GroupScape: Integrating Synchronous Groupware and the World Wide Web

Synchronous groupware applications support people collaborating in real time over a distance. The world wide web supports asynchronous collaboration by allowing people to share distributed information repositories. This paper presents a new technique for creating applications that tightly integrate synchronous groupware with the world wide web. The key points of the technique are: two new HTML tags allow synchronous views to be embedded within WWW pages without programming; lightweight connection of WWW documents and applications is achieved through the use of constraints, and the use of the model-view-controller architecture allows easy integration of applications and WWW pages that were developed separately. This technique has been demonstrated in the context of the new multiuser GroupScape HTML browser, developed using the Clock groupware development toolkit

Poverty reduction in coconut growing communities: Volume III: Project achievements and impact

This is the final version. Available from Oxford University Press via the DOI in this record.Mycoprotein is an alternative, nutritious protein source with a meat-like texture made from Fusarium venenatum, a naturally occurring fungus. Its unique method of production yields a significantly reduced carbon and water footprint relative to beef and chicken. Mycoprotein, sold as Quorn, is consumed in 17 countries, including the United States. In line with current dietary guidelines, mycoprotein is high in protein and fiber, and low in fat, cholesterol, sodium, and sugar. Mycoprotein may help maintain healthy blood cholesterol levels, promote muscle synthesis, control glucose and insulin levels, and increase satiety. It is possible that some susceptible consumers will become sensitized, and subsequently develop a specific allergy. However, a systematic evidence review indicates that incidence of allergic reactions remains exceptionally low. Mycoprotein's nutritional, health, and environmental benefits affirms its role in a healthful diet. Future research that focuses on the long-term clinical benefits of consuming a diet containing mycoprotein is warranted

A Visual Architectural Approach to Maintaining Web Applications

Web applications are complex software systems which contain a rich structure with many relations between their components. Web developers are faced with many challenges when they need to gain a better understanding of these applications to maintain or evolve them. Current development tools focus primarily on implementation, with little support for the application's evolution. Web developers need tools to assist in the evolution and maintenance of web applications. We presen

Detection of protein–protein interactions at the septin collar in Saccharomyces cerevisiae

Various methods can provide a readout of the physical interaction between two biomolecules. A recently described tripartite split-GFP system has the potential to report by direct visualization via a fluorescence signal the intimate association of minimally tagged proteins expressed at their endogenous level in their native cellular milieu and can capture transient or weak interactions. Here we document the utility of this tripartite split-GFP system to assess in living cells protein–protein interactions in a dynamic cytoskeletal structure—the septin collar at the yeast bud neck. We show, first, that for septin–septin interactions, this method yields a robust signal whose strength reflects the known spacing between the subunits in septin filaments and thus serves as a “molecular ruler.” Second, the method yields little or no spurious signal even with highly abundant cytosolic proteins readily accessible to the bud neck (including molecular chaperone Hsp82 and glycolytic enzyme Pgk1). Third, using two proteins (Bni5 and Hsl1) that have been shown by other means to bind directly to septins at the bud neck in vivo, we validate that the tripartite split-GFP method yields the same conclusions and further insights about specificity. Finally, we demonstrate the capacity of this approach to uncover additional new information by examining whether three other proteins reported to localize to the bud neck (Nis1, Bud4, and Hof1) are able to interact physically with any of the subunits in the septin collar and, if so, with which ones

Coordinate action of distinct sequence elements localizes checkpoint kinase Hsl1 to the septin collar at the bud neck in Saccharomyces cerevisiae

Passage through the eukaryotic cell cycle requires processes that are tightly regulated both spatially and temporally. Surveillance mechanisms (checkpoints) exert quality control and impose order on the timing and organization of downstream events by impeding cell cycle progression until the necessary components are available and undamaged and have acted in the proper sequence. In budding yeast, a checkpoint exists that does not allow timely execution of the G2/M transition unless and until a collar of septin filaments has properly assembled at the bud neck, which is the site where subsequent cytokinesis will occur. An essential component of this checkpoint is the large (1518-residue) protein kinase Hsl1, which localizes to the bud neck only if the septin collar has been correctly formed. Hsl1 reportedly interacts with particular septins; however, the precise molecular determinants in Hsl1 responsible for its recruitment to this cellular location during G2 have not been elucidated. We performed a comprehensive mutational dissection and accompanying image analysis to identify the sequence elements within Hsl1 responsible for its localization to the septins at the bud neck. Unexpectedly, we found that this targeting is multipartite. A segment of the central region of Hsl1 (residues 611–950), composed of two tandem, semiredundant but distinct septin-associating elements, is necessary and sufficient for binding to septin filaments both in vitro and in vivo. However, in addition to 611–950, efficient localization of Hsl1 to the septin collar in the cell obligatorily requires generalized targeting to the cytosolic face of the plasma membrane, a function normally provided by the C-terminal phosphatidylserine-binding KA1 domain (residues 1379–1518) in Hsl1 but that can be replaced by other, heterologous phosphatidylserine-binding sequences