1  - Tippkötter, Nils
T1  - New Approach for Enzymatic Hydrolysis of Lignocellulose with Selective Diffusion Separation of the Monosaccharide Products
T2  - Chemie Ingenieur Technik
N2  - Enzymatic hydrolysis of lignocellulosic material plays an important role in the classical biorefinery approach. Apart from the pretreatment of the raw material, hydrolysis is the basis for the conversion of the cellulose and hemicellulose fraction into fermentable sugars. After hydrolysis, usually a solid-liquid separation takes place, in order to separate the residual plant material from the sugar-rich fraction, which can be subsequently used in a fermentation step. In order to factor out the separation step, the usage of in alginate immobilized crude cellulose fiber beads (CFBs) were evaluated. Pretreated cellulose fibers are incorporated in an alginate matrix together with the relevant enzymes. In doing so, sugars diffuse trough the alginate matrix, allowing a simplified delivery into the surrounding fluid. This again reduces product inhibition of the glucose on the enzyme catalysts. By means of standardized bead production the hydrolysis in lab scale was possible. First results show that liberation of glucose and xylose is possible, allowing a maximum total sugar yield of 75 %.
Y1  - 2016
U6  - https://doi.org/10.1002/cite.201650301
SN  - 0009-286X
SN  - 1522-2640 (eISSN)
N1  - ProcessNet-Jahrestagung 2016 und 32. DECHEMA-Jahrestagung der Biotechnologen 2016, 12. - 15. September 2016, Eurogress Aachen
VL  - 88
IS  - 9
SP  - 1237
PB  - Wiley-VCH
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  - GEN
A1  - Rothkranz, Berit
A1  - Krafft, Simone
A1  - Tippkötter, Nils
T1  - Media optimization for sustainable fuel production: How to produce biohydrogen from renewable resources with Thermotoga neapolitana
T2  - Chemie Ingenieur Technik
N2  - Hydrogen is playing an increasingly important role in research and politics as an energy carrier of the future. Since hydrogen has commonly been produced from methane by steam reforming, the need for climate-friendly, alternative production routes is emerging. In addition to electrolysis, fermentative routes for the production of so-called biohydrogen are "green" alternatives. The application of microorganisms offers the advantage of sustainable production from renewable resources using easily manageable technologies. In this project, the hyperthermophilic, anaerobic microorganism Thermotoga neapolitana is used for the productio nof biohydrogen from renewable resources. The enzymatically hydrolyzed resources were used in fermentation leading to yield coefficients of 1.8 mole H₂ per mole glucose when using hydrolyzed straw and ryegrass supplemented with medium, respectively. These results are similar to the hydrogen yields when using Thermotoga basal medium with glucose (TBGY) as control group. In order to minimize the supplementation of the hydrolysate and thus increase the economic efficiency of the process, the essential media components were identified. The experiments revealed NaCl, KCl, and glucose as essential components for cell growth as well as biohydrogen production. When excluding NaCl, a decrease of 96% in hydrogen production occured.
Y1  - 2022
U6  - https://doi.org/10.1002/cite.202255305
SN  - 0009-286X
SN  - 1522-2640 (eISSN)
N1  - ProcessNet and DECHEMA‐BioTechNet Jahrestagungen 2022 together with 13th ESBES Symposium 2022, 12. - 15. September 2022, Eurogress Aachen
VL  - 94
IS  - 9
SP  - 1298
EP  - 1299
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Röhlen, Desiree
A1  - Pilas, Johanna
A1  - Dahmen, Markus
A1  - Keusgen, Michael
A1  - Selmer, Thorsten
A1  - Schöning, Michael Josef
T1  - Toward a Hybrid Biosensor System for Analysis of Organic and Volatile Fatty Acids in Fermentation Processes
JF  - Frontiers in Chemistry
N2  - Monitoring of organic acids (OA) and volatile fatty acids (VFA) is crucial for the control of anaerobic digestion. In case of unstable process conditions, an accumulation of these intermediates occurs. In the present work, two different enzyme-based biosensor arrays are combined and presented for facile electrochemical determination of several process-relevant analytes. Each biosensor utilizes a platinum sensor chip (14 × 14 mm²) with five individual working electrodes. The OA biosensor enables simultaneous measurement of ethanol, formate, d- and l-lactate, based on a bi-enzymatic detection principle. The second VFA biosensor provides an amperometric platform for quantification of acetate and propionate, mediated by oxidation of hydrogen peroxide. The cross-sensitivity of both biosensors toward potential interferents, typically present in fermentation samples, was investigated. The potential for practical application in complex media was successfully demonstrated in spiked sludge samples collected from three different biogas plants. Thereby, the results obtained by both of the biosensors were in good agreement to the applied reference measurements by photometry and gas chromatography, respectively. The proposed hybrid biosensor system was also used for long-term monitoring of a lab-scale biogas reactor (0.01 m³) for a period of 2 months. In combination with typically monitored parameters, such as gas quality, pH and FOS/TAC (volatile organic acids/total anorganic carbonate), the amperometric measurements of OA and VFA concentration could enhance the understanding of ongoing fermentation processes.
