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Polyakov, Alexander Y.,Smirnov, Nickolai B.,Cheong Hyun Roh,Cheol-Koo Hahn,Han-Su Cho,Kozhukhova, Elena A.,Govorkov, Anatolyi V.,Ryzhuk, Roman Valerievich,Kargin, Nikolay Ivanovich,In-Hwan Lee IEEE 2014 IEEE TRANSACTIONS ON NANOTECHNOLOGY Vol. No.
<P>Electrical properties of GaN films grown on Si by molecular beam epitaxy using various types of strain-relieving layers have been studied by means of Hall/van der Pauw measurements, capacitance-voltage profiling, admittance spectroscopy, and deep levels transient spectroscopy with electrical and optical injection. The electrical properties of all grown films were determined by relatively deep electron traps N1, N2, and N3 with aggregate concentration of ~10<SUP>17</SUP> cm<SUP>-3</SUP>. Freezing out of these traps led to the films freezing out down to the depth corresponding to the nearest underlying heterointerface where a strong band bending caused a sharp nonuniformity of charge carriers concentration. For AlN or Al-rich AlGaN underlying films, this band bending could cause formation of hole sheet charge leading to apparent conductivity to appear p-type in Hall. Other deep traps detected in the grown films were N4 and N5 acceptors with levels near E<SUB>c</SUB> - 0.6 eV, and hole traps H1 and H2 with levels near E<SUB>v</SUB> + 0.9 eV. Possible consequences of the observed phenomena for designing the thick GaN stand-off films in power transistors are briefly discussed.</P>
Sohn, Young Chang,Goo, Young-Wha,Kim, Dae-Hwan,Kim, Seung-Whan,Kang, Min-Jung,Nickolai A. Barlev,Shelley L. Berger,Vincent T. Chow,Suh, Pan-Gil,David O. Azorsa,Paul S. Meltzer,Lee, Kong-Ju,Lee, Young- 이화여자대학교 세포신호전달연구센터 2002 고사리 세포신호전달 심포지움 Vol. No.4
Activating signal cointegrator-2(ASC-2), also reported as AIB3, TRBP, RAP250, NRC and PRIP, directly binds to and functions as a coactivator molecule of nuclear receptors and many other transcription factors. In particular, our previous results from microinjection of anti-ASC2 antibody demonstrated that ASC-2 is required for transactivation by nuclear receptors and AP-1 in vivo. Here we show that ASC-2 belongs to a steady-state complex of approximately 2 MDa(ASCOM for ASC-2 complex) in HeLa nuclei, which contains mammalian homologues of Drosophila Trithorax group(Trx-G) proteins ALR-1, ALR-2, HALR and ASH2. ALR-1/2 and HALR contain a SET domain that specifically methylates histone H3 lysine 4(K4). We further demonstrate that retinoic acid receptor(RAR) transactivation requires retinoid-dependent recruitment of ASCOM to DNA-bound RAR in vivo. Thus, ASCOM represents the first mammalian coactivator complex with H3/K4-methylase activity, directly recruited to nuclear receptors.
Goo, Young-Hwa,Sohn, Young Chang,Kim, Dae-Hwan,Kim, Seung-Whan,Kang, Min-Jung,Jung, Dong-Ju,Kwak, Eunyee,Barlev, Nickolai A.,Berger, Shelley L.,Chow, Vincent T.,Roeder, Rober G.,Azora, David O.,Meltze 梨花女子大學校 藥學硏究所 2003 藥學硏究論文集 Vol.- No.12
Many transcription coactivators interact with nuclear receptors in a ligand- and C-terminal transactivation function (AF2)-dependent manner. These include activating signal cointegrator 2 (ASC-2), a recently isolated transcriptional coactivator molecule, which is amplified in human cancers and stimulates transactivation by nuclear receptors and numerous other transcription factors. In this report, we show that ASC-2 belongs to a steady-state complex of approximately 2 MDa (ASC-2 complex [ASCOM]) in HeLa nuclei. ASCOM contains retinoblastoma-binding protein RBQ-3, α/β-tubulins, and trithorax group proteins ALR-1, ALR-2, HALR, and ASH2. In particular, ALR-1/2 and HALR contain a highly conserved 130- to 140-amino-acid motif termed the SET domain, which was recently implicated in histone H3 lysine-specific methylation activities. Indeed, recombinant ALR-1, HALR, and immunopurified ASCOM exhibit very weak but specific H3-lysine 4 methylation activities in vitro, and transactivation by retinoic acid receptor appears to involve ligand-dependent recruitment of ASCOM and subsequent transient H3-lysjne 4 methylation of the promoter region in vivo. Thus, ASCOM may represent a distinct coactivator complex of nuclear receptors. Further characterization of ASCOM will lead to a better understanding of how nuclear receptors and other transcription factors mediate transcriptional activation.