118 research outputs found
Hydrologic and hydraulic report for Palo Verde Ranch
No full textabstract: This report was prepared to document surface water hydrology and floodplain conditions in accordance with current standards of practice. This information is intended to support issuance of building permits, re-approval of construction drawings to current standards, and issuance of floodplain use permits, if needed.Special study (Pima County Regional Flood Control District (Ariz.)) ; 3
Scatter plots and Bland-Altman plots comparing the reference CD4 counts versus Pima CD4.
No full textScatter and Bland-Altman plots for capillary blood directly applied to CD4 cartridges, Pima-D (1A and 1B), capillary blood collected in EDTA microtube, Pima-M (2A and 2B), venous blood,Pima-V (3A and 3B), or venous blood tested with the Pima at the reference laboratory, Pima-Lab (4A and 4B) with reference CD4 assay being BD Multitest reagent and BD Trucount Tubes using a BD FACSCalibur.</p
Scatter plots of FACSCalibur Vs PIMA measurements.
No full text<p>Scatter plots of FACSCalibur Vs PIMA measurements.</p
Bias results of PIMA Venous versus FACSCalibur measurements.
No full text<p>Bias results of PIMA Venous versus FACSCalibur measurements.</p
Cost-benefit analysis of Pima County's drug treatment alternative to prison program
Get PDFabstract: The Drug Treatment Alternative to Prison (DTAP) Program enables drug addicted criminal defendants to plead guilty to an offense and then enter a residential, therapeutic community treatment system for three years as an alternative to a prison sentence. The Program begins with three months of in-patient, residential drug treatment followed by wraparound recovery support services managed by a resources specialist, including transitional housing, literacy services, higher education, job training and placement services, and counseling, accompanied by drug testing, probation monitoring and regular court hearings.Report for 2013 is cumulative for the first two years
Bias results of PIMA Venous versus FACSCalibur measurements.
No full text<p>Bias results of PIMA Venous versus FACSCalibur measurements.</p
Bland-Altman plots comparing FACSCalibur and PIMA venous measurements.
No full text<p>Bland-Altman plots comparing FACSCalibur and PIMA venous measurements.</p
Real-time quantitative PCR analysis of the annexin genes in Pima-90 and XU142 fl.
No full text<p>Expression analysis of annexin genes in <i>G. barbadense</i> (Pima-90) vegetative tissues (R: roots; S: stems; L: leaves), reproductive tissues (C: carpels; −3: ovules in –3 DPA; 0: ovules in 0 DPA; 3: ovules in +3 DPA) and its allele gene expression in <i>G. hirsutum</i> fuzzless-lintless mutant (XU142 fl) reproductive tissues (M −3; ovules in –3 DPA; M0: ovules in 0 DPA; M3: ovules in +3 DPA). The comparative C<sub>T</sub> method was adopted and the expression was normalized to the levels of Pima-90 and XU142 fl. Error bars represent standard errors.</p
Substrate-induced conformational changes in the essential peripheral membrane-associated mannosyltransferase PimA from mycobacteria: implications for catalysis.
No full textInternational audiencePhosphatidyl-myo-inositol mannosyltransferase A (PimA) is an essential glycosyltransferase (GT) involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs), which are key components of the mycobacterial cell envelope. PimA is the paradigm of a large family of peripheral membrane-binding GTs for which the molecular mechanism of substrate/membrane recognition and catalysis is still unknown. Strong evidence is provided showing that PimA undergoes significant conformational changes upon substrate binding. Specifically, the binding of the donor GDP-Man triggered an important interdomain rearrangement that stabilized the enzyme and generated the binding site for the acceptor substrate, phosphatidyl-myo-inositol (PI). The interaction of PimA with the beta-phosphate of GDP-Man was essential for this conformational change to occur. In contrast, binding of PI had the opposite effect, inducing the formation of a more relaxed complex with PimA. Interestingly, GDP-Man stabilized and PI destabilized PimA by a similar enthalpic amount, suggesting that they formed or disrupted an equivalent number of interactions within the PimA complexes. Furthermore, molecular docking and site-directed mutagenesis experiments provided novel insights into the architecture of the myo-inositol 1-phosphate binding site and the involvement of an essential amphiphatic alpha-helix in membrane binding. Altogether, our experimental data support a model wherein the flexibility and conformational transitions confer the adaptability of PimA to the donor and acceptor substrates, which seems to be of importance during catalysis. The proposed mechanism has implications for the comprehension of the peripheral membrane-binding GTs at the molecular level
Molecular Recognition and Interfacial Catalysis by the Essential Phosphatidylinositol Mannosyltransferase PimA from Mycobacteria
No full textInternational audienceMycobacterial phosphatidylinositol mannosides (PIMs) and metabolically derived cell wall lipoglycans play important roles in host-pathogen interactions, but their biosynthetic pathways are poorly understood. Here we focus on Mycobacterium smeg-matis PimA, an essential enzyme responsible for the initial man-nosylation of phosphatidylinositol. The structure of PimA in complex with GDP-mannose shows the two-domain organization and the catalytic machinery typical of GT-B glycosyltrans-ferases. PimA is an amphitrophic enzyme that binds mono-disperse phosphatidylinositol, but its transferase activity is stimulated by high concentrations of non-substrate anionic sur-factants, indicating that the early stages of PIM biosynthesis involve lipid-water interfacial catalysis. Based on structural, cal-orimetric, and mutagenesis studies, we propose a model wherein PimA attaches to the membrane through its N-terminal domain, and this association leads to enzyme activation. Our results reveal a novel mode of phosphatidylinositol recognition and provide a template for the development of potential anti-mycobacterial compounds
- …
