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고현철(Several Previous Problems of the Study on Jo Gi-Chun",s Baekdusan) 한국문학회 2005 韓國文學論叢 Vol.39 No.-
This essay aims to investigate several previous problems of the study on Jo Gi-Chun's Baekdusan. The results of this essay are summarized as the following: First, this essay investigates differences between several Baekdusan Texts, that is, 1955 Text, 1986 Text(1987 Text, 1989 Text) and 1995 Text(2004 Text). And, it examines we should practical use 1955 Text in order to study Jo Gi-Chun's Baekdusan. Second, it investigates the fact that Kim Il-Sung intervened in the process of creating Jo Gi-Chun's Baekdusan, holding political intention in his bosom. Third, it investigates that several perspectives ― external, internal, and internal-critical ― of the study on North Korean Literature. And, it investigates internal-critical perspective is most suitable for the study on Jo Gi-Chun's Baekdusan among three perspectives. In conclusion, it is claimed that we should read Baekdusan(before-1955 Text) by focusing on the political history of North Korea in terms of the internal-critical perspective for the study on Jo Gi-Chun's Baekdusan.
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Baek, Du-San,Kim, Jeong-Ho,Kim, Ye-Jin,Kim, Yong-Sung American Chemical Society 2018 MOLECULAR PHARMACEUTICS Vol.15 No.2
<P>Neuropilin-1 (NRP1), which functions as a coreceptor for vascular endothelial growth factor (VEGF) and is implicated in vascular permeability and tumorigenesis, has been targeted by peptides that specifically bind to the VEGF-binding region on NRP1. Like natural VEGF ligands, all known peptides with NRP1-binding activity bind only through a carboxy (C)-terminal R/K-x-x-R/K sequence motif (x stands for any amino acids); this strict requirement is called the C-end rule (CendR). Here, we report immunoglobulin Fc-fused NRP1-specific peptides deviating from CendR. We screened a yeast surface-displayed Fc-fused non-CendR peptide library against NRP1 and isolated Fc-V12, wherein V12 peptide comprising 12 amino acids has a PPRV sequence at its C-terminal end. Although Fc-V12 lacked the CendR motif, it showed selective binding to the VEGF-binding region of NRP1 and triggered cellular internalization of NRP1, which resulted in enhanced extravasation into tumor tissues and tumor tissue penetration of the Fc-fused peptide along with the coinjected chemical drug in tumor-bearing mice. Through a saturation mutagenesis study, we identified that the Val residue at the C-terminus of Fc-V12 is crucial for NRP1 binding. We further improved NRP1 affinity of Fc-V12 (<I>K</I><SUB>D</SUB> = ∼761 nM) through directed evolution of the upstream sequence of PPRV to obtain Fc-V12–33 (<I>K</I><SUB>D</SUB> = ∼17.4 nM), which exhibited enhanced NRP1-mediated vascular permeability as compared with Fc-V12. Our results provide functional Fc-fused non-CendR peptides, which bind to the VEGF-binding region of NRP1 and enhance vascular permeability, expanding the sequence space of NRP1-targeting peptides.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/mpohbp/2018/mpohbp.2018.15.issue-2/acs.molpharmaceut.7b00761/production/images/medium/mp-2017-007613_0005.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/mp7b00761'>ACS Electronic Supporting Info</A></P>
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