Do electronic patient information systems improve efficiency and quality of care? An evaluation of utilisation of the Discovery HealthID application.

BACKGROUND: Electronic health records (EHRs) appear to offer a number of potential benefits, but practitioners are often hesitant to make the transition to using them. OBJECTIVES: To determine whether the use of one such system, designed and offered by a health insurer (HealthID; Discovery Health), makes a difference to the efficiency and quality of doctor-patient consultations. METHODS: A descriptive study using mixed methods was designed. A qualitative phase of individual interviews of purposefully sampled respondents was followed by a quantitative survey of a random sample of general practitioners and specialists who were registered users of the system. RESULTS: In the qualitative findings, 18 respondents reported their perceptions of the ease of use of the application, their motivation for using it, its functions and benefits, the impact on efficiency and quality of care, and the challenges they experienced. In addition, they reported on the details of the challenges of using the system, and made suggestions for improvements, particularly with regard to the need for training and IT support. The quantitative results from the majority of 93 respondents confirmed that while the use of the app improved patient care through positive effects on specific functions such as access to accurate patient records and easier Chronic Illness Benefit applications, they felt that it had an equivocal impact in other areas, such as maintaining patient confidentiality and enhancing teamwork and efficiency. The financial incentives offered by Discovery Health, as well as possibly the training and support provided, appear to be more influential for high-frequency than for low-frequency users. The majority said that it did not help with referrals or script writing, or with access to International Statistical Classification of Diseases and Related Health Problems, 10th revision (ICD-10) codes. CONCLUSIONS: EHR systems like Discovery Health's HealthID could improve the efficiency of medical consultations by increasing access to stored health information without requiring data entry by clinicians, and thereby have the potential to indirectly improve the quality of care, provided that certain conditions are met.

Human factors for capacity building: lessons learned from the OpenMRS implementers network.

OBJECTIVES: The overall objective of this project was to investigate ways to strengthen the OpenMRS community by (i) developing capacity and implementing a network focusing specifically on the needs of OpenMRS implementers, (ii) strengthening community-driven aspects of OpenMRS and providing a dedicated forum for implementation-specific issues, and; (iii) providing regional support for OpenMRS implementations as well as mentorship and training. METHODS: The methods used included (i) face-to-face networking using meetings and workshops; (ii) online collaboration tools, peer support and mentorship programmes; (iii) capacity and community development programmes, and; (iv) community outreach programmes. RESULTS: The community-driven approach, combined with a few simple interventions, has been a key factor in the growth and success of the OpenMRS Implementers Network. It has contributed to implementations in at least twenty-three different countries using basic online tools; and provided mentorship and peer support through an annual meeting, workshops and an internship program. The OpenMRS Implementers Network has formed collaborations with several other open source networks and is evolving regional OpenMRS Centres of Excellence to provide localized support for OpenMRS development and implementation. These initiatives are increasing the range of functionality and sustainability of open source software in the health domain, resulting in improved adoption and enterprise-readiness. CONCLUSIONS: Social organization and capacity development activities are important in growing a successful community-driven open source software model.

An informatics system to support knowledge management in the health sector--the South African National Health Knowledge Network.

This paper discusses the planning and development of a South African national health knowledge network. The methodology is in essence based on the principles of knowledge management and the drivers of a system of innovation. The knowledge network, SA HealthInfo, aims to provide a one-stop interactive forum/resource, for quality-controlled and evidence-based health research information, to a wide spectrum of users, at various levels of aggregation, with the necessary security arrangements and facilities for interaction among users to promote explicit (codified) and tacit knowledge flow. It will therefore stimulate the process of innovation within the South African health system.

2',3'-O-(2,4,6-trinitrophenyl)-8-azido-adenosine mono-, di-, and triphosphates as photoaffinity probes of the Ca2+-ATPase of sarcoplasmic reticulum. Regulatory/superfluorescent nucleotides label the catalytic site with high efficiency.

