60 research outputs found

    Thermal Expansion Anomaly in TTB Ferroelectrics: The Interplay between Framework Structure and Electric Polarization

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    Tetragonal tungsten bronze (TTB) makes up a large family of functional materials with fascinating dielectric, piezoelectric, or ferroelectric properties. Understanding the thermal expansion mechanisms associated with their physical properties is important for their practical applications as well as theoretical investigations. Fortunately, the appearance of anomalous thermal expansion in functional materials offers a chance to capture the physics behind them. Herein, we report an investigation of the thermal expansion anomalies in TTBs that are related to ferroelectric transitions and summarize recent progress in this field. The special role of Pb<sup>2+</sup> cation is elucidated. The interplay between the thermal expansion anomaly, electric polarization, and framework structure provides new insight into the structure–property relationships in functional materials

    Effects and Safety of Calcimimetics in End Stage Renal Disease Patients with Secondary Hyperparathyroidism: A Meta-Analysis

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    <div><h3>Purpose</h3><p>Secondary hyperparathyroidism (SHPT) is one of the most common abnormalities of mineral metabolism in patients with chronic kidney disease. We performed a meta-analysis to determine the effect and safety of cinacalcet in SHPT patients receiving dialysis.</p> <h3>Methods</h3><p>The meta-analysis was performed to determine the effect and safety of cinacalcet in SHPT patients receiving dialysis by using the search terms ‘cinacalcet’ or ‘mimpara’ or ‘sensipar’ or ‘calcimimetic’ or ‘R586’ on MEDLINE and EMBASE (January 1990 to February 2012).</p> <h3>Results</h3><p>Fifteen trials were included, all of which were performed between 2000 and 2011 enrolling a total of 3387 dialysis patients. Our study showed that calcimimetic agents effectively ameliorated iPTH levels(WMD, −294.36 pg/mL; 95% CI, −322.76 to −265.95, <em>P</em><0.001) in SHPT patients and reduced serum calcium (WMD, −0.81 mg/dL; 95% CI, −0.89 to −0.72, <em>P</em><0.001) and phosphorus disturbances(WMD, −0.29 mg/dL; 95% CI, −0.41 to −0.17, <em>P</em><0.001). The percentage of patients in whom there was a 30% decrease in serum iPTH levels by the end of the dosing was higher in cinacalcet group than that in control group(OR = 10.75, 95% CI: 6.65–17.37, <em>P</em><0.001). However, no significant difference was found in all-cause mortality and all adverse events between calcimimetics and control groups(OR = 0.86, 95% CI: 0.46–1.60, <em>P</em> = 0.630; OR = 1.30, 95% CI: 0.78–2.18, <em>P</em> = 0.320, respectively). Compared with the control therapy, there was a significant increase in the episodes of hypocalcemia (OR = 2.46, 95% CI: 1.58–3.82, <em>P</em><0.001), nausea (OR = 2.45, 95% CI: 1.29–4.66, <em>P</em> = 0.006), vomiting(OR = 2.78, 95% CI: 2.14–3.62, <em>P</em><0.001), diarrhea(OR = 1.51, 95% CI: 1.04–2.20, <em>P</em> = 0.030) and upper respiratory tract infection (OR = 1.79, 95% CI: 1.20–2.66, <em>P</em> = 0.004)in calcimimetics group.</p> <h3>Conclusions</h3><p>Calcimimetic treatment effectively improved biochemical parameters of SHPT patients receiving dialysis without increasing all-cause mortality and all adverse events.</p> </div

    Forest plot of iPTH of patients treated with calcimimetics and control therapy.

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    <p>Studies are identified by name of the first author and year of publication. Mean differences (MDs) are pooled using the fixed-effect model and shown on a scale of −500 to 500.</p

    Forest plot of serum calcium of patients treated with calcimimetics and control therapy.

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    <p>Studies are identified by name of the first author and year of publication. Mean differences (MDs) are pooled using the fixed-effect model and shown on a scale of −2 to 2.</p

    Characteristics of Trials of Calcimimetic Agents for SHPT in Dialysis Patients.

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    <p>Abbreviations: SHPT, secondary hyperparathyroidism; iPTH, intact PTH; HD, hemodialysis; Cin, Cinacalcet; Vit, Vitamin; d, day; w, week; mo, month;</p

    Forest plot of serum phosphate of patients treated with calcimimetics and control therapy.

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    <p>Studies are identified by name of the first author and year of publication. Mean differences (MDs) are pooled using the fixed-effect model and shown on a scale of −2 to 2.</p

    Legislative Documents

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    Also, variously referred to as: House bills; House documents; House legislative documents; legislative documents; General Court documents

    Image_10_Subunit Interaction Differences Between the Replication Factor C Complexes in Arabidopsis and Rice.JPEG

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    <p>Replication factor C (RFC) is a multisubunit complex that opens the sliding clamp and loads it onto the DNA chain in an ATP-dependent manner and is thus critical for high-speed DNA synthesis. In yeast (Saccharomyces cerevisiae) and humans, biochemical studies and structural analysis revealed interaction patterns between the subunits and architectures of the clamp loaders. Mutations of ScRFC1/2/3/4/5 lead to loss of cell viability and defective replication. However, the functions of RFC subunits in higher plants are unclear, except for AtRFC1/3/4, and the interaction and arrangement of the subunits have not been studied. Here, we identified rfc2-1/+, rfc3-2/+, and rfc5-1/+ mutants in Arabidopsis, and found that embryos and endosperm arrested at the 2/4-celled embryo proper stage and 6-8 nuclei stages, respectively. Subcellular localization analysis revealed that AtRFC1 and OsRFC1/4/5 proteins were localized in the nucleus, while AtRFC2/3/4/5 and OsRFC2/3 proteins were present both in the nucleus and cytoplasm. By using yeast two-hybrid (Y2H) and bimolecular fluorescence complementation (BiFC) techniques, we demonstrated the interactions of Arabidopsis and rice (Oryza sativa) RFC subunits, and proposed arrangements of the five subunits within the RFC complex, which were AtRFC5-AtRFC4-AtRFC3/2-AtRFC2/3-AtRFC1 and OsRFC5-OsRFC2-OsRFC3-OsRFC4-OsRFC1, respectively. In addition, AtRFC1 could interact with AtRFC2/3/4/5 in the presence of other subunits, while OsRFC1 directly interacted with the other four subunits. To further characterize the regions required for complex formation, truncated RFC proteins of the subunits were created. The results showed that C-termini of the RFC subunits are required for complex formation. Our studies indicate that the localization and interactions of RFCs in Arabidopsis and rice are distinctly discrepant.</p
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