Department of Physics

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https://hdl.handle.net/10919/24211

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Browsing Department of Physics by Department "Fralin Biomedical Research Institute"

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    Lessons learned from implementing the patient-centered medical home
    Green, Ellen P.; Wendland, John; Carver, M. Colette; Hughes Rinker, Cortney; Mun, Seong K. (Hindawi, 2012)
    The Patient-Centered Medical Home (PCMH) is a primary care model that provides coordinated and comprehensive care to patients to improve health outcomes. This paper addresses practical issues that arise when transitioning a traditional primary care practice into a PCMH recognized by the National Committee for Quality Assurance (NCQA). Individual organizations' experiences with this transition were gathered at a PCMH workshop in Alexandria, Virginia in June 2010. An analysis of their experiences has been used along with a literature review to reveal common challenges that must be addressed in ways that are responsive to the practice and patients' needs. These are: NCQA guidance, promoting provider buy-in, leveraging electronic medical records, changing office culture, and realigning workspace in the practice to accommodate services needed to carry out the intent of PCMH. The NCQA provides a set of standards for implementing the PCMH model, but these standards lack many specifics that will be relied on in location situations. While many researchers and providers have made critiques, we see this vagueness as allowing for greater flexibility in how a practice implements PCMH.
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    Structural, in silico, and functional analysis of a Disabled-2-derived peptide for recognition of sulfatides
    Song, Wei; Gottschalk, Carter J.; Tang, Tuo-Xian; Biscardi, Andrew; Ellena, Jeffrey F.; Finkielstein, Carla V.; Brown, Anne M.; Capelluto, Daniel G. S. (2020-08-11)
    Disabled-2 (Dab2) is an adaptor protein that regulates the extent of platelet aggregation by two mechanisms. In the first mechanism, Dab2 intracellularly downregulates the integrin alpha (IIb)beta (3) receptor, converting it to a low affinity state for adhesion and aggregation processes. In the second mechanism, Dab2 is released extracellularly and interacts with the pro-aggregatory mediators, the integrin alpha (IIb)beta (3) receptor and sulfatides, blocking their association to fibrinogen and P-selectin, respectively. Our previous research indicated that a 35-amino acid region within Dab2, which we refer to as the sulfatide-binding peptide (SBP), contains two potential sulfatide-binding motifs represented by two consecutive polybasic regions. Using molecular docking, nuclear magnetic resonance, lipid-binding assays, and surface plasmon resonance, this work identifies the critical Dab2 residues within SBP that are responsible for sulfatide binding. Molecular docking suggested that a hydrophilic region, primarily mediated by R42, is responsible for interaction with the sulfatide headgroup, whereas the C-terminal polybasic region contributes to interactions with acyl chains. Furthermore, we demonstrated that, in Dab2 SBP, R42 significantly contributes to the inhibition of platelet P-selectin surface expression. The Dab2 SBP residues that interact with sulfatides resemble those described for sphingolipid-binding in other proteins, suggesting that sulfatide-binding proteins share common binding mechanisms.