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Acta Crystallographica. Section F, Structural Biology Communications|June 9, 2020
Structure of heme d1-free cd1 nitrite reductase NirSThomas Klünemann, Wulf BlankenfeldtActa Crystallographica. Section F, Structural Biology and Crystallization Communications|June 7, 2006
The purification, crystallization and preliminary structural characterization of human MAWDBP, a member of the phenazine biosynthesis-like protein familyPetra Herde, Wulf BlankenfeldtCurrent Opinion in Structural Biology|September 13, 2014
The structural biology of phenazine biosynthesisWulf Blankenfeldt, James F ParsonsThe Journal of Biological Chemistry|October 16, 2009
Structures of the dual bromodomains of the P-TEFb-activating protein Brd4 at atomic resolutionFriederike Vollmuth, Wulf Blankenfeldt, Matthias GeyerChembiochem : a European Journal of Chemical Biology|August 24, 2017
Structures of the N-Terminal Domain of PqsA in Complex with Anthraniloyl- and 6-Fluoroanthraniloyl-AMP: Substrate Activation in Pseudomonas Quinolone Signal (PQS) BiosynthesisFlorian Witzgall, Wiebke Ewert, Wulf BlankenfeldtThe Journal of Biological Chemistry|July 22, 2018
Pseudomonas aeruginosa pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinasesJuliane Poppe, Joachim Reichelt, Wulf BlankenfeldtActa Crystallographica. Section D, Structural Biology|April 8, 2020
The crystal structure of the heme d1 biosynthesis-associated small c-type cytochrome NirC reveals mixed oligomeric states in crystalloThomas Klünemann, Steffi Henke, Wulf BlankenfeldtMolecular and Biochemical Parasitology|October 13, 2015
Structural basis for the relaxed substrate selectivity of Leishmania mexicana broad specificity aminotransferaseJiang Wen, Cristina Nowicki, Wulf BlankenfeldtBioorganic & Medicinal Chemistry|January 18, 2017
Recent developments in the isolation, biological function, biosynthesis, and synthesis of phenazine natural productsNikolaus Guttenberger, Wulf Blankenfeldt, Rolf BreinbauerActa Crystallographica. Section F, Structural Biology Communications|August 5, 2016
Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthusTobias Bock, Rolf Müller, Wulf BlankenfeldtPageof 13