TY  - JOUR
A1  - Arridge, Christopher S.
A1  - Achilleos, N.
A1  - Agarwal, Jessica
A1  - Agnor, C. B.
A1  - Ambrosi, R.
A1  - Andre, N.
A1  - Badman, S. V.
A1  - Baines, K.
A1  - Banfield, D.
A1  - Barthelemy, M.
A1  - Bisi, M. M.
A1  - Blum, J.
A1  - Bocanegra-Bahamon, T.
A1  - Bonfond, B.
A1  - Bracken, C.
A1  - Brandt, P.
A1  - Briand, C.
A1  - Briois, C.
A1  - Brooks, S.
A1  - Castillo-Rogez, J.
A1  - Cavalie, T.
A1  - Christophe, B.
A1  - Coates, Andrew J.
A1  - Collinson, G.
A1  - Cooper, John F.
A1  - Costa-Sitja, M.
A1  - Courtin, R.
A1  - Daglis, I. A.
A1  - De Pater, Imke
A1  - Desai, M.
A1  - Dirkx, D.
A1  - Dougherty, M. K.
A1  - Ebert, R. W.
A1  - Filacchione, Gianrico
A1  - Fletcher, Leigh N.
A1  - Fortney, J.
A1  - Gerth, I.
A1  - Grassi, D.
A1  - Grodent, D.
A1  - Grün, Eberhard
A1  - Gustin, J.
A1  - Hedman, M.
A1  - Helled, R.
A1  - Henri, P.
A1  - Hess, Sebastien
A1  - Hillier, J. K.
A1  - Hofstadter, M. H.
A1  - Holme, R.
A1  - Horanyi, M.
A1  - Hospodarsky, George B.
A1  - Hsu, S.
A1  - Irwin, P.
A1  - Jackman, C. M.
A1  - Karatekin, O.
A1  - Kempf, Sascha
A1  - Khalisi, E.
A1  - Konstantinidis, K.
A1  - Kruger, H.
A1  - Kurth, William S.
A1  - Labrianidis, C.
A1  - Lainey, V.
A1  - Lamy, L. L.
A1  - Laneuville, Matthieu
A1  - Lucchesi, D.
A1  - Luntzer, A.
A1  - MacArthur, J.
A1  - Maier, A.
A1  - Masters, A.
A1  - McKenna-Lawlor, S.
A1  - Melin, H.
A1  - Milillo, A.
A1  - Moragas-Klostermeyer, Georg
A1  - Morschhauser, Achim
A1  - Moses, J. I.
A1  - Mousis, O.
A1  - Nettelmann, N.
A1  - Neubauer, F. M.
A1  - Nordheim, T.
A1  - Noyelles, B.
A1  - Orton, G. S.
A1  - Owens, Mathew
A1  - Peron, R.
A1  - Plainaki, C.
A1  - Postberg, F.
A1  - Rambaux, N.
A1  - Retherford, K.
A1  - Reynaud, Serge
A1  - Roussos, Elias
A1  - Russell, C. T.
A1  - Rymer, Am.
A1  - Sallantin, R.
A1  - Sanchez-Lavega, A.
A1  - Santolik, O.
A1  - Saur, J.
A1  - Sayanagi, Km.
A1  - Schenk, P.
A1  - Schubert, J.
A1  - Sergis, N.
A1  - Sittler, E. C.
A1  - Smith, A.
A1  - Spahn, Frank
A1  - Srama, Ralf
A1  - Stallard, T.
A1  - Sterken, V.
A1  - Sternovsky, Zoltan
A1  - Tiscareno, M.
A1  - Tobie, G.
A1  - Tosi, F.
A1  - Trieloff, M.
A1  - Turrini, D.
A1  - Turtle, E. P.
A1  - Vinatier, S.
A1  - Wilson, R.
A1  - Zarkat, P.
