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| 1 | Matrine upregulates the cell cycle protein E2F-1 and triggers apoptosis via the mitochondrial pathway in K562 cells显示文摘 | Hua Jiang ChunHui Hou ShuBing Zhang HengYue Xie WeiYing Zhou QiHuang Jin XiaoDong Cheng RuoLan Qian XueJun Zhang | 2007 | European Journal of Pharmacology2007，，2： | 1 |
| 2 | CREB is activated in EPO induced HEL cells显示文摘cAMP response element binding protein (CREB) is a transcription factor in nucleus. The activating CREB can specifically bind to the cAMP response element (CRE). The present result showed that erythropoietin (EPO) could induce the phosphorylation of CREB on Serine133 (Pser133), as detected by western blot analysis. in addition, the EPO-dependent activation of CREB binding to CRE element was demonstrated by electrophoretic mobility shift assay. However, the binding of CREB to CRE element could be inhibited by anti-CREB-Pser133 antibody. The data obtained suggested that the EPO-mediated CREB phosphorylation might be critical to both the binding of CREB to the CRE element and the activation of the CREB transcription factor. | Chu Jiang Changyun Gui Ruolan Qian | 2000 | Chinese Science Bulletin2000，45，3： | 1 |
| 3 | Interactions between HMG proteins and the core sequence of DNaseI hypersensitive site 2 in the locus control region (LCR) of the human β-like globin gene cluster显示文摘 | Hui Zhao Shubing Zhang Chu Jiang Ruolan Qian | 2000 | Science in China Series C: Life Sciences2000，，6： | 1 |
| 4 | Interactions between HMG proteins (HMG1/2 and HMG14/17) and human ε-globin gene promoter (ε-promoter)显示文摘High mobility group (HMG) proteins are abundant non-histone proteins in the nuclei of eukaryocytes. It has been shown that HMG proteins may play important roles in the structure and function of chromatin. In the present study, the binding of HMG proteins (HMG1/2 and HMG14/17) to the human e-globin gene promoter (e-promo-ter, -177-+1 bp) has been examined by using both the in vitro nucleosome reconstitution and the electrophoresis mobility shift assay (EMSA). We found that HMG1/2 proteins could bind to the naked e-promoter DNA, however, HMG14/17 could not. Using the in vitro nucleosome reconstitution, we revealed that HMG14/17 could bind to the mononucleosome reconstituted in vitro with E-promoter, while HMG1/2 could not. Those results indicate that the binding of HMG proteins to e-promoter is dynamic as the nucleosome assembling and disassembling. We speculated that this selective binding of HMG proteins to e-promoter might play a critical role in the regulation of e-globin gene expression. | Chunhui Hou Jian Huang Shubing Zhang Ruolan Qian | 2002 | Chinese Science Bulletin2002，47，18： | 0 |
| 5 | Interactions between GATA transcription factors and the DNasel hypersensitive sites in the human p-globin gene LCR显示文摘In this study, we analyze the binding of nuclear proteins isolated from the hydroxyurea (Hu)-induced and uninduced HEL cells to the DNasel hypersensitive sites Ⅲ (HS3 -14991 --14716 bp) and Ⅳ(HS4 -18586-18306 bp) in the human p-globin gene locus control region (LCR). Using Western blot assay, we demonstrate that GATA-1 transcription factor in HEL cells is increased following the induction of Hu, while GATA-2 transcription factor is decreased. Based on both the competition EMSA and the Western blot assay, our data reveal that the nuclear protein isolated from the uninduced HEL cells, which can bind to the HS3 and HS4 core DNA sequences, is mainly GATA-2; however, the nuclear proteins isolated from the Hu-induced HEL cells, which can bind to the HS3 and HS4 core DNA sequences, are mainly GATA-1 and GATA-X (a kind of unknown GATA factor). These results suggest that the erythroid specific transcription factors (GATA-1 and GATA-2) in the Hu-induced and uninduced HEL cells can selectively bind to the HS3 | ZHANG Shubing, ZHAO Hui, JIANG Shu & QIAN RuolanShanghai Institute of Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China Correspondence should be addressed to Qian Ruolan | 2000 | Chinese Science Bulletin2000，45，21： | 0 |
| 6 | Interactions between the nuclear matrix proteins and the 5'-flanking cis-acting elements of the human ε-globin gene显示文摘An erythroid-specific nuclear matrix protein (termed ε-NMP_k) in K562 cells, which can specifically bind to the positive stage-specific regulatory element (ε-PRE Ⅱ, -446—-419 bp) upstream of the human ε-globin gene, has been identified by using gel mobility shift assay.Meanwhile, Southwestern blotting assay showed that the nuclear matrix protein ε-NMP_k in K562,cells may be composed of two polypeptides ( ~ 40 ku). In addition, it is observed in the gel mobility shift assay that the nuclear matrix proteins from K562, HEL and Raji cells can bind to the silencer DNA ( - 392— -177 bp) in the 5’-flanking sequence of human ε-globin gene respectively. However, the shift band K detected in K562 cells is different from shift band H/R in HEL and Raji cells, suggesting that a common nuclear matrix protein may exist in HEL and Raji cells. Results show that the nuclear matrix protein may play an important role in the regulation of the human ε-globin gene expression. | YAN Zhijiang QIAN Ruolan | 1999 | Chinese Science Bulletin1999，44，9： | 0 |
| 7 | Investigation of chromatin folding patterns by atomic force microscopy显示文摘The chromatin folding patterns in air and liquid were studied by atomicforce microscopy (AFM). A gentle water-air interface method was adopted to spreadchromatin from interphase nucleus of chicken erythrocyte. The chromatin was ah-sorbed on APS-Inica surfaCe and studied with AFM. Beads-on-a-string were observedand many higher-order structures such as superbeads with dimensions 40-60urn indiameter and 4-7 urn in height were found to string together to make chromatin fibers.When sample spreading and absorbing time were shortened, higher-order chromatinfibers with 60-120 urn in width were observed in air as well as under water environment. These chromatin structures may reflect chromatin folding patterns in the livingcells. | ZHANG Yi OUYANG Zhenqian HU Jun CHEN Shengfu LI Minqian(Shanghai institute of Nuclear Research, the Chinese Academy of Sciences, Shanghai 201800)ZHAO Hut, QIAN Ruolan(Shanghai institute of Cell Biology, the Chinese Academy of Sciences, Shanghai 200031 | 1999 | Nuclear Science and Techniques1999，10，2： | 0 |
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