Longitudinal evaluation of a course to build core competencies in implementation practice.

Background: Few training opportunities are available for implementation practitioners; we designed the Practicing Knowledge Translation (PKT) to address this gap. The goal of PKT is to train practitioners to use evidence and apply implementation science in healthcare settings. The aim of this study was to describe PKT and evaluate participant use of implementation science theories, models, and frameworks (TMFs), knowledge, self-efficacy, and satisfaction and feedback on the course.

Evaluation of the "Foundations in Knowledge Translation" training initiative: preparing end users to practice KT.

Background: Current knowledge translation (KT) training initiatives are primarily focused on preparing researchers to conduct KT research rather than on teaching KT practice to end users. Furthermore, training initiatives that focus on KT practice have not been rigorously evaluated and have focused on assessing short-term outcomes and participant satisfaction only. Thus, there is a need for longitudinal training evaluations that assess the sustainability of training outcomes and contextual factors that may influence outcomes.

Social support and the consequences of heart failure compared with other cardiac diseases: The contribution of support received within an attachment relationship.

Background: Interpersonal support is protective in heart disease, but sources of support and the quality of support may change over time, especially with aging and disease progression.

Aims: To determine if support received within an attachment relationship with a spouse is more protective than other types.

Methods: Subjects were sex- and age-matched cardiac outpatients with (n=40) or without (n=43) heart failure; they were studied with an observer-rated measure of attachment and self-report measures of other variables.

Cysteine residues in the transmembrane (TM) 9 to TM11 region of the human equilibrative nucleoside transporter subtype 1 play an important role in inhibitor binding and translocation function.

Inhibitor and substrate interactions with equilibrative nucleoside transporter 1 (ENT1; SLC29A1) are known to be affected by cysteine-modifying reagents. A previous study from our laboratory established Cys222 in transmembrane (TM) 6 as the residue responsible for methyl methanethiosulfonate (a membrane-permeable sulfhydryl modifier)-mediated enhancement of the binding of the ENT1 inhibitor nitrobenzylmercaptopurine riboside (NBMPR) in intact cells. However, the capacity of charged sulfhydryl reagents to inhibit the binding of NBMPR in broken cell preparations (allowing cytoplasmic access) was not affected by mutation of any of the cysteines (Cys87, 193, 213, or 222) in the N-terminal half of the protein.

Identification of cysteines involved in the effects of methanethiosulfonate reagents on human equilibrative nucleoside transporter 1.

Inhibitor and substrate interactions with equilibrative nucleoside transporter 1 (ENT1; SLC29A1) are known to be affected by cysteine-modifying reagents. Given that selective ENT1 inhibitors, such as nitrobenzylmercaptopurine riboside (NBMPR), bind to the N-terminal half of the ENT1 protein, we hypothesized that one or more of the four cysteine residues in this region were contributing to the effects of the sulfhydryl modifiers. Recombinant human ENT1 (hENT1), and the four cysteine-serine ENT1 mutants, were expressed in nucleoside transport-deficient PK15 cells and probed with a series of methanethiosulfonate (MTS) sulfhydryl-modifying reagents.

Characterization of mENT1Delta11, a novel alternative splice variant of the mouse equilibrative nucleoside transporter 1.

Mammalian cells require specific transport mechanisms for the cellular uptake and release of endogenous nucleosides such as adenosine, and nucleoside analogs used in chemotherapy. We have identified a novel splice variant of the mouse equilibrative nucleoside transporter, mENT1, that results from the exclusion of exon 11 during pre-RNA processing. This variant encodes a truncated protein (mENT1Delta11) missing the last three transmembrane domains of the full-length mENT1.