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In the United States alone, ∼14,000 children are hospitalised annually with acute heart failure. The science and art of caring for these patients continues to evolve. The International Pediatric Heart Failure Summit of Johns Hopkins All Children’s Heart Institute was held on February 4 and 5, 2015. The 2015 International Pediatric Heart Failure Summit of Johns Hopkins All Children’s Heart Institute was funded through the Andrews/Daicoff Cardiovascular Program Endowment, a philanthropic collaboration between All Children’s Hospital and the Morsani College of Medicine at the University of South Florida (USF). Sponsored by All Children’s Hospital Andrews/Daicoff Cardiovascular Program, the International Pediatric Heart Failure Summit assembled leaders in clinical and scientific disciplines related to paediatric heart failure and created a multi-disciplinary “think-tank”. The purpose of this manuscript is to summarise the lessons from the 2015 International Pediatric Heart Failure Summit of Johns Hopkins All Children’s Heart Institute, to describe the “state of the art” of the treatment of paediatric cardiac failure, and to discuss future directions for research in the domain of paediatric cardiac failure.
Recently, Christopher M. Tuckett offered in this journal a careful and incisive study of the question whether the scribe of P52 (PRyl 457) employed the nomina sacra forms. The extant text contains no words that were commonly abbreviated as such, though missing portions of the fragment would have contained three instances (lines 2, 5, 7) of the name ‘Jesus’. Tuckett concluded with C. H. Roberts's original opinion (later changed) that the abbreviations were probably not used in P52.Christopher M. Tuckett, ‘P52 and Nomina Sacra’, NTS 47 (2001) 544–8. I would like to call attention here to several factors which have a bearing on the question and which I believe balance the issue, or perhaps even tip the scales of probability a bit the other way.
Intense efforts have been directed at the stabilization of proteins because of their potential uses in organic synthesis, diagnostics, and the pharmaceutical industry. These efforts have resulted in a number of methods to stabilize enzymes including adsorbtion on inert supports or ion exchange resins, entrapment within a gel (with or without crosslinking of the gel or protein), covalent attachment to beads or polymeric supports, inclusion in micelles, chemical derivatization of the protein and mutagenesis. However, these methods do not provide a general approach to solving the problem of protein stability. We believed that the multi-site attachment of a carbohydrate-based macromolecule to the surface of a protein would provide structural stability and a water-like microenvironment for the protein under harsh reaction conditions.