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• "A robust protein host for anchoring chelating ligands and organocatalysts.", Reetz, Rentzsch, Pletsch, Taglieber, Hollmann, Mondière, Dickmann, Höcker, Cerrone, Haeger, Sterner, 2008

  Publication

  In order to put the previously proposed concept of directed evolution of hybrid catalysts (proteins that harbor synthetic transition-metal catalysts...

  Publication on epub.uni-regensburg.de: "A robust protein host for anchoring chelating ligands and organocatalysts." (external link, opens in a new window)

• "Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.", Guldan, Sterner, Babinger, 2008

  Publication

  The exclusive presence of glycerol-1-phosphate dehydrogenases (G1PDH) has been postulated to be a key feature that distinguishes archaea from...

  Publication on epub.uni-regensburg.de: "Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis." (external link, opens in a new window)

• "Computational design of enzymes", Sterner, Merkl, Raushel, 2008

  Publication

  The de novo design of enzymes with activities not found in natural biocatalysts is a major challenge for molecular biology. Sophisticated...

  Publication on epub.uni-regensburg.de: "Computational design of enzymes" (external link, opens in a new window)

• "Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily.", Xiang, Kolb, Fedorov, Meier, Fedorov, Nguyen, Sterner, Almo, Shoichet, Raushel, 2009

  Publication

  Dr0930, a member of the amidohydrolase superfamily in Deinococcus radiodurans, was cloned, expressed, and purified to homogeneity. The enzyme...

  Publication on epub.uni-regensburg.de: "Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily." (external link, opens in a new window)

• "Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release", Schlee, Deuss, Bruning, Ivens, Schwab, Hellmann, Mayans, Sterner, 2009

  Publication

  Anthranilate phosphoribosyltransferase from the hyperthermophilic archaeon Sulfolobus solfataricus (ssAnPRT) is encoded by the sstrpD gene and...

  Publication on epub.uni-regensburg.de: "Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release" (external link, opens in a new window)

• "High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels.", Höcker, Lochner, Seitz, Claren, Sterner, 2009

  Publication

  Ample evidence suggests that the ubiquitous (beta alpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of an ancestral (beta...

  Publication on epub.uni-regensburg.de: "High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels." (external link, opens in a new window)

• "TransCent: computational enzyme design by transferring active sites and considering constraints relevant for catalysis", Fischer, Enkler, Neudert, Bocola, Sterner, Merkl, 2009

  Publication

  Background: Computational enzyme design is far from being applicable for the general case. Due to computational complexity and limited knowledge of...

  Publication on epub.uni-regensburg.de: "TransCent: computational enzyme design by transferring active sites and considering constraints relevant for catalysis" (external link, opens in a new window)

• "Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds", Claren, Malisi, Höcker, Sterner, 2009

  Publication

  The generation of high levels of new catalytic activities on natural and artificial protein scaffolds is a major goal of enzyme engineering. Here, we...

  Publication on epub.uni-regensburg.de: "Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds" (external link, opens in a new window)

• "Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening", Seitz, Thoma, Schoch, Stihle, Benz, D'Arcy, Wiget, Ruf, Hennig, Sterner, 2010

  Publication

  The human glucocorticoid receptor ligand-binding domain (hGR-LBD) is an important drug target for the treatment of various diseases. However, the low...

  Publication on epub.uni-regensburg.de: "Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening" (external link, opens in a new window)

• "Computational and Experimental Evidence for the Evolution of a (βα)8-Barrel Protein from an Ancestral Quarter-Barrel Stabilised by Disulfide Bonds", Richter, Bosnali, Carstensen, Seitz, Durchschlag, Blanquart, Merkl, Sterner, 2010

  Publication

  The evolution of the prototypical (beta alpha)(8)-barrel protein imidazole glycerol phosphate synthase (HisF) was studied by complementary...

  Publication on epub.uni-regensburg.de: "Computational and Experimental Evidence for the Evolution of a (βα)8-Barrel Protein from an Ancestral Quarter-Barrel Stabilised by Disulfide Bonds" (external link, opens in a new window)