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팩시밀리의 主機板에 對한 技能的 試驗機의 設計 및 具現
김신택,이재훈,김명선,김한상,민형복 成均館大學校 科學技術硏究所 1992 論文集 Vol.43 No.2
본 연구는 팩시밀리의 주기판(main board)을 기능적으로 테스트하기 위해 구현한 FFTS(Functional Facsimile Test System)에 대한 기술이다. 본 연구의 목적은, 테스트시 수반되는 모든 작업을 자동화하고, 테스트 수행중 발생하는 여러가지 상태들을 자료화하는 것이다. 아울러 주기판에 대한 입출력 신호들의 종류와 그 특성들이 변경될 경우라도 소프트웨어의 수정만으로 그 것에 대처한 후 계속적으로 테스트를 수행할 수 있도록 한다. FFTS는 주기판에 접속되는 여러가지 장치들을 하드웨어적으로 에물레이션하며, 테스트용 전용언어, 그리고 그것에 대한 컴파일러를 포함한다. FFTS로 테스트를 수행하는 방법에는 대화식 모드(IAT)와 대화식 테스트에서 수행할 수 있는 모든 과정을 테스트용 언어로 저장한 후 그것을 반복하여 사용하는 배치 모드(Batch mode) 등이 있다. FFTS의 유용성을 실증하기 위해 여러 종류의 팩시밀리에 대하여 실험을 실시하였다. FFTS (Functional Facsimile Test System) is designed and implemented. It is possible to eliminate repeated test work and to analyze the data obtained through test. If the specification of the signals from/to main board of facsmile is changed, it is possible to cope with the change by modification of FFTS software. FFTS emulates the devices connected to the main board. FFTS is designed to test the main board either by using interactive(IAT) mode with graphic user interface or by using noninteractive(NIAT) mode with test command file which is coded manually or created from IAT mode. The operation of the FITS is verified for several types of main board of G3 class facsmiles.
플립플롭의 초기화 가능성을 고려한 디지털 회로에 대한 고장 검출율의 평가 기법
閔炯福,李宰勳,金信澤 성균관대학교 1998 학술회의지원논문목록집 Vol.1998 No.-
디지탈 회로의 검사 신호에 대한 고장 검출율을 정확하게 계산하기 위해 결함 시뮬레이터를 사용한다. 그러나 결함 시뮬레이터의 실행 시간은 회로를 구성하는 게이트 수의 제곱에 비례하여 오늘날의 대규모 회로에서는 많은 CPU 시간을 소모한다. 따라서 정확도는 떨어지지만 비교적 짧은 시간 안에 회로의 검사성을 평가하기 위한 검사성 분석 알고리즘이 제안되었다. COP는 빠르고 정확하느 순차회로에 적용할 수 없으며 STAFAN은 순차회로에 적용이 가능하지만 정상 회로 시뮬레이션의 사용으로 실행시간이 많이 소모된다. 본 저자들은 정확한 고장 검출율을 단시간에 얻기 위해서 EXTASEC을 제안한 바 있다. EXTASEC은 극히 일부 회로에서 정확도가 떨어지는 현상이 발생하였으며, 이 논문에서는 EXTASEC의 문제가 플립플롭의 초기화와 관련이 있는 것을 밝히고, 개선된 알고리즘 ITEM을 제안한다. ITEM은 후진선의 반복적 계산과 초기화되지 않는 플립플롭에 대한 분석으로 고장 검출율을 정확하고 빠르게 얻을 수가 있었다. Fault simulator has been used 10 compute exact Fault coverages of test vectors lor digital circuit. But it is time consuming because execution time is proportional to square of circuit size. Recently, several algorithms for testability analysis have been published to cope with these problems. COP iS very fast and accurate but cannot be used for sequential circuits, while STAFAN can be used for sequential circuits but nerds vast amount of execution time due to good circuit simulation. We proposed EXTASEC which gave fast and accurate fault coverage. But it shows noticeable errors fora few sequential circuits. In this paper, it 1s shown that the inaccuracy is due to uninitializable flipflops, and we propose ITEM to improve the EXTASEC algorithm. ITEM iS an improved evaluation method of fault coverage by analysis of backward lines and uninitializable flipflops. It is expected to perform efficiently for very large circuits where execution time is critical.
