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RISS 인기검색어
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- 저자 : Kieff, Elliott (검색결과 8 건)
- 무료
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- 유료
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Engineering a Deal: Toward a Private Ordering Solution to the Anticommons Problem
F. Scott Kieff,Troy A. Paredes,정연덕 서울대학교 기술과법센터 2007 Law & technology Vol.3 No.4
지적재산권의 anticommons3) 문제는 악명이 높다. 하나의 물건 또는 서비스에 다수의 지적재산권이 존재하는 경우에 장래 그 분야 사업에 진출하려는 기업이 주저하거나 부차적인 비용을 들거나 홀드 업(held up) 문제를 발생시킬 것을 염려하는 사람들도 많다. 이 논문은 현재의 법령 내에서 사적질 서형성(private ordering)에 기초한 해결방안을 제안하고 있다. 이러한 접근 방식은 유한책임회사를 설립하고, 지적재산권자들이 사업을 영위하는데 실질적인 이해관계를 갖고서 이러한 기업에 참여하도록 하는 인센티브를 제공하는 것이다. 그러나, 현재 지적재산권자들은 홀드아웃(hold out)4)과 같은 기회주의적으로 상황에 따라 이익만을 추구하는 행동을 하지 않도록 하는 사회적인 압력도 받고있다. 지적재산권자에 대한 보상과 자기 규제(self restraint)를 적절히 행하여 관련된 지적재산권자들에 대한 행동을 조정하는 것이 이 논문에서 제안된 구조이다. 제시된 접근방식은 변호사들이 거래비용 엔지니어(transaction cost engineer)로서의 역할을 하여 문제를 처리할 수 있도록 설계되었다.
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Kim, Jung-Eun,Kim, Sang Yong,Lim, Sue Yeon,Kieff, Elliott,Song, Yoon-Jae American Society for Microbiology 2014 Molecular and cellular biology Vol.34 No.3
<P>We have previously reported that interleukin-1 (IL-1) receptor-associated kinase (IRAK1) is essential for Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1)-induced p65/RelA serine 536 phosphorylation and NF-κB activation but not for IκB kinase α (IKKα) or IKKβ activation (Y. J. Song, K. Y. Jen, V. Soni, E. Kieff, and E. Cahir-McFarland, Proc. Natl. Acad. Sci. U. S. A. 103:2689–2694, 2006, doi:10.1073/pnas.0511096103). Since the kinase activity of IRAK1 is not required for LMP1-induced NF-κB activation, IRAK1 is proposed to function as a scaffold protein to recruit a p65/RelA serine 536 kinase(s) to enhance NF-κB-dependent transcriptional activity. We now report that Ca<SUP>2+</SUP>/calmodulin-dependent protein kinase II (CaMKII) interacts with IRAK1 and is critical for LMP1-induced p65/RelA serine 536 phosphorylation and NF-κB activation. CaMKII bound the death domain of IRAK1 and directly phosphorylated p65/RelA at serine 536 <I>in vitro</I>. Downregulation of CaMKII activity or expression significantly reduced LMP1-induced p65/RelA serine 536 phosphorylation and NF-κB activation. Furthermore, LMP1-induced CaMKII activation and p65/RelA serine 536 phosphorylation were significantly reduced in IRAK1 knockout (KO) mouse embryonic fibroblasts (MEFs). Thus, IRAK1 may recruit and activate CaMKII, which phosphorylates p65/RelA serine 536 to enhance the transactivation potential of NF-κB in LMP1-induced NF-κB activation pathway.</P>
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Epstein–Barr virus latent genes
강명수,Elliott Kieff 생화학분자생물학회 2015 Experimental and molecular medicine Vol.47 No.-
Latent Epstein–Barr virus (EBV) infection has a substantial role in causing many human disorders. The persistence of these viral genomes in all malignant cells, yet with the expression of limited latent genes, is consistent with the notion that EBV latentgenes are important for malignant cell growth. While the EBV-encoded nuclear antigen-1 (EBNA-1) and latent membrane protein-2A (LMP-2A) are critical, the EBNA-leader proteins, EBNA-2, EBNA-3A, EBNA-3C and LMP-1, are individually essentialfor in vitro transformation of primary B cells to lymphoblastoid cell lines. EBV-encoded RNAs and EBNA-3Bs are dispensable. In this review, the roles of EBV latent genes are summarized.
