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We investigated the temperature-dependent stability on the inverted-staggered back-channel-etched a-Si:H thin film transistors (TFTs) made at a process temperature of 150 °C on plastic foil substrates. The shift of threshold voltage (ΔVt) increases with the stressing time and the stressing temperature. Different from TFTs made at temperatures of 300 °C or above, our low-temperature processed TFTs show an abnormal saturation of ΔVt at 50 °C (323 K) in a constant gate-bias stress experiment. Around the same temperature, we observed abrupt increases in both the gate leakage current and the off current. Because of the low process temperature, the gate dielectric is less stable and more defective compared to that made at high process temperatures. A substantial amount of charges, trapped inside the dielectric during TFT fabrication and gate-bias stressing, was thermionically emitted into the channel by the Poole–Frenkel emission mechanism at a stressing temperature of 50 °C, leading to the abnormal phenomena. [ABSTRACT FROM AUTHOR]

A study was conducted to examine the temperature-dependent stability on the inverted-staggered back-channel-etched a-Si:H thin film transistors (TFTs) prepared at a process temperature of 150 degree Celsius on plastic foil susbtrates. The results helped to identify the mechanism responsible for abnormal TFT fabrication and gate-bias stressing temperature dependent stability.

This paper presents a SPICE-based simulator, FlexiAnalyzer, for flexible thin-film transistor (TFT) circuits. This simulator performs four types of analysis: yield analysis, aging analysis, performance analysis, and weak spot analysis. This simulator considers three important effects: 1) threshold voltage variation of manufacturing process; 2) threshold voltage shift due to aging effect; and 3) mobility change due to bending effect. Six different OLED pixel drivers designed in 8- μm amorphous silicon TFT technology were used in simulation results. The proposed tool provides a good solution for designers to evaluate the performance and yield of flexible TFT circuits. [ABSTRACT FROM PUBLISHER]

The transition of thin-film transistor (TFT) backplanes from rigid plate glass to flexible substrates requires the development of a generic TFT backplane technology on a clear plastic substrate. To be sufficiently stable under bias stress, amorphous-silicon (a-Si:H) TFTs must be deposited at elevated temperatures, therefore the substrate must withstand high temperatures. We fabricated a-Si:H TFT backplanes on a clear plastic substrate at 200degC. The measured stability of the TFTs under gate bias stress was superior to TFTs fabricated at 150degC. The substrate was dimensionally stable within the measurement resolution of 1, allowing for well-aligned 8 times 8 and 32 times 32 arrays of pixels. The operation of the backplane is demonstrated with an electrophoretic display. This result is a step toward the drop-in replacement of glass substrates by plastic foil. [ABSTRACT FROM PUBLISHER]

An amorphous-silicon thin-film transistor (TFT) process with a 180 °C maximum temperature using plasma-enhanced chemical vapor deposition has been developed on both novel clear polymer and glass substrates. The gate leakage current, threshold voltage, mobility, and on/off ratio of the TFTs are comparable with those of standard TFTs on glass with deposition temperature of 300 °C-350 °C. Active-matrix pixel circuits for organic light-emitting displays (LEDs) on both glass and clear plastic substrates were fabricated with these TFTs. Leakage current in the switching TFT is low enough to allow data storage for video graphics array timings. The pixels provide suitable drive current for bright displays at a modest drive voltage. Test active matrices with integrated polymer LEDs on glass showed good pixel uniformity, behaved electrically as expected for the TFT characteristics, and were as bright as 1500 cd/m². [ABSTRACT FROM AUTHOR]

Using formalin inactivated Actinobacillus pleuropneumoniae antigens and aqueous ethylcellulose dispersions, microspheres of oral vaccines were developed by a co-spray drying process. The present study attempted to determine whether the dosage formulations of microspheres could form enteric matrices. To assess the enteric characteristics, an in vitro dissolution test was performed with the AQ6-AP microspheres; 95% of the A. pleuropneumoniae protein was released within 3 h at pH 7, but there was no release at pH 1.5. The scanning microscopy revealed that the surface structure of AQ6-AP microspheres became porous at neutral pH. The SDS-PAGE analysis showed that the release rate of proteins from the microspheres was pH dependent not only for the AQ6-AP formulation but also when antigens of A. pleuropneumoniae were replaced with porcine serum. The results suggest that the A. pleuropneumoniae antigens were entrapped in the AQ6 microspheres under the acidic conditions. In a mouse model, oral immunization with AQ6-AP microspheres containing A. pleuropneumoniae evoked systemic IgG and mucosal IgA responses against A. pleuropneumoniae antigens. Thus, the present method may further provide an opportunity to develop oral vaccines and mucosal immunity. [ABSTRACT FROM AUTHOR]

