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Identifying accurate biomarkers of cognitive decline is essential for advancing early diagnosis and prevention therapies in Alzheimer's disease. The Alzheimer's disease DREAM Challenge was designed as a computational crowdsourced project to benchmark the current state-of-the-art in predicting cognitive outcomes in Alzheimer's disease based on high dimensional, publicly available genetic and structural imaging data. This meta-analysis failed to identify a meaningful predictor developed from either data modality, suggesting that alternate approaches should be considered for prediction of cognitive performance.

Bit-alterable flash memory is a cutting-edge technology that enables a novel operation, called page-level erase operation, to erase a flash page within a block arbitrarily. Though the page-level erase operation can ease the overhead of the live-page copying during a garbage collection process, it also introduces a new wear-leveling problem. In such the problem, flash pages within the same block will receive different program/erase (P/E) cycles during runtime. Some specific pages storing hot data will be worn out soon; therefore, the lifespan of the bit-alterable flash memory will be short due to the uneven worn out of flash pages. Consequently, it becomes a critical issue with the bit-alterable flash memory, and the state-of-art wear-leveling designs cannot resolve this problem. For tackling the problem, this study presents a duo-phase data management scheme considering the page-level wear-leveling issue. The duo-phase mechanism simultaneously cares about page- and block-level wear-leveling issues. On the page-level wear-leveling problem, the duo-phase scheme identifies hot flash pages via the few bits and softly restricts the hot flash page to store hot data without sacrificing storage capacity. On the other hand, our proposed mechanism also figures out the solution to minimize the number of copied live pages for the block-level wear-leveling issue. According to the experimental results, our duo-phase scheme can prolong the lifespan of the bit-alterable flash memory by 1.5 to 1.9 times, compared with the state-of-art garbage collection mechanisms. [ABSTRACT FROM AUTHOR]

By binding to short and highly conserved DNA sequences in genomes, DNA-binding proteins initiate, enhance or repress biological processes. Accurately identifying such binding sites, often represented by position weight matrices (PWMs), is an important step in understanding the control mechanisms of cells. When given coordinates of a DNA-binding domain (DBD) bound with DNA, a potential function can be used to estimate the change of binding affinity after base substitutions, where the changes can be summarized as a PWM. This technique provides an effective alternative when the chromatin immunoprecipitation data are unavailable for PWM inference. To facilitate the procedure of predicting PWMs based on protein-DNA complexes or even structures of the unbound state, the web server, DBD2BS, is presented in this study. The DBD2BS uses an atom-level knowledge-based potential function to predict PWMs characterizing the sequences to which the query DBD structure can bind. For unbound queries, a list of 1066 DBD-DNA complexes (including 1813 protein chains) is compiled for use as templates for synthesizing bound structures. The DBD2BS provides users with an easy-to-use interface for visualizing the PWMs predicted based on different templates and the spatial relationships of the query protein, the DBDs and the DNAs. The DBD2BS is the first attempt to predict PWMs of DBDs from unbound structures rather than from bound ones. This approach increases the number of existing protein structures that can be exploited when analyzing protein-DNA interactions. In a recent study, the authors showed that the kernel adopted by the DBD2BS can generate PWMs consistent with those obtained from the experimental data. The use of DBD2BS to predict PWMs can be incorporated with sequence-based methods to discover binding sites in genome-wide studies. Available at: http://dbd2bs.csie.ntu.edu.tw/, http://dbd2bs.csbb.ntu.edu.tw/, and http://dbd2bs.ee.ncku.edu.tw.