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Neuroplin-1 (NRP1), a receptor for vascular endothelial growth factor (VEGF) family members, has three distinct extracellular domains, a1a2, b1b2, and c. To determine the VEGF(165) and placenta growth factor 2 (PlGF-2)-binding sites of NRP1, recombinant NRP1 domains were expressed in mammalian cells as Myc-tagged, soluble proteins, and used in(More)
We have reported previously that Noggin is a heparin-binding protein and associates with the cell surface through heparan sulfate proteoglycans, where it remains functional for the binding of bone morphogenetic proteins (BMPs). Here we report that the binding of Noggin to the cell surface is highly selective for heparan sulfate and that specific structural(More)
This article proposes a model of student school engagement, comprising aspirations, belonging, and productivity. From this model, items for the Student School Engagement Measure (SSEM) were developed. The SSEM was validated with data from 396 eighth graders in an urban school district. Utilizing structural equation modeling, the second-order empirical model(More)
The following guidelines are an interpretation of the evidence presented in the 2010 International Consensus on Cardiopulmonary Resuscitation and Emergency Cardiovascular Care Science With Treatment Recommendations 1). They apply primarily to newly born infants undergoing transition from intrauterine to extrauterine life, but the recommendations are also(More)
Fibrillin-1 assembly into microfibrils and elastic fiber formation involves interactions with glycosaminoglycans. We have used BIAcore technology to investigate fibrillin-1 interactions with heparin and with heparin saccharides that are analogous to S-domains of heparan sulfate. We have identified four high affinity heparin-binding sites on fibrillin-1,(More)
The binding of interleukin-8 (IL-8) to heparan sulfate (HS) proteoglycans on the surface of endothelial cells is crucial for the recruitment of neutrophils to an inflammatory site. Fluorescence anisotropy measurements yielded an IL-8 dimerization constant of 120 nM. The binding affinities, obtained by isothermal fluorescence titration, of size-defined(More)
The serpin heparin cofactor II (HCII) is a glycosaminoglycan-activated inhibitor of thrombin that circulates at a high concentration in the blood. The antithrombotic effect of heparin, however, is due primarily to the specific interaction of a fraction of heparin chains with the related serpin antithrombin (AT). What currently prevents selective therapeutic(More)
Our accelerating computational demand and the rise of multicore hardware have made parallel programs increasingly pervasive and critical. Yet, these programs remain extremely difficult to write, test, analyze, debug, and verify. In this article, we provide our view on why parallel programs, specifically multithreaded programs, are difficult to get right. We(More)