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Ninety per cent of financial customers feel that their relationship with their financial institutions (FIs) is based solely on simple transactional activities, such as making a deposit or withdrawing money. Today’s digitally minded customers, however, expect tailored, seamless and secure user experiences that excite and delight, such as those provided by leading brands like Google, Apple, Facebook and Amazon. FIs must cater to the elevated standards for user experience and take advantage of how people share, consume and exchange data every day. FIs must reinvent themselves in order to stay relevant and keep up with the customers’ expectations for how to spend, save, borrow and plan their financial future in the digital economy. With nearly 57 per cent of US consumers identified as financially unhealthy, FIs have the opportunity to take on the role of trusted advisers for holistic financial health. This paper identifies three different directions for FIs t execute a ‘playing to win’ strategy: becoming an all-inclusive destination of customers’ financial needs, providing financial solutions embedded into the dominant digital destinations of their customers and enabling a financial marketplace. To win, FIs must provide superior experiences and personalised services that help customers get the most out of their money.

We present here a new approach that enabled the identification of a new protein from a bacterial strain with unknown genomic background using a combination of inverted PCR with degenerate primers derived from N-terminal protein sequences and high resolution peptide mass determination of proteolytic digests from two-dimensional electrophoretic separation. Proteins of the sulfate-reducing bacterium Desulfotignum phosphitoxidansspecifically induced in the presence of phosphite were separated by two-dimensional gel electrophoresis as a series of apparent soluble and membrane-bound isoforms with molecular masses of ∼35 kDa. Inverted PCR based on N-terminal sequences and high resolution peptide mass fingerprinting by Fourier transform-ion cyclotron resonance mass spectrometry provided the identification of a new NAD(P) epimerase/dehydratase by specific assignment of peptide masses to a single ORF, excluding other possible ORF candidates. The protein identification was ascertained by chromatographic separation and sequencing of internal proteolytic peptides. Metal ion affinity isolation of tryptic peptides and high resolution mass spectrometry provided the identification of five phosphorylations identified in the domains 23–47 and 91–118 of the protein. In agreement with the phosphorylations identified, direct molecular weight determination of the soluble protein eluted from the two-dimensional gels by mass spectrometry provided a molecular mass of 35,400 Da, which is consistent with an average degree of three phosphorylations.

The goal of this research is to use eyegaze tracking data to provide insights into designing radiology workstations. We designed a look-alike radiology task with artificial stimuli. The task involved a comparative visual search of two side-by-side images, using two different interaction techniques. We tracked the eyegaze of four radiologists while they performed the task and measured the duration of the fixations on the controls, the left and right images, and on the artificial targets. Response time differences between the two interaction techniques exceeded the differences of fixations on the controls. Fixations on the left-side images are longer than the right-side images, and the search for multifeatured targets occurs in two phases: first a regular scan path search phase for a likely target and then a confirmation phase of several fixations on the target in each side-by-side image. We conclude that eyegaze tracking shows that disruption of visual search leads to cognitive disruption; subjects use the left image as a reference image and multiple saccades between left and right side images are necessary, because of the limitations of the visual working memory.

The "one-size-fits-all" approach for radiology workstation design is not good enough anymore. While most of the picture archiving and communication system (PACS) vendors are racing to add more features to the radiology workstation, there is little interest in addressing the specific needs of other hospital departments. Significant delays in the availability of radiology reports are often caused by the fact there is not enough Intensive Care Unit (ICU) volume to justify a full time radiologist. Consequently, the radiologist assigned to cover the ICU exams, most likely working from a different building, will read the ICU exams only at certain times, depending on the limitations for remote image availability. This paper addresses the main objectives in designing a digital radiology workstation for use in the medical ICU (MICU), requiring enhancements to current PACS systems. Our suggestions for PACS improvement follow the ICU digital workflow starting with the transfer of the images from the modality, continuing with the presentation of the radiology examination to different types of users (radiologists or ICU staff), up to the creation and distribution of the reports.

Intercellular adhesion molecule-1 (ICAM-1) is a heavily N‐glycosylated transmembrane protein comprising five extracellular Ig-like domains. The soluble isoform of ICAM-1 (sICAM-1), consisting of its extracellular part, is elevated in the cerebrospinal fluid of patients with severe brain trauma. In mouse astrocytes, recombinant mouse sICAM-1 induces the production of the CXC chemokine macrophage inflammatory protein-2 (MIP-2). MIP-2 induction is glycosylation dependent, as it is strongly enhanced when sICAM-1 carries sialylated, complex-type N-glycans as synthesized by wild-type Chinese hamster ovary (CHO) cells. The present study was aimed at elucidating the N-glycosylation of mouse sICAM-1 expressed in wild-type CHO cells with regard to sialylation, N-glycan profile, and N-glycosylation sites. Ion-exchange chromatography and matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) of the released N-glycans showed that sICAM-1 mostly carried di- and trisialylated complex-type N-glycans with or without one fucose. In some sialylated N-glycans, one N-acetylneuraminic acid was replaced by N-glycolylneuraminic acid, and ∼4% carried a higher number of sialic acid residues than of antennae. The N-glycosylation sites of mouse sICAM-1 were analyzed by MALDI-Fourier transform ion cyclotron resonance (FTICR)-MS and nanoLC-ESI-FTICR-MS of tryptic digests of mouse sICAM-1 expressed in the Lec1 mutant of CHO cells. All nine consensus sequences for N-glycosylation were found to be glycosylated. These results show that the N-glycans that enhance the MIP-2‐inducing activity of mouse sICAM-1 are mostly di- and trisialylated complex-type N-glycans including a small fraction carrying more sialic acid residues than antennae and that the nine N-glycosylation sites of mouse sICAM-1 are all glycosylated.