| 1. |
|
|
| 2. |
|
|
| 3. |
- Benkner, S., et al.
(författare)
-
The PEPPHER approach to programmability and performance portability for heterogeneous many-core architectures
- 2012
-
Ingår i: Advances in Parallel Computing. - : IOS Press. - 1879-808X .- 0927-5452. ; 22, s. 361-368, s. 361-368
-
Konferensbidrag (refereegranskat)abstract
- The European FP7 project PEPPHER is addressing programmability and performance portability for current and emerging heterogeneous many-core architectures. As its main idea, the project proposes a multi-level parallel execution model comprised of potentially parallelized components existing in variants suitable for different types of cores, memory configurations, input characteristics, optimization criteria, and couples this with dynamic and static resource and architecture aware scheduling mechanisms. Crucial to PEPPHER is that components can be made performance aware, allowing for more efficient dynamic and static scheduling on the concrete, available resources. The flexibility provided in the software model, combined with a customizable, heterogeneous, memory and topology aware run-time system is key to efficiently exploiting the resources of each concrete hardware configuration. The project takes a holistic approach, relying on existing paradigms, interfaces, and languages for the parallelization of components, and develops a prototype framework, a methodology for extending the framework, and guidelines for constructing performance portable software and systems-including paths to migration of existing software-for heterogeneous many-core processors. This paper gives a high-level project overview, and presents a specific example showing how the PEPPHER component variant model and resource-aware run-time system enable performance portability of a numerical kernel. © 2012 The authors and IOS Press. All rights reserved.
|
|
| 4. |
|
|
| 5. |
|
|
| 6. |
|
|
| 7. |
|
|
| 8. |
|
|
| 9. |
- Sonderegger, S, et al.
(författare)
-
Wingless (Wnt)-3A induces trophoblast migration and matrix metalloproteinase-2 secretion through canonical Wnt signaling and protein kinase B/AKT activation
- 2010
-
Ingår i: Endocrinology. - : The Endocrine Society. - 1945-7170 .- 0013-7227. ; 151:1, s. 211-220
-
Tidskriftsartikel (refereegranskat)abstract
- Invasion of human trophoblasts is promoted through activation of wingless (Wnt) signaling, suggesting a role of the pathway in placental development and morphogenesis. However, details on the process such as involvement of canonical and/or noncanonical Wnt signaling cascades as well as their target genes are largely unknown. Hence, signal transduction via canonical Wnt signaling or phosphatidylinositide 3-kinase (PI3K)/AKT and their cross talk as well as trophoblast-specific protease expression were investigated in trophoblastic SGHPL-5 cells and primary extravillous trophoblasts purified from first-trimester placentas. Western blot analyses revealed that the recombinant Wnt ligand Wnt-3A increased phosphorylation of AKT and the downstream kinase glycogen synthase kinase (GSK)-3β as well as accumulation of activated, nuclear β-catenin. In accordance, luciferase expression of a canonical Wnt/TCF reporter and cell migration in first-trimester villous explant cultures and of SGHPL-5 cells were stimulated. Chemical inhibition of PI3K abolished Wnt-dependent phosphorylation of AKT and GSK-3β and trophoblast motility but did not affect appearance of activated β-catenin or Wnt/TCF reporter activity. In contrast, inhibition of the canonical pathway through soluble Dickkopf-1 did not influence AKT and GSK-3β phosphorylation but reduced Wnt reporter activity, accumulation of active β-catenin, and cell migration. Both inhibitors decreased Wnt-3A-induced secretion of pro- and active matrix metalloproteinase-2 from SGHPL-5 cells and pure EVT. The data suggest that Wnt-3A may activate canonical Wnt signaling and PI3K/AKT through distinct receptors. The two signaling cascades act independently in trophoblasts; however, both pathways promote Wnt-dependent migration and the release of matrix metalloproteinase-2, which has been identified as novel Wnt target in invasive trophoblasts.
|
|
| 10. |
|
|
