http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
고익환 ( Ko Ick Hwan ),강신욱 ( Kang Shin Uk ),정태성 ( Cheong Tae Sung ),황만하 ( Hwang Man Ha ) 한국농공학회 2006 한국농공학회 학술대회초록집 Vol.2006 No.-
Existing methods for channel routing have a problem that the reservoir outflow for the demands is overestimated for considering the loss related in delay. K-MODSIM model use the backrouting algorithm to calculate optimal outflow for the demands which calculation is made by iteration method. The results show that the K-MODSIM model is in good agreement with the outflow data obtained in the Geam River basin.
실시간 물 관리 운용을 위한 유역 유출 모의 모형 개발
황만하 ( Hwang Man-ha ),맹승진 ( Maeng Sung-jin ),고익환 ( Ko Ick-hwan ),박정인 ( Park Jeong-in ),류소라 ( Ryoo So-ra ) 한국농공학회 2003 한국농공학회 학술대회초록집 Vol.2003 No.-
The development of a basin-wide runoff analysis model is to analysis monthly and daily hydrologic runoff components including surface runoff, subsurface runoff, return flow, etc. at key operation station in the targeted basin. A short-term water demand forecasting technology will be developed taking into account the patterns of municipal, industrial and agricultural water uses. For the development and utilization of runoff analysis model, relevant basin information including historical precipitation and river water stage data, geophysical basin characteristics, and water intake and consumptions needs to be collected and stored into the hydrologic database of Integrated Real-time Water Information System. The well-known SSARR model was selected for the basis of continuous daily runoff model for forecasting short and long-term natural flows.
Lee, Jea Hwang,Park, Ki Jun,Jang, Jun Ki,Jeon, Yeong Ha,Ko, Kwan Young,Kwon, Joon Hyun,Lee, Seung-Rock,Kim, Ick Young American Society for Biochemistry and Molecular Bi 2015 The Journal of biological chemistry Vol.290 No.50
<P>Cytosolic valosin-containing protein (p97(VCP)) is translocated to the ER membrane by binding to selenoprotein S (SelS), which is an ER membrane protein, during endoplasmic reticulum-associated degradation (ERAD). Selenoprotein K (SelK) is another known p97(VCP)-binding selenoprotein, and the expression of both SelS and SelK is increased under ER stress. To understand the regulatory mechanisms of SelS, SelK, and p97(VCP) during ERAD, the interaction of the selenoproteins with p97(VCP) was investigated using N2a cells and HEK293 cells. Both SelS and SelK co-precipitated with p97(VCP). However, the association between SelS and SelK did not occur in the absence of p97(VCP). SelS had the ability to recruit p97(VCP) to the ER membrane but SelK did not. The interaction between SelK and p97(VCP) did not occur in SelS knockdown cells, whereas SelS interacted with p97(VCP) in the presence or absence of SelK. These results suggest that p97(VCP) is first translocated to the ER membrane via its interaction with SelS, and then SelK associates with the complex on the ER membrane. Therefore, the interaction between SelK and p97(VCP) is SelS-dependent, and the resulting ERAD complex (SelS-p97(VCP)-SelK) plays an important role in ERAD and ER stress.</P>
Lee, Jea Hwang,Kwon, Joon Hyun,Jeon, Yeong Ha,Ko, Kwan Young,Lee, Seung-Rock,Kim, Ick Young American Society for Biochemistry and Molecular Bi 2014 The Journal of biological chemistry Vol.289 No.20
<P>During endoplasmic reticulum (ER)-associated degradation, p97(VCP) is recruited to the ER membrane through interactions with transmembrane proteins, such as selenoprotein S (SelS), selenoprotein K (SelK), hrd1, and gp78. SelS has a single-spanning transmembrane domain and protects cells from ER stress-induced apoptosis through interaction with p97(VCP). The cytosolic tail of SelS consists of a coiled-coil domain, a putative VCP-interacting motif (VIM), and an unpronounced glycine- and proline-rich secondary structure. To understand the regulatory mechanism of SelS during ER stress, we investigated the interaction of the protein with p97(VCP) using mouse neuroblastoma cells and human embryonic kidney 293 cells. The SelS expression level increased when ER stress was induced. In addition, the effect of ER stress was enhanced, and recruitment of p97(VCP) to the ER membrane was inhibited in SelS knockdown cells. The effect of SelS knockdown was rescued by ectopic expression of SelS U188C. p97(VCP) interacted with SelS U188C and was recruited to the ER membrane. The expression of SelS[ΔVIM], which is a VIM deletion mutant of SelS, also showed both a recovery effect and an interaction with p97(VCP) in cells. However, mutants in which the proline residue positions 178 or 183 of SelS were changed to alanine or were deleted did not interact with p97(VCP). The proline mutants did not rescue ER stress in SelS knockdown cells. These results suggest that both Pro<SUP>178</SUP> and Pro<SUP>183</SUP> of SelS play important roles in the translocation of p97(VCP) to the ER membrane and protect cells from ER stress.</P>