Dias, Ricardo, João Louren{\c c}o, and Gon{\c c}alo Cunha. "
Developing libraries using software transactional memory."
Comput. Sci. Inf. Syst.. 5 (2008): 103-117.
AbstractSoftware transactional memory is a promising programming model that adapts many concepts borrowed from the databases world to control concurrent accesses to main memory (RAM). This paper discusses how to support revertible operations, such as memory allocation and release, within software libraries that will be used in software memory transactional contexts. The proposal is based in the extension of the transaction life cycle state diagram with new states associated to the execution of user-defined handlers. The proposed approach is evaluated in terms of functionality and performance by way of a use case study and performance tests. Results demonstrate that the proposal and its current implementation are flexible, generic and efficient
Dias, Ricardo, João Louren{\c c}o, and Gon{\c c}alo Cunha. "
Developing Libraries Using Software Transactional Memory."
CoRTA 2008: Proceedings of the Conference on Compilers, Related Technologies and Applications. Instituto Politécnico de Bragan{\c c}a - ESTG, 2008.
AbstractSoftware transactional memory (STM) is a promising programming model that adapts many concepts borrowed from the databases world to control concurrent accesses to main memory (RAM) locations. This paper aims at discussing how to support apparently irreversible operations within a memory transaction.
Monteiro, R. C. C., M. M. R. A. Lima, and C. S. Clemente. "
Development of structural ceramics from fly ash and shale."
Materials Science Forum. 587-588 (2008): 787-791.
AbstractThe possibility of using fly ash and shale as alternative raw materials for the production of structural ceramics was investigated. Fly ash is a by-product from coal-burning power plants, and shale is a sedimentary rock that if ground finely enough can exhibit a clay-like plasticity. Ceramic samples containing 10-50 wt% fly ash were formed from mechanical mixing of both kinds of powders that were packed and sintered in the temperature range 950-1200°C It was verified that powders with larger fly ash content exhibited lower packing density resulting in compacts with a lower sintered density. Although an increase in fly ash content was associated to a larger presence of porosity in the sintered samples, as confirmed by microstructural analysis, all studied compositions when sintered at the highest temperatures exhibited satisfactory values for water absorption (< 10%), for flexural strength (20-64 MPa) and for hardness (20-30 GPa) indicating that they have potential to be applied in the production of structural ceramics.
Dell'acqua, S., S. R. Pauleta, E. Monzani, AS Pereira, L. Casella, JJG Moura, and I. Moura. "
Electron transfer complex between nitrous oxide reductase and cytochrome c(552) from Pseudomonas nautica: Kinetic, nuclear magnetic resonance, and docking studies."
Biochemistry. 47 (2008): 10852-10862.
AbstractThe multicopper enzyme nitrous oxide reductase (N2OR) catalyzes the final step of denitrification, the two-electron reduction of N2O to N-2. This enzyme is a functional homodimer containing two different multicopper sites: CuA and CuZ. CuA is a binuclear copper site that transfers electrons to the tetranuclear copper sulfide CuZ, the catalytic site. In this study, Pseudomonas nautica cytochrome C-552 was identified as the physiological electron donor. The kinetic data show differences when physiological and artificial electron donors are compared [cytochrome vs methylviologen (MV)]. In the presence of cytochrome c(552), the reaction rate is dependent on the ET reaction and independent of the N2O concentration. With MV, electron donation is faster than substrate reduction. From the study of cytochrome c(552) concentration dependence, we estimate the following kinetic parameters: K-mc512 = 50.2 +/- 9.0 mu M and V-maxc551 1.8 +/- 10.6 units/mg. The N2O concentration dependence indicates a K-mN2O of 14.0 +/- 2.9 mu M using MV as the electron donor. The pH effect on the kinetic parameters is different when MV or cytochrome c(552) is used as the electron donor (pK(a) = 6.6 or 8.3, respectively). The kinetic study also revealed the hydrophobic nature of the interaction, and direct electron transfer studies showed that CuA is the center that receives electrons from the physiological electron donor. The formation of the electron transfer complex was observed by H-1 NMR protein-protein titrations and was modeled with a molecular docking program (BiGGER). The proposed docked complexes corroborated the ET studies giving a large number of solutions in which cytochrome c(552) is placed near a hydrophobic patch located around the CuA center.