A Mnemonic for Pharmacists to Ensure Optimal Monitoring and Safety of Total Parenteral Nutrition: I AM FULL.

Objective: To present a guideline-derived mnemonic that provides a systematic monitoring process to increase pharmacists' confidence in total parenteral nutrition (TPN) monitoring and improve safety and efficacy of TPN use.

Data Sources: The American Society for Parenteral and Enteral Nutrition (ASPEN) guidelines were reviewed. Additional resources included a literature search of PubMed (1980 to May 2016) using the search terms: total parenteral nutrition, mnemonic, indications, allergy, macronutrients, micronutrients, fluid, comorbidities, labs, peripheral line, and central line.

Serendipitous discovery of light-induced (In Situ) formation of an Azo-bridged dimeric sulfonated naphthol as a potent PTP1B inhibitor.

Background: Protein tyrosine phosphatases (PTPs) like dual specificity phosphatase 5 (DUSP5) and protein tyrosine phosphatase 1B (PTP1B) are drug targets for diseases that include cancer, diabetes, and vascular disorders such as hemangiomas. The PTPs are also known to be notoriously difficult targets for designing inihibitors that become viable drug leads. Therefore, the pipeline for approved drugs in this class is minimal.

Docking into Mycobacterium tuberculosis Thioredoxin Reductase Protein Yields Pyrazolone Lead Molecules for Methicillin-Resistant Staphylococcus aureus.

The thioredoxin/thioredoxin reductase system (Trx/TrxR) is an attractive drug target because of its involvement in a number of important physiological processes, from DNA synthesis to regulating signal transduction. This study describes the finding of pyrazolone compounds that are active against . Initially, the project was focused on discovering small molecules that may have antibacterial properties targeting the thioredoxin reductase.

Identification of inhibitors that target dual-specificity phosphatase 5 provide new insights into the binding requirements for the two phosphate pockets.

Background: Dual-specificity phosphatase-5 (DUSP5) plays a central role in vascular development and disease. We present a p-nitrophenol phosphate (pNPP) based enzymatic assay to screen for inhibitors of the phosphatase domain of DUSP5.

Methods: pNPP is a mimic of the phosphorylated tyrosine on the ERK2 substrate (pERK2) and binds the DUSP5 phosphatase domain with a Km of 7.