Performance and Reliability Analysis of Cross-Layer Optimizations of NAND Flash Controllers

NAND flash memories are becoming the predominant technology in the implementation of mass storage systems for both embedded and high-performance applications. However, when considering data and code storage in non-volatile memories (NVMs), such as NAND flash memories, reliability and performance be- come a serious concern for systems' designer. Designing NAND flash based systems based on worst-case scenarios leads to waste of resources in terms of performance, power consumption, and storage capacity. This is clearly in contrast with the request for run-time reconfigurability, adaptivity, and resource optimiza- tion in nowadays computing systems. There is a clear trend toward supporting differentiated access modes in flash memory controllers, each one setting a differentiated trade-off point in the performance-reliability optimization space. This is supported by the possibility of tuning the NAND flash memory performance, reli- ability and power consumption acting on several tuning knobs such as the flash programming algorithm and the flash error correcting code. However, to successfully exploit these degrees of freedom, it is mandatory to clearly understand the effect the combined tuning of these parameters have on the full NVM sub-system. This paper performs a comprehensive quantitative analysis of the benefits provided by the run-time reconfigurability of an MLC NAND flash controller through the combined effect of an adaptable memory programming circuitry coupled with run-time adaptation of the ECC correction capability. The full non- volatile memory (NVM) sub-system is taken into account, starting from the characterization of the low level circuitry to the effect of the adaptation on a wide set of realistic benchmarks in order to provide the readers a clear figure of the benefit this combined adaptation would provide at the system leve

MM2-thalamic Creutzfeldt-Jakob disease-Neuropathological, biochemical and transmission studies identify a distinctive prion strain

In Creutzfeldt-Jakob disease (CJD), molecular typing based on the size of the protease resistant core of the disease-associated prion protein (PrP(Sc) ) and the M/V polymorphism at codon 129 of the PRNP gene correlates with the clinico-pathologic subtypes. Approximately 95% of the sporadic 129MM CJD patients are characterized by cerebral deposition of type 1 PrP(Sc) and correspond to the classic clinical CJD phenotype. The rare 129MM CJD patients with type 2 PrP(Sc) are further subdivided in a cortical and a thalamic form also indicated as sporadic fatal insomnia. We observed two young patients with MM2-thalamic CJD. Main neuropathological features were diffuse, synaptic PrP immunoreactivity in the cerebral cortex and severe neuronal loss and gliosis in the thalamus and olivary nucleus. Western blot analysis showed the presence of type 2A PrP(Sc) . Challenge of transgenic mice expressing 129MM human PrP showed that MM2-thalamic sporadic CJD (sCJD) was able to transmit the disease, at variance with MM2-cortical sCJD. The affected mice showed deposition of type 2A PrP(Sc) , a scenario that is unprecedented in this mouse line. These data indicate that MM2-thalamic sCJD is caused by a prion strain distinct from the other sCJD subtypes including the MM2-cortical form

Synthetic prions with novel strain-specified properties

Prions are infectious proteins that possess multiple self-propagating structures. The information for strains and structural specific barriers appears to be contained exclusively in the folding of the pathological isoform, PrP(Sc). Many recent studies determined that de novo prion strains could be generated in vitro from the structural conversion of recombinant (rec) prion protein (PrP) into amyloidal structures. Our aim was to elucidate the conformational diversity of pathological recPrP amyloids and their biological activities, as well as to gain novel insights in characterizing molecular events involved in mammalian prion conversion and propagation. To this end we generated infectious materials that possess different conformational structures. Our methodology for the prion conversion of recPrP required only purified rec full-length mouse (Mo) PrP and common chemicals. Neither infected brain extracts nor amplified PrP(Sc) were used. Following two different in vitro protocols recMoPrP converted to amyloid fibrils without any seeding factor. Mouse hypothalamic GT1 and neuroblastoma N2a cell lines were infected with these amyloid preparations as fast screening methodology to characterize the infectious materials. Remarkably, a large number of amyloid preparations were able to induce the conformational change of endogenous PrPC to harbor several distinctive proteinase-resistant PrP forms. One such preparation was characterized in vivo habouring a synthetic prion with novel strain specified neuropathological and biochemical properties

Wide angle and out-of-plane correlations in 7Li fragmentation

SIGLEAvailable from British Library Document Supply Centre- DSC:D86320 / BLDSC - British Library Document Supply CentreGBUnited Kingdo