평판과 보의 연성구조물의 진동에너지 전달특성 분석에 관한 연구
김정태,이형택 弘益大學校 科學技術硏究所 1989 科學技術硏究論文集 Vol.9 No.1
The transmission of sound and vibration through structures is of interest in many noise control problems, including architectural acoustics, sound transmission through air craft, spacecraft and ship, and transmission of noise through machinery and engine enclosures. Statistical Energy Analysis provides a simple and accurate method of approaching these problems. In this paper, comparing the measured coupling loss factor of plate-beam with measured coupling loss factor of mass on the junction will be inspected.
Lee, Young Hun,Park, Jun Hyoung,Cheon, Dong Huey,Kim, Taeyoung,Park, Yae Eun,Oh, Eok-Soo,Lee, Ji Eun,Lee, Seung-Taek Portland Press Ltd. 2017 Biochemical journal Vol. No.
<P>Syndecans (SDCs) are transmembrane proteoglycans that are involved in cell adhesion and cell communication. Specifically, SDC2 plays a key role in tumorigenesis, metastasis, and angiogenesis. Previously, we found that rat SDC2 is shed by matrix metalloproteinase-7 (MMP-7) in colon cancer cells. Here, we analyzed the susceptibility of rat SDC2 to various MMPs. We found that the rat SDC2 ectodomain (ECD) fused to the C-terminal Fc region, which was expressed in mammalian cells, was cleaved more efficiently by MMP-14 than MMP-7. Likewise, when anchored on the surface of HeLa cells, rat SDC2 was cleaved more efficiently by the treatment of MMP-14 than MMP-7 and was shed more readily by membrane-anchored MMP-14 than soluble MMP-14. Furthermore, MMP-14 cleaved recombinant SDC2-ECD expressed in <I>Escherichia coli</I> into multiple fragments. Using N-terminal amino acid sequencing and the top-down proteomics approach, we determined that the major cleavage sites were S<SUP>88</SUP>↓L<SUP>89</SUP>, T<SUP>98</SUP>↓M<SUP>99</SUP>, T<SUP>100</SUP>↓L<SUP>101</SUP>, D<SUP>132</SUP>↓P<SUP>133</SUP>, and N<SUP>148</SUP>↓L<SUP>149</SUP> for rat SDC2-ECD and S<SUP>55</SUP>↓G<SUP>56</SUP>, S<SUP>65</SUP>↓P<SUP>66</SUP>, P<SUP>75</SUP>↓K<SUP>76</SUP>, N<SUP>92</SUP>↓I<SUP>93</SUP> D<SUP>122</SUP>↓P<SUP>123</SUP>, and S<SUP>138</SUP>↓L<SUP>139</SUP> for human SDC2-ECD. Finally, the rat and human SDC2-ECD lost the ability to suppress vascular endothelial growth factor-induced formation of capillary-like tubes by human umbilical vein endothelial cells following cleavage by MMP-14, but its major cleavage-site mutant of rat SDC2-ECD did not. These results suggest that MMP-14 is a novel enzyme responsible for degrading SDC2 and impairing its physiological roles including angiogenesis.</P>
Lee, Jae Taek,Lee, Seung Sik,Mondal, Suvendu,Tripathi, Bhumi Nath,Kim, Siu,Lee, Keun Woo,Hong, Sung Hyun,Bai, Hyoung-Woo,Cho, Jae-Young,Chung, Byung Yeoup Korean Society for Molecular and Cellular Biology 2016 Molecules and cells Vol.39 No.8
Alkyl hydroperoxide reductase subunit C from Pseudomonas aeruginosa PAO1 (PaAhpC) is a member of the 2-Cys peroxiredoxin family. Here, we examined the peroxidase and molecular chaperone functions of PaAhpC using a site-directed mutagenesis approach by substitution of Ser and Thr residues with Cys at positions 78 and 105 located between two catalytic cysteines. Substitution of Ser with Cys at position 78 enhanced the chaperone activity of the mutant (S78C-PaAhpC) by approximately 9-fold compared with that of the wild-type protein (WT-PaAhpC). This increased activity may have been associated with the proportionate increase in the high-molecular-weight (HMW) fraction and enhanced hydrophobicity of S78C-PaAhpC. Homology modeling revealed that mutation of $Ser^{78}$ to $Cys^{78}$ resulted in a more compact decameric structure than that observed in WT-PaAhpC and decreased the atomic distance between the two neighboring sulfur atoms of $Cys^{78}$ in the dimer-dimer interface of S78C-PaAhpC, which could be responsible for the enhanced hydrophobic interaction at the dimer-dimer interface. Furthermore, complementation assays showed that S78C-PaAhpC exhibited greatly improved the heat tolerance, resulting in enhanced1 survival under thermal stress. Thus, addition of Cys at position 78 in PaAhpC modulated the functional shifting of this protein from a peroxidase to a chaperone.
