• Proceedings of the Korean Society of Sericultural Science Conference
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• 2001.10a
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• pp.63-63
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• 2001

no Abstract, See Full Text

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2002.11a
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• pp.137-137
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• 2002

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2002.11a
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• pp.138-138
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• 2002

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2002.10a
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• pp.141-141
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• 2002

No Abstract, See Full Text

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2002.10a
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• pp.145-145
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• 2002

No Abstract, See Full Text

• International Journal of Industrial Entomology and Biomaterials
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• v.4 no.1
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• pp.43-49
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• 2002

We have cloned cDNAs encoding toxin from the spider, Araneus ventricosus, and constructed a recombinant baculovirus expressing the insecticidal toxin. The cDNAs encoding toxin were cloned from the cDNA library of A. ventricosus. Sequence analysis of the cDNAs encoding the toxin of A. ventricosus revealed that the 240 bp cDNA for AvTox-1 and 192 bp cDNA for AvTox-2 have an open reading frame of 80 and 64 amino acid residues, respectively. The deduced protein sequence of the toxin genes of AvTox-1 and AvTox-2 was aligned to that of the snack Anemonia sulcata and scorpion Centruroides limpidus limpidus, respectively. Northern blot analysis indicated that AvTox-2 toxin gene showed a fat body-spe-cific expression pattern at the transcriptional level. Furthermore, we have explored the possibility of improving baculovirus by incorporating the A. vontricosus toxin gene into Bombyx mori nuclear polyhedrosis virus genome under the control of polyhedrin promoter, The AvTox-2 toxin gene was expressed as approximately 5.8 kDa band in the recombinant baculovirus-injected silkworm larvae. Bioassays with the recombinant virus expressing AvTox-2 on 5th instar silkworm larvae demonstrated a decrease in the time to kill $(LT_{50} days)$ compared to wild-type BmNPV-Kl $(LT_{50} 6.72 days)$ in the injection of 10 viruses. These results indicate that A. ventricosus toxin is a novel member of the spider toxin family, suggesting that the toxin gene can be used in recombinant baculoviruses to reduce insect feeding damage and increase the speed of insect kill.

• International Journal of Industrial Entomology and Biomaterials
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• v.19 no.2
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• pp.259-264
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• 2009

The AvChit gene encodes for a chitinase from the spider, Araneus ventricosus. This spider, A. ventricosus, is an abundant species in Korea. Arabidopsis thaliana plants were transformed with the AvChit gene using Agrobacterium tumefaciens. Thirteen transgenic lines expressing the AvChit gene were obtained. Functional expression of the AvChit gene in transgenic Arabidopsis was confirmed by Southern, northern and western blot analysis. The AvChit cDNA was expressed as a 61 kDa polypeptide in baculovirus-infected insect Sf9 cells. AvChit protein extracted from transgenic Arabidopsis exhibited high levels of chitinase activity. Phytopathological tests showed that two transgenic Arabidopsis lines expressing the AvChit gene displayed high levels of resistance to gray mold disease (Botrytis cinerea).

• Korean journal of applied entomology
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• v.37 no.1
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• pp.73-80
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• 1998

The natural enemies of Black pine bast scale (Matsucoccus thunbergianae) were surveyed total 24species, 7families, 4orders in predatory insects and 29species 1 lfamilies in a predatory spiders. In insect, Coleoptera IOspecies, Hymenoptera 7species, Hemiptera 6species, Dermaptera 1 species were investigated. Among them high frequency and population density were Chilocorus rubidus, Harmonia axyridis of Coleoptera, Brachyponera chinensis, Vesp~ilac rabro flavofasciata of Hymonoptea, Sphedanolestes impressicollis, Velinos nodipes of Hemiptera. Anatis halonis, Anisostictu kobensis of Coleoptea and Cydnocoris russatus of Hemiptea were newly investigated. In spiders, Araneidae gspecies, Thomisidae Sspecies, Lycosidae 3species, Salticidae 3species, Pisauridae 2species, Theridiidae 2species, Tetragnathidae 2species, Oxyopidae lspecies, Gnaphosidae I species, Clubionidae I species, Atypidae 1 species were investigated. Which high frequency and concentrating predatory species were Argiope bruennichii, Araneus ventricosus, Neoscona melloteei, Neoscona scylloides of Araneidae, Lycosa suzurii, Pirata sp. of Lycosidae, Marpissu elongata of Salticidae, Dolomedes stellatus of Pisauridae, Oxyopes sertatus of Oxyopidae. Neosconu scylloides, Cvclosa laticauda of Araneidae, Synema globosum, Xysticus ephippiatus, Misumenops tricu~pidat~o~f .T~h, omisidae, Marpissa elongata, Dendryphantes atratus of Salitidae, Perenethis .fascigera of Pisauridae, Tetragnatha pinicola of Tetragnathidae, Zelotes asiaticus of Gnaphosidae.

• Journal of the Korean Wood Science and Technology
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• v.47 no.3
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• pp.371-380
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• 2019

Termites are pests that cause serious economic and cultural damage by digesting wood cellulose. Termites are arthropods and have an epidermis surrounded by a chitin layer. To maintain a healthy epidermis, termites have chitinase (${\beta}$-1,4-poly-N-acetyl glucosamidinase, EC 3.2.1.14), an enzyme that hydrolyzes the ${\beta}$-1,4 bond of chitin. In this study, the amino acid sequence of the gene, which is presumed to be termite chitinolytic enzyme (NCBI accession no. KC477099), was obtained from a transcriptomic analysis of Reticulitermes speratus KMT001 in Bukhan Mountain, Korea. An NCBI protein BLAST search confirmed that the protein is a glycoside hydrolase family 18 (GH18). The highest homology value found was 47%, with a chitinase from Araneus ventricosus. Phylogenetic analysis indicated that the KC477099 protein has the same origins as those of arthropods but has a very low similarity with other arthropod chitinases, resulting in separation at an early stage of evolution. The KC477099 protein contains two conserved motifs, which encode the general enzymatic characteristics of the GH18 group. The amino acid sequences $Asp^{156}-Trp^{157}-Glu^{158}$, which play an important role in the enzymatic activity of the GH18 group, were also present. This study suggests that the termite KC477099 protein is a new type of chitinase, which is evolutionarily distant from other insect chitinases.

• Applied Microscopy
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• v.39 no.2
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• pp.101-106
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• 2009

The dorsal lingual papillae of Sorex caecutiens were studied morphologically using scanning electron microscopy. Three types of lingual papillae were found: filiform papillae, fungiform papillae and circumvallate papillae. Filiform papillae were observed in most part of the tongue except on the lateral surface. There were basically three types of filiform papillae distinguished mainly by their morphological shape and structure. Numerous fungiform papillae were spread throughout the whole tongue, especially concentrated in lateral sides. The size varied according to the position of fungiform papillae, becoming larger as it reached to the rear. Strict pair-wise distribution was not observable, but fungiform papillae were mostly located in orderly manner. There were two large circumvallate papillae at the posterior region of the tongue. There were two thick pads around the center part where several bodies were gathered together. Overall research provided similar results with other close species such as common shrew (S. araneus). The circumvallate papillae of S. caecutiens were different from other Sorex species. They were circular, as in bats and other Sorex species, and had two distinguishable pads while others had only one.