Y1  - 2018
U6  - https://doi.org/10.3389/fchem.2018.00284
IS  - 6
PB  - Frontiers
CY  - Lausanne
ER  - 
TY  - JOUR
A1  - Röhlen, Desiree
A1  - Pilas, Johanna
A1  - Schöning, Michael Josef
A1  - Selmer, Thorsten
T1  - Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid
JF  - Applied Biochemistry and Biotechnology
N2  - Three amperometric biosensors have been developed for the detection of L-malic acid, fumaric acid, and L -aspartic acid, all based on the combination of a malate-specific dehydrogenase (MDH, EC 1.1.1.37) and diaphorase (DIA, EC 1.8.1.4). The stepwise expansion of the malate platform with the enzymes fumarate hydratase (FH, EC 4.2.1.2) and aspartate ammonia-lyase (ASPA, EC 4.3.1.1) resulted in multi-enzyme reaction cascades and, thus, augmentation of the substrate spectrum of the sensors. Electrochemical measurements were carried out in presence of the cofactor β-nicotinamide adenine dinucleotide (NAD+) and the redox mediator hexacyanoferrate (III) (HCFIII). The amperometric detection is mediated by oxidation of hexacyanoferrate (II) (HCFII) at an applied potential of + 0.3 V vs. Ag/AgCl. For each biosensor, optimum working conditions were defined by adjustment of cofactor concentrations, buffer pH, and immobilization procedure. Under these improved conditions, amperometric responses were linear up to 3.0 mM for L-malate and fumarate, respectively, with a corresponding sensitivity of 0.7 μA mM−1 (L-malate biosensor) and 0.4 μA mM−1 (fumarate biosensor). The L-aspartate detection system displayed a linear range of 1.0–10.0 mM with a sensitivity of 0.09 μA mM−1. The sensor characteristics suggest that the developed platform provides a promising method for the detection and differentiation of the three substrates.
Y1  - 2017
U6  - https://doi.org/10.1007/s12010-017-2578-1
SN  - 1559-0291
VL  - 183
SP  - 566
EP  - 581
PB  - Springer
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Rösch, C.
A1  - Kratz, F.
A1  - Hering, T.
A1  - Trautmann, S.
A1  - Umanskaya, N.
A1  - Tippkötter, Nils
A1  - Müller-Renno, C.M.
A1  - Ulber, Roland
A1  - Hannig, M.
A1  - Ziegler, C.
T1  - Albumin-lysozyme interactions: cooperative adsorption on titanium and enzymatic activity
JF  - Colloids and Surfaces B: Biointerfaces
N2  - The interplay of albumin (BSA) and lysozyme (LYZ) adsorbed simultaneously on titanium was analyzed by gel electrophoresis and BCA assay. It was found that BSA and lysozyme adsorb cooperatively. Additionally, the isoelectric point of the respective protein influences the adsorption. Also, the enzymatic activity of lysozyme and amylase (AMY) in mixtures with BSA was considered with respect to a possible influence of protein-protein interaction on enzyme activity. Indeed, an increase of lysozyme activity in the presence of BSA could be observed. In contrast, BSA does not influence the activity of amylase.
Y1  - 2016
U6  - https://doi.org/10.1016/j.colsurfb.2016.09.048
VL  - 149
IS  - 1
SP  - 115
EP  - 121
PB  - Elsevier
CY  - Amsterdam
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  - https://doi.org/10.1124/dmd.114.057976
SN  - 1521-009X
VL  - 42
IS  - 8
SP  - 1301
EP  - 1313
PB  - ASPET
CY  - Bethesda, Md.
ER  - 
TY  - CHAP
A1  - Samuelsson, K.
A1  - Scheer, Nico
A1  - Wilson, I.
A1  - Wolf, C.R.
A1  - Henderson, C.J.
