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Hf<SUB>0.5</SUB>Zr<SUB>0.5</SUB>O₂ 기반의 Ferroelectric Memristor 제작 및 시냅스 특성 평가
박진혁(Jin-Hyeok Pak),송정수(Jeong-Su Song),여정은(Jung-Eun Yeo),이인화(In-Hwa Lee),조한성(Han-Seong Cho),홍진우(Jin-Woo Hong) 대한전자공학회 2023 대한전자공학회 학술대회 Vol.2023 No.11
Due to the limitations of Moores Law, scaling down components in traditional CMOS processing and von Neumann architecture has gradually approached its constraints. Notably, Neuromorphic computing technology, which seeks to emulate the human brain, has gained significant attention. In this study, we have fabricated a two-terminal device which is based on Hf0.5Zr0.5O2 (HZO) thin films and is known as a Ferroelectric Tunnel Junction (FTJ). After device fabrication, we conducted P-V and I-V measurements to assess ferroelectric and memory properties. Then we evaluated the crystalline structure of HZO thin films through XRD analysis. Finally, we successfully implemented Synaptic Functions by applying pulse input.
Lee, In-Seon,Choi, Won Ho,Kim, Ji Young,Jeong, Jin-Yong,Kim, Mi-Jung,Nam, Joo-Hyun,Kim, Jong-Hyeok,Seo, Sang-Beom,Pak, Jhang Ho Wiley Subscription Services, Inc., A Wiley Company 2008 Journal of cellular biochemistry Vol.104 No.2
<P>Pax5, a member of the paired box gene family of transcription factors, is a B cell-specific activator protein (BSAP) that plays important roles in controlling the expression of lineage- and differentiation-stage specific genes during B lymphopoiesis. We identified two putative Pax5 binding sites in a 668 bp of the murine 1-cys peroxiredoxin (1-cysPrx) promoter region. These sites were located at positions −278 to −262 and −50 to −34 from the translation start site. Gel mobility shift assays showed that recombinant Pax5 protein bound specifically to the nucleotide regions −56 to −24 (MP1 probe) and −284 to −253 (MP2 probe). Furthermore, endogenous Pax5 protein from B lymphoblast cells (IM-9) formed a DNA-protein complex with MP1 and MP2 probes, indicating that Pax5 binding occurs specifically at these sequences in vivo. Transient transfection studies showed that expression of exogenous Pax5 resulted in dose-dependent increases in 1-cysPrx promoter activity, implying that Pax5 functions as a positive transcription factor for 1-cysPrx expression. Further transient cotransfection studies showed that coexpression of Pax5 and histone acetyltransferases (HATs), such as p300, cAMP-response-element-binding protein (CBP) and p300/CBP associated factor (PCAF) enhanced the Pax5-mediated 1-cysPrx promoter activity. Immunoprecipitation studies indicated that Pax5 directly binds to HATs. Chromatin immunoprecipitation assays showed that the recruitment of Pax5 to the promoter induced histone H3 and H4 hyperacetylation of chromatin. Lipopolysaccharides (LPS) stimulation of murine splenocytes resulted in coordinated expression of Pax5 and 1-cysPrx proteins. These findings suggest that Pax5 may function as a transactivator of 1-cysPrx gene expression. J. Cell. Biochem. 104: 465–476, 2008. © 2008 Wiley-Liss, Inc.</P>