A Systematic Review of the Use of the Palliative Care Outcome Scale and the Support Team Assessment Schedule in Palliative Care.

Context: The Palliative care Outcome Scale (POS) and the Support Team Assessment Schedule (STAS) are two outcome measures used in palliative care settings to assess palliative concerns, needs, and quality of care.

Objectives: This systematic review builds on the findings of a previous review to appraise the use of the POS and STAS since 2010, particularly the context and nature of their use.

Methods: MEDLINE, Embase, PsycINFO, British Nursing Index, and CINAHL were searched for studies published between February 2010 and June 2014.

Glycosylation status of serum in inflammatory arthritis in response to anti-TNF treatment.

Objective: Glycosylation is the most common post-translational modification and is altered in disease. The typical glycosylation change in patients with inflammatory arthritis (IA) is a decrease in galactosylation levels on IgG. The aim of this study is to evaluate the effect of anti-TNF therapy on whole serum glycosylation from IA patients and determine whether these alterations in the glycome change upon treatment of the disease.

New insight into the functions of the interleukin-17 receptor adaptor protein Act1 in psoriatic arthritis.

Recent genome-wide association studies have implicated the tumor necrosis factor receptor-associated factor 3-interacting protein 2 (TRAF3IP2) gene and its product, nuclear factor-kappa-B activator 1 (Act1), in the development of psoriatic arthritis (PsA). The high level of sequence homology of the TRAF3IP2 (Act1) gene across the animal kingdom and the presence of the Act1 protein in multiple cell types strongly suggest that the protein is of importance in normal cellular function. Act1 is an adaptor protein for the interleukin-17 (IL-17) receptor, and recent observations have highlighted the significance of IL-17 signaling and localized inflammation in autoimmune diseases.

Engineering coordination assemblies of dinuclear CuII complexes.

Hybrid organic-inorganic coordination assemblies are synthesized using modified aminocarboxylic acid ligands as the structure-directing agents. The synthetic approach results in two novel dinuclear copper(II) complexes, K2[CuII(hnida)]2.2H2O (1) and K4[CuII(chnida)]2.

The 1st European Summer School on 'proteomic basics'--the students view. 12-18 August, 2007 Kloster Neustift, Brixen/Bressanone, South Tyrol, Italy.

Fifty postgraduate and postdoctoral delegates from all over Europe attended the week-long '1st European Summer School on Proteomic Basics' in Kloster Neustift in the Italian South Tyrol in August 2007. Invited proteomics experts gave tutorial lectures on Proteomics techniques with an emphasis on sample preparation, protein separation and purification in the first of an annual series of Proteomics Summer Schools funded by the EU and the Volkswagen Stiftung.

Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR.

This report describes NMR-spectroscopic investigations of the conformational dynamics of disulfide bonds in hen-egg-white lysozyme substitution mutants. The following four systems have been investigated: 2SS(alpha), a lysozyme variant that contains C64A, C76A, C80A and C94A substitutions, was studied in water at pH 2 and 3.8 and in urea (8 M, pH 2); 2SS(beta) lysozyme, which has C6S, C30A, C115A and C127A substitutions, was studied in water (pH 2) and urea (8 M, pH 2).

Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9.

The 61 kDa colicin E9 protein toxin enters the cytoplasm of susceptible cells by interacting with outer membrane and periplasmic helper proteins, and kills them by hydrolysing their DNA. The membrane translocation function is located in the N-terminal domain of the colicin, with a key signal sequence being a pentapeptide region that governs the interaction with the helper protein TolB (the TolB box). Previous NMR studies (Collins et al.

Structural dynamics of the receptor-binding domain of colicin E9.

Colicin E9 is a 61 kDa antibacterial protein secreted by E. coli. In order for it to enter the cytoplasm of susceptible bacteria and kill them by hydrolysing their DNA, the colicin must first interact with an outer membrane receptor on the target cell, BtuB, and a translocation pathway involving Tol proteins.

Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB.

In order for the 61 kDa colicin E9 protein toxin to enter the cytoplasm of susceptible cells and kill them by hydrolysing their DNA, the colicin must interact with the outer membrane BtuB receptor and Tol translocation pathway of target cells. The translocation function is located in the N-terminal domain of the colicin molecule. (1)H, (1)H-(1)H-(15)N and (1)H-(13)C-(15)N NMR studies of intact colicin E9, its DNase domain, minimal receptor-binding domain and two N-terminal constructs containing the translocation domain showed that the region of the translocation domain that governs the interaction of colicin E9 with TolB is largely unstructured and highly flexible.