Science-based communication to decrease disparities in adult pneumococcal vaccination rates.

Objectives: The objective of our study was to determine the effects of science-based communications on the attitude toward pneumococcal vaccination and understand how nonwhite racial and ethnic populations respond to these messages.

Design: Our team tested several science-based communications using a nationally representative survey, and validated them in a local community pharmacy as a field experiment.

Setting And Participants: The nationally representative sample phase was a survey of 3276 participants, conducted by YouGov, a leading online survey firm.

A pharmacist-driven academic detailing program to increase adult pneumococcal vaccination.

Objectives: To describe our statewide, pharmacist-led education campaign to increase knowledge and awareness of pneumococcal immunization recommendations.

Setting: Immunization providers and residents in the state of Rhode Island.

Practice Description: A clinical pathway (i.

Sequences flanking Arg336 in factor VIIIa modulate factor Xa-catalyzed cleavage rates at this site and cofactor function.

Factor (F)VIII can be activated to FVIIIa by FXa following cleavages at Arg(372), Arg(740), and Arg(1689). FXa also cleaves FVIII/FVIIIa at Arg(336) and Arg(562) resulting in inactivation of the cofactor. These inactivating cleavages occur on a slower time scale than the activating ones.

The role of P4-P3' residues flanking Arg336 in facilitating activated protein C-catalyzed cleavage and inactivation of factor VIIIa.

Introduction: Activated protein C (APC) inactivates factor VIIIa (FVIIIa) through cleavages at Arg336 in the A1 subunit and Arg562 in the A2 subunit. Proteolysis at Arg336 occurs 25-fold faster than at Arg562. Replacing residues flanking Arg336 en bloc with the corresponding residues surrounding Arg562 markedly reduced the rate of cleavage at Arg336, indicating a role for these residues in the catalysis mechanism.

Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface.

Factor VIII consists of a heavy chain (A1A2B domains) and light chain (A3C1C2 domains), whereas the contiguous A1A2 domains are separate subunits in the cofactor, factor VIIIa. The intrinsic instability of the cofactor results from weak affinity interactions of the A2 subunit within factor VIIIa. The charged residues Glu272, Asp519, Glu665, and Glu1984 appear buried at the interface of the A2 domain with either the A1 or A3 domain, and thus may impact protein stability.

Luciferase from the Italian firefly Luciola italica: molecular cloning and expression.

The cDNA encoding the luciferase from the Italian firefly Luciola italica was cloned using reverse transcriptase-PCR and a gene-specific primer set based on the DNA sequence of Luciola mingrelica. The cDNA sequence of L. italica luciferase was determined to be 1647 base pairs in length with an open reading frame of 548 amino acids.