Web-based technology has a dramatic impact on learning and teaching. A framework that delineates the relationships between learner control and learning effectiveness is absent. This study aims to fill this void. Our work focuses on the effectiveness of a technology-mediated virtual learning environment (TVLE) in the context of basic information technology skills training. Grounded in the technology-mediated learning literature, this study presents a framework that addresses the relationship between the learner control and learning effectiveness, which contains four categories: learning achievement, self-efficacy, satisfaction, and learning climate. In order to compare the learning effectiveness under traditional classroom and TVLE, we conducted a field experiment. Data were collected from a junior high school of Taiwan. A total of 210 usable responses were analysed. We identified four results from this study. (1) Students in the TVLE environment achieve better learning performance than their counterparts in the traditional environment; (2) Students in the TVLE environment report higher levels of computer self-efficacy than their counterparts in the traditional environment; (3) Students in the TVLE environment report higher levels of satisfaction than students in the traditional environment; and (4) Students in the TVLE environment report higher levels of learning climate than their counterparts in the traditional environment. The implications of this study are discussed, and further research directions are proposed.

This study fabricates and characterizes ultraviolet (UV) photosensors with ZnO nanorods (NRs). The NR arrays were selectively grown in the gap between interdigitated (IDT) electrodes of devices using hydrothermal solution processes and a lithography-based technique. Compared with a conventional ZnO photosensor without NRs, the proposed UV NR photosensors have much higher photoresponse in the UV region. Additionally, the photoconductive gain of an NR photosensor increased as UV illumination time increased; it varied at 34.45-5.32 x 10(2) under illumination by 18.28 mW/cm(2) optical power. Consequently, the substantial photoconductive gain can be attributed to high surface-to-volume ratio of ZnO NRs. The high density of hole-trap states on NR surfaces lead to a persistent photoconductivity (PPC) state, promoting the transport of carriers through devices.

Summary Influenza A virus RNA synthesis is catalyzed by the viral polymerase comprised of the PA, PB1 and PB2 proteins. We show that the host DDX21 RNA helicase restricts influenza A virus by binding PB1 and inhibiting polymerase assembly, resulting in reduced viral RNA and protein synthesis. Later during infection, the viral NS1 protein overcomes this restriction by binding to DDX21 and displacing PB1. DDX21 binds to a region of the NS1 N-terminal domain that also participates in other critical functions. A virus mutant whose NS1 protein is unable to bind DDX21 exhibits reduced viral protein synthesis at both late and early times of infection, a phenotype converted to wild-type upon DDX21 knockdown. As sequential interaction of PB1 and NS1 with DDX21 leads to temporal regulation of viral gene expression, influenza A virus likely uses the DDX21-NS1 interaction not only to overcome restriction but also to regulate the viral life cycle.

Previous studies showed that ZAPL (PARP-13.1) exerts its antiviral activity via its N-terminal zinc fingers that bind the mRNAs of some viruses, leading to mRNA degradation. Here we identify a different antiviral activity of ZAPL that is directed against influenza A virus. This ZAPL antiviral activity involves its C-terminal PARP domain, which binds the viral PB2 and PA polymerase proteins, leading to their proteasomal degradation. After the PB2 and PA proteins are poly(ADP-ribosylated), they are associated with the region of ZAPL that includes both the PARP domain and the adjacent WWE domain that is known to bind poly(ADP-ribose) chains. These ZAPL-associated PB2 and PA proteins are then ubiquitinated, followed by proteasomal degradation. This antiviral activity is counteracted by the viral PB1 polymerase protein, which binds close to the PARP domain and causes PB2 and PA to dissociate from ZAPL and escape degradation, explaining why ZAPL only moderately inhibits influenza A virus replication. Hence influenza A virus has partially won the battle against this newly identified ZAPL antiviral activity. Eliminating PB1 binding to ZAPL would be expected to substantially increase the inhibition of influenza A virus replication, so that the PB1 interface with ZAPL is a potential target for antiviral development.ZAPL PARP domain | influenza A virus polymerase protein subunits | proteasomal degradation | ubiquitination | poly(ADP-ribosylation)

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