Patrick Fadden

TL;DR: An amino-terminal domain of hsp90 whose crystal structure has recently been solved and determined to contain a geldanamycin-binding site is studied and it is demonstrated that, in solution, drug binding is exclusive to this domain.

TL;DR: It is shown that aldehyde dehydrogenase 1 and QR2 are selective targets of the quinolines and may provide new insights into the mechanism of action of these drugs.

TL;DR: The results indicate that multiple phosphorylation sites are involved in the control of PHAS-I, and all five sites identified fit a (Ser/Thr)-Pro motif, suggesting that theosphorylation of PHas-I in cells is mediated by a proline-directed protein kinase.

TL;DR: It is shown that the relaxant effect of the catalytic subunit in smooth muscle is markedly potentiated by the addition of the regulatory subunits of SMPP-1M, and that myosin dephosphorylation is regulated in vivo via targeting subunits that specifically alter the substrate specificity of PP-1C toward myOSin.

TL;DR: Control of the translational repressor, PHAS-I, was investigated by expressing proteins with Ser/Thr → Ala mutations in the five (S/T)P phosphorylation sites, which results in the most dramatic decreases in eIF4E binding in vitro.