Amorphous-silicon (a-Si) thin-film transistors (TFTs) were fabricated on a free-standing new clear plastic substrate with high glass transition temperature (Tg) of > 315 °C and low coefficient of thermal expansion of < 10 ppm/°C. Maximum process temperatures on the substrates were 250 °C and 280 °C, close to the temperatures used in industrial a-Si TFT production on glass substrates. The first TFTs made at 280 °C have dc characteristics comparable to TFTs made on glass. The stability of the 250 °C TFTs on clear plastic is approaching that of TFTs made on glass at 300 °C-350 °C. TFT characteristics and stability depend only on process temperature and not on substrate type. [ABSTRACT FROM AUTHOR]

This study describes magnetically driven suppression of cross-reactions among molecules. First, the magnetic nanoparticles are coated with bio-probes and dispersed in liquid. The bio-probes can then bind with homologous or heterologous bio-targets. When alternating-current (ac) magnetic fields are applied, magnetic nanoparticles rotate driven by ac magnetic fields. Thus, the bio-targets bound on the surface of magnetic nanoparticles experience a centrifugal force. The centrifugal force can be manipulated by adjusting the angular frequency of the rotating magnetic nanoparticles. The angular frequency is determined by the applied ac magnetic field frequency. Since the binding force for good binding is much higher than that of poor binding, frequency manipulation is needed for the centrifugal force to be higher than the poor-binding force but lower than the good-binding force. Therefore, poor binding which contributes to cross reactions between molecules can be suppressed efficiently by control of the ac magnetic field frequency., (Copyright (c) 2009 Elsevier B.V. All rights reserved.)

This paper reports on a retrospective study of the antibody responses to structural and non-structural proteins of FMD virus O Taiwan 97 in six pig herds in Taiwan in the year after the 1997 Taiwanese FMD outbreak. All herds were vaccinated against FMD after the outbreak as part of the countrywide control program. Three of the herds had confirmed FMD infections (herds N, O and P) and three herds remained non-infected (herds K, L and M). The serum neutralizing antibody titers and the non-structural protein ELISA (NSP) antibody responses in sows and 1-month-old pigs in the infected herds were higher than in the non-infected herds, but over time a number of positive NSP reactors were detected. From the serological studies and the herd monitoring and investigations it was considered that the FMD NSP positive reactors may not have constituted a true reservoir of FMD virus infection especially in herds where susceptible pigs were no longer present post-exposure or post-vaccination. Pigs vaccinated with an unpurified FMD type O vaccines being used at that time also showed false positive responses for NSP antibodies.

The immune response to structural and non-structural proteins (NSPs) was studied on sequential serum samples in swine from O/Taiwan/97 FMDV challenge studies, outbreaks and after vaccination. The results showed that pigs vaccinated with a commercial vaccine prior to or after infection maintained high neutralizing antibody titers with gradual decline from peak titers over the duration of this study. However, neutralizing antibody titers in non-vaccinated pigs only reached moderate levels 2-4 weeks post infection and remained low thereafter. For the 3B and 3ABC NSP antibody ELISA responses, there were gradually decreasing levels of NSP antibody over time. In multiple vaccinations, all pigs showed significant increases in neutralizing antibodies after booster vaccination. For the 3B NSP antibody ELISA after vaccination, the mean S/P ratios for pigs vaccinated with all three FMD vaccines were all below the 0.23 cut-off value set by the manufacture, but some sera from individual vaccinated pigs gave results above this cut-off after primary or secondary vaccination. However, with the 3ABC NSP antibody ELISA, all sera from vaccinated pigs had negative results for NSP antibody for all time points.

