Evaluating the effect of data standardization and validation on patient matching accuracy

Objective This study evaluated the degree to which recommendations for demographic data standardization improve patient matching accuracy using real-world datasets. Materials and Methods We used 4 manually reviewed datasets, containing a random selection of matches and nonmatches. Matching datasets included health information exchange (HIE) records, public health registry records, Social Security Death Master File records, and newborn screening records. Standardized fields including last name, telephone number, social security number, date of birth, and address. Matching performance was evaluated using 4 metrics: sensitivity, specificity, positive predictive value, and accuracy. Results Standardizing address was independently associated with improved matching sensitivities for both the public health and HIE datasets of approximately 0.6% and 4.5%. Overall accuracy was unchanged for both datasets due to reduced match specificity. We observed no similar impact for address standardization in the death master file dataset. Standardizing last name yielded improved matching sensitivity of 0.6% for the HIE dataset, while overall accuracy remained the same due to a decrease in match specificity. We noted no similar impact for other datasets. Standardizing other individual fields (telephone, date of birth, or social security number) showed no matching improvements. As standardizing address and last name improved matching sensitivity, we examined the combined effect of address and last name standardization, which showed that standardization improved sensitivity from 81.3% to 91.6% for the HIE dataset. Conclusions Data standardization can improve match rates, thus ensuring that patients and clinicians have better data on which to make decisions to enhance care quality and safety

Structural Characterization of Minor Ampullate Spidroin Domains and Their Distinct Roles in Fibroin Solubility and Fiber Formation

10.1371/journal.pone.0056142PLoS ONE82

Plasticity in Major Ampullate Silk Production in Relation to Spider Phylogeny and Ecology

Spider major ampullate silk is a high-performance biomaterial that has received much attention. However, most studies ignore plasticity in silk properties. A better understanding of silk plasticity could clarify the relative importance of chemical composition versus processing of silk dope for silk properties. It could also provide insight into how control of silk properties relates to spider ecology and silk uses

Biomimetic spinning of artificial spider silk from a chimeric minispidroin.

Herein we present a chimeric recombinant spider silk protein (spidroin) whose aqueous solubility equals that of native spider silk dope and a spinning device that is based solely on aqueous buffers, shear forces and lowered pH. The process recapitulates the complex molecular mechanisms that dictate native spider silk spinning and is highly efficient; spidroin from one liter of bacterial shake-flask culture is enough to spin a kilometer of the hitherto toughest as-spun artificial spider silk fiber

Spidroin N-terminal Domain Promotes a pH-dependent Association of Silk Proteins during Self-assembly*

Spider silks are spun from concentrated solutions of spidroin proteins. The appropriate timing of spidroin assembly into organized fibers must be highly regulated to avoid premature fiber formation. Chemical and physical signals presented to the silk proteins as they pass from the ampulle and through the tapered duct include changes in ionic environment and pH as well as the introduction of shear forces. Here, we show that the N-terminal domain of spidroins from the major ampullate gland (MaSp-NTDs) for both Nephila and Latrodectus spiders associate noncovalently as homodimers. The MaSp-NTDs are highly pH-responsive and undergo a structural transition in the physiological pH range of the spider duct. Tryptophan fluorescence of the MaSp-NTDs reveals a change in conformation when pH is decreased, and the pH at which the transition occurs is determined by the amount and type of salt present. Size exclusion chromatography and pulldown assays both indicate that the lower pH conformation is associated with a significantly increased MaSp-NTD homodimer stability. By transducing the duct pH signal into specific protein-protein interactions, this conserved spidroin domain likely contributes significantly to the silk-spinning process. Based on these results, we propose a model of spider silk assembly dynamics as mediated through the MaSp-NTD