188 research outputs found

    From Dumb Wireless Sensors to Smart Networks using Network Coding

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    The vision of wireless sensor networks is one of a smart collection of tiny, dumb devices. These motes may be individually cheap, unintelligent, imprecise, and unreliable. Yet they are able to derive strength from numbers, rendering the whole to be strong, reliable and robust. Our approach is to adopt a distributed and randomized mindset and rely on in network processing and network coding. Our general abstraction is that nodes should act only locally and independently, and the desired global behavior should arise as a collective property of the network. We summarize our work and present how these ideas can be applied for communication and storage in sensor networks.Comment: To be presented at the Inaugural Workshop of the Center for Information Theory and Its Applications, University of California - San Diego, La Jolla, CA, February 6 - 10, 200

    NEW STABILITY INDICATING METHOD DEVELOPMENT AND VALIDATION OF CAPECITABINE AND DOCETAXEL IN BULK AND PHARMACEUTICAL DOSAGE FORM BY USING RP-HPLC

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    Objective: The current investigation was pointed at developing and progressively validating novel, simple, responsive and stable RP-HPLC method for the measurement of active pharmaceutical ingredients of Capecitabine and Docetaxel. Methods: A simple, selective, validated and well-defined stability that shows gradient RP-HPLC methodology for the quantitative determination of Capecitabine and Docetaxel. The chromatographic strategy utilized Inertsil ODS column of dimensions 250x4.6 mm, 5 micron, using isocratic elution with a mobile phase of acetonitrile and water (50:50). A flow rate of 1 ml/min and a detector wavelength of 220 nm utilizing the PDA detector were given in the instrumental settings. Using the impurity-spiked solution, the chromatographic approach was streamlined. Validation of the proposed method was carried out according to an international conference on harmonization (ICH) guidelines. Results: LOD and LOQ for the two active ingredients and their impurities were established with respect to test concentration. The calibration charts plotted were linear with a regression coefficient of R2>0.999, means the linearity was within the limit. Recovery, specificity, linearity, accuracy, robustness, ruggedness were determined as a part of method validation and the results were found to be within the acceptable range. Conclusion: The proposed method to be fast, simple, feasible and affordable in assay condition. During stability tests, it can be used for routine analysis of production samples and to verify the quality of drug samples during stability studies

    STABILITY INDICATIVE AND COST EFFECTIVE ANALYTICAL METHOD DEVELOPMENT AND VALIDATION OF FENOFIBRIC ACID AND PITAVASTATIN BY USING RP-HPLC

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    Objective: The current investigation was pointed at developing and progressively validating novel, simple, responsive and stable RP-HPLC method for the measurement of active pharmaceutical ingredients of Fenofibric acid and Pitavastatin. Methods: A simple, selective, validated and well-defined stability that shows gradient RP-HPLC methodology for the quantitative determination of Fenofibric acid and Pitavastatin. The chromatographic strategy utilized X-bridge phenyl column of dimensions 250x4.6 mm, 5 micron, using isocratic elution with a mobile phase of acetonitrile and 0.1 percent formic acid (60:40). A flow rate of 1 ml/min and a detector wavelength of 242 nm utilizing the PDA detector were given in the instrumental settings. Results: Validation of the proposed method was carried out according to an international conference on harmonization (ICH) guidelines. LOD and LOQ for the two active ingredients were established with respect to test concentration. The calibration charts plotted were linear with a regression coefficient of R2 > 0.999, means the linearity was within the limit. Recovery, specificity, linearity, accuracy, robustness, ruggedness were determined as a part of method validation and the results were found to be within the acceptable range. Conclusion: The proposed method to be fast, simple, feasible and affordable in assay condition. During stability tests, it can be used for routine analysis of the selected drugs

    Structure Related to Morphine

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    Synthesis of 2-N-heptyl-5,9-dimethyl-6,7-benzomorphan from 3,4-lutidine was effected in three step process and only a-form could be obtained through phosphoric acid cyclisation. This a-form of benzomorphan was converted in three steps to a-2N-hepthyl-2-hydroxy-5,9-dimethyl-6,7-benzomorphan, which was also synthesised from alternative route. Infrared spectrum of the base confirmed the presence of a-from

    Critical Role of the Secondary Binding Pocket in Modulating the Enzymatic Activity of DUSP5 toward Phosphorylated ERKs

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    DUSP5 is an inducible nuclear dual-specificity phosphatase that specifically interacts with and deactivates extracellular signal-regulated kinases ERK1 and ERK2, which are responsible for cell proliferation, differentiation, and survival. The phosphatase domain (PD) of DUSP5 has unique structural features absent from other nuclear DUSPs, such as the presence of a secondary anion-binding site in the proximity of the reaction center and a glutamic acid E264 positioned next to the catalytic cysteine C263, as well as a remote intramolecular disulfide linkage. The overall 400 ns molecular dynamics simulations indicate that the secondary binding site of DUSP5 PD acts as an allosteric regulator of the phosphatase activity of DUSP5. Our studies have identified E264 as a critical constituent of the dual binding pocket, which regulates the catalytic activity of DUSP5 by forming a salt bridge with arginine R269. Molecular dynamics studies showed that initial occupation of the secondary binding pocket leads to the breakage of the salt bridge, which then allows the occupation of the active site. Indeed, biochemical analysis using the pERK assay on mutant E264Q demonstrated that mutation of glutamic acid E264 leads to an increase in the DUSP5 catalytic activity. The role of the secondary binding site in assembling the DUSP5–pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197–C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5
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