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- 저자 : Seul Ong Ohk (검색결과 3 건)
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Lee, Eun-Chang,Ohk, Seul-Ong,Suh, Bo-Young,Park, Na-Hee,Kim, Beom-Joon,Kim, Dong-Hak,Chun, Young-Jin Korean Society of ToxicologyKorea Environmental Mu 2010 Toxicological Research Vol.27 No.1
The Malassezia fungi are responsible for various human skin disorders including dandruff and seborrheic dermatitis. Of the Malassezia fungi, Malassezia globosa (M. globosa) is one of the most common in human scalp. The completed genome sequence of M. globosa contains four putative cytochrome P450 genes. To determine the roles of Malassezia P450 enzymes in the biosynthesis of ergosterol, we isolated MGL3996 gene from M. globosa chromosomal DNA by PCR. The MGL3996 gene encodes an enzyme of 616 amino acids, which shows strong similarity with known CYP52s of other species. MGL3996 gene was cloned and expressed in Pichia pastoris (P. pastoris) heterologous yeast expression system. Using the yeast microsomes expressing MGL3996 protein, a typical P450 CO-difference spectrum was shown with absorption maximum at 448 nm. SDS-PAGE analysis revealed a protein band of apparent molecular weight 69 kDa and Western blot with anti-histidine tag antibody showed that MGL3996 was successfully expressed in P. pastoris. Cloning and expression of a new P450 gene is an important step to study the P450 monooxygenase system of M. globosa and to understand the role of P450 enzymes in pathophysiology of dandruff.
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Eun Chang Lee,Seul Ong Ohk,Bo Young Suh,Nahee Park,Beom Joon Kim,Donghak Kim,Young-Jin Chun 한국독성학회 2010 Toxicological Research Vol.26 No.1
The Malassezia fungi are responsible for various human skin disorders including dandruff and seborrheic dermatitis. Of the Malassezia fungi, Malassezia globosa (M. globosa) is one of the most common in human scalp. The completed genome sequence of M. globosa contains four putative cytochrome P450 genes. To determine the roles of Malassezia P450 enzymes in the biosynthesis of ergosterol, we isolated MGL3996 gene from M. globosa chromosomal DNA by PCR. The MGL3996 gene encodes an enzyme of 616 amino acids, which shows strong similarity with known CYP52s of other species. MGL3996 gene was cloned and expressed in Pichia pastoris (P. pastoris) heterologous yeast expression system. Using the yeast microsomes expressing MGL3996 protein, a typical P450 CO-difference spectrum was shown with absorption maximum at 448 nm. SDS-PAGE analysis revealed a protein band of apparent molecular weight 69 kDa and Western blot with anti-histidine tag antibody showed that MGL3996 was successfully expressed in P. pastoris. Cloning and expression of a new P450 gene is an important step to study the P450 monooxygenase system of M. globosa and to understand the role of P450 enzymes in pathophysiology of dandruff.
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<i>trans</i>-Stilbenoids: potent and selective inhibitors for human cytochrome P450 1B1
Chun, Young-Jin,Lim, Chaemin,Ohk, Seul Ong,Lee, Ji Min,Lee, Jin Hee,Choi, Sun,Kim, Sanghee Royal Society of Chemistry 2011 MedChemComm Vol.2 No.5
<P>On the basis of our previous insights into the structural requirements of stilbenoids for the inhibition of cytochrome P450 1B1 (CYP1B1), a series of 2,4-dimethoxy group-containing stilbenes was prepared and evaluated for their inhibitory effects on the activity of CYP1s with the ultimate goal of identifying a potent and selective CYP1B1 inhibitor. Among the thirteen derivatives prepared, five compounds exhibited similar or greater potency compared to the previous lead compound, 2,4,3′,5′-tetramethoxystilbene (2,4,3′,5′-TMS), in inhibiting CYP1B1. In particular, 2,2′,3′,4,6′-pentamethoxystilbene was found to be a more selective and more potent CYP1B1 inhibitor than 2,4,3′,5′-TMS. 2,4,2′,6′-TMS showed remarkably potent inhibitory activity against CYP1B1 (IC<SUB>50</SUB> = 1.77 ± 0.14 nM) and also had a very high selectivity toward CYP1 isoenzymes. Molecular modeling was performed to determine the key molecular interactions with the CYP1B1 and CYP1A2 structures. On the basis of these structural and biological studies, the design of more potent and more selective drug-like derivatives can be envisaged.</P> <P>Graphic Abstract</P><P>The inhibitory potency and selectivity against cytochrome P450 subfamily 1 (CYP1) depends strongly on the substitution pattern. 2,2′,3′,4,6′-Pentamethoxystilbene was found to be the most selective and potent CYP1B1 inhibitor to date. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c0md00242a'> </P>
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