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  • Cell Research
    Wu 1 Ye Zhang 1 and Yu fei Shen 1 1 National Laboratory of Medical Molecular Biology Department of Biochemistry and Molecular Biology Institute of Basic Medical Sciences Chinese Academy of Medical Sciences Peking Union Medical College 5 Dongdan Santiao Beijing 100005 China 2 Current address Yale University School of Medicine Section of Pulmonary and Critical Care Medicine New Haven CT 06520 USA Correspondence Yu fei Shen Ye Zhang Tel 86 10 65295939 E mail yfshen imicams ac cn yfscams gmail com yezhang pumc edu cn The SWI SNF chromatin remodeling complexes utilize energy from ATP hydrolysis to reposition nucleosomes and regulate the expression of human genes Here we studied the roles of human Brahma hBrm and Brahma related gene 1 Brg1 the ATPase subunits of the SWI SNF complexes in regulating human genes Our results indicate that both hBrm and Brg1 interact with Signal transducer and activator of transcription Stat 1 in vitro However Stat1 in its native form only recruits hBrm to IFNγ activated sequences GAS of individual genes by contrast in a stress induced phosphorylated form Stat1 mainly binds to Brg1 Under basal conditions hBrm is recruited by native Stat1 to the GAS and exists in a mSin3 HDAC co repressor complex on the hsp90α gene which shows a compact chromatin structure Upon heat shock hBrm is acetylated by p300 and dissociates from the co repressor complex which the phosphorylated Stat1 is increased and binds and recruits Brg1 to the GAS leading to elevated induction of the gene This hBrm Brg1 switch also occurs at the GAS of all of the three examined immune genes in heat shocked cells however this switch only occurs in specific cell types upon exposure to IFNγ Regardless of the stimulus the hBrm Brg1 switch at the GAS elicits an increase in

    Original URL path: http://www.cell-research.com/arts.asp?id=440 (2016-02-14)
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  • Cell Research
    Key Laboratory of Molecular Biology and Research Center for Structural Biology Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Shanghai 200031 China 2 Graduate School of Chinese Academy of Sciences 320 Yue Yang Road Shanghai 200031 China 3 International Joint Cancer Institute Second Military Medical University 800 Xiang Yin Road Shanghai 200433 China 4 Current address Memorial Sloan Kettering Cancer Center RRL 269 430 E 67th Street New York NY 10021 USA Correspondence Jianping Ding Tel 86 21 54921619 E mail jpding sibs ac cn Interleukin 2 IL 2 signaling plays a pivotal role in the activation of immune responses and drugs that block this pathway have been shown to be effective for the immunosuppression in patients with organ transplantation to alleviate eliminate allograft rejection The first humanized monoclonal antibody mAb daclizumab falls into this category and shows high specificity and affinity against a key component of the IL 2 receptor complex namely IL 2R α To reveal the molecular mechanism of the inhibition of the IL 2 signaling pathway by daclizumab we determined the crystal structures of the daclizumab Fab in free form and in complex with the IL 2R α ectodomain at 2 6 and 2 8 Å resolution respectively The daclizumab Fab adopts a similar conformation in the presence or absence of the IL 2R α ectodomain The antigen binding site of daclizumab is mainly composed of five complementarity determining regions CDRs that form a large positively charged surface depression and two flanking patches that are generally hydrophobic The conformational epitope consists of several discontinuous segments of the IL 2Rα ectodomain a large portion of which overlaps with the regions that interact with IL 2 suggesting that the binding of daclizumab to IL 2Rα would prevent the IL 2 binding

    Original URL path: http://www.cell-research.com/arts.asp?id=441 (2016-02-14)
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  • Cell Research
    Degradation Lab Department of Pathophysiology Guangzhou Medical College Guangzhou Guangdong 510182 China 2 Division of Basic Biomedical Sciences Sanford School of Medicine of the University of South Dakota Vermillion SD 57069 USA 3 The Prevention Program Barbara Ann Karmanos Cancer Institute Wayne State University Detroit MI 48201 USA 4 Department of Pathology School of Medicine Wayne State University Detroit MI 48201 USA Correspondence Jinbao Liu Xuejun Wang Tel 86 20 81340720 86 20 81340720 E mail liujinbao1 yahoo com cn xuejun wang usd edu Intracellular protein degradation by the ubiquitin proteasome system is ATP dependent and the optimal ATP concentration to activate proteasome function in vitro is 100 μM Intracellular ATP levels are generally in the low millimolar range but ATP at a level within this range was shown to inhibit proteasome peptidase activities in vitro Here we report new evidence that supports a hypothesis that intracellular ATP at the physiological levels bidirectionally regulates 26S proteasome proteolytic function in the cell First we confirmed that ATP exerted bidirectional regulation on the 26S proteasome in vitro with the optimal ATP concentration between 50 and 100 μM stimulating proteasome chymotrypsin like activities Second we found that manipulating intracellular ATP levels also led

    Original URL path: http://www.cell-research.com/arts.asp?id=442 (2016-02-14)
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  • Cell Research
    1 2 3 Feng Yan 1 2 Phil Yao 2 Zhihong Yang 4 Weihong Wan 4 Xiwei Wang 1 2 Jing Liu 1 Xinjiao Gao 1 Ariane Abrieu 5 Tongge Zhu 1 2 Jiancun Zhang 1 Zhen Dou 1 2 and Xuebiao Yao 1 1 Anhui Key Laboratory for Cellular Dynamics and Chemical Biology Hefei 230027 China 2 Georgia Cancer Coalition Atlanta GA 30310 USA 3 Beijing University of Chinese

    Original URL path: http://www.cell-research.com/arts.asp?id=443 (2016-02-14)
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  • Cell Research
    that modulates DNA methylation and gene transcription via hydroxylation of 5 methylcytosine Haikuo Zhang 1 Xin Zhang 1 Erin Clark 1 Michelle Mulcahey 2 Stephen Huang 2 and Yujiang Geno Shi 1 1 Division of Endocrinology Diabetes and Hypertension Department of Medicine Brigham and Women s Hospital Harvard Medical School 221 Longwood Avenue Boston MA 02115 USA 2 Division of Endocrinology Childern s hospital Boston Harvard Medical School Boston MA

    Original URL path: http://www.cell-research.com/arts.asp?id=444 (2016-02-14)
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  • Cell Research

    (No additional info available in detailed archive for this subpage)
    Original URL path: /artsmore1.asp?id=30 (2016-02-14)


  • Cell Research
    2 A special issue on NF κB signaling and function Shao Cong Sun 1 and Zheng Gang Liu 2 1 Department of Immunology The University of Texas MD Anderson Cancer Center and The University of Texas Graduate School of Biomedical Sciences at Houston 7455 Fannin Street Box 902 Houston TX 77030 USA ssun mdanderson org 2 Cell and Cancer Biology Branch Center for Cancer Research National Cancer Institute National Institutes

    Original URL path: http://www.cell-research.com/arts.asp?id=416 (2016-02-14)
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  • Cell Research
    Thomson Reuters 2013 Free Sample Issue Submission Advanced Online Publication Current Issue Top 10 VOLUME 21 ISSUE 1 1 2011 3 5 SUMO wrestling in cell movement Miia M Rytinki and Jorma J Palvimo Institute of Biomedicine University of Eastern Finland P O Box 1627 FI 70211 Kuopio Finland Correspondence Jorma J Palvimo E mail jorma palvimo uef fi Cell Research 2011 21 3 5 doi 10 1038 cr 2010

    Original URL path: http://www.cell-research.com/arts.asp?id=417 (2016-02-14)
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