In this paper, we tackle one fundamental problem in Underwater Sensor Networks (UWSNs): robust, scalable and energy efficient routing. UWSNs are significantly different from terrestrial sensor networks in the following aspects: low bandwidth, high latency, node float mobility (resulting in high network dynamics), high error probability, and 3-dimensional space. These new features bring many challenges to the network protocol design of UWSNs. In this paper, we propose a novel routing protocol, called vector-based forwarding (VBF), aiming to provide robust, scalable and energy efficient routing. VBF is essentially a location-based routing approach. No state information is required on the sensor nodes and only a small fraction of the nodes are involved in routing. Moreover, packets are forwarded in redundant and interleaved paths, which add robustness to VBF. Further, we develop a localized and distributed self-adaptation algorithm, which helps to enhance the performance of VBF. The self-adaptation algorithm allows the nodes to weigh the benefit to forward packets and reduce energy consumption by discarding the low benefit packets. We evaluate the performance of VBF through extensive simulations. Our experiment results show that for networks with small or medium node mobility (1 m/s-3 m/s), VBF can effectively accomplish the goals of robustness, energy efficiency, and high success of data delivery.
Our findings demonstrated that LncRNA SNHG4 promoted tumour growth by sponging miR-224-3p and represented a poor prognostic factor in patients with osteosarcoma.
Cullins, critical members of the cullin-RING ubiquitin ligases (CRLs), are often aberrantly expressed in different cancers. However, the underlying mechanisms regarding aberrant expression of these cullins and the specific substrates of CRLs in different cancers are mostly unknown. Here, we demonstrate that overexpressed CUL4B in human osteosarcoma cells forms an E3 complex with DNA damage binding protein 1 (DDB1) and DDB1- and CUL4-associated factor 13 (DCAF13). In vitro and in vivo analyses indicated that the CRL4BDCAF13 E3 ligase specifically recognized the tumor suppressor PTEN (phosphatase and tensin homolog deleted on chromosome 10) for degradation, and disruption of this E3 ligase resulted in PTEN accumulation. Further analyses indicated that miR-300 directly targeted the 3′ UTR of CUL4B, and DNA hypermethylation of a CpG island in the miR-300 promoter region contributed to the downregulation of miR-300. Interestingly, ectopic expression of miR-300 or treatment with 5-AZA-2′-deoxycytidine, a DNA methylation inhibitor, decreased the stability of CRL4BDCAF13 E3 ligase and reduced PTEN ubiquitination. By applying in vitro screening to identify small molecules that specifically inhibit CUL4B-DDB1 interaction, we found that TSC01131 could greatly inhibit osteosarcoma cell growth and could disrupt the stability of the CRL4BDCAF13 E3 ligase. Collectively, our findings shed new light on the molecular mechanism of CUL4B function and might also provide a new avenue for osteosarcoma therapy.
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