High barrier Yb/p-InP metal-insulator-semiconductor (MIS) and metal-semiconductor (MS) junctions were fabricated by evaporation of Yb on InP:Zn substrates. The capacitance-voltage (C-V) and current-voltage (I-V) characteristics of these devices were measured over a wide range of temperatures. From the room-temperature forward I-V data, the values of 1.06 and 1.30 for the ideality factor (n) were obtained for the MIS and MS diodes, respectively. The higher value of n was attributed to an order of magnitude higher density of interface states in the MS junction than in the MIS diodes. The I-V/T data over the temperature range 190–400 K, indicated that the forward current transport in the Yb/p-InP MIS junction was controlled by the thermionic-field emission (TFE) mechanism. The analysis of the reverse saturation current I0 in terms of the TFE model provided a value of 1.07±0.03 V for the zero bias, zero temperature barrier height (φ0) which was in close agreement with the value of φ0=1.03±0.04 V, provided by the C-V data. For the MS diode, the temperature dependence of the forward I-V characteristics over the temperature range 250–350 K were well described by the thermionic emission process. However, the value of φ0=0.80±0.04 V, determined from the I-V data was much smaller than the value of φ0=0.96±0.04 V, obtained from the C-V data.

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A novel investigation on the finite-size effects on the spin resonance properties of cobalt ferrite (CoFe2O4) nanoparticles has been performed using a room temperature ferromagnetic resonance (FMR) technique.

Temperature plays a vital role in the hydrothermal synthesis of the nanoparticles. Herein, we have provided a very detailed spin dynamic investigation on the varying size Fe3O4 nanoparticles using FMR technique.

Apoptotic signals are transduced by five death domain-containing receptors--TNFR1, Fas, DR3, DR4, and DR5--by binding to their ligands. The intracellular portion of all these receptors contains a region, approximately 80 amino acids long, referred to as the "death domain" (DD). On activation by its ligand, the DD recruits various proteins that mediate cell death. These proteins, in turn, recruit other proteins via their DDs or death effector domains (DED). The actual destruction of the cell, however, is accomplished by serial activation of a family of proteases referred to as caspases. Cell death is, in part, regulated by transmembrane decoy receptors that contain either none of or only part of the DD. This article briefly reviews what is known about the receptors and other proteins involved in apoptosis. In addition, because numerous proteins that mediate apoptosis have been discovered independently and simultaneously and thus are known by many different names, a comprehensive cross-referenced list of these proteins is provided.