Doc2RDFa: Semantic Annotation for Web Documents

Ever since its conception, the amount of data published on the worldwide web has been rapidly growing to the point where it has become an important source of both general and domain specific information. However, the majority of documents published online are not machine readable by default. Many researchers believe that the answer to this problem is to semantically annotate these documents, and thereby contribute to the linked "Web of Data". Yet, the process of annotating web documents remains an open challenge. While some efforts towards simplifying this process have been made in the recent years, there is still a lack of semantic content creation tools that integrate well with information worker toolsets. Towards this end, we introduce Doc2RDFa, an HTML rich text processor with the ability to automatically and manually annotate domain-specific Content

Evaluation of Visually Expanding Lighting Techniques by Design and Non-design Students

Housing, Design, and Consumer Resource

Purification and G Protein Subunit Regulation of a Phospholipase C-β from Xenopus laevis Oocytes

Xenopus oocytes exhibit both pertussis toxin-sensitive and -insensitive inositol lipid signaling responses to G protein-coupled receptor activation. The G protein subunits Galphai, Galphao, Galphaq, Galphas, and Gbetagamma all have been proposed to function as activators of phospholipase C in oocytes. Ma et al. (Ma, H.-W., Blitzer, R. D., Healy, E. C., Premont, R. T., Landau, E. M., and Iyengar, R. J. Biol. Chem. 268, 19915-19918) cloned a Xenopus phospholipase C (PLC-betaX) that exhibits homology to the PLC-beta class of isoenzymes. Although this enzyme was proposed to function as a signaling protein in the pertussis toxin-sensitive inositol lipid signaling pathway of oocytes, its regulation by G protein subunits has not been directly assessed. As such we have utilized baculovirus-promoted overexpression of PLC-betaX in Sf9 insect cells and have purified a recombinant 150-kDa isoenzyme. PLC-betaX catalyzes hydrolysis of phosphatidylinositol(4,5)bisphosphate and phosphatidylinositol(4)monophosphate, and reaction velocity is dependent on Ca2+. Recombinant PLC-betaX was activated by both Galphaq and Gbetagamma. PLC-betaX exhibited a higher apparent affinity for Galphaq than Gbetagamma, and Galphaq was more efficacious than Gbetagamma at lower concentrations of PLC-betaX. Relative to other PLC-beta isoenzymes, PLC-betaX was less sensitive to stimulation by Galphaq than PLC-beta1 but similar to PLC-beta2 and PLC-betaT. PLC-betaX was more sensitive to stimulation by Gbetagamma than PLC-beta1 but less sensitive than PLC-beta2 and PLC-betaT. In contrast PLC-betaX was not activated by the pertussis toxin substrate G proteins Galphai1, Galphai2, Galphai3, or Galphao. These results are consistent with the idea that PLC-betaX is regulated by alpha-subunits of the Gq family and by Gbetagamma and do not support the idea that alpha-subunits of pertussis toxin-sensitive G proteins are directly involved in regulation of this protein

Report on the CCT Supplementary Comparison S1 of Infrared Spectral Normal Emittance/Emissivity

open9openHanssen, L; Wilthan, B; Filtz, J -R; Hameury, J; Girard, F; Battuello, M; Ishii, J; Hollandt, J; Monte, CHanssen, L; Wilthan, B; Filtz, J. R; Hameury, J; Girard, Ferruccio; Battuello, Mauro; Ishii, J; Hollandt, J; Monte, C

Protein Kinase C-Promoted Inhibition of G␣ 11 -Stimulated Phospholipase C-␤ Activity

