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        Spontaneous transposition of HzSINE1 into CYP321A2 is undetectable in the field populations of Helicoverpa zea

        Li Shengyun,Chen Song,Dong Shuanglin,Zhang Min,Deng Zhongyuan,Ni Xinzhi,Huang Jinyong,Li Xianchun 한국응용곤충학회 2021 Journal of Asia-Pacific Entomology Vol.24 No.3

        The enrichment of transposable elements (TEs) within allelochemical- and insecticide-metabolizing P450 alleles in Helicoverpa zea enables these P450s to gain TE-introduced adaptive variations otherwise not readily available to cope with the ever-changing and diverse xenobiotic stress factors in varying cropping systems. The critical role of each TE-inserted P450 allele depends on whether the inserted P450 allele is more adaptive than its TE-free counterpart or not. Previous study has reported a HzSINE1-inserted CYP321A2 allele in a laboratory strain of H. zea reared with xenobiotic-free artificial diets. Here we show that the HzSINE1-inserted CYP321A2 allele transcribes into two HzSINE1 sequence-containing mutant mRNA isoforms of different length that encode an identical C terminus-truncated and heme-binding region deleted non-functional P450. Nonetheless, HzSINE1 insertion does not disrupt the regulatory functional aspect of CYP321A2 since this allele is constitutively expressed and highly inducible by the allelochemicals xanthotoxin, quercetin and chlorogenic acid. Furthermore, while the HzSINE1-inserted CYP321A2 allele is fixed in the laboratory strain, the insertion is purged in the bifenthrin-resistant strain and the Georgia field population of H. zea. To sum up, the HzSINE1-inserted CYP321A2 allele represents an allelochemical-inducible non-functional P450 allele that is selected against in the field populations frequently encountering toxic plant allelochemicals and synthetic insecticides. However, such an insertion can reach fixation under the xenobiotic-free laboratory rearing conditions most likely due to random genetic drift across multiple generations.

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        Desulfurization of coke oven gas using char-supported Fe-Zn-Mo catalysts: Mechanisms and thermodynamics

        Jinxiao Dou,Xianchun Li,Arash Tahmasebi,Jing Xu,Jianglong Yu 한국화학공학회 2015 Korean Journal of Chemical Engineering Vol.32 No.11

        Sulfidation properties of char-supported Fe-Zn-Mo sorbents prepared by ultrasonic impregnation method were investigated during simultaneous removal of H2S and COS from coke oven gas (COG) using a fixed-bed quartz reactor. Sorbent samples before and after sulfidation were analyzed using X-Ray diffraction (XRD) and Fourier transform infrared spectroscopy (FT-IR). The experimental results showed that the addition of Mo significantly improved the desulfurization properties (i.e., breakthrough time, sulfur capacity and desulfurization efficiency) of Fe-Zn sorbents. Desulfurization reactions were exothermic and thermodynamically favorable in the temperature range of 200- 400 oC. Thermodynamic analysis of the sorbents indicated that higher concentration of H2S and lower concentration of H2 favors the reaction of metal oxides with H2S to form metal sulfides.

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        Molecular cloning and expression analysis of soluble and membrane-bound trehalase genes in the cotton bollworm, Helicoverpa armigera

        Long Ma,Wu Dai,Xianchun Li,Yalin Zhang,Chunni Zhang 한국응용곤충학회 2015 Journal of Asia-Pacific Entomology Vol.18 No.2

        Trehalase plays a significant role in various physiological processes in insects. In this study, we cloned and characterized a soluble trehalase gene (HaTreh-1) and a membrane-bound trehalase gene (HaTreh-2) from Helicoverpa armigera, a serious polyphagous pest of crops. HaTreh-1 contained an open reading frame of 1716 bp that encodes a protein of 572 amino acids. HaTreh-2 has an open reading frame of 1938 bp, encoding a protein of 646 amino acids. Sequence alignment and phylogenetic analysis of the two putative proteins revealed that HaTreh-1 and HaTreh-2 belong to soluble and membrane-bound trehalase groups, respectively. Quantitative real-time PCR (qPCR) analyses of the spatiotemporal expression pattern of HaTreh in H. armigera revealed that HaTreh-1 was expressed mainly in the midgut, with lower expression in the integument and head, Malpighian tubules, trachea, and fat body. The expression levels of HaTreh-2 were detected in all 6 tissues, and HaTreh-2 was mainly expressed in the midgut and head. Expression of HaTreh-1 was higher throughout the larval stages, but lower on days 1 and 2 of the pupal stage. Expression of HaTreh-2 was higher during the 4th- and 5th-instar larval stages. Taken together, these results suggest that HaTreh-1 and HaTreh-2 have different functions in various developmental stages and tissues.

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