5 resultados para New Space Vector Modulation

em University of Queensland eSpace - Australia


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Streaming video application requires high security as well as high computational performance. In video encryption, traditional selective algorithms have been used to partially encrypt the relatively important data in order to satisfy the streaming performance requirement. Most video selective encryption algorithms are inherited from still image encryption algorithms, the encryption on motion vector data is not considered. The assumption is that motion vector data are not as important as pixel image data. Unfortunately, in some cases, motion vector itself may be sufficient enough to leak out useful video information. Normally motion vector data consume over half of the whole video stream bandwidth, neglecting their security may be unwise. In this paper, we target this security problem and illustrate attacks at two different levels that can restore useful video information using motion vectors only. Further, an information analysis is made and a motion vector information model is built. Based on this model, we describe a new motion vector encryption algorithm called MVEA. We show the experimental results of MVEA. The security strength and performance of the algorithm are also evaluated.

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Music similarity query based on acoustic content is becoming important with the ever-increasing growth of the music information from emerging applications such as digital libraries and WWW. However, relative techniques are still in their infancy and much less than satisfactory. In this paper, we present a novel index structure, called Composite Feature tree, CF-tree, to facilitate efficient content-based music search adopting multiple musical features. Before constructing the tree structure, we use PCA to transform the extracted features into a new space sorted by the importance of acoustic features. The CF-tree is a balanced multi-way tree structure where each level represents the data space at different dimensionalities. The PCA transformed data and reduced dimensions in the upper levels can alleviate suffering from dimensionality curse. To accurately mimic human perception, an extension, named CF+-tree, is proposed, which further applies multivariable regression to determine the weight of each individual feature. We conduct extensive experiments to evaluate the proposed structures against state-of-art techniques. The experimental results demonstrate superiority of our technique.

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The aim of this study was to investigate whether peptides from the extracellular loops of the tight junction protein occludin could be used as a new principle for tight junction modulation. Peptides of 4 to 47 amino acids in length and covering the two extracellular loops of the tight junction protein occludin were synthesized, and their effect on the tight junction permeability in Caco-2 cells was investigated using [C-14] mannitol as a paracellular marker. Lipopeptide derivatives of one of the active occludin peptides (OPs), synthesized by adding a lipoamino acid containing 14 carbon atoms (C-14-) to the N terminus of the peptide, were also investigated. Peptides corresponding to the N terminus of the first extracellular loop of occludin increased the permeability of the tight junctions without causing short-term toxicity. However, the peptides had an effect only when added to the basolateral side of the cells, which could be partly explained by degradation by apical peptidases and aggregate formation. By contrast, the lipopeptide C-14-OP90-103, which protects the peptide from degradation and aggregation, displayed a rapid apical effect. The L- and D-diastereomers of C-14-OP90-103 had distinctly different effects. The D-isomer, which releases intact OP90-103 from the lipoamino acid, displayed a rapid and transient increase in tight junction permeability. The L- isomer, which releases OP90-103 more rapidly, gave a more sustained increase in tight junction permeability. In conclusion, C-14-OP90-103 represents a prototype of a new class of tight junction modulators that act on the extracellular domains of tight junction proteins.