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학업우수 초등학생 자녀를 둔 어머니의 진로지도 경험에 관한 질적 연구
하정,이항심,정혜윤,김은덕,유성경 한국직업능력개발원 2007 직업능력개발연구 Vol.10 No.3
본 연구는 학업우수 초등학생 자녀를 둔 어머니의 진로지도 경험을 한국의 사회·문화적 맥락에서 밝히고자 하였다. 이를 위해 서울지역에 살고 있는 초등학교 6학년인 학업우수아의 어머니 9명을 심층면담하고, 질적 연구 방법으로 분석하였다. 연구 결과, 107개의 개념과 44개의 하위 범주, 그리고 14개의 범주가 도출되었다. 어머니들의 진로지도 경험을 포괄하는 핵심범주로는 '자녀의 성취를 위해 자녀의 특성을 존중하고 자녀의 자율성을 키우면서 자신이 바람직하다고 여기는 방향으로 이끌어감'으로 밝혀졌다. 연구 결과를 바탕으로 학업우수 초등학생 자녀를 둔 어머니의 진로지도 경험의 실체를 논의하였으며, 부모를 대상으로 한 진로교육프로그램의 필요성과 후속 연구에 대한 제언을 하였다. This study examined the experience about career guidance of mother who has a academically talented child in Korea. Nine mothers were interviewed and the interview data were analyzed based on the Qualitative Research Method. Result has107 concepts, 44 subcategories and 14 categories. The core category is "The mothers consider their children's characteristics for the children's accomplishment and foster children's self-control and lead their children to desirable object the mothers view".Implications of the results and suggestions for future research are discussed.
함봉진,심은정,김하경,김종흔 大韓神經精神醫學會 2007 신경정신의학 Vol.46 No.5
Cancer statistics shows a high risk and increasing incidence of cancer among Koreans. Considerable burdens related to cancer and its treatment causes significant psychosocial distress among cancer patients and their family. Due to early detection and progress in cancer treatments, cancer is becoming a chronic illness and the quality of life and long-term impact of cancer is receiving increasing attention. Psycho-oncology is a subspecialty of oncology that addresses a psychosocial dimension of cancer throughout 'the continuum of cancer care', viz. from prevention and early detection to palliative and end-of-life care. This paper reviews the development of psycho-oncology and its current status in international and national context so as to promote efforts toward an integrative cancer care in Korea.
Shim, Ha Eun,Song, Lee,Jeon, Jongho 대한방사성의약품학회 2018 Journal of radiopharmaceuticals and molecular prob Vol.4 No.2
We demonstrate a detail protocol for the radiosynthesis of an $^{125}I$-labeled MSTP prosthetic group and its application to the efficient radiolabeling of human serum albumin (HSA). Radioiodination of the precursor (2) was carried out by using $[^{125}I]$NaI and chloramine T as an oxidant at room temperature for 15 min. After HPLC purification of the crude product, the purified $^{125}I$-labeled MSTP ($[^{125}I]1$) was obtained with high radiochemical yield ($73{\pm}5%$, n = 3) and excellent radiochemical purity (>99%). Site-specific reaction between ($[^{125}I]1$) and HSA gave the $^{125}I$-labeled human serum albumin ($[^{125}I]3$) with more than 99% of radiochemical yield as determined by radio-thin-layer chromatography (radio-TLC). These results clearly demonstrate that the present radiolabeling method will be useful for the efficient and convenient radiolabeling of thiol-bearing biomolecules.
Prediction of radiation-induced degradation for a FAPbBr3 perovskite solar cell
Shim Ha Eun,Park Jinhyung,Yeon Yeong Heum,Lee Nam-Ho,Gwon Hui-Jeong 한국물리학회 2022 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.80 No.3
This study used the equivalent displacement damage dose (EDDD) model to predict radiation-induced damage of formamidinium lead–bromide ( FAPbBr3) perovskite solar cells. The response characteristics of FAPbBr3 perovskites irradiated with 60Co gamma rays were estimated using the light current voltage (LIV) curve, and radiation damage was analyzed in terms of atomic displacement caused by secondary electrons emitted due to gamma rays. The EDDD model was derived in consideration of the nonionizing energy loss of gamma rays ( NIEL ), fluence of gamma rays ( Φ ) , and power factor n. Here, the NIEL was the product of the slowed spectrum of secondary electrons calculated in Geant4 and the NIEL of electrons ( NIEL e) obtained using the SR-NIEL web calculator. In terms of the maximum power output ( P max ), the prediction curve for radiation-induced damage derived using the EDDD model was consistent with the experimental results.
