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1.
Sensors (Basel) ; 24(8)2024 Apr 17.
Article in English | MEDLINE | ID: mdl-38676188

ABSTRACT

With the proliferation of electronic devices and electricity-based mobility solutions, the significance of wireless power transfer technology has increased substantially. However, ensuring secure and reliable power transmission to authorized users remains a significant challenge. Addressing this complex issue requires an integrated approach that balances efficiency, stability, and security considerations. While current efforts primarily focus on improving charging efficiency and user convenience, integrating robust security measures into wireless charging infrastructure is challenging due to its inherently open nature and susceptibility to external interference. Technical advancements are required to strengthen the security of the wireless charging infrastructure; however, these should be balanced with power loss management. This study tackles two core issues: the increasing hardware requirements for billing system authentication protocols and the interception of wireless charging signals by unauthorized users, leading to power theft and subsequent losses. To address these challenges, we propose a mechanism termed "LazyFrog". This mechanism dynamically adjusts the frequency hopping schedule, activating frequency changes only in response to detected threats during remote charging or upon identifying unauthorized access attempts. The proposed mechanism compares the expected power reception at the device with the actual power supplied by the charging station, enabling the detection of abnormal power losses. By minimizing unnecessary frequency changes and optimizing energy consumption, LazyFrog reduces hardware requirements. Moreover, we have implemented a relative distance estimation mechanism to facilitate efficient power transfer as wireless devices move within the charging environment. With these features, LazyFrog demonstrates a secure, flexible, and energy-efficient wireless charging system ready for practical application.

2.
Parasitol Res ; 106(3): 627-35, 2010 Feb.
Article in English | MEDLINE | ID: mdl-20076970

ABSTRACT

Spirometra erinacei is a pseudophyllidean tapeworm which inhabits the intestines of cats and dogs. The infections are usually asymptomatic in these animals, but the infection of the plerocercoid larvae of the parasite, spargana, cause sparganosis in other vertebrates, including human. In this study, we identified a gene encoding the copper/zinc-superoxide dismutase of S. erinacei (SeCuZn-SOD) and partially characterized the biochemical and functional properties of the enzyme. The open reading frame of SeCuZnSOD was 465 bp that encodes 154 amino acids. The characteristic amino acid residues and motifs required for coordinating copper and zinc enzymatic function were well conserved. The genomic length of the SeCuZnSOD was 1,985 bp consisting of three exons that are separated by two introns. SeCuZnSOD is a typical cytosolic form which shares similar biochemical properties, including broad pH optima and inhibition profile by KCN and H(2)O(2), with cytosolic Cu/Zn-SODs of other organisms. SeCuZnSOD was functionally expressed in both S. erinacei plerocercoid larvae and adult worms, and its expression level was significantly increased when the plerocercoid larvae were treated with paraquat. The enzyme may play essential roles for survival of the parasite not only by protecting itself from endogenous oxidative stress, but also by detoxifying oxidative killing of the parasite by host immune effector cells.


Subject(s)
Spirometra/enzymology , Superoxide Dismutase/genetics , Superoxide Dismutase/metabolism , Animals , Binding Sites , Conserved Sequence , DNA, Helminth/chemistry , DNA, Helminth/genetics , Dogs , Enzyme Inhibitors/pharmacology , Enzyme Stability , Exons , Gene Expression Profiling , Hydrogen Peroxide/pharmacology , Hydrogen-Ion Concentration , Introns , Molecular Sequence Data , Open Reading Frames , Potassium Cyanide/pharmacology , Sequence Analysis, DNA , Snakes , Spirometra/isolation & purification , Superoxide Dismutase/chemistry
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