@misc{AskinEmmerichFritscheGoppeletal.2012, author = {Askin, Elif and Emmerich-Fritsche, Angelika and Goppel, Anna and Hemmerling, Mario and Kapaun, Nina and Lohmann, Georg and M{\"u}ller, Sebastian and Niederberger, Andreas and Pabel, Katharina and Putzer, Max and Roth-Isigkeit, David and Seidler, Christoph and Tiedemann, Paul and Vasel, J. Justus and Weiß, Norman}, title = {MenschenRechtsMagazin : Informationen | Meinungen | Analysen}, volume = {17}, number = {2}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, issn = {1434-2820}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-62122}, year = {2012}, abstract = {Aus dem Inhalt: - Themenschwerpunkt: Menschenrechte und Staatsb{\"u}rgerschaft - Gibt es Menschenrechte ohne B{\"u}rgerschaft? - Menschenw{\"u}rde und Staatsb{\"u}rgerschaft - Die General Comments des Menschenrechtsausschusses der Vereinten Nationen - ein Beitrag zur Rechtsentwicklung im V{\"o}lkerrecht - Politische Selbstbestimmung als Menschenrecht und im V{\"o}lkerrecht - Libyen und der von außen unterst{\"u}tzte Systemwechsel}, language = {de} } @article{StalzRothSchleuderetal.2006, author = {Stalz, Holger and Roth, Udo and Schleuder, Detlev and Macht, Marcus and Haebel, Sophie and Strupat, Kerstin and Peter-Katalinic, Jasna and Hanisch, Franz-Georg}, title = {The Geodia cydonium galectin exhibits prototype and chimera-type characteristics and a unique sequence polymorphism within its carbohydrate recognition domain}, doi = {10.1093/glycob/cwj086}, year = {2006}, abstract = {The ancestral galectin from the sponge Geodia cydonium (GCG) is classified on a structural basis to the prototype subfamily, whereas its carbohydrate-binding specificity is related to that of the mammalian chimera-type galectin-3. This dual coordination reveals GCG as a potential precursor of the later evolved galectin subfamilies, which is reflected in the primary structure of the protein. This study provides evidence that GCG is the LECT1 gene product, while neither a previously described LECT2 gene nor a functional LECT2 gene product was found in the specimen under investigation. The electrophoretically separated protein isomers with apparent molecular masses of 13, 15, and 16 kDa correspond to variants of the LECT1 protein-exhibiting peptide sequence polymorphisms that concern critical positions of the carbohydrate recognition domain (13 kDa: Leu51, Asn55, His130, Gly137; 15 kDa: Ser51, Asn55, Asn130, Gly137; 16 kDa: Ser51, Tyr55, Asn130, Glu137). Four residues, highly conserved in the galectin family, are substituted. None of the residues claimed to be involved in interactions with GalNAc alpha 1-3 moieties at an extended binding subsite of galectin-3 was identified in the corresponding positions of GCG. Apparently, the substitutions do not confer distinct binding characteristics to the GCG variants as evidenced by binding studies with a recombinantly expressed 15-kDa isoform. The natural isoforms as well as the recombinant 15-kDa isoform oligomerize by the formation of non-covalent heteromeric or homomeric complexes. A phosphorylation of the galectin was confirmed neither by mass spectrometry nor by alkaline phosphatase treatment combined with isoelectric focusing}, language = {en} } @article{LiebeckHidalgoRothetal.2017, author = {Liebeck, Bernd Michael and Hidalgo, Natalia and Roth, Georg and Popescu, Crisan and B{\"o}ker, Alexander}, title = {Synthesis and characterization of Methyl Cellulose/Keratin Hydrolysate Composite Membranes}, series = {Polymers / Molecular Diversity Preservation International}, volume = {9}, journal = {Polymers / Molecular Diversity Preservation International}, publisher = {MDPI}, address = {Basel}, issn = {2073-4360}, doi = {10.3390/polym9030091}, pages = {13}, year = {2017}, abstract = {It is known that aqueous keratin hydrolysate solutions can be produced from feathers using superheated water as solvent. This method is optimized in this study by varying the time and temperature of the heat treatment in order to obtain a high solute content in the solution. With the dissolved polypeptides, films are produced using methyl cellulose as supporting material. Thereby, novel composite membranes are produced from bio-waste. It is expected that these materials exhibit both protein and polysaccharide properties. The influence of the embedded keratin hydrolysates on the methyl cellulose structure is investigated using Fourier transform infrared spectroscopy (FTIR) and wide angle X-ray diffraction (WAXD). Adsorption peaks of both components are present in the spectra of the membranes, while the X-ray analysis shows that the polypeptides are incorporated into the semi-crystalline methyl cellulose structure. This behavior significantly influences the mechanical properties of the composite films as is shown by tensile tests. Since further processing steps, e.g., crosslinking, may involve a heat treatment, thermogravimetric analysis (TGA) is applied to obtain information on the thermal stability of the composite materials.}, language = {en} } @book{AmendTrautBayerleDunckeretal.2018, author = {Amend-Traut, Anja and Bayerle, Katrin and Duncker, Arne Dirk and Dusil, Stephan and Forster, Wolfgang and Frassek, Ralf and Hermann, Hans-Georg and Koch, Elisabeth and Lettmaier, Saskia and L{\"o}hning, Martin and Ludyga, Hannes and Maetschke, Matthias and Mayenburg, David von and Meder, Stephan and Repgen, Tilman and Roth, Andreas and Saar, Stefan Christoph and Schlinker, Steffen and Schmoeckel, Matthias and Schumann, Eva and Thier, Andreas}, title = {Familienrecht \S\S 1297-1921}, series = {Historisch-kritischer Kommentar zum BGB ; 4}, journal = {Historisch-kritischer Kommentar zum BGB ; 4}, publisher = {Mohr Siebeck}, address = {T{\"u}bingen}, isbn = {978-3-16-156399-7}, pages = {XXXVIII,1622}, year = {2018}, language = {de} }