Mitsubishi

About: Mitsubishi is a company organization based out in Tokyo, Japan. It is known for research contribution in the topics: Layer (electronics) & Signal. The organization has 53115 authors who have published 54821 publications receiving 870150 citations. The organization is also known as: Mitsubishi Group of Companies & Mitsubishi Companies.

Iterative Methods for Cancellation of Intercarrier Interference in OFDM Systems

Abstract: We consider orthogonal frequency-division multiplexing systems with intercarrier interference (ICI) due to insufficient cyclic prefix and/or temporal variations Intersymbol interference (ISI) and ICI lead to an error floor in conventional receivers We suggest two techniques for the equalization of ICI The first, called "operator-perturbation technique" is an iterative technique for the inversion of a linear system of equations Alternatively, we show that serial or parallel interference cancellation can be used to drastically reduce the error floor Simulations show that, depending on the SNR and the origin of the ICI, one of the schemes performs best In all cases, our schemes lead to a drastic reduction of the bit error rate

Multiple assignment scheme for sharing secret

Abstract: In a secret sharing scheme, a datumd is broken into shadows which are shared by a set of trustees. The family {P?⊆P:P? can reconstructd} is called the access structure of the scheme. A (k, n)-threshold scheme is a secret sharing scheme having the access structure {P?⊆P: |P?|?k}. In this paper, by observing a simple set-theoretic property of an access structure, we propose its mathematical definition. Then we verify the definition by proving that every family satisfying the definition is realized by assigning two more shadows of a threshold scheme to trustees.

The effect of nonstoichiometry on the positive temperature dependence of strength of Ni3AI and Ni3Ga

Abstract: Compression tests have been carried out on the polycrystalline Ni3Al and Ni3Ga alloys over the temperature range 77 ~ 1000 K. The flow stress and the temperature dependence of strength are found to be sensitive to small composition change within the phase field. The anomalous strengthening of these compounds with temperature is more significant for Al-and Ga-rich deviations than for Ni-rich deviations from stoichiometry. The change in activation constant of these compounds derived from the flow stress increment appears to be discontinuous at the stoichiometric composition. The influence of deviations from stoichiometry on the temperature dependence of strength could be accounted for by the phase stability concept proposed by the present authors. It is concluded that the phase stability of the Ni3Al and Ni3Ga alloys with respect to the D022 phase as well as the D019 phase are reduced as the composition of the minority component is increased. This change leads to the relatively reduced {100} antiphase boundary energy which increases the propensity for the cross slip onto cube plane.

The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains

Abstract: There is much evidence to indicate that cholesterol forms lateral membrane microdomains (rafts), and to suggest their important role in cellular signaling. However, no probe has been produced to analyze cholesterol behavior, especially cholesterol movement in rafts, in real time. To obtain a potent tool for analyzing cholesterol dynamics in rafts, we prepared and characterized several truncated fragments of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin, whose chemically modified form has been recently shown to bind selectively to rafts. BIAcore and structural analyses demonstrate that the C-terminal domain (domain 4) of the toxin is the smallest functional unit that has the same cholesterol-binding activity as the full-size toxin with structural stability. Cell membrane-bound recombinant domain 4 was detected in the floating low-density fractions and was found to be cofractionated with the raft-associated protein Lck, indicating that recombinant domain 4 also binds selectively to cholesterol-rich rafts. Furthermore, an enhanced green fluorescent protein-domain 4 fusion protein stains membrane surfaces in a cholesterol-dependent manner in living cells. Therefore, domain 4 of θ-toxin is an essential cholesterol-binding unit targeting to cholesterol in membrane rafts, providing a very useful tool for further studies on lipid rafts on cell surfaces and inside cells.