We analyzed 14 protein spots of crude proteins from B. dorsalis larvae post-treatment with trichlorphon in two-dimensional gel electrophoresis through mass spectrometry and protein sequencing. We found functional proteins that are responsible for signal transduction (pkaap and dual specificity tyrosine-phosphorylation-regulated kinase), immunity (hemolectin), synthesis and decomposition (twinstar, cathepsin B, RE66325p), oxidative stress metabolism
( glutathione S transferase and CG7320), energy metabolism (Act57B), and cytoskeleton formation (actin). These Citarinostat order proteins appear to be involved in the resistance response to trichlorphon.”
“Pronounced magnetic-field- and bias-sensitive features of the transport properties of a Fe/SiO2/p-Si hybrid structure in planar geometry at temperature variation are investigated. Comparative analysis of two Fe/SiO2/p-Si samples, one with a continuous Fe film and the other with two electrodes formed from a Fe layer and separated by Elafibranor a micron gap,
shows that these features are due to the metal-insulator-semiconductor (MIS) transition with a Schottky barrier near the interface between SiO2 and p-Si. Resistance
of such a MIS transition depends exponentially on temperature and bias. In the structure with a continuous ferromagnetic film, the competition between conductivities of the MIS transition and the Fe layer results in the effect of current channel switching between the Fe layer and a semiconductor substrate. Within certain limits, this process PFTα nmr can be controlled by a bias current and a magnetic field. Positive magnetoresistance of the structures at high temperatures is determined, most likely, by disorder-induced weak localization. In the structure with the gap, negative magnetoresistance is observed at certain temperature and bias. Its occurrence should be attributed to an inversion layer formed in the semiconductor near the SiO2/p-Si interface when MIS transition is in the inversion regime. (c) 2011 American Institute of Physics. [doi:10.1063/1.