We have synthesized a new class of ATP photo-affinity analogs, 2',3'-O-(2,4,6-trinitrophenyl)-8-azido (TNP-8N3)-ATP, -ADP, and -AMP, and their radiolabeled derivatives, and characterized their interaction with sarcoplasmic reticulum vesicles. The nucleotides bind with high affinity (Kd = 0.04-0.4 microM) to the catalytic site of the Ca2+-ATPase. TNP-8N3-ATP and TNP-8N3-ADP, at low concentrations (less than 10 microM), accelerate ATPase activity 1.5- and 1.4-fold, respectively, indicating that they bind to a regulatory site. In the same concentration range, they all undergo a large increase in fluorescence ("superfluorescence") during enzyme turnover in the presence of ATP and Ca2+, or on phosphorylation from Pi in a Ca2+-depleted medium. Irradiation at alkaline pH results in specific covalent incorporation of the nucleotide at the catalytic site on the A1 tryptic subfragment. The efficiency of catalytic site labeling is greatest (up to 80% of available sites/irradiation period) in the presence of ATP, Ca2+, and Mg2+, conditions in which the probe binds only to the regulatory and superfluorescent sites. The covalently attached nucleotide exhibits fluorescence enhancement on enzyme turnover in the presence of acetyl phosphate plus Ca2+ or on phosphorylation from Pi in a Ca2+-depleted medium, but not in the presence of ATP plus Ca2+. The results suggest that the catalytic, regulatory, and superfluorescent nucleotide sites are at the same locus and that the binding domain includes portions of the A1 subfragment. The high efficiency with which the site is photolabeled during turnover is ascribed to water exclusion and possibly cleft closure in E2-P.

ATP regulation of sarcoplasmic reticulum Ca2+-ATPase. Metal-free ATP and 8-bromo-ATP bind with high affinity to the catalytic site of phosphorylated ATPase and accelerate dephosphorylation.

To localize and characterize the regulatory nucleotide site of skeletal muscle sarcoplasmic reticulum Ca2+-ATPase, we have investigated the effects of ADP, ATP, and analogues of these nucleotides on the rate of dephosphorylation of both native ATPase and ATPase modified with fluorescein 5'-isothiocyanate (FITC), a reagent which hinders access of nucleotides to the ATPase catalytic site without affecting phosphorylation from Pi. Dephosphorylation of the phosphoenzyme formed from Pi was monitored by rapid filtration or stopped-flow fluorescence, mostly at 20 degrees C, pH 6.0, and in the absence of potassium. Fluorescence measurements were made possible through the use of 8-bromo-ATP, which selectively quenched certain tryptophan residues of the ATPase, thereby allowing the intrinsic fluorescence changes associated with dephosphorylation to be measured in the presence of bound nucleotide. ATP, 8-bromo-ATP, and trinitrophenyladenosine diand triphosphate, but not ADP, enhanced the rate of dephosphorylation of native ATPase 2-3-fold when added in the absence of divalent cations. Millimolar concentrations of Mg2+ eliminated the accelerating effects. Acceleration in the absence of Mg2+ was observed at relatively low concentrations of ATP and 8-bromo-ATP (0.01-0.1 mM) and binding of metal-free ATP and ADP, but not Mg.ATP, to the phosphoenzyme in this concentration range was demonstrated directly. Modification of the ATPase with FITC blocked nucleotide binding in the submillimolar concentration range and eliminated the nucleotide-induced acceleration of dephosphorylation. These results show that dephosphorylation, under these conditions, is regulated by ATP but not by Mg.ATP or ADP, and that the catalytic site is the locus of this "regulatory" ATP binding site.

Mechanism of action of the calcium pump of sarcoplasmic reticulum of skeletal muscle.

The Ca2+-adenosine triphosphatase (ATPase) of skeletal muscle sarcoplasmic reticulum is a single protein species that pumps calcium ions at the expense of adenosine triphosphate (ATP). The reaction cycle includes phosphorylated intermediates which change the affinity and orientation of calcium sites. The monomer appears to be fully functional. Cross-linking and fluorescence studies indicate that ATP binds to a domain that approaches the phosphorylation site and becomes occluded during the reaction cycle. Interactions between these and the calcium channel, possibly via an energy transduction domain, ensure efficient coupling of catalytic and transport cycles.