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Selected AbstractsA modified Mini Nutritional Assessment without BMI can effectively assess the nutritional status of neuropsychiatric patientsJOURNAL OF CLINICAL NURSING, Issue 13 2009Alan C Tsai Aim and objectives., To determine whether a modified version of the Mini Nutritional Assessment (MNA) without body mass index (BMI) can effectively identify individuals at risk of malnutrition among patients with neuropsychiatric disorders. Background., Neuropsychiatric patients have an additional risk of nutritional disorder due to functional impairments and drug effects. However, their nutritional status is generally neglected. It is important to find a tool that is simple, easy to use and non-invasive. Design., The study involved 105 patients in the acute phase of confirmed neuropsychiatric disorders in an area hospital. All subjects were cognitively able to have effective verbal communication. Method., The study included serum biochemical and anthropometric measurements and an on-site, in-person interview using a structured questionnaire to elicit personal data, health condition and answers to questions in the MNA. Subjects' nutritional statuses were graded with a MNA that adopted population-specific anthropometric cut-off points or one further with the BMI question removed and its assigned score redistributed to other anthropometric questions. Results., Both versions of the modified MNA effectively graded the nutritional status of neuropsychiatric patients and showed good correlations with the major nutritional indicators such as BMI, calf circumference and the length of hospital stay. Conclusions., The MNA can effectively assess the nutritional status of neuropsychiatric patients and enhance timely detection and intervention of their nutritional disorders. A modified MNA without the BMI question can maintain the full functionality of the tool. The version does not require weight and height measurements and thus will enhance the usefulness of the instrument. Relevance to clinical practice., Neuropsychiatric patients are a high-risk group of nutritional disorders. The MNA, especially the one without BMI, has the potential to improve professional efficiency of the primary care workers. [source] Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ringMOLECULAR MICROBIOLOGY, Issue 6 2007Daisuke Shiomi Summary In bacteria, the actin-like FtsA protein interacts with the tubulin-like FtsZ protein, helping to assemble the cytokinetic Z ring, anchor it to the cytoplasmic membrane and recruit other essential divisome proteins. FtsA also interacts with itself, but it is not clear whether this self-interaction is required for its full functionality. Here we describe new dominant negative missense mutations in Escherichia coli ftsA that specifically inhibit FtsA homodimerization and simultaneously cause disruption of Z rings. The negative effects of one mutation, M71A, were suppressed by altering levels of certain division proteins or by additional mutations in ftsA that promote increased integrity of the Z ring. Remarkably, when FtsA, FtsA-M71A, and other mutants of FtsA that compromise self-interaction were connected in a tandem repeat, they were at least partially functional and suppressed defects of an ftsZ84(ts) mutation. This gain of function by FtsA tandems further suggested that FtsA monomers cause deleterious interactions with FtsZ and that increased dimerization or oligomerization of FtsA enhances its ability to promote Z-ring integrity. Therefore, we propose that FtsZ assembly is regulated by the extent of FtsA oligomerization. [source] The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twistACTA CRYSTALLOGRAPHICA SECTION D, Issue 5 2009Kevin P. Madauss Inhibition of acetyl-CoA carboxylase (ACC) may prevent lipid-induced insulin resistance and type 2 diabetes, making the enzyme an attractive pharmaceutical target. Although the enzyme is highly conserved amongst animals, only the yeast enzyme structure is available for rational drug design. The use of biophysical assays has permitted the identification of a specific C-terminal truncation of the 826-residue human ACC2 carboxyl transferase (CT) domain that is both functionally competent to bind inhibitors and crystallizes in their presence. This C-terminal truncation led to the determination of the human ACC2 CT domain,CP-640186 complex crystal structure, which revealed distinctions from the yeast-enzyme complex. The human ACC2 CT-domain C-terminus is comprised of three intertwined ,-helices that extend outwards from the enzyme on the opposite side to the ligand-binding site. Differences in the observed inhibitor conformation between the yeast and human structures are caused by differing residues in the binding pocket. [source] Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation, and protects against proteolytic degradationBIOTECHNOLOGY & BIOENGINEERING, Issue 5 2001Mathieu Nasseau Abstract How can enzymes be protected against denaturation and proteolysis while keeping them in a fully functional state? One solution is to encapsulate the enzymes into liposomes, which enhances their stability against denaturation and proteases. However, the permeability barrier of the lipid membrane drastically reduces the activity of enzyme entrapped in the liposome by reducing the internal concentration of the substrate. To overcome this problem, we permeabilized the wall of the liposome by reconstitution of a porin from Escherichia coli. In this way, we recovered the full functionality of the enzyme while retaining the protection against denaturation and proteolytic enzymes. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 75: 615,618, 2001. [source] | ||||||||||