• Journal of Sericultural and Entomological Science
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• v.35 no.2
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• pp.93-99
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• 1993

Studies were carried out to investigate physiological and biochemical analysis of recessive lethal mutant "nmn" and to observe the cuticle formation and dermal gland. All nmn homozygous larvae continued to eat a few mulberry leaves, and died without entering into molt. In case of artificial hatching, eggs had a higher nmn individual segregation ratio than in hibernating eggs. The percentage of nmn individuals with the hatching days was alike during 3days period. As a result of histological observation, nmn mutants dermal gland was different from normal dermal gland in form and size. Normal was formed new cuticle in the middle of the molting, but not in nmn mutant. Total protein content in haemolymph of the normal larva was more than that of nmn smutant and there was a difference between normal and nmn mutant protein components.omponents.

• The Korean Journal of Zoology
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• v.38 no.1
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• pp.106-114
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• 1995

배추흰나비의 조직과 발생시기에 따른 발생 특이 큐티클단백질의 질적 분포를 조사하기 위해 전기영동법, western blotting 및 autoradiography 법을 사용하였다. SDS-PAGE에서 유충기에는 4개, 용기에는 3개의 단백질이 발생 특이 큐티클단백질로 확인되었다. 전기영동적 이동도로 보아 유충기의 62 Kd 큐티클단백질은 지방체 표피, 혈림프에 모두 분포하며. 22 Kd, 16 Kd 단백질은 지방체와 표피, 그리고 19 Kd 단백질은 지방체에서 확인되고 있으며, 용기의 37 Kd 단백질은 표피에서. 28 Kd, 27 Kd 단백질은 표피와 지방체에 분포하는 양상을 보이고 있다 면역학적 방법으로 발생 특이 큐티클단백질의 동질성을 조사한 결과 용기의 27 Kd 단백질은 표피와 지방체에서 반응을 나타내며, 유충기의 22 Kd 단백질은 단지 표피에서만 미약하게 이의 동질성을 보여주고 있다 즉, 27 Kd 단백질은 지방체 22 Kd 단백질은 표피에서 기원하고 있어 발생 특이 큐티클단백질의 합성부위는 한 조직에서 기원하는 것이 아니라 각기 상이한 조직으로 부터 생성되는 것으로 사료된다.

• Journal of Applied Biological Chemistry
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• v.65 no.4
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• pp.307-312
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• 2022

A hair essence containing α-tocopheryl acetate, retinyl palmitate, and phytantriol (TRP-hair essence) was prepared. TRP-hair essence was excellent in thermal stability to the extent that it did not harden at all even at 210 ℃. TRP-hair essence potently protected the hair from heat stress, significantly reducing the protein leakage in heat-treated hair (p <0.001). Treatment of TRP-hair essence to dyed human hair significantly protected hair against heat stress (p <0.05) as well as improved hair cuticle and color persistence (p <0.05). In addition, as a result of directly treating human hair with TRP-hair essence, the cuticle and tensile strength of human hair were significantly improved (p <0.05). These results suggest that TRP-hair essence can be effective for hair protection and hair quality improvement.

• International Journal of Industrial Entomology and Biomaterials
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• v.6 no.1
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• pp.87-92
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• 2003

We describe here the cloning, expression and characterization of a cDNA encoding a putative chemosensory protein (CSP) from the mole cricket, Gryllotalpa orientalis. The G. orientalis chemosensory protein cDNA sequences comprised of 384 bp with 128 amino acid residues. The G. orientalis chemosensory protein showed 75.4% protein sequence identity to the Locusta migratoria CSP, Northern blot analysis revealed that signal was stronger in head than leg and cuticle, indicating that the head part containing antennae is a main site for G. orientalis chemosensory protein synthesis. The cDNA encoding G. orientalis chemosensory protein was expressed as approximately 12 kDa polypeptide in baculovirus-infected insect cells.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2004.05a
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• pp.147-147
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• 2004

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2004.10a
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• pp.63-63
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• 2004

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2004.10a
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• pp.62-62
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• 2004

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2003.10a
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• pp.103-103
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• 2003

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2004.04a
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• pp.51-51
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• 2004

• Journal of Microbiology and Biotechnology
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• v.22 no.7
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• pp.889-893
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• 2012

Appressorium is a specialized infection structure of filamentous pathogenic fungi and plays an important role in establishing a pathogenic relationship with the host. The Egh16/Egh16H family members are involved in appressorium formation and pathogenesis in pathogenic filamentous fungi. In this study, a homolog of Egh16H, Magas1, was identified from an entomopathogenic fungus, Metarhizium acridum. The Magas1 protein shared a number of conserved motifs with other Egh16/Egh16H family members and specifically expressed during the appressorium development period. Magas1-EGFP fusion expression showed that Magas1 protein was not localized inside the cell. Deletion of the Magas1 gene had no impact on vegetative growth, conidiation and appressorium formation, but resulted in a decreased mortality of host insect when topically inoculated. However, the mortality was not significant between the Magas1 deletion mutant and wild-type treatment when the cuticle was bypassed by injecting conidia directly into the hemocoel. Our results suggested that Magas1 may influence virulence by affecting the penetration of the insects' cuticle.