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Optimal Calibration for Rotating Analyzer Ellipsometer
Sunglim Park,DaeGab Gweon 대한기계학회 2005 JOURNAL OF MECHANICAL SCIENCE AND TECHNOLOGY Vol.19 No.11S
We have modeled most errors, which affect the measurement accuracy, with Jone’s matrix. From the simulation, we can characterize the errors and take good aids for selecting components and designing ellipsometer. The traditional residual method has good performance when there are only azimuth angle errors and extinction errors, but it has not good performance when there are other errors. We have proposed the optimal calibration method for overcoming the residual method. The optimal method selects error values to have the least square difference between the measured thickness and the simulated thickness. We can reduce the design variables to three, incident angle error, and azimuth angle errors of polarizer and analyzer. The optimization results are slightly different from the residual method, and have smaller standard deviation of errors than the residual method. The experiment shows good agreement with the simulations.
Redox Regulation Facilitates Optimal Peptide Selection by MHC Class I during Antigen Processing
Park, Boyoun,Lee, Sungwook,Kim, Eunkyung,Cho, Kwangmin,Riddell, Stanley R.,Cho, Sunglim,Ahn, Kwangseog Elsevier 2006 Cell Vol.127 No.2
<P><B>Summary</B></P><P>Activated CD8<SUP>+</SUP> T cells discriminate infected and tumor cells from normal self by recognizing MHC class I-bound peptides on the surface of antigen-presenting cells. The mechanism by which MHC class I molecules select optimal peptides against a background of prevailing suboptimal peptides and in a considerably proteolytic ER environment remained unknown. Here, we identify protein disulfide isomerase (PDI), an enzyme critical to the formation of correct disulfide bonds in proteins, as a component of the peptide-loading complex. We show that PDI stabilizes a peptide-receptive site by regulating the oxidation state of the disulfide bond in the MHC peptide-binding groove, a function that is essential for selecting optimal peptides. Furthermore, we demonstrate that human cytomegalovirus US3 protein inhibits CD8<SUP>+</SUP> T cell recognition by mediating PDI degradation, verifying the functional relevance of PDI-catalyzed peptide editing in controlling intracellular pathogens. These results establish a link between thiol-based redox regulation and antigen processing.</P>
이성림(Sunglim Lee),박근수(Kunsoo Park) 한국정보과학회 2003 한국정보과학회 학술발표논문집 Vol.30 No.2Ⅰ
접미사 배열은 긴 문자열에 대해 효율적인 문자열 검색을 가능하게 하는 자료구조이다. 접미사 배열은 무자열의 접미사들의 사전식 정렬순서를 배열로 저장한다. 비슷한 효과를 가진 접미사 트리에 비해서 접미사 배열은 저장 공간을 적게 차지하기 때문에 생명정보과학의 염기 서열 등 큰 크기의 문자열의 처리에 더욱 유리하다. 본 논문에서는 2003년에 발표된 Ko-Aluru, K□rkk□inen-Sanders 및 기존의 Manber-Myers 등 세 개의 접미사 배열 생성 알고리즘들의 염기 서열 입력 자료에 대한 실행 시간 및 기억 장치 사용량을 실험을 통해 비교한다. 특히 Ko-Aluru와 K□rkk□inen-Sanders 알고리즘을 실행 시간 및 저장 공간의 이론적인 복잡도가 O(n)으로 동일하기 때문에 실험을 통해서 계산 복잡도에 숨어있는 상수를 비교한다. 실험 결과 K□rkk□inen-Sanders 알고리즘이 가장 효율적임을 보인다.
