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- 검색키워드
- 저자 : Plavec, Janez (검색결과 3 건)
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Eduard Plavec,Miroslav Petrini?,Mladen Vidovi? 한국전자파학회JEES 2021 Journal of Electromagnetic Engineering and Science Vol.21 No.2
The aim of almost any electromagnetic actuator development is to increase the electromagnetic force with which an actuator acts on a plunger with as fast a time response as possible while maintaining the dimensions as small as possible. This paper presents research on the impact of the lower core angle on the force and time response of a DC solenoid electromagnetic actuator. The research method is based on the analytical analysis of the magnetic path of the DC solenoid electromagnetic actuator and a comparison with the numerical simulation results. A transient numerical simulation was performed on a 2D axial-symmetric model of the electromagnetic actuator and included simultaneously solving time-dependent partial differential equations of the electromagnetic actuator’s magnetic, electrical, and mechanical subsystems. The magnetic subsystem was analyzed by the finite element method (FEM) using the ANSYS Electronics software package. The three prototype models with different lower core angles were produced and tested in the accredited Laboratory Center of KONČAR Electrical Engineering Institute. The obtained measurements are compared with the analytical results and numerical simulation results.
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Mario Kekez,Natasa Bauer,Ela Saric,Jasmina Rokov-Plavec 한국식물학회 2016 Journal of Plant Biology Vol.59 No.1
Aminoacyl-tRNA synthetases (aaRSs) decipher the genetic code, covalently linking amino acids to cognate tRNAs, thus preparing substrates for the process of translation. Although aaRSs funtion primarily in translation and are localized in cytosol, mitochondria and chloroplasts there are many reports on their additional functions and subcellular destinations beyond translation. However, data on plant aaRSs are scarce. Initial analysis of amino acid sequence of Arabidopsis thaliana seryl-tRNA synthetase (SerRS) suggested that protein contains putative nuclear localization signals. GFP-localization experiments in transiently transformed epidermal onion cells and Arabidopsis protoplasts gave ambiguous results because in some cells SerRS appeared to be dually localized to both cytosol and nucleus. However, data obtained on transgenic lines expressing SerRS-TAP and GFP-SerRS revealed exclusive cytosolic location of SerRS. Subcellular distribution of SerRS did not change during stress. Cytosolic Arabidopsis SerRS was expressed and purified. The enzyme efficiently aminoacylated eukaryotic and bacterial tRNAsSer, that are structurally very different. Given the fact that the same behavior was previously shown for monocot maize SerRS, it seems that plant SerRSs exhibit unusually broad tRNASer specificity, unlike SerRSs from other organisms. Possible functional implications of this unique characteristic of plant SerRSs are discussed.
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Recovery of the Formation and Function of Oxidized G-Quadruplexes by a Pyrene-Modified Guanine Tract
Takahashi, Shuntaro,Kim, Ki Tae,Podbevš,ek, Peter,Plavec, Janez,Kim, Byeang Hyean,Sugimoto, Naoki American Chemical Society 2018 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY - Vol.140 No.17
<P>Oxidation is one of the frequent causes of DNA damage, especially to guanine bases. Guanine bases in the G-quadruplex (G4) are sensitive to damage by oxidation, resulting in transformation to 8-oxo-7,8-dihydroguanine (8-oxoG). Because the formation of G4 represses the expression of some cancer-related genes, the presence of 8-oxoG in a G4 sequence might affect G4 formation and induce cancer progression. Thus, oxidized-G4 formation must be controlled using a chemical approach. In the present study, we investigated the effect of introduction of 8-oxoG into a G4 sequence on the formation and function of the G4 structure. The 8-oxoG-containing G4 derived from the promoter region of the human vascular endothelial growth factor (<I>VEGF</I>) gene differed topologically from unoxidized G4. The oxidized <I>VEGF</I> G4 did not act as a replication block and was not stabilized by the G4-binding protein nucleolin. To recover G4 function, we developed an oligonucleotide consisting of a pyrene-modified guanine tract that replaces the oxidized guanine tract and forms stable intermolecular G4s with the other intact guanine tracts. When this oligonucleotide was used, the oxidized G4 stalled replication and was stabilized by nucleolin as with the unmodified G4. This strategy generally enables recovery of the function of any oxidized G4s and therefore has potential for cancer therapy.</P> [FIG OMISSION]</BR>
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