ED  - Chackalamannil, Samuel
T1  - Genetically Humanized Animal Models
T2  - Comprehensive Medicinal Chemistry III. 3rd Edition
N2  - Genetically humanized mice for proteins involved in drug metabolism and toxicity and mice engrafted with human hepatocytes are emerging as promising in vivo models for improved prediction of the pharmacokinetic, drug–drug interaction, and safety characteristics of compounds in humans. This is an overview on the genetically humanized and chimeric liver-humanized mouse models, which are illustrated with examples of their utility in drug metabolism and toxicity studies. The models are compared to give guidance for selection of the most appropriate model by highlighting advantages and disadvantages to be carefully considered when used for studies in drug discovery and development.
KW  - Chimeric liver-humanized mice
KW  - Drug distribution
KW  - Drug metabolism
KW  - Toxicology
KW  - Knockout mice
Y1  - 2017
SN  - 978-0-12-803201-5
U6  - https://doi.org/10.1016/B978-0-12-409547-2.12376-5
SP  - 130
EP  - 149
PB  - Elsevier
CY  - Saint Louis
ER  - 
TY  - JOUR
A1  - Scheele, S.
A1  - Bongaerts, Johannes
A1  - Maurer, K.-H.
A1  - Freudl, R.
T1  - Sekretion einer Kofaktor-haltigen Oxidase durch Corynebacterium glutamicum
JF  - Chemie - Ingenieur - Technik (CIT)
Y1  - 2009
SN  - 1522-2640 (E-Journal); 0009-286X (Print)
VL  - Vol. 81
IS  - Iss. 8
SP  - 1309
ER  - 
TY  - JOUR
A1  - Scheele, Sandra
A1  - Oertel, Dan
A1  - Bongaerts, Johannes
A1  - Evers, Stefan
A1  - Hellmuth, Hendrik
A1  - Maurer, Karl-Heinz
A1  - Bott, Michael
A1  - Freudl, Roland
T1  - Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol–xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum
JF  - Microbial biotechnology
Y1  - 2013
SN  - 1751-7915
SP  - 202
EP  - 206
PB  - Wiley-Blackwell
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Scheer, Nico
A1  - Balimane, Praveen
A1  - Hayward, Michael D.
A1  - Buechel, Sandra
A1  - Kauselmann, Gunther
A1  - Wolf, C. Roland
T1  - Generation and Characterization of a Novel Multidrug Resistance Protein 2 Humanized Mouse Line
JF  - Drug Metabolism and Disposition
N2  - The multidrug resistance protein (MRP) 2 is predominantly expressed in liver, intestine, and kidney, where it plays an important role in the excretion of a range of drugs and their metabolites or endogenous compounds into bile, feces, and urine. Mrp knockout [Mrp2(−/−)] mice have been used recently to study the role of MRP2 in drug disposition. Here, we describe the first generation and initial characterization of a mouse line humanized for MRP2 (huMRP2), which is nulled for the mouse Mrp2 gene and expresses the human transporter in the organs and cell types where MRP2 is normally expressed. Analysis of the mRNA expression for selected cytochrome P450 and transporter genes revealed no major changes in huMRP2 mice compared with wild-type controls. We show that human MRP2 is able to compensate functionally for the loss of the mouse transporter as demonstrated by comparable bilirubin levels in the humanized mice and wild-type controls, in contrast to the hyperbilirubinemia phenotype that is observed in MRP2(−/−) mice. The huMRP2 mouse provides a model to study the role of the human transporter in drug disposition and in assessing the in vivo consequences of inhibiting this transporter by compounds interacting with human MRP2.
Y1  - 2012
U6  - https://doi.org/10.1124/dmd.112.047605
SN  - 1521-0111
VL  - 40
IS  - 11
SP  - 2212
EP  - 2218
PB  - ASPET
CY  - Bethesda, Md.
ER  - 
TY  - JOUR
A1  - Scheer, Nico
A1  - Campos-Ortega, José A.
T1  - Use of the Gal4-UAS technique for targeted gene expression in the zebrafish
JF  - Mechanism of Development
Y1  - 1999
U6  - https://doi.org/10.1016/S0925-4773(98)00209-3
SN  - 0925-4773
VL  - 80
IS  - 2
SP  - 153
EP  - 158
ER  - 
TY  - CHAP
A1  - Scheer, Nico
A1  - Chu, Xiaoyan
A1  - Salphati, Laurent
A1  - Zamek-Gliszczynski, Maciej J.
ED  - Nicholls, Glynis
T1  - Knockout and humanized animal models to study membrane transporters in drug development
T2  - Drug Transporters: Volume 1: Role and Importance in ADME and Drug Development
Y1  - 2016
SN  - 978-1-78262-379-3
U6  - https://doi.org/10.1039/9781782623793-00298
SP  - 298
EP  - 332
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  -