T1  - The science case for an orbital mission to Uranus: Exploring the origins and evolution of ice giant planets
JF  - Planetary and space science
N2  - Giant planets helped to shape the conditions we see in the Solar System today and they account for more than 99% of the mass of the Sun's planetary system. They can be subdivided into the Ice Giants (Uranus and Neptune) and the Gas Giants (Jupiter and Saturn), which differ from each other in a number of fundamental ways. Uranus, in particular is the most challenging to our understanding of planetary formation and evolution, with its large obliquity, low self-luminosity, highly asymmetrical internal field, and puzzling internal structure. Uranus also has a rich planetary system consisting of a system of inner natural satellites and complex ring system, five major natural icy satellites, a system of irregular moons with varied dynamical histories, and a highly asymmetrical magnetosphere. Voyager 2 is the only spacecraft to have explored Uranus, with a flyby in 1986, and no mission is currently planned to this enigmatic system. However, a mission to the uranian system would open a new window on the origin and evolution of the Solar System and would provide crucial information on a wide variety of physicochemical processes in our Solar System. These have clear implications for understanding exoplanetary systems. In this paper we describe the science case for an orbital mission to Uranus with an atmospheric entry probe to sample the composition and atmospheric physics in Uranus' atmosphere. The characteristics of such an orbiter and a strawman scientific payload are described and we discuss the technical challenges for such a mission. This paper is based on a white paper submitted to the European Space Agency's call for science themes for its large-class mission programme in 2013.
KW  - Uranus
KW  - Magnetosphere
KW  - Atmosphere
KW  - Natural satellites
KW  - Rings
KW  - Planetary interior
Y1  - 2014
U6  - https://doi.org/10.1016/j.pss.2014.08.009
SN  - 0032-0633
VL  - 104
SP  - 122
EP  - 140
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Wolff-Boenisch, D.
A1  - Track, T.
A1  - Schenk, D.
A1  - Oberhänsli, Roland
T1  - Sorptionsverhalten von 2,4,6-Trinitrotoluol und 1,3-Dinitrobenzol an unterschidlichen Bodenmodellsubstanzen
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Inal, Sahika
A1  - Kölsch, Jonas D.
A1  - Sellrie, Frank
A1  - Schenk, Jörg A.
A1  - Wischerhoff, Erik
A1  - Laschewsky, André
A1  - Neher, Dieter
T1  - A water soluble fluorescent polymer as a dual colour sensor for temperature and a specific protein
JF  - Journal of materials chemistry : B, Materials for biology and medicine
N2  - We present two thermoresponsive water soluble copolymers prepared via free radical statistical copolymerization of N-isopropylacrylamide (NIPAm) and of oligo(ethylene glycol) methacrylates (OEGMAs), respectively, with a solvatochromic 7-(diethylamino)-3-carboxy-coumarin (DEAC)-functionalized monomer. In aqueous solutions, the NIPAm-based copolymer exhibits characteristic changes in its fluorescence profile in response to a change in solution temperature as well as to the presence of a specific protein, namely an anti-DEAC antibody. This polymer emits only weakly at low temperatures, but exhibits a marked fluorescence enhancement accompanied by a change in its emission colour when heated above its cloud point. Such drastic changes in the fluorescence and absorbance spectra are observed also upon injection of the anti-DEAC antibody, attributed to the specific binding of the antibody to DEAC moieties. Importantly, protein binding occurs exclusively when the polymer is in the well hydrated state below the cloud point, enabling a temperature control on the molecular recognition event. On the other hand, heating of the polymer-antibody complexes releases a fraction of the bound antibody. In the presence of the DEAC-functionalized monomer in this mixture, the released antibody competitively binds to the monomer and the antibody-free chains of the polymer undergo a more effective collapse and inter-aggregation. In contrast, the emission properties of the OEGMA-based analogous copolymer are rather insensitive to the thermally induced phase transition or to antibody binding. These opposite behaviours underline the need for a carefully tailored molecular design of responsive polymers aimed at specific applications, such as biosensing.
Y1  - 2013
U6  - https://doi.org/10.1039/c3tb21245a
SN  - 2050-750X
SN  - 2050-7518
VL  - 1
IS  - 46
SP  - 6373
EP  - 6381
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - JOUR
A1  - Inal, Sahika
A1  - Kölsch, Jonas D.
A1  - Selrie, Frank
A1  - Schenk, Jörg A.