ABSTRACT The effects of protein kinase C (PKC) activation on inositol lipid signaling were examined. Using the turkey erythrocyte model of receptor-regulated phosphoinositide hydrolysis, we developed a membrane reconstitution assay to study directly the effects of activation of PKC on the activities of G␣ 11 , independent of potential effects on the receptor or on PLC-␤. Membranes isolated from erythrocytes pretreated with 4␤-phorbol-12␤-myristate-13␣-acetate (PMA) exhibited a decreased capacity for G␣ 11 -mediated activation of purified, reconstituted PLC-␤1. This inhibitory effect was dependent on both the time and concentration of PMA incubation and occurred as a decrease in the efficacy of GTP␥S for activation of PLC-␤1, both in the presence and absence of agonist; no change in the apparent affinity for the guanine nucleotide occurred. Similar inhibitory effects were observed after treatment with the PKC activator phorbol-12,13-dibutyrate but not after treatment with an inactive phorbol ester. The inhibitory effects of PMA were prevented by coaddition of the PKC inhibitor bisindolylmaleimide. Although the effects of PKC could be localized to the membrane, no phosphorylation of G␣ 11 occurred either in vitro in the presence of purified PKC or in intact erythrocytes after PMA treatment. These results support the hypothesis that a signaling protein other than G␣ 11 is the target for PKC and that PKCpromoted phosphorylation of this protein results in a phosphorylation-dependent suppression of G␣ 11 -mediated PLC-␤1 activation. Various receptors transduce signals through heterotrimeric G proteins of the G q family, resulting in activation of phospholipase C (PLC)-␤ isoenzymes and subsequent cleavage of membrane phosphatidylinositol(4,5)P 2 [PtdIns(4,5)P 2 ] to the second messengers inositol(1,4,5)P 3 [Ins(1,4,5)P 3 ] and diacylglycerol Agonist-induced desensitization is an important regulatory process in inositol lipid signaling The turkey erythrocyte is a well-characterized model of receptor-promoted inositol phospholipid signaling and is particularly useful because the three primary proteins in the pathway, i.e., the turkey P2Y 1 recepto

Regulation of transcription factor activity by interconnected, post-translational modifications

Transcription factors comprise just over 7% of the human proteome and serve as gatekeepers of cellular function, integrating external signal information into gene expression programs that reconfigure cellular physiology at the most basic levels. Surface-initiated cell signaling pathways converge on transcription factors, decorating these proteins with an array of post-translational modifications (PTMs) that are often interdependent, being linked in time, space, and combinatorial function. These PTMs orchestrate every activity of a transcription factor over its entire lifespan—from subcellular localization to protein–protein interactions, sequence-specific DNA binding, transcriptional regulatory activity, and protein stability—and play key roles in the epigenetic regulation of gene expression. The multitude of PTMs of transcription factors also offers numerous potential points of intervention for development of therapeutic agents to treat a wide spectrum of diseases. We review PTMs most commonly targeting transcription factors, focusing on recent reports of sequential and linked PTMs of individual factors

Events Matter: Extraction of Events from Court Decisions

The analysis of court decisions and associated events is part of the daily life of many legal practitioners. Unfortunately, since court decision texts can often be long and complex, bringing all events relating to a case in order, to understand their connections and durations is a time-consuming task. Automated court decision timeline generation could provide a visual overview of what happened throughout a case by representing the main legal events, together with relevant temporal information. Tools and technologies to extract events from court decisions however are still underdeveloped. To this end, in the current paper we compare the effectiveness of three different extraction mechanisms, namely deep learning, conditional random fields, and rule-based method, to facilitate automated extraction of events and their components (i.e., the event type, who was involved, and when it happened). In addition, we provide a corpus of manually annotated decisions of the European Court of Human Rights, which shall serve as a gold standard not only for our own evaluation, but also for the research community for comparison and further experiments

EVects of phenytoin and carbamazepine on calcium transport in Caco-2 cells

Abstract Adverse eVects of anti-seizure/anti-epileptic medications on bone density have been observed and reported since the early 1960s. Phenytoin and carbamazepine are two commonly prescribed anti-epileptic drugs most frequently associated with osteomalacia including fractures, bone demineralization, and reduced bone formation. The mechanism by which anti-epileptic drugs induce bone loss is not fully explained. We hypothesized that anti-epileptic drugs may impair dietary calcium absorption in the intestine. Using Caco-2 cells, a model transport system for study of the function of the intestinal epithelium, we determined the eVects of several anti-epileptic drugs on intestinal epithelial calcium transport. In our system, phenytoin and carbamazepine dose-dependently inhibit active calcium transport from the apical to basolateral side of Caco-2 cells under physiologic calcium conditions. Vitamin D ameliorates the anti-epileptic drug-induced decrease in calcium permeability