A Mobile App for the Precise Measurement of Healthcare Provider Activity Times to Support Time-Driven Activity Based Costing Studies.

The duration of activities performed by healthcare providers are pivotal to Time-Driven Activity-Based Costing (TDABC) models. This study examines the use of a smartphone mobile application technology to record activity times. This study validates the accuracy of activity times recorded on a smartphone mobile application, dTool, compared to observed length of time recordings in the operating room. For analysis, we performed two one-sided tests for the measurements "Case Start" and "Case End". Equivalence bounds were specified in terms of raw mean difference of 1 min (upper) and -1 min (lower). The total number of comparisons in the observer protocol was 72 (32 "case start" patient comparisons and 40 "case end" patient comparisons measured over 45 individual OR cases). Given equivalence bounds of -1.000 and 1.000 (on a raw scale) and an alpha of 0.05, both equivalence tests were significant: provider and third-party observer protocol presented t(40) = 3.228 and p = < 0.001; observer timing protocol presented t(68.68) = 56.762, p = < 0.001. Conclusions: With this novel smartphone technology, a healthcare provider can reliably self-record activity LoT using dTool while providing patient care. Future TDABC studies incorporating this technology will reduce the potential operational barriers to implementation.

Dynamic multi-site phosphorylation by Fyn and Abl drives the interaction between CRKL and the novel scaffolding receptors DCBLD1 and DCBLD2.

Discoidin, CUB, and LCCL domain containing 2 (DCBLD2) is a neuropilin-like transmembrane scaffolding receptor with known and anticipated roles in vascular remodeling and neuronal positioning. DCBLD2 is also up-regulated in several cancers and can drive glioblastomas downstream of activated epidermal growth factor receptor. While a few studies have shown either a positive or negative role for DCBLD2 in regulating growth factor receptor signaling, little is known about the conserved signaling features of DCBLD family members that drive their molecular activities. We previously identified DCBLD2 tyrosine phosphorylation sites in intracellular YxxP motifs that are required for the phosphorylation-dependent binding of the signaling adaptors CRK and CRKL (CT10 regulator of kinase and CRK-like). These intracellular YxxP motifs are highly conserved across vertebrates and between DCBLD family members. Here, we demonstrate that, as for DCBLD2, DCBLD1 YxxP motifs are required for CRKL-SH2 (Src homology 2) binding. We report that Src family kinases (SFKs) and Abl differentially promote the interaction between the CRKL-SH2 domain and DCBLD1 and DCBLD2, and while SFKs and Abl each promote DCBLD1 and DCBLD2 binding to the CRKL-SH2 domain, the effect of Abl is more pronounced for DCBLD1. Using high-performance liquid chromatography coupled with tandem mass spectrometry, we quantified phosphorylation at several YxxP sites in DCBLD1 and DCBLD2, mapping site-specific preferences for SFKs and Abl. Together, these data provide a platform to decipher the signaling mechanisms by which these novel receptors drive their biological activities.