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Kim, HyoJin,Noh, Sung Jin,Kang, Yeong-Rok,Lee, Manwoo,Jeong, Dong Hyeok,Kim, Jung Ki,Yang, Kwangmo,Ro, Tae-Ik,Shin, Sung Gyun,Kye, Yong Uk,Cho, Moo-Hyun,Kim, Guinyun Elsevier 2015 Nuclear instruments & methods in physics research. Vol.349 No.-
<P><B>Abstract</B></P> <P>The isomeric yield ratios of <SUP>133m,g</SUP>Ce and <SUP>137m,g</SUP>Ce produced from the <SUP>nat</SUP>Ce(γ,xn) reactions were determined by using the activation and the off-line γ-ray spectrometric technique with the end-point bremsstrahlung energies of 55-, 60-, and 65-MeV at 100-MeV electron linac of the Pohang accelerator laboratory. The induced activities in the irradiated foils were measured by using an energy- and efficiency-calibrated HPGe detector coupled to a PC based multi-channel analyzer. The necessary corrections were made to improve the accuracy of the experimental results. The experimental results at bremsstrahlung energies of 55-, 60-, and 65-MeV were 0.324±0.089, 0.331±0.086, and 0.403±0.089 for the <SUP>133m,g</SUP>Ce, and 0.210±0.062, 0.221±0.061, and 0.262±0.061 for the <SUP>137m,g</SUP>Ce, respectively. The present results for <SUP>nat</SUP>Ce(γ,xn)<SUP>133m,g;137m,g</SUP>Ce in this energy region were obtained for the first time which has no comparable literature data. The obtained isomeric yield ratios are compared with the calculated values based on the statistical model code TALYS 1.6.</P>
Invited Mini Review : The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
( Harikrishna Reddy R ),( Hackyoung Kim ),( Kwangmo Noh ),( Young Jun Kim ) 생화학분자생물학회(구 한국생화학분자생물학회) 2014 BMB Reports Vol.47 No.4
RNA polymerase II carboxyl-terminal domain (pol II CTD) phosphatases are a newly emerging family of phosphatases that are members of DXDX (T/V). The subfamily includes Small CTD phosphatases, like SCP1, SCP2, SCP3, TIMM50, HSPC129 and UBLCP. Extensive study of SCP1 has elicited the diversified roles of the small C terminal domain phosphatase. The SCP1 plays a vital role in various biological activities, like neuronal gene silencing and preferential Ser5 dephosphorylation, acts as a cardiac hypertrophy inducer with the help of its intronic miRNAs, and has shown a key role in cell cycle regulation. This short review offers an explanation of the mechanism of action of small CTD phosphatases, in different biological activities and metabolic processes. [BMB Reports 2014; 47(4): 192-196]
( Young Jun Kim ),( Hackyoung Kim ),( Kwangmo Noh ) 한국질량분석학회 2014 Mass spectrometry letters Vol.5 No.3
Microglia are the confined immune cells of the central nervous system (CNS). In response to injury or infection, microglia readily become activated and release proinflammatory mediators that are believed to contribute to microglia-mediated neurodegeneration. In the present study, inflammation was induced in the immortalized murine microglial cell line BV-2 by lipopolysaccharide (LPS) treatment. We firstly performed phosphoproteomics analysis and phosphoinositide lipidomics analysis with LPS activated microglia in order to compare phosphorylation patterns in active and inactive microglia and to detect the pattern of changes in phosphoinositide regulation upon activation of microglia. Mass spectrometry analysis of the phosphoproteome of the LPS treatment group compared to that of the untreated control group revealed a notable increase in the diversity of cellular phosphorylation upon LPS treatment. Additionally, a lipidomics analysis detected significant increases in the amounts of phosphoinositide species in the LPS treatment. This investigation could provide an insight for understanding molecular mechanisms underlying microglia-mediated neurodegenerative diseases.
