• Title/Summary/Keyword: DARP

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Hop-by-Hop Dynamic Addressing Based Routing Protocol for Monitoring of long range Underwater Pipeline

  • Abbas, Muhammad Zahid;Bakar, Kamalrulnizam Abu;Ayaz, Muhammad;Mohamed, Mohammad Hafiz;Tariq, Moeenuddin
    • KSII Transactions on Internet and Information Systems (TIIS)
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    • v.11 no.2
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    • pp.731-763
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    • 2017
  • In Underwater Linear Sensor Networks (UW-LSN) routing process, nodes without proper address make it difficult to determine relative sensor details specially the position of the node. In addition, it effects to determine the exact leakage position with minimized delay for long range underwater pipeline monitoring. Several studies have been made to overcome the mentioned issues. However, little attention has been given to minimize communication delay using dynamic addressing schemes. This paper presents the novel solution called Hop-by-Hop Dynamic Addressing based Routing Protocol for Pipeline Monitoring (H2-DARP-PM) to deal with nodes addressing and communication delay. H2-DARP-PM assigns a dynamic hop address to every participating node in an efficient manner. Dynamic addressing mechanism employed by H2-DARP-PM differentiates the heterogeneous types of sensor nodes thereby helping to control the traffic flows between the nodes. The proposed dynamic addressing mechanism provides support in the selection of an appropriate next hop neighbour. Simulation results and analytical model illustrate that H2-DARP-PM addressing support distribution of topology into different ranges of heterogeneous sensors and sinks to mitigate the higher delay issue. One of the distinguishing characteristics of H2-DARP-PM has the capability to operate with a fewer number of sensor nodes deployed for long-range underwater pipeline monitoring.

Structural and Biochemical Characterization of the Two Drosophila Low Molecular Weight-Protein Tyrosine Phosphatases DARP and Primo-1

  • Lee, Hye Seon;Mo, Yeajin;Shin, Ho-Chul;Kim, Seung Jun;Ku, Bonsu
    • Molecules and Cells
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    • v.43 no.12
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    • pp.1035-1045
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    • 2020
  • The Drosophila genome contains four low molecular weight-protein tyrosine phosphatase (LMW-PTP) members: Primo-1, Primo-2, CG14297, and CG31469. The lack of intensive biochemical analysis has limited our understanding of these proteins. Primo-1 and CG31469 were previously classified as pseudophosphatases, but CG31469 was also suggested to be a putative protein arginine phosphatase. Herein, we present the crystal structures of CG31469 and Primo-1, which are the first Drosophila LMW-PTP structures. Structural analysis showed that the two proteins adopt the typical LMW-PTP fold and have a canonically arranged P-loop. Intriguingly, while Primo-1 is presumed to be a canonical LMW-PTP, CG31469 is unique as it contains a threonine residue at the fifth position of the P-loop motif instead of highly conserved isoleucine and a characteristically narrow active site pocket, which should facilitate the accommodation of phosphoarginine. Subsequent biochemical analysis revealed that Primo-1 and CG31469 are enzymatically active on phosphotyrosine and phosphoarginine, respectively, refuting their classification as pseudophosphatases. Collectively, we provide structural and biochemical data on two Drosophila proteins: Primo-1, the canonical LMW-PTP protein, and CG31469, the first investigated eukaryotic protein arginine phosphatase. We named CG31469 as DARP, which stands for Drosophila ARginine Phosphatase.

Anti-cancer Effects of Samultang-Gami on HeLa, HepG2, AGS Cells (사물탕가미방(四物湯加味方)의 항암효과에 대한 실험적 연구)

  • Jung, Jae-Joong;Goo, Sun-Young;Goo, Sun-Young;Sung, Jung-Suk;Kim, Dong-Il
    • The Journal of Korean Obstetrics and Gynecology
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    • v.23 no.3
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    • pp.38-55
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    • 2010
  • Purpose: This study was designed to find out the anti-cancer effects of Samultang-Gami which was composed of Rehmanniae Radix(RR), Angelicae Gigantis Radix(AGR), Cnidii Rhizoma(CR), Paeoniae Radix(PR), Cortex Moutan Radicis(CMR), Hedyotis Diffusa(HD) and Caesalpinia Sappan on HeLa, HepG2 and AGS cells. Methods: Various cancer cell lines including HeLa, HepG2 and AGS cells, were used. In vitro anti-cancer effects were measured by MTT assay using cancer cell lines treated with various concentrations of 70% ethanol extract of Samultang-Gami. Expression of cell cycle arrest mediators including Bax, Bcl-2, p53 and DARP-1 proteins were measured by Western blot analysis. Results: 1. Samultang-Gami decreased the viability of HeLa and HepG cells in a dosedependent manner. 2. AGR, CMR, PR and HD decreased the viability of HeLa, HepG2 and AGS cells. 3. We could observe that the decreased Bax and Bcl-2 expression level and the increased PARP-1 expression level by Samultang-Gami extracts treated in HeLa cells. 4. We could observe that the decreased Bcl-2 expression level and the increased Bax, p53 and PARP-1 expression level by RR extracts treated in HeLa cells. and also could observe that the reduction of the protein level of Bcl-2, p53 and PARP-1 and the increase of the protein level of Bax by PR in HeLa cells. 5. We could observe that the increased p53 expression level, the decreased PARP-1's that and the unchanged Bax and Bcl-2's that by Samultang-Gami extracts treated in HepG2 cells. 6. We could observe that the reduced Bcl-2 expression level by each of RR extracts and PR extracts in HepG2 cells. 7. The treatment of Samultang-Gami in AGS cells didn't have any effect on the expression level of Bax, Bcl-2, p53 and PARP-1. 8. We could observe that the increased p53 and PARP-1 expression level by each of CR, RR and PR extracts in AGS cells. Conclusion: Taken together, we suggest that Samultang-Gami exhibits cytotoxic effects on HeLa, HepG2 and AGS cells, causing apoptosis. The results showed that Samultang-Gami may do so by regulating the expression of specific target molecules that promote efficient apoptotic cell death in a dose-dependent manner.