University of Victoria

About: University of Victoria is a education organization based out in Victoria, British Columbia, Canada. It is known for research contribution in the topics: Population & Galaxy. The organization has 14994 authors who have published 41051 publications receiving 1447972 citations. The organization is also known as: Victoria College.

What makes a good bug report

Abstract: In software development, bug reports provide crucial information to developers. However, these reports widely differ in their quality. We conducted a survey among developers and users of APACHE, ECLIPSE, and MOZILLA to find out what makes a good bug report.The analysis of the 466 responses revealed an information mismatch between what developers need and what users supply. Most developers consider steps to reproduce, stack traces, and test cases as helpful, which are at the same time most difficult to provide for users. Such insight is helpful to design new bug tracking tools that guide users at collecting and providing more helpful information.Our CUEZILLA prototype is such a tool and measures the quality of new bug reports; it also recommends which elements should be added to improve the quality. We trained CUEZILLA on a sample of 289 bug reports, rated by developers as part of the survey. In our experiments, CUEZILLA was able to predict the quality of 31--48% of bug reports accurately.

An inverted continental Moho and serpentinization of the forearc mantle

Abstract: Volatiles that are transported by subducting lithospheric plates to depths greater than 100 km are thought to induce partial melting in the overlying mantle wedge, resulting in arc magmatism and the addition of significant quantities of material to the overlying lithosphere. Asthenospheric flow and upwelling within the wedge produce increased lithospheric temperatures in this back-arc region, but the forearc mantle (in the corner of the wedge) is thought to be significantly cooler. Here we explore the structure of the mantle wedge in the southern Cascadia subduction zone using scattered teleseismic waves recorded on a dense portable array of broadband seismometers. We find very low shear-wave velocities in the cold forearc mantle indicated by the exceptional occurrence of an 'inverted' continental Moho, which reverts to normal polarity seaward of the Cascade arc. This observation provides compelling evidence for a highly hydrated and serpentinized forearc region, consistent with thermal and petrological models of the forearc mantle wedge. This serpentinized material is thought to have low strength and may therefore control the down-dip rupture limit of great thrust earthquakes, as well as the nature of large-scale flow in the mantle wedge.

Institutions in Economics: The Old and the New Institutionalism

Abstract: 1. Definitions and issues 2. Formalism and anti-formalism 3. Individualism and holism 4. Rationality and rule following 5. Evolution and design 6. Efficiency and reform 7. Conflicts and complementarities.

Engineering Self-Adaptive Systems through Feedback Loops

Abstract: To deal with the increasing complexity of software systems and uncertainty of their environments, software engineers have turned to self-adaptivity. Self-adaptive systems are capable of dealing with a continuously changing environment and emerging requirements that may be unknown at design-time. However, building such systems cost-effectively and in a predictable manner is a major engineering challenge. In this paper, we explore the state-of-the-art in engineering self-adaptive systems and identify potential improvements in the design process. Our most important finding is that in designing self-adaptive systems, the feedback loops that control self-adaptation must become first-class entities. We explore feedback loops from the perspective of control engineering and within existing self-adaptive systems in nature and biology. Finally, we identify the critical challenges our community must address to enable systematic and well-organized engineering of self-adaptive and self-managing software systems.

Single-pot, solid-phase-enhanced sample preparation for proteomics experiments.

Abstract: A critical step in proteomics analysis is the optimal extraction and processing of protein material to ensure the highest sensitivity in downstream detection. Achieving this requires a sample-handling technology that exhibits unbiased protein manipulation, flexibility in reagent use, and virtually lossless processing. Addressing these needs, the single-pot, solid-phase-enhanced sample-preparation (SP3) technology is a paramagnetic bead–based approach for rapid, robust, and efficient processing of protein samples for proteomic analysis. SP3 uses a hydrophilic interaction mechanism for exchange or removal of components that are commonly used to facilitate cell or tissue lysis, protein solubilization, and enzymatic digestion (e.g., detergents, chaotropes, salts, buffers, acids, and solvents) before downstream proteomic analysis. The SP3 protocol consists of nonselective protein binding and rinsing steps that are enabled through the use of ethanol-driven solvation capture on the surface of hydrophilic beads, and elution of purified material in aqueous conditions. In contrast to alternative approaches, SP3 combines compatibility with a substantial collection of solution additives with virtually lossless and unbiased recovery of proteins independent of input quantity, all in a simplified single-tube protocol. The SP3 protocol is simple and efficient, and can be easily completed by a standard user in ~30 min, including reagent preparation. As a result of these properties, SP3 has successfully been used to facilitate examination of a broad range of sample types spanning simple and complex protein mixtures in large and very small amounts, across numerous organisms. This work describes the steps and extensive considerations involved in performing SP3 in bottom-up proteomics, using a simplified protein cleanup scenario for illustration. This protocol describes a single-pot, solid-phase-enhanced sample-preparation (SP3) method for rapid, robust, and efficient processing of protein samples for proteomic analysis.