Structural basis for phosphoserine-proline recognition by group IV WW domains

By Mark A. Verdecia, M. Bowman, K. Lu, T. Hunter, J. Noel. Nature Structural Biology, 2000

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Survivin, versatile modulation of cell division and apoptosis in cancer (2003, background): “One can take the view that this does not automatically rule out that survivin may still function as an inhibitor of effector caspases similar to other IAPs (Salvesen and Duckett, 2002), and arguments to explain the lack of activity in cell-free systems may include folding requirements of the recombi”
Cell death by mitotic catastrophe: a molecular definition (2004, background): “Direct regulation of caspase activity by survivin has been proposed (Li et al., 1999), but later disputed (Verdecia et al., 2000).”
Elongation by RNA polymerase II: the short and long of it. (2004, background): “backbone and amino acids Y1–S7 bound to the WW domain of Pin1 (PDB code 1f8a) (Verdecia et al. 2000).”
Structural basis for the inhibition of caspase-3 by XIAP. (2001, positive): “The core BIR domain (residues 163–240) closely resembles its solution structure (Sun et al., 1999) and 1999; Chantalat et al., 2000; Muchmore et al., 2000; Verdecia et al., 2000).”
The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain. (2003, neutral): “with Thr et al., 2003; Verdecia et al., 2000). abrogates peptide binding (Figure 1A ), presumably due to a steric clash of the additional ␥-methyl group with”