The NIH Open Citation Collection: A public access, broad coverage resource.

Citation data have remained hidden behind proprietary, restrictive licensing agreements, which raises barriers to entry for analysts wishing to use the data, increases the expense of performing large-scale analyses, and reduces the robustness and reproducibility of the conclusions. For the past several years, the National Institutes of Health (NIH) Office of Portfolio Analysis (OPA) has been aggregating and enhancing citation data that can be shared publicly. Here, we describe the NIH Open Citation Collection (NIH-OCC), a public access database for biomedical research that is made freely available to the community. This dataset, which has been carefully generated from unrestricted data sources such as MedLine, PubMed Central (PMC), and CrossRef, now underlies the citation statistics delivered in the NIH iCite analytic platform. We have also included data from a machine learning pipeline that identifies, extracts, resolves, and disambiguates references from full-text articles available on the internet. Open citation links are available to the public in a major update of iCite (https://icite.od.nih.gov).

Climate change, human health, and biomedical research: analysis of the National Institutes of Health research portfolio.

BACKGROUND: According to a wide variety of analyses and projections, the potential effects of global climate change on human health are large and diverse. The U.S. National Institutes of Health (NIH), through its basic, clinical, and population research portfolio of grants, has been increasing efforts to understand how the complex interrelationships among humans, ecosystems, climate, climate variability, and climate change affect domestic and global health. OBJECTIVES: In this commentary we present a systematic review and categorization of the fiscal year (FY) 2008 NIH climate and health research portfolio. METHODS: A list of candidate climate and health projects funded from FY 2008 budget appropriations were identified and characterized based on their relevance to climate change and health and based on climate pathway, health impact, study type, and objective. RESULTS: This analysis identified seven FY 2008 projects focused on climate change, 85 climate-related projects, and 706 projects that focused on disease areas associated with climate change but did not study those associations. Of the nearly 53,000 awards that NIH made in 2008, approximately 0.17% focused on or were related to climate. CONCLUSIONS: Given the nature and scale of the potential effects of climate change on human health and the degree of uncertainty that we have about these effects, we think that it is helpful for the NIH to engage in open discussions with science and policy communities about government-wide needs and opportunities in climate and health, and about how NIH's strengths in human health research can contribute to understanding the health implications of global climate change. This internal review has been used to inform more recent initiatives by the NIH in climate and health.

The role of lic2B in lipopolysaccharide biosynthesis in Haemophilus influenzae strain Eagan.

Lipopolysaccharide (LPS) biosynthesis in Haemophilus influenzae involves genes from the lic2 locus that are required for chain extension from the middle heptose (HepII) of the conserved triheptosyl inner-core moiety. Lic2C initiates the process by attaching the first glucose to HepII, but the gene encoding for the enzyme adding the next ß-D-Glcp- is uncharacterized. Lic2B is the candidate glucosyltransferase; however, in previous investigations, mutation of lic2B resulted in no hexose extension from HepII, likely due to a polar effect on the lic2C gene. In this study we complemented a lic2B knock-out mutant of H. influenzae strain Eagan with a functional lic2C gene and investigated its LPS by mass spectrometry and 2D NMR spectroscopy. Lic2B was found to encode a glucosyltransferase responsible for the linkage of ß-D-Glcp-(1→4)-α-D-Glcp-(1→ extending from O-3 of the central heptose of the triheptosyl inner-core moiety, l-α-D-Hepp-(1→2)-[PEtn→6]-l-α-D-Hepp-(1→3)-l-α-D-Hepp-(1→5)-[PPEtn→4]-α-Kdo-(2→6)-lipid A.