Ha Eun Shim,Jongho Jeon,Lee Song 대한방사성의약품학회 2018 Journal of radiopharmaceuticals and molecular prob Vol.4 No.2
We demonstrate a detail protocol for the radiosynthesis of an 125I-labeled MSTP prosthetic group and its application to the efficient radiolabeling of human serum albumin (HSA). Radioiodination of the precursor (2) was carried out by using [125I]NaI and chloramine T as an oxidant at room temperature for 15 min. After HPLC purification of the crude product, the purified 125I-labeled MSTP ([125I]1) was obtained with high radiochemical yield (73 ± 5%, n = 3) and excellent radiochemical purity (>99%). Site-specific reaction between ([125I]1) and HSA gave the 125I-labeled human serum albumin ([125I]3) with more than 99% of radiochemical yield as determined by radio-thin-layer chromatography (radio-TLC). These results clearly demonstrate that the present radiolabeling method will be useful for the efficient and convenient radiolabeling of thiol-bearing biomolecules
Ha Eun Shim,Dong-Eun Lee,Chang Heon Lee,Dae Seong Choi,Do Hee Kim 대한방사성의약품학회 2019 Journal of radiopharmaceuticals and molecular prob Vol.5 No.1
Recently, antibody-like scaffold proteins have received a great deal of interest in diagnosis and therapyapplications because of their intrinsic features that are often required for tumor imaging and therapy. Intrinsicissues that are associated with therapeutic application of antibody-like scaffold proteins, particularly in cancertreatment, include an efficient and straightforward radiolabeling for understanding in vivo biodistribution andexcretion route, and monitoring therapeutic responses. Herein, we report an efficient and straightforwardmethod for radiolabeling of antibody-like scaffold proteins with the [99mTc(OH2)3(CO)3]+ (99mTc-tricarbonyl) byusing a site-specific direct labeling method via hexahistidine-tag, which is a widely used for general purificationof recombinant proteins with His-affinity chromatography. Repebody is a new class of antibody-like scaffoldprotein that consists of highly diverse leucine-rich repeat (LRR) modules. Although all possible biomedicalapplications with repebody are ongoing, it’s in vivo biodistribution and excretion pathway has not yet beenexplored. In this study, hexahistidine (His6)-tag bearing repebody (rEgH9) was labeled with [99mTc]-tricarbonyl. Repebody protein was radiolabeled with high radiolabeling efficiency (>90%) and radiolabeled compound wasmore than 99% pure after purification. These results clearly demonstrate that the present radiolabeling methodwill be useful molecular imaging study.
Ha Eun Shim,You Ree Nam,Dong-Eun Lee 대한방사성의약품학회 2019 Journal of radiopharmaceuticals and molecular prob Vol.5 No.2
In order to understand the in vivo biodistribution of repebody protein (RB), an efficient and simple radiolabelingmethod for the protein is needed. We demonstrate a detailed protocol for the radiosynthesis of an 111Inradiolabeled tetrazine prosthetic group and its application to the efficient radiolabeling of trans-cyclooctenegroupconjugated repebody protein using inverse-electron-demand Diels-Alder reaction. First, 1,2,4,5-tetrazine(Tz) conjugated with a DOTA chelator, was used for preparing the radiolabeled DOTA complex with 111In. Second, the trans-cyclooctene (TCO) functionalized repebody protein was synthesized which allows forthe preparation of radiolabeled proteins by copper-free click chemistry. Following incubation with the 111InradiolabeledDOTA complex (111In-Tz), the TCO-functionalized RB (TCO-RB) was radiolabeled successfullywith 111In, with a high radiochemical yield (69.5%) and radiochemical purity (>99%). The radiolabeling ofrepebody protein by copper-free click chemistry was accomplished within 20 min, with great efficiency inaqueous conditions. These results clearly indicate that the present radiolabeling method will be useful for theefficient and convenient radiolabeling of trans-cyclooctene-group containing biomolecules.
