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Träfflista för sökning "WFRF:(Biondi A) srt2:(2005-2009)"

Sökning: WFRF:(Biondi A) > (2005-2009)

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  • Moorman, AV, et al. (författare)
  • No prognostic effect of additional chromosomal abnormalities in children with acute lymphoblastic leukemia and 11q23 abnormalities
  • 2005
  • Ingår i: Leukemia. - London : Nature Publishing Group. - 0887-6924 .- 1476-5551. ; 19:4, s. 557-563
  • Tidskriftsartikel (refereegranskat)abstract
    • This study characterized the additional chromosomal abnormalities (ACA) associated with 11q23 rearrangements in 450 infants and children with acute lymphoblastic leukemia ( ALL) and examined the impact of these ACA on survival. Overall, 213 (47%) cases had ACA but the incidence varied according to patient age and 11q23 subgroup. Infants and patients with t(4; 11)(q21; q23) had the lowest incidence of ACA (50/182 (27%) and 57/216 (26%) respectively), whereas patients with del( 11)( q23) had the highest incidence (66/93 (71%)). Del( 11)( q23) abnormalities were heterogeneous and occasionally secondary to t( 9; 22)(q34; q11.2). Thus, patients with del( 11)( q23) comprised a separate biological entity, which was clearly distinct from those with an 11q23 translocation. The most frequent specific ACA were trisomy X ( n = 38), abnormal 12p ( n = 32), abnormal 9p ( n = 28) and del( 6q) ( n = 19). The presence of ACA did not change the 5 year event-free survival estimates among children (56% (95% CI 46 - 65%) vs 62% (54 - 69%)) or infants (22% ( 15 - 29%) vs 18% ( 9 - 29%)), nor when the different 11q23 subgroups were analyzed separately. This study has conclusively demonstrated that there is no prognostic effect of secondary chromosomal changes in association with 11q23 abnormalities in childhood ALL. However, characterization of these ACA is important to determine their potential role in initiation of MLL driven leukemogenesis.
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  • Hindie, Valerie, et al. (författare)
  • Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1.
  • 2009
  • Ingår i: Nature Chemical Biology. - : Springer Science and Business Media LLC. - 1552-4450 .- 1552-4469. ; 5:10
  • Tidskriftsartikel (refereegranskat)abstract
    • Protein phosphorylation transduces a large set of intracellular signals. One mechanism by which phosphorylation mediates signal transduction is by prompting conformational changes in the target protein or interacting proteins. Previous work described an allosteric site mediating phosphorylation-dependent activation of AGC kinases. The AGC kinase PDK1 is activated by the docking of a phosphorylated motif from substrates. Here we present the crystallography of PDK1 bound to a rationally developed low-molecular-weight activator and describe the conformational changes induced by small compounds in the crystal and in solution using a fluorescence-based assay and deuterium exchange experiments. Our results indicate that the binding of the compound produces local changes at the target site, the PIF binding pocket, and also allosteric changes at the ATP binding site and the activation loop. Altogether, we present molecular details of the allosteric changes induced by small compounds that trigger the activation of PDK1 through mimicry of phosphorylation-dependent conformational changes.
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