http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Shin, Jaeil,Lou, Xiaochu,Kweon, Dae-Hyuk,Shin, Yeon-Kyun Biochemical Society 2014 The Biochemical journal Vol.459 No.1
<P>SNAREpins must be formed between two membranes to allow vesicle fusion, a required process for neurotransmitter release. Although its post-fusion structure has been well characterized, pre-fusion conformations have been elusive. We used single-molecule FRET and EPR to investigate the SNAREpin assembled between two nanodisc membranes. The SNAREpin shows at least three distinct dynamic states, which might represent pre-fusion intermediates. Although the N-terminal half above the conserved ionic layer maintains a robust helical bundle structure, the membrane-proximal C-terminal half shows high FRET, representing a helical bundle (45%), low FRET, reflecting a frayed conformation (39%) or mid FRET revealing an as-yet unidentified structure (16%). It is generally thought that SNAREpins are trapped at a partially zipped conformation in the pre-fusion state, and complete SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor) assembly happens concomitantly with membrane fusion. However, our results show that the complete SNARE complex can be formed without membrane fusion, which suggests that the complete SNAREpin formation could precede membrane fusion, providing an ideal access to the fusion regulators such as complexins and synaptotagmin 1.</P>
Yang, Yoosoo,Shin, Jae Yoon,Oh, Jung-Mi,Jung, Chang Hwa,Hwang, Yunha,Kim, Sehyun,Kim, Jun-Seob,Yoon, Kee-Jung,Ryu, Ji-Young,Shin, Jaeil,Hwang, Jae Sung,Yoon, Tae-Young,Shin, Yeon-Kyun,Kweon, Dae-Hyuk National Academy of Sciences 2010 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.107 No.51
<P>Neuronal SNARE proteins mediate neurotransmitter release at the synapse by facilitating the fusion of vesicles to the presynaptic plasma membrane. Cognate v-SNAREs and t-SNAREs from the vesicle and the plasma membrane, respectively, zip up and bring about the apposition of two membranes attached at the C-terminal ends. Here, we demonstrate that SNARE zippering can be modulated in the midways by wedging with small hydrophobic molecules. Myricetin, which intercalated into the hydrophobic inner core near the middle of the SNARE complex, stopped SNARE zippering in motion and accumulated the trans-complex, where the N-terminal region of v-SNARE VAMP2 is in the coiled coil with the frayed C-terminal region. Delphinidin and cyanidin inhibited N-terminal nucleation of SNARE zippering. Neuronal SNARE complex in PC12 cells showed the same pattern of vulnerability to small hydrophobic molecules. We propose that the half-zipped trans-SNARE complex is a crucial intermediate waiting for a calcium trigger that leads to fusion pore opening.</P>
Adaptive Paired Page Prebackup Scheme for MLC NAND Flash Memory
Jaeil Lee,Dongkun Shin IEEE 2014 IEEE transactions on computer-aided design of inte Vol.33 No.7
<P>Multilevel cell (MLC) NAND flash memory is more cost effective compared with single-level cell NAND flash memory as it can store two or more bits in a memory cell. However, in MLC flash memory, a programming operation can corrupt the paired page under abnormal termination. In order to solve the paired page problem, a backup scheme is generally used, which inevitably causes performance degradation and shortens the lifespan of flash memory. In this paper, we propose a more efficient paired page prebackup scheme for MLC flash memory. It adaptively exploits interleaving, copyback operations, and parity data to reduce the prebackup overhead. In experiments, the proposed scheme reduced the backup overhead by up to 78%.</P>
Synaptotagmin-1 Is an Antagonist for Munc18-1 in SNARE Zippering
Lou, Xiaochu,Shin, Jaeil,Yang, Yoosoo,Kim, Jaewook,Shin, Yeon-Kyun American Society for Biochemistry and Molecular Bi 2015 The Journal of biological chemistry Vol.290 No.16
<P>In neuroexocytosis, SNAREs and Munc18-1 may consist of the minimal membrane fusion machinery. Consistent with this notion, we observed, using single molecule fluorescence assays, that Munc18-1 stimulates SNARE zippering and SNARE-dependent lipid mixing in the absence of a major Ca<SUP>2+</SUP> sensor synaptotagmin-1 (Syt1), providing the structural basis for the conserved function of Sec1/Munc18 proteins in exocytosis. However, when full-length Syt1 is present, no enhancement of SNARE zippering and no acceleration of Ca<SUP>2+</SUP>-triggered content mixing by Munc18-1 are observed. Thus, our results show that Syt1 acts as an antagonist for Munc18-1 in SNARE zippering and fusion pore opening. Although the Sec1/Munc18 family may serve as part of the fusion machinery in other exocytotic pathways, Munc18-1 may have evolved to play a different role, such as regulating syntaxin-1a in neuroexocytosis.</P>
XML 전자서명을 지원하는 XML 기반 전자상거래 시스템의 설계 및 구현
김세영(Seyoung Kim),이재일(Jaeil Lee),박정환(Junghwan Park),신동규(Dongkyoo Shin) 한국정보과학회 2001 한국정보과학회 학술발표논문집 Vol.28 No.2Ⅰ
정보통신 기술의 비약적인 발전으로 인해 인터넷은 현재 필수 불가결한 생활의 도구가 되고 있으며, 개인 및 기업에서의 인터넷 활용이 급증함에 따라 인터넷 그 자체를 사업수담으로 이용하여 추세가 가속화되고 있다. 또한, 최근 차세대 웹 표준문서 포맷으로 부상되고 있는 XML(eXtensible Markup Language)을 사용한 B2B 전자상거래 표준인 ebXML(e-business eXtensible Markup Language), Microsoft의 Biztalk Framework, CommerceNet의 eCo Framework, XML/EDI 등의 개발이 활발히 진행되고 있다. 이에 본 논문에서는 기업 간 문서교환을 위한 XML 전자상거래 시스템을 구현하고, 전체 시스템 내에서 보안상의 요구를 충족하기 위하여 W3C(World Wide Web Consortium)의 XML 전자서명(Xml-Dsig : Disital Signature) 표준에 입각한 기업 간 문서 교환시의 인증 및 보안을 위한 시스템을 설계하였다.