• 한국진공학회:학술대회논문집
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• 한국진공학회 1999년도 제17회 학술발표회 논문개요집
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• pp.243-243
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• 1999

• 한국표면공학회지
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• 제41권3호
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• pp.83-87
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• 2008

This study described the effects of RF power, DC bias voltage, chamber pressure and gas mixing ratio on the etch rates of TiN thin film and selectivity of TiN thin film to $SiO_2$ with $BCl_3$/Ar gas mixture. When the gas mixing ratio was $BCl_3$(20%)/Ar(80%) with other conditions were fixed, the maximum etch rate of TiN thin film was 170.6 nm/min. When the DC bias voltage increased from -50 V to -200 V, the etch rate of TiN thin film increased from 15 nm/min to 452 nm/min. As the RF power increased and chamber pressure decreased, the etch rate of TiN thin film showed an increasing tendency. When the gas mixing ratio was $BCl_3$(20%)/Ar(80%) under others conditions were fixed, the intensity of optical emission spectra from radical or ion such as Ar(750.4 nm), $Cl^+$(481.9 nm) and $Cl^{2+}$(460.8 nm) was highest. The TiN thin film was effectively removed by the chemically assisted physical etching in $BCl_3$/Ar ICP plasma.

• 한국재료학회:학술대회논문집
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• 한국재료학회 1997년도 한국재료학회 추계학술발표회
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• pp.104-104
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• 1997

• 생명과학회지
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• 제20권9호
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• pp.1409-1414
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• 2010

이 연구는 실험용 쥐를 대상으로 운동에 따라 골격근에서 일어나는 세포고사 경로 중 내인성 경로와 외인성경로에 의해 이루어지는 세포고사의 신호기전을 확인하여 운동이 세포고사에 어떠한 영향을 미치는지에 대한 구명하는데 있다. 이를 위해 ICR계 수컷 흰쥐 20마리를 일주일의 적응기간을 거쳐 통제집단(CON: n=10)과 운동집단(EX: n=10)으로 배정하였다. 운동은 8주간 주 5회 실시하였고, 트레드밀 속도 16.4 m/min와 경사도 4%로 설정하여 40분간 지속적인 운동을 실시하였다. 세포고사의 신호 경로 중 내인성 경로에 대한 검증 결과 Bcl-2, Bax 단백질, 그리고 Bcl-2/ Bax ratio는 그룹간 통계적 유의성은 나타나지 않았다. 반면, 세포고사의 경로 중 외인성 경로에 대한 검증 결과 caspase-8 단백질의 발현은 운동집단이 통제집단보다 유의하게 낮은 것으로 나타났으며(p<0.05), 세포고사 억제 단백질인 HSP70 단백질 발현은 운동집단이 통제집단보다 높게 나타났다. 더욱이, 세포고사 최종인자인 caspase-3의 활성화는 이루어 지지 않은 것으로 관찰되었다. 따라서 세포사멸의 신호경로 중 내인성 경로에 작용하는 Bcl-2와 Bax보다는 외인성 경로인 caspase-8과 HSP70의 영향으로 caspase-3가 분할되지 못하여 세포고사가 일어나지 않은 것으로 사료된다.

• 한국표면공학회지
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• 제42권6호
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• pp.251-255
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• 2009

In this study, the plasma etching of the TaN thin film with $O_2/BCl_3$/Ar gas chemistries was investigated. The equipment for the etching was an inductively coupled plasma (ICP) system. The etch rate of the TaN thin film and the selectivity of TaN to $SiO_2$ and PR was studied as a function of the process parameters, including the amount of $O_2$ added, an RF power, a DC-bias voltage and the process pressure. When the gas mixing ratio was $O_2$(3 sccm)/$BCl_3$(6 sccm)/Ar(14 sccm), with the other conditions fixed, the highest etch rate was obtained. As the RF power and the dc-bias voltage were increased, the etch rate of the TaN thin film was increased. X-ray photoelectron spectroscopy (XPS) was used to investigate the chemical states of the surface of the TaN thin film.

• Transactions on Electrical and Electronic Materials
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• 제12권4호
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• pp.144-147
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• 2011

In this work, we present a study regarding the etching characteristics on titanium nitride (TiN) thin films using an inductively coupled plasma system. The TiN thin film was etched using a $N_2/BCl_3$/Ar plasma. The studied etching parameters were the gas mixing ratio, the radio frequency (RF) power, the direct current (DC)-bias voltages, and the process pressures. The baseline conditions were as follows: RF power = 500 W, DC-bias voltage = -150 V, substrate temperature = $40^{\circ}C$, and process pressure = 15 mTorr. The maximum etch rate and the selectivity of the TiN to the $SiO_2$ thin film were 62.38 nm/min and 5.7, respectively. The X-ray photoelectron spectroscopy results showed no accumulation of etching byproducts from the etched surface of the TiN thin film. Based on the experimental results, the etched TiN thin film was obtained by the chemical etching found in the reactive ion etching mechanism.

