A Qualitative Study of the Change-of-Shift Report at the Patients' Bedside.

Concerns about patient bedside change-of-shift reporting at a community hospital in northern Indiana stimulated the development of this qualitative phenomenological study. A review of the literature revealed a research deficit in acute care nurses' perceptions of bedside reporting in relation to compliance. The research question addressed in this study was, "What are acute care nurses' perceptions of the change-of-shift report at the patients' bedside?" Personal interviews were conducted on 7 medical, surgical, and intensive care unit nurse participants at a community hospital in northern Indiana.

A Qualitative Study of the Change-of-Shift Report at the Patients' Bedside.

Concerns about patient bedside change-of-shift reporting at a community hospital in northern Indiana stimulated the development of this qualitative phenomenological study. A review of the literature revealed a research deficit in acute care nurses' perceptions of bedside reporting in relation to compliance. The research question addressed in this study was, "What are acute care nurses' perceptions of the change-of-shift report at the patients' bedside?" Personal interviews were conducted on 7 medical, surgical, and intensive care unit nurse participants at a community hospital in northern Indiana.

Injectable formulations for an intravitreal sustained-release application of a novel single-chain VEGF antibody fragment.

Sustained-release formulations of a single-chain anti-VEGF-A antibody fragment were investigated in vitro toward their potential use for intravitreal applications. The hydrophobic polyester hexylsubstituted poly(lactic acid) (hexPLA) was selected as the sustained-release excipient for its biodegradability and semi-solid aggregate state, allowing an easy and mild formulation procedure. The lyophilized antibody fragment ESBA903 was micronized and incorporated into the liquid polymer matrix by cryo-milling, forming homogeneous and injectable suspensions.

Generic approach for the generation of stable humanized single-chain Fv fragments from rabbit monoclonal antibodies.

Despite their favorable pharmacokinetic properties, single-chain Fv antibody fragments (scFvs) are not commonly used as therapeutics, mainly due to generally low stabilities and poor production yields. In this work, we describe the identification and optimization of a human scFv scaffold, termed FW1.4, which is suitable for humanization and stabilization of a broad variety of rabbit antibody variable domains.

Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.

Asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. The functions of the protein subunits of oligoasccharyltransferase, apart from the catalytic Stt3p, are ill defined. Here we describe functional and structural investigations of the Ost3/6p components of the yeast enzyme.

A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli.

Sulfotransferases are a versatile class of enzymes involved in numerous physiological processes. In mammals, adenosine 3'-phosphate-5'-phosphosulfate (PAPS) is the universal sulfuryl donor, and PAPS-dependent sulfurylation of small molecules, including hormones, sugars, and antibiotics, is a critical step in hepatic detoxification and extracellular signaling. In contrast, little is known about sulfotransferases in bacteria, which make use of sulfurylated molecules as mediators of cell-cell interactions and host-pathogen interactions.

Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB.

Disulfide bond formation is a critical step in the folding of many secretory proteins. In bacteria, disulfide bonds are introduced by the periplasmic dithiol oxidase DsbA, which transfers its catalytic disulfide bond to folding polypeptides. Reduced DsbA is reoxidized by ubiquinone Q8, catalyzed by inner membrane quinone reductase DsbB.

Evidence for proton shuffling in a thioredoxin-like protein during catalysis.

Proteins of the thioredoxin (Trx) superfamily catalyze disulfide-bond formation, reduction and isomerization in substrate proteins both in prokaryotic and in eukaryotic cells. All members of the Trx family with thiol-disulfide oxidoreductase activity contain the characteristic Cys-X-X-Cys motif in their active site. Here, using Poisson-Boltzmann-based protonation-state calculations based on 100-ns molecular dynamics simulations, we investigate the catalytic mechanism of DsbL, the most oxidizing Trx-like protein known to date.

DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli.

Disulfide bond formation in the Escherichia coli periplasm requires the transfer of electrons from substrate proteins to DsbA, which is recycled as an oxidant by the membrane protein DsbB. The highly virulent, uropathogenic E. coli strain CFT073 contains a second, homologous pair of proteins, DsbL and DsbI, which are encoded in a tri-cistronic operon together with a periplasmic, uropathogen-specific arylsulfate sulfotransferase (ASST).

The heat-sensitive Escherichia coli grpE280 phenotype: impaired interaction of GrpE(G122D) with DnaK.

GrpE is the nucleotide-exchange factor of the DnaK chaperone system. Escherichia coli cells with the classical temperature-sensitive grpE280 phenotype do not grow under heat-shock conditions and have been found to carry the G122D point mutation in GrpE. To date, the molecular mechanism of this defect has not been investigated in detail.

Immediate response of the DnaK molecular chaperone system to heat shock.

The familiar heat shock response in cells comprises the enhanced expression of molecular chaperones. In recent experiments with the Hsp70 system of Escherichia coli, the co-chaperone GrpE has been found to undergo a reversible thermal transition in the physiological temperature range. Here, we tested whether this thermal transition is of functional significance in the complete DnaK/DnaJ/GrpE chaperone system.

Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures.

Temperature directly controls functional properties of the DnaK/DnaJ/GrpE chaperone system. The rate of the high to low affinity conversion of DnaK shows a non-Arrhenius temperature dependence and above approximately 40 degrees C even decreases. In the same temperature range, the ADP/ATP exchange factor GrpE undergoes an extensive, fully reversible thermal transition (Grimshaw, J.