Project RENEW: A Nursing Informatics Led Initiative to Reduce Documentation Burden.

Documentation burden within the United States has grown to unprecedented proportions. Poor usability of the electronic health record has been identified as one of the root causes of documentation burden. By using a structured review process, the nursing informatics team at Northwestern Medicine Healthcare identified opportunities for improved usability.

Fall Risk Prediction Models During the Initial COVID-19 Surge: Could Predictive Analytics Be Used in a Resource-Constrained Environment?

During the first COVID surge, multiple changes in nurse staffing and workflows were made to support care delivery in a resource-constrained environment. We hypothesized that there was a higher rate of inpatient falls during the COVID surge. Furthermore, we predicted that an automated predictive analytic algorithm would perform as well as the Johns Hopkins Fall Risk Assessment.

Comparison of Two Different Models to Predict Fall Risk in Hospitalized Patients.

Background: Fall prevention is a patient safety and economic priority for health care organizations. An automated model within the electronic medical record (EMR) that accurately predicts risk for falling would be valuable for mitigation of inpatient falls. The aim of this study was to validate the reliability of an EMR-based computerized predictive model (ROF Model) for inpatient falls.

Cdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique Features.

Eukaryotic initiation factor 2 (eIF2), a heterotrimeric guanosine triphosphatase, has a central role in protein biosynthesis by supplying methionylated initiator tRNA to the ribosomal translation initiation complex and by serving as a target for translational control in response to stress. Recent work identified a novel step indispensable for eIF2 function: assembly of eIF2 from its three subunits by the cell proliferation protein Cdc123. We report the first crystal structure of a Cdc123 representative, that from Schizosaccharomyces pombe, both isolated and bound to domain III of Saccharomyces cerevisiae eIF2γ.

Insights into the cellular mechanism of the yeast ubiquitin ligase APC/C-Cdh1 from the analysis of in vivo degrons.

The anaphase-promoting complex/cyclosome (APC/C) controls a variety of cellular processes through its ability to target numerous protein substrates for timely degradation. Substrate selection by this ubiquitin ligase depends on related activator proteins, Cdc20 and Cdh1, which bind and activate the APC/C at distinct cell cycle stages. Biochemical and structural studies revealed that Cdc20 and Cdh1 carry conserved receptor domains to recognize specific sequence motifs in substrates, such as D and KEN boxes.