Three commercialized ELISA kits for the detection of antibodies to the non-structural proteins (NSPs) of FMD virus were compared, using sera from uninfected, vaccinated, challenged and naturally infected pigs. The kinetics of the antibody response to NSPs was compared on sequential serum samples in swine from challenge studies and outbreaks. The results showed that ELISA A (UBI) and ELISA B (CEDI) had better sensitivity than that of the 3ABC recombinant protein-based ELISA C (Chekit). The peak for detection of antibodies to NSPs in ELISA C was significantly delayed in sera from natural infection and challenged swine as compared to the ELISA A and B. The sensitivity of the three ELISAs gradually declined during the 6-month post-infection as antibodies to NSP decline. ELISA kits A and B detected NSP antibody in 50% of challenged pigs by the 9-10th-day and 7-8th-day post-challenge, respectively. ELISA B and C had better specificity than ELISA A on sequential serum samples obtained from swine immunized with a type O FMD vaccine commercially available in Taiwan. Antibody to NSPs before vaccination was not detected in swine not exposed to FMD virus, however, antibody to NSPs was found in sera of some pigs after vaccination. All assays had significantly lower specificity when testing sera from repeatedly vaccinated sows and finishers in 1997 that were tested after the 1997 FMD outbreak. However, when testing sera from repeatedly vaccinated sows or finishers in 2003-2004, the specificity for ELISAs A, B and C were significantly better than those in 1997. This effect was less marked for ELISA A. The ELISA B was the best test in terms of the highest sensitivity and specificity and the lowest reactivity with residual NSP in vaccinates.

A case of pneumocephalus and respiratory depression after dural puncture during lumbar epidural analgesia is reported. The loss of resistance to air technique was employed to identify the epidural space. Severe respiratory depression and stuporous consciousness developed one hour after a bolus of 2 mg morphine was given epidurally at the end of operation. With computerized tomographic brain scanning and continuous observation of clinical course, the neurologic symptoms were thought to be a mixed complication of pneumocephalus and possible intrathecal morphine overdose. We suggest that in order to avoid iatrogenic pneumocephalus by inadvertent dural puncture in the attempt to identify the epidural space the use of the loss of resistance to normal saline technique or the hanging-drop technique is more reliable than the loss of resistance to air technique. A small test dose prior to a full dose is given and should not be omitted to further confirm the proper placement of the epidural catheter during epidural analgesia.

Using cDNA probes obtained from library screening and anchored polymerase chain reaction, we have isolated and characterized three overlapping mouse genomic clones that contain the mouse lipocortin I (Lipo I) structural gene. Restriction enzyme mapping, Southern blotting, and DNA sequencing were carried out on the cloned genomic DNA. Lipo I spans about 17 kb and is divided into 13 exons encoding a protein of 346 amino acid residues. The promoter region of the gene has a TATA box and a CCAAT box located upstream of the transcription initiation site at -31 and -76 bp, respectively. Analysis of the strain distribution pattern of Lipo 1 in BXD and AKXD collections of recombinant inbred strains establishes that Lipo I is located on chromosome 19 in close proximity to Ea-4. While no striking relationship exists between the exon/intron structure of the gene and the four repeated 70-amino-acid domains of the protein, three of the four 17-amino-acid repeats believed to be responsible for Ca2+/phospholipid binding are encoded by the last codon of one exon and the first 16 codons of the following exon. This pattern supports the gene duplication theory, and the similarity in gene structure between mouse Lipo I and Lipo II suggests they have a recent evolutionary ancestor.

The lymph node homing receptor core polypeptide (mLHRc) is composed of a tandem collection of domains: a lectin domain, an epidermal growth factor (EGF) domain, and two repeats common in complement regulatory proteins. Here we demonstrate localization of mLHRc to chromosome 1, the portion syntenic with chromosome 1 in man. This locus is inseparable in mouse strains from the murine lymphocyte cell surface marker Ly-22. The data indicate that Ly-22 is an allelic determinant on the LHR resulting from a single amino acid interchange within the EGF domain. Cross-blocking experiments demonstrate that anti-Ly-22 and MEL-14 recognize independent epitopes and that Ly-22 is distinct from the carbohydrate binding region. Application of anti-Ly-22 in the in vitro binding assay shows inhibition of binding of lymphocytes to high endothelial venules (HEVs). The localization of the Ly-22 epitope in this novel chimeric protein suggests direct participation of the EGF domain in the adhesion of lymphocytes to HEV.