Kim, Young Jun,Kim, Hackyoung,Noh, Kwangmo Korean Society for Mass Spectrometry 2014 Mass spectrometry letters Vol.5 No.3
Microglia are the confined immune cells of the central nervous system (CNS). In response to injury or infection, microglia readily become activated and release proinflammatory mediators that are believed to contribute to microglia-mediated neurodegeneration. In the present study, inflammation was induced in the immortalized murine microglial cell line BV-2 by lipopolysaccharide (LPS) treatment. We firstly performed phosphoproteomics analysis and phosphoinositide lipidomics analysis with LPS activated microglia in order to compare phosphorylation patterns in active and inactive microglia and to detect the pattern of changes in phosphoinositide regulation upon activation of microglia. Mass spectrometry analysis of the phosphoproteome of the LPS treatment group compared to that of the untreated control group revealed a notable increase in the diversity of cellular phosphorylation upon LPS treatment. Additionally, a lipidomics analysis detected significant increases in the amounts of phosphoinositide species in the LPS treatment. This investigation could provide an insight for understanding molecular mechanisms underlying microglia-mediated neurodegenerative diseases.
Analysis of Phosphatidylinositol 3,4,5-Trisphosphates of PTEN Expression on Mammalian Cells
Jahan, Nusrat,Park, Taeseong,Kim, Young Hwan,Lee, Dongsun,Kim, Hackyoung,Noh, Kwangmo,Kim, Young Jun Korean Society for Mass Spectrometry 2013 Mass spectrometry letters Vol.4 No.3
The goal of this study is to find an experimental condition which enables us to perform enzymatic studies on the cellular behavior of PTEN (phosphatase and tensine homolog) through identification of molecular species of phosphatidylinositol 3,4,5-trisphosphates and their quantitative analysis in a mammalian cell line using mass spectrometry. We initially exployed a two-step extraction process using HCl for extraction of phosphatidylinositol 3,4,5-trisphosphates from two mammalian cell lines and further analyzed the extracted phosphatidylinositol 3,4,5-trisphosphates using tandem mass spectrometry for the identification of them. We finally quantified the concentration of phosphatidylinositol 3,4,5-trisphosphates using internal standard calibration. From these observation, we found that HEK 293-T cells is a good model to examine the enzymatic behavior of PTEN in a cell, and the minimum amount of phosphatidylinositol 3,4,5-trisphosphates is more than 50 pmol for quantification in a mass spectrometer. These results suggest that the well-optimized experimental conditions are required for the investigation of the cellular PTEN in terms of the catalytic mechanism and further for the detailed identification of cellular substrates.
Analysis of Phosphatidylinositol 3,4,5-Trisphosphates of PTEN Expression on Mammalian Cells
( Nusrat Jahan ),( Taeseong Park ),( Young Hwan Kim ),( Dongsun Lee ),( Hackyoung Kim ),( Kwangmo Noh ),( Young Jun Kim ) 한국질량분석학회 2013 Mass spectrometry letters Vol.4 No.3
The goal of this study is to find an experimental condition which enables us to perform enzymatic studies on the cellular behavior of PTEN (phosphatase and tensine homolog) through identification of molecular species of phosphatidylinositol 3,4,5- trisphosphates and their quantitative analysis in a mammalian cell line using mass spectrometry. We initially exployed a two-step extraction process using HCl for extraction of phosphatidylinositol 3,4,5-trisphosphates from two mammalian cell lines and further analyzed the extracted phosphatidylinositol 3,4,5-trisphosphates using tandem mass spectrometry for the identification of them. We finally quantified the concentration of phosphatidylinositol 3,4,5-trisphosphates using internal standard calibration. From these observation, we found that HEK 293-T cells is a good model to examine the enzymatic behavior of PTEN in a cell, and the minimum amount of phosphatidylinositol 3,4,5-trisphosphates is more than 50 pmol for quantification in a mass spectrometer. These results suggest that the well-optimized experimental conditions are required for the investigation of the cellular PTEN in terms of the catalytic mechanism and further for the detailed identification of cellular substrates.