Lee, Chan Hyoung,Kim, Hee Taek,Yun, Eun Ju,Lee, Ah Reum,Kim, Sa Rang,Kim, Jae-Han,Choi, In-Geol,Kim, Kyoung Heon American Society for Microbiology 2014 Applied and environmental microbiology Vol.80 No.19
<P>Marine red macroalgae have emerged to be renewable biomass for the production of chemicals and biofuels, because carbohydrates that form the major component of red macroalgae can be hydrolyzed into fermentable sugars. The main carbohydrate in red algae is agarose, and it is composed of <SMALL>d</SMALL>-galactose and 3,6-anhydro-<SMALL>l</SMALL>-galactose (AHG), which are alternately bonded by β1-4 and α1-3 linkages. In this study, a novel β-galactosidase that can act on agarooligosaccharides (AOSs) to release galactose was discovered in a marine bacterium (<I>Vibrio</I> sp. strain EJY3); the enzyme is annotated as <I>Vibrio</I> sp. EJY3 agarolytic β-galactosidase (<I>Vej</I>ABG). Unlike the <I>lacZ</I>-encoded β-galactosidase from <I>Escherichia coli</I>, <I>Vej</I>ABG does not hydrolyze common substrates like lactose and can act only on the galactose moiety at the nonreducing end of AOS. The optimum pH and temperature of <I>Vej</I>ABG on an agarotriose substrate were 7 and 35°C, respectively. Its catalytic efficiency with agarotriose was also similar to that with agaropentaose or agaroheptaose. Since agarotriose lingers as the unreacted residual oligomer in the currently available saccharification system using β-agarases and acid prehydrolysis, the agarotriose-hydrolyzing capability of this novel β-galactosidase offers an enormous advantage in the saccharification of agarose or agar in red macroalgae for its use as a biomass feedstock for fermentable sugar production.</P>
Jin-Hyoung Cho,Dong-Hoon Kwak,Kyu-Tae Chang,Ji-Su Kim,Jae-Sung Ryu,So-Dam Lee,So-Hyun Lee,Ju-Taek Lee,Da-Hyun Park,Seul-Yi Lee,Young-Choon Lee,Young-kug Choo 한국당과학회 2010 한국당과학회 학술대회 Vol.2010 No.1
Ganglioside are ubiquitous membrane component in mammalian cells and suggested to play important roles in various cell functions such as cell-cell recognition, differentiation and transmembrane signaling. These compounds are localized in a glycosphingolipid-enriched microdomain on the cell surface and regulated by the glycosphingolipid composition. However, the role that gangliosides play in immune rejection response by xenotransplantation is not yet clearly understood. In this study, differential expression patterens of gangliosides between human vein endothelial cells (ECV304) and micro-pig aortic endothelial cells (MPAECs, primary cultured) was investigated. we examined expression level of high-performance thin-layer chromatography (HPTLC) showed that ECV304 cells contained GM3 and GM2 as major gangliosides. However, MPAECs contained only GM3 as major ganglioside. Furthermore, we confirmed that human serum induces cell death of MPAECs. As a results suggest that differential expression patterens of gangliosides of ECV304, MPAECs are related immune rejection response and cell death with xenogeneic serum in xenotransplantation by biomarker. This study was supported by a grant from the Korean Rural Development Administration Agenda Program, 2010030106112200103) and a research grant from the Ministry of Education, Science and Technology (KGC5401011), Republic of Korea.