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The structural and functional characterization of the N-terminal domain of the Toll-like receptor signalling adaptor TRIF/TICAM-1 is presented. The 2.22 Å resolution crystal structure was determined by selenomethionine-based SAD phasing using a protein containing two additional introduced methionines.

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Nucleocytoplasmic trafficking of dUTPase, an enzyme essential for DNA integrity, is regulated by phosphorylation. The mechanism underlying this control is revealed by three-dimensional structures and cellular investigations.
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