Generating Actionable Insights from Patient Medical Records and Structured Clinical Knowledge.

While adherence to clinical guidelines improves the quality and consistency of care, personalized healthcare also requires a deep understanding of individual disease models and treatment plans. The structured preparation of medical routine data in a certain clinical context, e.g. a treatment pathway outlined in a medical guideline, is currently a challenging task. Medical data is often stored in diverse formats and systems, and the relevant clinical knowledge defining the context is not available in machine-readable formats. We present an approach to extract information from medical free text documentation by using structured clinical knowledge to guide information extraction into a structured and encoded format, overcoming the known challenges for natural language processing algorithms. Preliminary results have been encouraging, as one of our methods managed to extract 100% of all data-points with 85% accuracy in details. These advancements show the potential of our approach to effectively use unstructured clinical data to elevate the quality of patient care and reduce the workload of medical personnel.

The Hidden Intricacies of Aquaporins: Remarkable Details in a Common Structural Scaffold.

Evolution turned aquaporins (AQPs) into the most efficient facilitators of passive water flow through cell membranes at no expense of solute discrimination. In spite of a plethora of solved AQP structures, many structural details remain hidden. Here, by combining extensive sequence- and structural-based analysis of a unique set of 20 non-redundant high-resolution structures and molecular dynamics simulations of four representatives, key aspects of AQP stability, gating, selectivity, pore geometry, and oligomerization, with a potential impact on channel functionality, are identified. The general view of AQPs possessing a continuous open water pore is challenged and it is depicted that AQPs' selectivity is not exclusively shaped by pore-lining residues but also by the relative arrangement of transmembrane helices. Moreover, this analysis reveals that hydrophobic interactions constitute the main determinant of protein thermal stability. Finally, a numbering scheme of the conserved AQP scaffold is established, facilitating direct comparison of, for example, disease-causing mutations and prediction of potential structural consequences. Additionally, the results pave the way for the design of optimized AQP water channels to be utilized in biotechnological applications.