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숙명박물관 브랜드 프로모션을 위한 통합적 브랜드 개발 -2D, 3D, 4D 디자인 프로세스를 중심으로-
길혜경,김보현,오정은,이서연,이지원,이진민,장미정,이성애 숙명여자대학교 산업디자인연구소 2017 숙명디자인학 연구 Vol.24 No.-
본 연구는 여성생활사 중심의 유물 박물관인 숙명박물관의 인지도와 브랜딩의 문제를 해결하기 위해 브랜드·스페이스·마케팅을 활용한 통합 브랜드 개발 프로세스를 제안하는데 목적이 있다. 아울러 본 연구는 박물관의 브랜드를 프로모션하고 그래픽, 제품, 공간의 통합 브랜드를 구축하는 일련의 프로세스를 밝히는데 목적이 있다. 이에 본 연구의 시간적 범위는 2017년 3월부터 6월까지 총 15주간 숙명여대 환경디자인학과 <브랜드·스페이스·마케팅>수업에서 진행된 수업의 결과물로서 4개 팀 중, 1개 팀의 작업물로 한다. 본 연구의 대상적 범위는 ‘숙명여자대학교 숙명박물관'의 2D~4D까지의 전반으로 설정한다. 그 결과, 제품부터 공간까지 숙명박물관의 통합된 브랜딩은 일 관성과 객관성, 스토리성을 얻을 수 있었다. ’숙명박물관'은 학교의 박물관이라는 장점을 극대화시켜 가치와 스토리를 부여하고 하나의 브랜드로 리뉴얼했다는 점에서 의의가 있다. 또한 향후 보편적인 박물관들의 차별화된 브랜드 개발의 참고자료로 활용될 수 있을 것으로 기대하며 브랜드 개발에 있어서 G·I, P·I, S·I의 통합 브랜드 메뉴의 기초 자료로 활용될 것으로 사료된다.
Investigation of persistent infection with bovine viral diarrhea in Korean native cattle
Hye-Young Jeoung(Hye-Young Jeoung),Eun-Yong Lee(Eun-Yong Lee),Se-Jin Park(Se-Jin Park),Hyung-Woo Kang(Hyung-Woo Kang),Ji-Young Park(Ji-Young Park),Kyoung-Ki Lee(Kyoung-Ki Lee),Bok-Kyung Ku(Bok-Kyung K 한국예방수의학회 2022 한국예방수의학회 학술대회자료집 Vol.2022 No.-
Molecular characterization and variability of the genes from EHV-1 in Korea
Hye-young Jeoung(Hye-young Jeoung),Hyung-Woo Kang(Hyung-Woo Kang),Eun-Yong Lee(Eun-Yong Lee),Kyoung-Ki Lee(Kyoung-Ki Lee),Ji-Young Park(Ji-Young Park),Bok-Khyung Ku(Bok-Khyung Ku) 한국예방수의학회 2022 한국예방수의학회 학술대회자료집 Vol.2022 No.-
Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates
Lee, Eun-Jeoung,Shin, Sung-Hwa,Hyun, Sung-Hee,Chun, Jae-Sun,Kang, Sang-Sun The Korean Society for Integrative Biology 2011 Animal cells and systems Vol.15 No.2
The transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, is expressed in a broad range of tissues. Nitric oxide (NO) as a gaseous signal mediator shows a variety of important biological effects. In many instances, NO has been shown to exhibit its activities via a protein S-nitrosylation mechanism in order to regulate its protein functions. With functional assays via site-directed mutagenesis, we demonstrate herein that NO induces the S-nitrosylation of TRPV4 $Ca^{2+}$ channel on the $Cys^{853}$ residue, and the S-nitrosylation of $Cys^{853}$ reduced its channel sensitivity to 4-${\alpha}$ phorbol 12,13-didecanoate and the interaction between TRPV4 and calmodulin. A patch clamp experiment and $Ca^{2+}$ image analysis show that the S-nitrosylation of $Cys^{853}$ modulates the TRPV4 channel as an inhibitor. Thus, our data suggest a novel regulatory mechanism of TRPV4 via NO-mediated S-nitrosylation on its $Cys^{853}$ residue.
Regulation of Nek6 Functions by Its SUMOylation on the $K^{252}$ Residue
Lee, Eun-Jeoung,Hyun, Sung-Hee,Chun, Jae-Sun,Shin, Sung-Hwa,Lee, Kyung-Eun,Park, In-Suk,Kang, Sang-Sun The Korean Society for Integrative Biology 2007 Integrative biosciences Vol.11 No.2
Nek6 belongs to NIMA1 (never in mitosis, gene A) related kinase, which was originally identified in Aspergillus nidulans as a serine/threonine kinase critical for cell cycle progression. We noticed that the putative SUMOylation site is localized on the $K^{252}$ residue in $^{251}FKsD^{254}$ of Nek6, based on the consensus sequence ${\Phi}KxE$; where ${\Phi}$ represents L, I, V or F and x is any amino acid. We observed that the Nek6 SUMO mutant (K252R) has decreased protein kinase activity, nuclear speckle localization and protein stability, compared with that of the Nek6 wild type. However, the Nek6 SUMO mutant increased the cell survival rate of COS-1 cells as determined by FACS analysis. Therefore, our data suggest that SUMOylation on the $K^{252}$ residue of Nek6 is required for its normal functions, such as proper nuclear localization, kinase activity and protein stability, to control cell cycle.
Lee, Eun-Jeoung,Hyun, Sung-Hee,Chun, Jae-Sun,Ahn, Hye-Rim,Kang, Sang-Sun The Korean Society for Integrative Biology 2007 Integrative biosciences Vol.11 No.1
Tau plays a role in numerous neuronal processes, such as vesicle transport, microtubule-plasma membrane interaction and intracellular localization of proteins. SUMO (Small Ubiquitin-like Modifier) modification (SUMOylation) appears to regulate diverse cellular processes including nuclear transport, signal transduction, apoptosis, autophagy, cell cycle control, ubiquitin-dependent degradation, as well as gene transcription. We noticed that putative SUMOylation site is localized at $^{340}K$ of $Tau(^{339}VKSE^{342})$ with the consensus sequence information (${\Phi}KxE$ ; where ${\Phi}$ represents L, I, V or F and x is any amino acid). In this report, we demonstrated that $^{340}K$ of Tau is the SUMOylation site and that a point mutant of Tau S214E (an analog of the phospho $^{214}S$ Tau) promotes its SUMOylation at $^{340}K$ and its nuclear or nuclear vicinity localization, by co-immunoprecipitation and confocal microscopy analysis. Further, we demonstrate that the Tau S214E (neither Tau S214A nor Tau K340R) mutant increases its protein stability. However, the SUMOylation at $^{340}K$ of Tau did not influence cell survival, as determined by FACS analysis. Therefore, our results suggested that the phosphorylation of Tau on $^{214}S$ residue promotes its SUMOylation on $^{340}K$ residue and nuclear vicinity localization, and increases its stability, without influencing cell survival.