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이진아,백기환,한아름,최두영 圓光大學校 醫科學硏究所 2008 圓光醫科學 Vol.23 No.2
우연히 발견된 복부 종괴로 병원에 내원 한 15세 여아에서 방사선학적 검사에서 우측 신장부위에 콩팥세포암종(renal cell carcinoma)이 의심되었으나 수술 후 Willms 종양으로 진단되어 NWTS-Ⅳ 지침에 따라 합병증 및 재발없이 치료중인 사춘기 Wilms종양 1례를 경험하였기에 문헌고찰과 함께 보고하는 바이다. Wilms' tumor or Nephroblastoma is the second most common mailgnant abdominal tumor in childhood. It usually occurs in children between 2-5 yr of age and is very rare in adolescent and adults. In here, we report the case of a 15-year-old female with Wilms' tumor. On imaging studies, we confirmed the presence of a 22×18×13cm mass in the right kidney. A radical transabdominal nephrectomy was performed and the mass showed histologically Wilms' tumor. She received combination chemotherapy according to NWTS(national Wilms' tumor study)-Ⅳ guidelines and have been alive and well for the last 8 months without severe complication or relapse.
Design and fabrication of the low conversion loss Self Oscillating Mixer for Q-band
Sang-Jin Lee,Dan An,Mun-Kyo Lee,Jin-Man Jin,Du-Hyun Ko,Chang-Sik Cho,Seong-Dae Lee,Tae-Jong Baek,Seong-Chan Kim,Hyung-Moo Park,Jin-Koo Rhee 대한전자공학회 2005 ITC-CSCC :International Technical Conference on Ci Vol.2005 No.1
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>