4 research outputs found

    E-Journals and the Big Deal: A Review of the Literature

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    Faced with shrinking budgets and increased subscription prices, many academic libraries are seeking ways to reduce the cost of e-journal access. A common target for cuts is the “Big Deal,” or large bundled subscription model, a term coined by Kenneth Frazier in a 2001 paper criticizing the effects of the Big Deal on the academic community. The purpose of this literature review is to examine issues related to reducing e-journal costs, including criteria for subscription retention or cancellation, decision-making strategies, impacts of cancellations, and other options for e-journal content provision. Commonly used criteria for decision-making include usage statistics, overlap analysis, and input from subject specialists. The most commonly used strategy for guiding the process and aggregating data is the rubric or decision grid. While the e-journal landscape supports several access models, such as Pay-Per-View, cloud access, and interlibrary loan, the Big Deal continues to dominate. Trends over the past several years point to dwindling support for the Big Deal however, due largely to significant annual rate increases and loss of content control

    Dietary modulation and structure prediction of rat mucosal pentraxin (Mptx) protein and loss of function in humans

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    Mucosal pentraxin (Mptx), identified in rats, is a short pentraxin of unknown function. Other subfamily members are Serum amyloid P component (SAP), C-reactive protein (CRP) and Jeltraxin. Rat Mptx mRNA is predominantly expressed in colon and in vivo is strongly (30-fold) regulated by dietary heme and calcium, modulators of colon cancer risk. This renders Mptx a potential nutrient sensitive biomarker of gut health. To support a role as biomarker, we examined whether the pentraxin protein structure is conserved, whether Mptx protein is nutrient-sensitively expressed and whether Mptx is expressed in mouse and human. Sequence comparison and 3D modelling showed that rat Mptx is highly homologous to the other pentraxins. The calcium-binding site and subunit interaction sites are highly conserved, while a loop deletion and charged residues contribute to a distinctive “top” face of the pentamer. In accordance with mRNA expression, Mptx protein is strongly down-regulated in rat colon mucosa in response to high dietary heme intake. Mptx mRNA is expressed in rat and mouse colon, but not in human colon. A stop codon at the beginning of human exon two indicates loss of function, which may be related to differences in intestinal cell turnover between man and rodents
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