A1  - Wischerhoff, Erik
A1  - Laschewsky, André
A1  - Neher, Dieter
T1  - A water soluble fluorescent polymer as a dual colour sensor for temperature and a specific protein
N2  - We present two thermoresponsive water soluble copolymers prepared via free radical statistical copolymerization of N-isopropylacrylamide (NIPAm) and of oligo(ethylene glycol) methacrylates (OEGMAs), respectively, with a solvatochromic 7-(diethylamino)-3-carboxy-coumarin (DEAC)-functionalized monomer. In aqueous solutions, the NIPAm-based copolymer exhibits characteristic changes in its fluorescence profile in response to a change in solution temperature as well as to the presence of a specific protein, namely an anti-DEAC antibody. This polymer emits only weakly at low temperatures, but exhibits a marked fluorescence enhancement accompanied by a change in its emission colour when heated above its cloud point. Such drastic changes in the fluorescence and absorbance spectra are observed also upon injection of the anti-DEAC antibody, attributed to the specific binding of the antibody to DEAC moieties. Importantly, protein binding occurs exclusively when the polymer is in the well hydrated state below the cloud point, enabling a temperature control on the molecular recognition event. On the other hand, heating of the polymer-antibody complexes releases a fraction of the bound antibody. In the presence of the DEAC-functionalized monomer in this mixture, the released antibody competitively binds to the monomer and the antibody-free chains of the polymer undergo a more effective collapse and inter-aggregation. In contrast, the emission properties of the OEGMA-based analogous copolymer are rather insensitive to the thermally induced phase transition or to antibody binding. These opposite behaviours underline the need for a carefully tailored molecular design of responsive polymers aimed at specific applications, such as biosensing.
Y1  - 2013
UR  - http://pubs.rsc.org/en/content/articlepdf/2013/tb/c3tb21245a
U6  - https://doi.org/10.1039/c3tb21245a
ER  - 
TY  - GEN
A1  - Inal, Sahika
A1  - Kölsch, Jonas D.
A1  - Sellrie, Frank
A1  - Schenk, Jörg A.
A1  - Wischerhoff, Erik
A1  - Laschewsky, André
A1  - Neher, Dieter
T1  - A water soluble fluorescent polymer as a dual colour sensor for temperature and a specific protein
N2  - We present two thermoresponsive water soluble copolymers prepared via free radical statistical copolymerization of N-isopropylacrylamide (NIPAm) and of oligo(ethylene glycol) methacrylates (OEGMAs), respectively, with a solvatochromic 7-(diethylamino)-3-carboxy-coumarin (DEAC)- functionalized monomer. In aqueous solutions, the NIPAm-based copolymer exhibits characteristic changes in its fluorescence profile in response to a change in solution temperature as well as to the presence of a specific protein, namely an anti-DEAC antibody. This polymer emits only weakly at low temperatures, but exhibits a marked fluorescence enhancement accompanied by a change in its emission colour when heated above its cloud point. Such drastic changes in the fluorescence and absorbance spectra are observed also upon injection of the anti-DEAC antibody, attributed to the specific binding of the antibody to DEAC moieties. Importantly, protein binding occurs exclusively when the polymer is in the well hydrated state below the cloud point, enabling a temperature control on the molecular recognition event. On the other hand, heating of the polymer–antibody complexes releases a fraction of the bound antibody. In the presence of the DEAC-functionalized monomer in this mixture, the released antibody competitively binds to the monomer and the antibody-free chains of the polymer undergo a more effective collapse and inter-aggregation. In contrast, the emission properties of the OEGMA-based analogous copolymer are rather insensitive to the thermally induced phase transition or to antibody binding. These opposite behaviours underline the need for a carefully tailored molecular design of responsive polymers aimed at specific applications, such as biosensing.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 249 
KW  - intramolecular charge-transfer
KW  - phase-transitions
KW  - responsive polymers
KW  - sensitivity
KW  - thermometer
KW  - dyes
KW  - modulation
KW  - assemblies
KW  - antibodies
KW  - binding
Y1  - 2013
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-95336
SP  - 6373
EP  - 6381
ER  -