Assisting End-users in Filling Out Web Services

With the quick advance of web service technologies, end-users can conduct various on-line tasks, such as shopping on-line. Usually, end-users compose a set of services to accomplish a task, and need to enter values to services to invoke the composite services. Quite often, users re-visit websites and use services to perform re-occurring tasks. The users are required to enter the same information into various web services to accomplish such re-occurring tasks. However, repetitively typing the same information into services is a tedious job for end-users. It can negatively impact user experience when an end-user needs to type the re-occurring information repetitively into web services. Recent studies have proposed several approaches to help users fill in values to services automatically. However, prior studies mainly suffer the following drawbacks: (1) limited support of collecting and analyzing user inputs; (2) poor accuracy of filling values to services; (3) not designed for service composition. To overcome the aforementioned drawbacks, we need maximize the reuse of previous user inputs across services and end-users. In this thesis, we introduce our approaches that prevent end-users from entering the same information into repetitive on-line tasks. More specifically, we improve the process of filling out services in the following 4 aspects: First, we investigate the characteristics of input parameters. We propose an ontology-based approach to automatically categorize parameters and fill values to the categorized input parameters. Second, we propose a comprehensive framework that leverages user contexts and usage patterns into the process of filling values to services. Third, we propose an approach for maximizing the value propagation among services and end-users by linking a set of semantically related parameters together and similar end-users. Last, we propose a ranking-based framework that ranks a list of previous user inputs for an input parameter to save a user from unnecessary data entries. Our framework learns and analyzes interactions of user inputs and input parameters to rank user inputs for input parameters under different contexts.

THE HERPESVIRUS NUCLEAR EGRESS COMPLEX COMPONENT, UL31, IS RECRUITED TO SITES OF DNA DAMAGE THROUGH POLY(ADP-RIBOSE) BINDING

The herpes simplex virus (HSV) UL31 gene encodes a conserved member of the herpesvirus nuclear egress complex that not only functions in the egress of DNA-containing capsids from the nucleus, but is also required for optimal viral genome expression, replication and packaging into capsids. Here, we report that the UL31 protein from HSV-2 and the orthologous protein, ORF69, from Kaposi's sarcoma-associated herpesvirus (KSHV) are recruited to sites of DNA damage. Recruitment of UL31 to sites of DNA damage occurred in HSV-2 infected cells, but did not require other viral proteins. The N-terminus of UL31 contains sequences resembling a poly(ADP-ribose) (PAR) binding motif. As protein poly-ADP ribosylation (PARylation) is a hallmark of the DNA damage response we examined the relationship between PARylation and UL31 recruitment to DNA damage. While the PAR polymerase (PARP)1/2 inhibitor, olaparib, prevented UL31 recruitment to damaged DNA, KU55933 inhibition of signaling through the ataxia telangiectasia mutated (ATM) DNA damage response pathway had no effect. These findings were further supported by experiments demonstrating direct and specific interaction between HSV-2 UL31 and PAR using purified components. Co-transfection with the viral kinase Us3, known to phosphorylate UL31, inhibited UL31 recruitment to DNA damage but also prevented the recruitment of other proteins recruited to DNA damage sites. The viral E3 ubiquitin ligase ICP0 was observed to co-localize with UL31 in transfected cells in a manner that is independent of the PAR-binding ability of UL31. However, inhibition of PARP1/2/3 did not reduce the ability of HSV-2 to replicate and we observed reduced PAR levels in the nuclei of infected cells. This study reveals a previously unrecognized function for UL31 orthologs and may suggest that the recognition of PAR by UL31 is coupled to the nuclear egress of herpesvirus capsids, influences viral DNA replication and packaging, or possibly modulates the DNA damage response mounted by virally infected cells.