Publikationen
Zhang N N, Müller B, Kirkeby T Ø, Kara S*, Loderer C.* Development of a Thioredoxin-Based Cofactor Regeneration System for NADPH-Dependent Oxidoreductases. ChemCatChem 2021, 14(7):e202101625.
Eltoukhy L, Loderer C.* A Multi-enzyme Cascade for the Biosynthesis of AICA Ribonucleoside Di- and Triphosphate. ChemBioChem 2021, 22:1–8.
Schell E, Nouairia G, Steiner E, Weber N, Lundin D, Loderer C.* Structural determinants and distribution of phosphate specificity in ribonucleotide reductases. J Biol Chem 2021, 297(2):101008.
Frisch J, Maršić T, Loderer C.* A Novel One-Pot Enzyme Cascade for the Biosynthesis of Cladribine Triphosphate. Biomolecules 2021, 11(3):346.
Sun Z., Popp PF, Loderer C, Revilla-Guarinos A. Genetically engineered bacterial biohybrid microswimmers for sensing applications. Sensors 2020, 20(1):180.
Revilla-Guarinos A, Zhang Q, Loderer C, Alcántara C, Müller C, Rahnamaeian C, Vilcinskas A, Gebhard S, Zúñiga M, Mascher T.* ABC transporter DerAB of Lactobacillus casei mediates resistance against insect-derived defensins. Appl Env Microbiol. 2020, 86(14)
Loderer C*, Holmfeldt K, Lundin D. Non-host class II ribonucleotide reductase in Thermus viruses: sequence adaptation and host interaction. PeerJ 2019, 7:e6700.
Loderer C, Wagner D, Morgenstern F, Spieß A, Ansorge-Schumacher M.* Discovery of a novel thermostable Zn2+ -dependent alcohol dehydrogenase from Chloroflexus aurantiacus through conserved domains mining. J Appl Microbiol. 2018, 124(2):480-490.
Rozmann-Grinberg I, Lundin D, Hasan M, Crona C, Jonna VR, Loderer C, Sahlin M, Markova M, Borovok I, Berggren G, Hofer A, Logan D, Sjöberg BM.* Unique ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit. eLife. 2018, 7:e31529.
Loderer C, Crona M, Sahlin M, Rozmann-Grinberg I, Lundin D, Hofer A, Sjöberg BM.* A unique cysteine-rich Zn-finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover. J Biol Chem. 2017, 292(46):19044-19054.
Loderer C, Ansorger-Schumacher M.* Magic Mushrooms: Screening for Novel Biocatalysts in the Phylum Basidiomycota. Adv Biosci Biotech. 2016, 7(11), 446
Dhoke G V, Loderer C, Davari M D, Ansorge-Schumacher M, Schwaneberg U, Bocola M.* Activity prediction of substrates in NADH-dependent carbonyl reductase by docking requires catalytic constraints and charge parameterization of catalytic zinc environment. J Comput Aided Mol Des. 2015, 29(11):1057-69.
Loderer C, Dhoke G V, Kroutil W, Bocola M, Ansorge-Schumacher M.* Investigation of structural determinants for the substrate specificity in the zinc-dependent alcohol dehydrogenase CPCR2 from Candida parapsilosis. Chembiochem. 2015, 16(10):1512-9.
Grosch JH, Loderer C, Jestel T, Ansorge-Schumacher M, Spieß AC.* Carbonyl reductase of Candida parapsilosis–Stability analysis and stabilization strategy. J mol catal B enzym. 2015 112, 45-53
Loderer C, Morgenstern F, Ansorge-Schumacher M.* A Zinc-Dependent Alcohol Dehydrogenase (ADH) from Thauera aromatica, Reducing Cyclic α- and β-Diketones. Adv Synth Catal. 2015, 357(8) 1872-80.
Loderer C, Ansorge-Schumacher M.* Enzyme-catalyzed regio- and enantioselective preparative scale synthesis of (S)-2-hydroxy alkanones. RSC Adv. 2015, 5:38271-76.
Man H, Loderer C, Ansorge-Schumacher M, Grogan G.* Structure of NADH-Dependent Carbonyl Reductase (CPCR2) from Candida parapsilosis Provides Insight into Mutations that Improve Catalytic Properties. ChemCatChem. 2014, 6(4):1103–1111.
Grosch JH, Loderer C, Ansorge‐Schumacher M, Spieß AC.* Candida parapsilosis‐Carbonylreduktase (CPCR2)–Struktur‐und Stabilitätsanalyse. CIT. 2015, 86(9), 1413-1414
Angelov A, Loderer C, Pompei S, Liebl W.* Novel family of carbohydrate-binding modules revealed by the genome sequence of Spirochaeta thermophila DSM 6192. Appl Env Microbiol. 2011, 77(15), 5483-5489
Jaber E, Thiele K, Kindzierski V, Loderer C, Rybak K, Jürgens G, Mayer U, Söllner R. Wanner G, Assaad FF.* A putative TRAPPII tethering factor is required for cell plate assembly during cytokinesis in Arabidopsis. New Phyt. 2010, 187(3), 751-763