We present and analyze video-microscopy-based single-particle-tracking measurements of the budding yeast (Saccharomyces cerevisiae) membrane protein, Pma1, fluorescently labeled either by direct fusion to the switchable fluorescent protein, mEos3.2, or by a novel, light-touch, labeling scheme, in which a 5 amino acid tag is directly fused to the C-terminus of Pma1, which then binds mEos3.2.
View Article and Find Full Text PDFBackground: Scalable and safe approaches for heart failure guideline-directed medical therapy (GDMT) optimization are needed.
Objectives: The authors assessed the safety and effectiveness of a virtual care team guided strategy on GDMT optimization in hospitalized patients with heart failure with reduced ejection fraction (HFrEF).
Methods: In a multicenter implementation trial, we allocated 252 hospital encounters in patients with left ventricular ejection fraction ≤40% to a virtual care team guided strategy (107 encounters among 83 patients) or usual care (145 encounters among 115 patients) across 3 centers in an integrated health system.
Background And Purpose: While the successful provision of telestroke care has been well documented in the literature, studies on the impact of comprehensive teleneurology service (TN) to hospital measures are lacking. We evaluated 3 traditional health services metrics of hospital performance: time from consult request to consult completion, inpatient length of stay (LOS), and the rate of patients transferred for tertiary care.
Methods: Medical records (n = 899) from 3 community hospitals and our TN consultation database were retrospectively reviewed during the 2 years before (n = 703, 3 hospitals) and 4 months (n = 2 hospitals) to 2 years (n = 1 hospital) after implementation (n = 196) of a TN program for routine and urgent consult requests.
We present a novel method to fluorescently label proteins, post-translationally, within live Saccharomycescerevisiae. The premise underlying this work is that fluorescent protein (FP) tags are less disruptive to normal processing and function when they are attached post-translationally, because target proteins are allowed to fold properly and reach their final subcellular location before being labeled. We accomplish this post-translational labeling by expressing the target protein fused to a short peptide tag (SpyTag), which is then covalently labeled in situ by controlled expression of an open isopeptide domain (SpyoIPD, a more stable derivative of the SpyCatcher protein) fused to an FP.
View Article and Find Full Text PDFAll diseases can be fundamentally viewed as the result of malfunctioning cellular pathways. Protein engineering offers the potential to develop new tools that will allow these dysfunctional pathways to be better understood, in addition to potentially providing new routes to restore proper function. Here we discuss different approaches that can be used to change the intracellular activity of a protein by intervening at the protein level: targeted protein sequestration, protein recruitment, protein degradation, and selective inhibition of binding interfaces.
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