Shim, Ha Eun,Mushtaq, Sajid,Song, Lee,Lee, Chang Heon,Lee, Hyosun,Jeon, Jongho Elsevier 2018 Bioorganic & medicinal chemistry letters Vol.28 No.17
<P><B>Abstract</B></P> <P>In this report, we describe the radiosynthesis of a new thiol-targeting prosthetic group for efficient radioactive iodine labeling of biomolecules. Radioiodination using the precursor <B>3</B> was performed to obtain <SUP>125</SUP>I-labeled tetrazole <B>4b</B> with high radiochemical yield (73%) and radiochemical purity. Using the radiolabeled <B>4b</B>, a single free cysteine containing peptide and human serum albumin were labeled with <SUP>125</SUP>I in modest-to-good radiochemical yields (65–99%) under mildly reactive conditions. A biodistribution study of [<SUP>125</SUP>I]<B>7</B> in normal ICR mice exhibited lower thyroid uptake values than those of <SUP>125</SUP>I-labeled human serum albumin prepared via a traditional radiolabeling method. Thus, [<SUP>125</SUP>I]<B>7</B> could be employed as an effective radiotracer for molecular imaging and biodistribution studies. The results clearly demonstrate that <B>4b</B> has the potential to be effectively implemented as a prosthetic group in the preparation of radiolabeled biomolecules.</P> <P><B>Highlights</B></P> <P> <UL> <LI> <SUP>125</SUP>I-labeled MSTP was synthesized in high radiochemical yield and radiochemical purity. </LI> <LI> Purified <SUP>125</SUP>I-labeled MSTP showed highly selective reactivity for thiol groups. </LI> <LI> <SUP>125</SUP>I-labeled MSTP were efficiently reacted with free cysteine containing biomolecules. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
Shim, Ha Eun,Lee, Jae Young,Lee, Chang Heon,Mushtaq, Sajid,Song, Ha Yeon,Song, Lee,Choi, Seong-Jin,Lee, Kyuhong,Jeon, Jongho Elsevier 2018 CHEMOSPHERE - Vol.207 No.-
<P><B>Abstract</B></P> <P>To assess the risk posed by a toxic chemical to human health, it is essential to quantify its uptake in a living subject. This study aims to investigate the biological distribution of inhaled polyhexamethylene guanidine (PHMG) aerosol particle, which is known to cause severe pulmonary damage. By labeling with indium-111 (<SUP>111</SUP>In), we quantified the uptake of PHMG for up to 7 days after inhalation exposure in rats. The data demonstrate that PHMG is only slowly cleared, with approximately 74% of inhaled particles persisting in the lungs after 168 h. Approximately 5.3% of inhaled particles were also translocated to the liver after 168 h, although the level of redistribution to other tissues, including the kidneys and spleen, was minimal. These observations suggest that large uptake and slow clearance may underlie the fatal inhalation toxicity of PHMG in humans.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Polyhexamethylene guanidine (PHMG), a humidifier disinfectant, was labeled with In-111. </LI> <LI> Aerosol particles comprising radiolabeled PHMG was exposed to rats for biodistribution study. </LI> <LI> Biological uptake and translocation level of inhaled PHMG was quantified for 1 week. </LI> <LI> Approximately 74% of inhaled PHMG was retained in the lungs 1 week after exposure. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
Shim, Ha Eun,Kim, Do Hee,Lee, Chang Heon,Choi, Dae seong,Lee, Dong-Eun 대한방사성의약품학회 2019 Journal of radiopharmaceuticals and molecular prob Vol.5 No.1
Recently, antibody-like scaffold proteins have received a great deal of interest in diagnosis and therapy applications because of their intrinsic features that are often required for tumor imaging and therapy. Intrinsic issues that are associated with therapeutic application of antibody-like scaffold proteins, particularly in cancer treatment, include an efficient and straightforward radiolabeling for understanding in vivo biodistribution and excretion route, and monitoring therapeutic responses. Herein, we report an efficient and straightforward method for radiolabeling of antibody-like scaffold proteins with the $[^{99m}Tc(OH_2)_3(CO)_3]^+$ ($^{99m}Tc$-tricarbonyl) by using a site-specific direct labeling method via hexahistidine-tag, which is a widely used for general purification of recombinant proteins with His-affinity chromatography. Repebody is a new class of antibody-like scaffold protein that consists of highly diverse leucine-rich repeat (LRR) modules. Although all possible biomedical applications with repebody are ongoing, it's in vivo biodistribution and excretion pathway has not yet been explored. In this study, hexahistidine ($His_6$)-tag bearing repebody (rEgH9) was labeled with [$^{99m}Tc$]-tricarbonyl. Repebody protein was radiolabeled with high radiolabeling efficiency (>90%) and radiolabeled compound was more than 99% pure after purification. These results clearly demonstrate that the present radiolabeling method will be useful molecular imaging study.