• Tuberculosis and Respiratory Diseases
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• 제61권4호
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• pp.366-373
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• 2006

연구배경 : Paraquat는 P-450 reductase에 의해 반응성 산소유리기(ROS)를 발생시켜 세포막, 단백질, 핵산 등과 반응함으로써 세포손상을 유도하며 급성 폐 손상을 일으킨다. 최근 급성 폐 손상 및 급성 호흡곤란 증후군에 있어서 폐상피세포의 아포프토시스가 중요한 역할을 한다고 알려지기 시작하였다. 이에 반응성 산소유리기에 의한 폐 손상의 대표적 물질인 paraquat로 인한 폐상피세포의 세포죽음이 아포프토시스인지 확인하고 dexamethasone, N-acetylcysteine, 그리고 bcl-2가 paraquat로 인한 폐상피 세포죽음에 어떠한 영향을 미치는지 등을 연구하였다. 방법 : 폐상피세포주인 A549와 BEAS-2B 세포주, 그리고 bcl-2 construct를 유전자 주입한 A549 pcDNA3-bcl-2 세포주를 이용하였다. 아포프토시스는 Annexin V assay를 이용하여서 판정하였으며 세포독성 검사는 MTT assay를 이용하였다. Paraquat는 0, $1{\mu}M$, $10{\mu}M$, $100{\mu}$M, 1 mM, 10 mM의 농도로 사용하였다. Dexamethasone은 $1{\mu}M$의 농도로 paraquat 투여 12시간 전에 전처치하였고, N-acetylcysteine은 1 mM의 농도로 paraquat 투여 1시간 전에 전처치하였다. 결과 : 양 세포주 모두에서 paraquat는 농도와 시간 경과에 따라서 세포죽음을 증가시켰고, 이러한 세포죽음은 아포프토시스였다. N-acetylcysteine과 dexamethasone은 시간과 농도에 따라 약간의 차이가 있으나 전반적으로 10~30%의 방어효과가 있었다. Bcl-2를 과발현시킨 A549-bcl-2 세포주에서 A549-neo 세포주에 비해 paraquat에 의한 세포독성이 약 20~30% 정도 차단되었다. 결론 : Paraquat는 폐상피세포에서 아포프토시스를 유도하며, paraquat에 의한 아포프토시스는 마이토콘드리아 경로에 의해 일어날 것으로 추정된다.

• Molecules and Cells
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• 제21권1호
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• pp.1-6
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• 2006

Bcl-2/adenovirus E1B 19 kDa-interacting protein 3 (BNIP3) is a mitochondrial pro-apoptotic protein that has a single Bcl-2 homology 3 (BH3) domain and a COOH-terminal transmembrane (TM) domain. Although it belongs to the Bcl-2 family and can heterodimerize with Bcl-2, its pro-apoptotic activity is distinct from those of other members of the Bcl-2 family. For example, cell death mediated by BNIP3 is independent of caspases and shows several characteristics of necrosis. Furthermore, the TM domain, but not the BH3 domain, is required for dimerization, mitochondrial targeting and pro-apoptotic activity. BNIP3 plays an important role in hypoxia-induced death of normal and malignant cells. Its expression is markedly increased in the hypoxic regions of some solid tumors and appears to be regulated by hypoxia-inducible factor (HIF), which binds to a site on the BNIP3 promoter. Silencing, followed by methylation, of the BNIP3 gene occurs in a significant proportion of cancer cases, especially in pancreatic cancers. BNIP3 also has a role in the death of cardiac myocytes in ischemia. Further studies of BNIP3 should provide insight into hypoxic cell death and may contribute to improved treatment of cancers and cardiovascular diseases.

• Transactions on Electrical and Electronic Materials
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• 제13권3호
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• pp.157-161
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• 2012

In this study, we investigated the etching characteristics of ITO thin films and the effects of inert gases added to $Cl_2/BCl_3$ inductivity coupled plasma. The maximum etch rate of ITO thin film was 130.0 nm/min upon the addition of Ar (6 sccm) to the $Cl_2/BCl_3$ (4:16 sccm) plasma, which was higher than that with He or $N_2$ added to the plasma. The ion bombardment by $Ar^+$ sputtering was due to the relatively low volatility of the by-products formed in the $Cl_2/BCl_3$ (4:16 sccm) plasma. The surface of the etched ITO thin film was characterized by x-ray photoelectron spectroscopy (XPS) and atomic force microscopy (AFM). From the XPS results, it is concluded that the proper addition of Ar and He to the $Cl_2/BCl_3$ plasma removes carbon and by-products from the surface of the etched ITO thin film.

• Molecules and Cells
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• 제24권3호
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• pp.378-387
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• 2007

The Bcl-2 family of proteins interacts at the mitochondria to regulate apoptosis. However, the anti-apoptotic Bcl-2 and $Bcl-X_L$ are not completely localized to the mitochondria. In an attempt to generate Bcl-2 and $Bcl-X_L$ chimeras that are constitutively localized to the mitochondria, we substituted their C-terminal transmembrane tail or both the C-terminal transmembrane tail and the adjacent loop with the equivalent regions from Bak or Bax mutant (BaxS184V) as these regions determine the mitochondrial localization of Bak and Bax. The effects of these substitutions on subcellular localization and their activities were assessed following expression in HeLa and CHO K1 cells. The substitution of the C-terminal tail or the C-terminal tail and the adjacent loop of Bcl-2 with the equivalent regions from Bak or the Bax mutant resulted in its association with the mitochondria. This change in subcellular localization of Bcl-2 chimeras triggered cells to undergo apoptotic-like cell death. The localization of this Bcl-2 chimera to the mitochondria may be associated with the disruption of mitochondrial membrane potential. Unlike Bcl-2, the loop structure adjacent to the C-terminal tail in $Bcl-X_L$ is crucial for its localization. To localize the $Bcl-X_L$ chimeras to the mitochondria, the loop structure next to the C-terminal tail in $Bcl-X_L$ protein must remain intact and cannot be substituted by the loop from Bax or Bak. The chimeric $Bcl-X_L$ with both its C-terminal tail and the loop structure replaced by the equivalent regions of Bak or Bax mutant localized throughout the entire cytosol. The $Bcl-X_L$ chimeras that are targeted to the mitochondria and the wild type $Bcl-X_L$ provided same protection against cell death under several death inducing conditions.