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Epstein–Barr virus latent genes
Kang, Myung-Soo,Kieff, Elliott Nature Publishing Group 2015 Experimental and molecular medicine Vol.47 No.1
<P>Latent Epstein–Barr virus (EBV) infection has a substantial role in causing many human disorders. The persistence of these viral genomes in all malignant cells, yet with the expression of limited latent genes, is consistent with the notion that EBV latent genes are important for malignant cell growth. While the EBV-encoded nuclear antigen-1 (EBNA-1) and latent membrane protein-2A (LMP-2A) are critical, the EBNA-leader proteins, EBNA-2, EBNA-3A, EBNA-3C and LMP-1, are individually essential for <I>in vitro</I> transformation of primary B cells to lymphoblastoid cell lines. EBV-encoded RNAs and EBNA-3Bs are dispensable. In this review, the roles of EBV latent genes are summarized.</P>
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Small molecule and peptide-mediated inhibition of Epstein-Barr virus nuclear antigen 1 dimerization
Kim, Sun Young,Song, Kyung-A,Kieff, Elliott,Kang, Myung-Soo Elsevier 2012 Biochemical and biophysical research communication Vol.424 No.2
<P>Latent Epstein-Barr virus (EBV) infection is associated with human B cell lymphomas and certain carcinomas. EBV episome persistence, replication, and gene expression are dependent on EBV-encoded nuclear antigen 1 (EBNA1)'s DNA binding domain (DBD)/dimerization domain (DD)-mediated sequence-specific DNA binding activity. Homodimerization of EBNA1 is essential for EBNA1 DNA binding and transactivation. In this study, we characterized a novel small molecule EBNA1 inhibitor EiK1, screened from the previous high throughput screening (HTS). The EiK1 compound specifically inhibited the EBNA1-dependent, OriP-enhanced transcription, but not EBNA1-independent transcription. A Surface Plasmon Resonance Biacore assay revealed that EiK1 associates with EBNA1 amino acid 459-607 DBD/DD. Consistent with the SPR data, in vitro gel shift assays showed that EiK1 suppressed the activity of EBNA1 binding to the cognate familial repeats (FR) sequence, but not control RBP-Jκ binding to the Jκ site. Subsequently, a cross-linker-mediated in vitro multimerization assay and EBNA1 homodimerization-dependent yeast two-hybrid assay showed that EiK1 significantly inhibited EBNA1 dimerization. In an attempt to identify more highly specific peptide inhibitors, small peptides encompassing the EBNA1 DBD/DD were screened for inhibition of EBNA1 DBD-mediated DNA binding function. The small peptide P85, covering EBNA1 a.a. 560-574, significantly blocked EBNA1 DNA binding activity in vitro, prevented dimerization in vitro and in vivo, associated with EBNA1 in vitro, and repressed EBNA1-dependent transcription in vivo. Collectively, this study describes two novel inhibitors of EBNA1 dimerization. This study demonstrates that EBNA1 homodimerization can be effectively targeted by a small molecule or peptide.</P>
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Lee, E.K.,Kim, S.Y.,Noh, K.W.,Joo, E.H.,Zhao, B.,Kieff, E.,Kang, M.S. Elsevier/North-Holland 2014 ANTIVIRAL RESEARCH Vol.104 No.-
The replication and persistence of extra chromosomal Epstein-Barr virus (EBV) episome in latently infected cells are primarily dependent on the binding of EBV-encoded nuclear antigen 1 (EBNA1) to the cognate EBV oriP element. In continuation of the previous study, herein we characterized EBNA1 small molecule inhibitors (H20, H31) and their underlying inhibitory mechanisms. In silico docking analyses predicted that H20 fits into a pocket in the EBNA1 DNA binding domain (DBD). However, H20 did not significantly affect EBNA1 binding to its cognate sequence. A limited structure-relationship study of H20 identified a hydrophobic compound H31, as an EBNA1 inhibitor. An in vitro EBNA1 EMSA and in vivo EGFP-EBNA1 confocal microscopy analysis showed that H31 inhibited EBNA1-dependent oriP sequence-specific DNA binding activity, but not sequence-nonspecific chromosomal association. Consistent with this, H31 repressed the EBNA1-dependent transcription, replication, and persistence of an EBV oriP plasmid. Furthermore, H31 induced progressive loss of EBV episome. In addition, H31 selectively retarded the growth of EBV-infected LCL or Burkitt's lymphoma cells. These data indicate that H31 inhibition of EBNA1-dependent DNA binding decreases transcription from and persistence of EBV episome in EBV-infected cells. These new compounds might be useful probes for dissecting EBNA1 functions in vitro and in vivo.
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