Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases

Molecular shape and prominent role of β-strand swapping in organization of dUTPase oligomers

(2009) Enikő Takács et al.   FEBS LETTERS

Keeping Uracil Out of DNA: Physiological Role, Structure and Catalytic Mechanism of dUTPases

(2008) Beáta G Vértessy et al.   ACCOUNTS OF CHEMICAL RESEARCH

Active site of mycobacterial dUTPase: Structural characteristics and a built-in sensor

(2008) Balázs Varga et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

A Double Role for a Strictly Conserved Serine: Further Insights into the dUTPase Catalytic Mechanism

(2008) Lorena González Palmén et al.   BIOCHEMISTRY

Functional Analysis of the Mycobacterium tuberculosis FAD-Dependent Thymidylate Synthase, ThyX, Reveals New Amino Acid Residues Contributing to an Extended ThyX Motif

(2008) J. E. Ulmer et al.   JOURNAL OF BACTERIOLOGY

Experimental study on dUTPase-inhibitor candidate and dUTPase/disaccharide mixtures by PCS and ENS

(2007) B. Varga et al.   JOURNAL OF MOLECULAR STRUCTURE

Methylene substitution at the α–β bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site

(2007) Júlia Kovári et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS