Publications by authors named "Jennifer Fournier"

The issue of the respect of intimacy is raised particularly for people with a motor disability who are dependent on others to perform everyday tasks and are forced to live in a medical-social care facility. Their description of their experiences, difficulties and aspirations offers a better understanding of their needs with a view to providing them with a suitable response.

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N-Glycan analysis is routinely performed for biotherapeutic protein characterization. A recently introduced N-glycan analysis kit using RapiFluor-MS (RFMS) labeling provides time savings over reductive amination labeling methods while also providing enhanced fluorescence (FLR) and mass spectrometry (MS) responses. This article demonstrates the semiautomation of this kit using an Andrew Alliance pipetting robot that promises further gains in productivity.

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Advanced access scheduling is a system designed to allow patients to be seen same day or next day or in the future according to their preference. The scheduling system has been associated with patients being seen earlier in the course of illness and patients being hospitalized less often. The advanced access system focuses on timely access to primary healthcare, ideally within 48 hours.

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Identification of phosphopeptides by MS is challenging due to their relatively low abundance in proteomic samples and their limited ionization efficiency. Various affinity enrichment methods have been used in the literature. Titanium dioxide SPE devices have been recently proposed as an alternative to immobilized metal affinity chromatography for phosphopeptide enrichment.

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A mixed-mode chromatographic (MMC) sorbent was prepared by functionalizing the silica sorbent with a pentafluorophenyl (PFP) ligand. The resulting stationary phase provided a reversed-phase (RP) retention mode along with a relatively mild strong cation-exchange (SCX) retention interaction. While the mechanism of interaction is not entirely clear, it is believed that the silanols in the vicinity of the perfluorinated ligand act as strongly acidic sites.

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Glycopeptides are typically prepared by cleaving the proteins with specific proteolytic enzymes, such as trypsin. The resulting glycopeptides tend to have weak mass spectrometry ion signals (ESI or MALDI) due to their relatively large molecular weight. The identification of glycosylation sites with tandem mass spectrometry is further complicated by fragmentation of both the peptide backbone and the glycan moiety.

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