With the aim of increasing conversion efficiency, the series-internal resistance of dye-sensitized solar cells (DSCs) was investigated with electrochemical impedance spectroscopy measurement based on an equivalent circuit of DSCs. It was found that series-internal resistance correlates positively with the sheet resistance of the transparent conducting oxide and the thickness of the electrolyte layer and negatively with the roughness factor of the platinum counter electrode. A cell sensitized with a black dye with series-internal resistance of 1.8Ωcm2 was fabricated and showed conversion efficiency of 10.2% when measured with a metal mask under an air mass of 1.5 sunlight.
Pasteurella multocida toxin (PMT), one of the virulence factors produced by the bacteria, exerts its toxicity by up-regulating various signaling cascades downstream of the heterotrimeric GTPases Gq and G12/13 in an unknown fashion. Here, we present the crystal structure of the C-terminal region (residues 575-1,285) of PMT, which carries an intracellularly active moiety. The overall structure of C-terminal region of PMT displays a Trojan horse-like shape, composed of three domains with a ''feet''-,''body''-, and ''head''-type arrangement, which were designated C1, C2, and C3 from the N to the C terminus, respectively. The C1 domain, showing marked similarity in steric structure to the N-terminal domain of Clostridium difficile toxin B, was found to lead the toxin molecule to the plasma membrane. The C3 domain possesses the Cys-HisAsp catalytic triad that is organized only when the Cys is released from a disulfide bond. The steric alignment of the triad corresponded well to that of papain or other enzymes carrying CysHis-Asp. PMT toxicities on target cells were completely abrogated when one of the amino acids constituting the triad was mutated. Our results indicate that PMT is an enzyme toxin carrying the cysteine protease-like catalytic triad dependent on the redox state and functions on the cytoplasmic face of the plasma membrane of target cells.crystallography ͉ cysteine protease ͉ membrane targeting
Toll-like receptors (TLR) in the innate immune system have not been identified in non-mammalian vertebrates. Two types of TLR were cloned from a chicken bursa cDNA library using degenerate primers based on the consensus sequences of mouse and Drosophila Toll and designated as chicken TLR (chTLR) type 1 and type 2. Of the nine human TLRs reported to date, these chTLRs showed the highest homology to human TLR2. The extracellular regions of type 1 and type 2 contained a distinct ϳ200-amino acid stretch and were 45.3 and 46.3% homologous to that of human TLR2. The intracellular Toll/interleukin-1R homology domain of type 1 and type 2 was perfectly identical to each other and highly homologous (80.7%) to that of human TLR2. Both types were widely detected by reverse transcriptase-polymerase chain reaction and immunoblotting in various chicken organs, especially those rich in connective tissue. Both genes were mapped to chromosome 4q1.1, suggesting that they arose by gene duplication. By reporter gene assay, type 2 and to a lesser extent type 1, selectively signaled the presence of mycoplasma macrophage-activating lipopeptide-2/M161Ag in the human embryonic kidney 293 cell system. Cotransfection of type 2 and human CD14 or MD-2 into human embryonic kidney 293 cells allowed the response to Escherichia coli lipopolysaccharide (LPS), whereas type 1 did not signal LPS or any other microbial components tested. These results indicated that chTLR type 2 covers two major microbe patterns, lipoproteins and LPS, which are regulated by TLR2 and TLR4 in mammals. In oviparous animals, the duplicated TLRs in the pattern-recognition system may function for host-pathogen discrimination in a manner that is distinct from that in mammals.
The increase of cytotoxic NK cells in the peripheral blood and the endometrium may affect the therapeutic results of IVF-ET. It was suggested that modifications of NK cytotoxicity or of NK subpopulations might contribute to the improvements of IVF outcomes.
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