Human Cytomegalovirus UL18 Utilizes US6 for Evading the NK and T-Cell Responses
Kim, Youngkyun,Park, Boyoun,Cho, Sunglim,Shin, Jinwook,Cho, Kwangmin,Jun, Youngsoo,Ahn, Kwangseog Public Library of Science 2008 PLoS pathogens Vol.4 No.8
<▼1><P>Human cytomegalovirus (HCMV) US6 glycoprotein inhibits TAP function, resulting in down-regulation of MHC class I molecules at the cell surface. Cells lacking MHC class I molecules are susceptible to NK cell lysis. HCMV expresses UL18, a MHC class I homolog that functions as a surrogate to prevent host cell lysis. Despite a high level of sequence and structural homology between UL18 and MHC class I molecules, surface expression of MHC class I, but not UL18, is down regulated by US6. Here, we describe a mechanism of action by which HCMV UL18 avoids attack by the self-derived TAP inhibitor US6. UL18 abrogates US6 inhibition of ATP binding by TAP and, thereby, restores TAP-mediated peptide translocation. In addition, UL18 together with US6 interferes with the physical association between MHC class I molecules and TAP that is required for optimal peptide loading. Thus, regardless of the recovery of TAP function, surface expression of MHC class I molecules remains decreased. UL18 represents a unique immune evasion protein that has evolved to evade both the NK and the T cell immune responses.</P></▼1><▼2><P><B>Author Summary</B></P><P>HCMV establishes a lifelong latent infection and causes serious disease in immunocompromised individuals. Cytotoxic T lymphocytes (CTL) and natural killer (NK) cells are the primary effectors for the immune defense against HCMV. However, HCMV has evolved to evade both the innate and adaptive cellular immunity to viral infection. HCMV US6 glycoprotein inhibits TAP function, resulting in down-regulation of MHC class I, while HCMV UL18 is an MHC class I homolog that functions as a surrogate to prevent host cell lysis. Despite significant sequence and structural homology between UL18 and MHC class I molecules, US6 down regulates surface expression of MHC class I, but not UL18. Here, we describe a mechanism by which UL18 circumvents the self-derived TAP inhibitor, US6. UL18 abrogates US6 inhibition of TAP-ATP binding and restores TAP-mediated peptide translocation, thereby making peptides available for the assembly and subsequent surface expression of UL18. Together UL18 and US6 inhibit binding of MHC class I to TAP, thus down regulating surface expression of MHC class I molecules. UL18 represents a unique immune evasion protein resistant to both the NK and T cell immune responses. Our data provide a molecular basis for persistent HCMV infection and will aid in the development of a therapeutic vaccine.</P></▼2>
Kim, Jaemin,Chae, Daehwan,Lee, Wi Hyoung,Park, Janghoon,Shin, Jaehak,Kwon, Byeong-Chan,Ko, Sunglim Elsevier 2018 ORGANIC ELECTRONICS Vol.59 No.-
<P><B>Abstract</B></P> <P>Thin film transistors (TFTs) constitute important components employed in several printed electronic applications. Many electronic devices comprise TFTs, and their performances are determined by transistor specifications. As such, the optimum performance of a TFT assumes paramount importance in electronic applications. This paper reports the enhanced performance of an organic TFT (OTFT) achieved through use of the structural scaling technique employed during the gravure printing process. Extremely thin 30 nm-thick gravure printed Ag was used as source-drain electrodes while dielectric and semiconductor layers were gravure printed using D series and SP series from Merck, respectively. By scaling thicknesses of the source–drain electrode and dielectric layer, the electrical performance of an OTFT was found to have improved, during the roll-to-roll gravure printing process, in terms of an enhanced mobility of 0.295 cm<SUP>2</SUP> V<SUP>-1</SUP> s<SUP>-1</SUP> and an on–off current ratio of 10<SUP>6</SUP>. Additionally, OTFTs fabricated using the proposed roll-to-roll gravure printing process exhibit a yield percentage of 95% with a maximum operating speed of 15 m min<SUP>−1</SUP>. Furthermore, the OTFT demonstrated uniform electrical characteristics owing to use of an amorphous polymer semiconductor, which reduces the variability of each transistor.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Sharp channel length and pattern edge were appropriately fulfilled by high printing speed of 15 m min<SUP>−1</SUP>. </LI> <LI> The study fabricated OTFT devices by employing a 3-layer roll-to-roll and single-layer inkjet printing processes. </LI> <LI> Highly thin about 30 nm-thick Ag source–drain electrode layer contributes to an enhanced yield percentage. </LI> <LI> Roll-to-roll gravure and inkjet printed OTFT shows excellent performance compared with other previous study of solution processed polymer OTFT. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>