Impacts of Post-Hospitalization Accessible Health Technology and Caregiver Support on 90-Day Acute Care Use and Self-Care Assistance: A Randomized Clinical Trial.

Hospitalized patients often are readmitted soon after discharge, with many hospitalizations being potentially preventable. The authors evaluated a mobile health intervention designed to improve post-hospitalization support for older adults with common chronic conditions. All participants enrolled with an informal caregiver or "CarePartner" (CP).

Effects of Accessible Health Technology and Caregiver Support Posthospitalization on 30-Day Readmission Risk: A Randomized Trial.

Introduction: Patients with chronic illness often require ongoing support postdischarge. This study evaluated a simple-to-use, mobile health-based program designed to improve postdischarge follow-up via (1) tailored communication to patients using automated calls, (2) structured feedback to informal caregivers, and (3) automated alerts to clinicians about urgent problems.

Methods: A total of 283 patients with common medical diagnoses, including chronic obstructive pulmonary disease, coronary artery disease, pneumonia, and diabetes, were recruited from a university hospital, a community hospital, and a US Department of Veterans Affairs hospital.

Improving Post-Hospitalization Transition Outcomes through Accessible Health Information Technology and Caregiver Support: Protocol for a Randomized Controlled Trial.

Objective: The goal of this trial is to evaluate a novel intervention designed to improve post-hospitalization support for older adults with chronic conditions via: direct tailored communication to patients using regular automated calls post discharge, support for informal caregivers outside of the patient's household via structured automated feedback about the patient's status plus advice about how caregivers can help, and support for care management including a web-based disease management tool and alerts about potential problems.

Methods: 846 older adults with common chronic conditions are being identified upon hospital admission. Patients are asked to identify a "CarePartner" (CP) living outside their household, i.

Molecular basis of Diamond-Blackfan anemia: structure and function analysis of RPS19.

Diamond-Blackfan anemia (DBA) is a rare congenital disease linked to mutations in the ribosomal protein genes rps19, rps24 and rps17. It belongs to the emerging class of ribosomal disorders. To understand the impact of DBA mutations on RPS19 function, we have solved the crystal structure of RPS19 from Pyrococcus abyssi.

Assembly of C1 and the MBL- and ficolin-MASP complexes: structural insights.

The classical pathway C1 complex, and the MBL-MASP and ficolin-MASP complexes involved in activation of the lectin pathway have several features in common. Both types of complexes are assembled from two subunits: an oligomeric recognition protein (C1q, MBL, L-, H- or M-ficolin), and a protease component, which is either a tetramer (C1s-C1r-C1r-C1s) or a dimer ((MASP)(2)). Recent functional and 3-D structural investigations have revealed that C1r/C1s and the MASPs associate through a common mechanism involving their N-terminal CUB1-EGF region.

The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin.

MAp19 is an alternative splicing product of the MASP-2 gene comprising the N-terminal CUB1-epidermal growth factor (EGF) segment of MASP-2, plus four additional residues at its C-terminal end. Like full-length MASP-2, it forms Ca(2+)-dependent complexes with mannan-binding lectin (MBL) and L-ficolin. The x-ray structure of human MAp19 was solved to a resolution of 2.

X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement.

C1, the complex that triggers the classical pathway of complement, is assembled from two modular proteases C1r and C1s and a recognition protein C1q. The N-terminal CUB1-EGF segments of C1r and C1s are key elements of the C1 architecture, because they mediate both Ca2+-dependent C1r-C1s association and interaction with C1q. The crystal structure of the interaction domain of C1s has been solved and refined to 1.