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  • Cell Research
    Sample Issue Submission Advanced Online Publication Current Issue Top 10 VOLUME 21 ISSUE 7 7 2011 998 1001 TLR induced activation of Btk Role for endosomal MHC class II molecules revealed Joan Ní Gabhann and Caroline A Jefferies Molecular and Cellular Therapeutics and RSCI Research Institute Royal College of Surgeons in Ireland Dublin Ireland Correspondence Caroline A Jefferies E mail cjefferies rcsi ie Cell Research 2011 21 998 1001 doi

    Original URL path: http://www.cell-research.com/arts.asp?id=325 (2016-02-14)
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  • Cell Research
    edu Embryonic signaling pathways often lead to a switch from default repression to transcriptional activation of target genes A major consequence of Wnt signaling is stabilization of β catenin which associates with T cell factors TCFs and converts them from repressors into transcriptional activators The molecular mechanisms responsible for this conversion remain poorly understood Several studies have reported on the regulation of TCF by phosphorylation yet its physiological significance has

    Original URL path: http://www.cell-research.com/arts.asp?id=326 (2016-02-14)
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  • Cell Research
    Molecular Biology Baylor College of Medicine One Baylor Plaza Houston TX 77030 USA 3 Department of Molecular and Human Genetics Baylor College of Medicine One Baylor Plaza Houston TX 77030 USA Correspondence Zhou Songyang E mail songyang bcm edu Human telomeres are bound and protected by protein complexes assembled around the six core telomeric proteins RAP1 TRF1 TRF2 TIN2 TPP1 and POT1 The function of these proteins on telomeres has been studied extensively Recently increasing evidence has suggested possible roles for these proteins outside of telomeres However the non canonical extra telomeric function of human telomeric proteins remains poorly understood To this end we systematically investigated the binding sites of telomeric proteins along human chromosomes by performing whole genome chromatin immunoprecipitation ChIP for RAP1 and TRF2 ChIP sequencing ChIP seq revealed that RAP1 and TRF2 could be found on a small number of interstitial sites including regions that are proximal to genes Some of these binding sites contain short telomere repeats suggesting that telomeric proteins could directly bind to interstitial sites Interestingly only a small fraction of the available interstitial telomere repeat containing regions were occupied by RAP1 and TRF2 Ectopically expressed TRF2 was able to occupy additional interstitial telomere

    Original URL path: http://www.cell-research.com/arts.asp?id=327 (2016-02-14)
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  • Cell Research
    d Italie Lyon 69364 France 2 CNRS and University of Nice Sophia Antipolis Institut de Pharmacologie Mol閏ulaire et Cellulaire 06560 Sophia Antipolis France 3 Laboratory of Biology and Pathology of Genomes of University of Nice Sophia Antipolis CNRS UMR6267 INSERM U998 Faculty of Medicine Nice France 4 Dipartimento di Genetica e Microbiologia Adriano Buzzati Traverso Universit di Pavia Pavia Italy 5 Department of Medical Genetics CHU of Nice Nice France Correspondence Eric Gilson Tel 33 472728453 E mail Eric Gilson unice fr The study of the proteins that bind to telomeric DNA in mammals has provided a deep understanding of the mechanisms involved in chromosome end protection However very little is known on the binding of these proteins to nontelomeric DNA sequences The TTAGGG DNA repeat proteins 1 and 2 TRF1 and TRF2 bind to mammalian telomeres as part of the shelterin complex and are essential for maintaining chromosome end stability In this study we combined chromatin immunoprecipitation with high throughput sequencing to map at high sensitivity and resolution the human chromosomal sites to which TRF1 and TRF2 bind While most of the identified sequences correspond to telomeric regions we showed that these two proteins also bind to extratelomeric sites

    Original URL path: http://www.cell-research.com/arts.asp?id=328 (2016-02-14)
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  • Cell Research
    China 2 Key Laboratory of Structural Biology Chinese Academy of Sciences Hefei 230026 China Correspondence Maikun Teng Liwen Niu Tel 86 551 3606314 E mail mkteng ustc edu cn lwniu ustc edu cn The cleavage factor I m CF I m consists of a 25 kDa subunit CF I m 25 and one of three larger subunits CF I m 59 CF I m 68 CF I m 72 and is an essential protein complex for pre mRNA 3 end cleavage and polyadenylation It recognizes the upstream sequence of the poly A site in a sequence dependent manner Here we report the crystal structure of human CF I m comprising CF I m 25 and the RNA recognition motif domain of CF I m 68 CF I m 68RRM and the crystal structure of the CF I m RNA complex These structures show that two CF I m 68RRM molecules bind to the CF I m 25 dimer via a novel RRM protein interaction mode forming a heterotetramer The RNA bound structure shows that two UGUAA RNA sequences with anti parallel orientation bind to one CF I m 25 CF I m 68RRM heterotetramer providing structural basis for the mechanism

    Original URL path: http://www.cell-research.com/arts.asp?id=329 (2016-02-14)
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  • Cell Research
    Biology Sealy Center for Molecular Science The University of Texas Medical Branch at Galveston 301 University Boulevard Galveston TX 77555 USA 3 Department of Molecular Medicine City of Hope National Medical Center and Beckman Research Institute 1500 East Duarte Road Duarte CA 91010 USA 4 Department of Molecular Pharmacology City of Hope National Medical Center and Beckman Research Institute 1500 East Duarte Road Duarte CA 91010 USA 5 Department of Pathology City of Hope National Medical Center and Beckman Research Institute 1500 East Duarte Road Duarte CA 91010 USA 6 Department of Surgery City of Hope National Medical Center and Beckman Research Institute 1500 East Duarte Road Duarte CA 91010 USA Correspondence Binghui Shen Li Zheng E mail bshen coh org lzheng coh org DNA replication and repair are critical processes for all living organisms to ensure faithful duplication and transmission of genetic information Flap endonuclease 1 Fen1 a structure specific nuclease plays an important role in multiple DNA metabolic pathways and maintenance of genome stability Human FEN1 mutations that impair its exonuclease activity have been linked to cancer development FEN1 interacts with multiple proteins including proliferation cell nuclear antigen PCNA to form various functional complexes Interactions with these proteins are considered to be the key molecular mechanisms mediating FEN1 s key biological functions The current challenge is to experimentally demonstrate the biological consequence of a specific interaction without compromising other functions of a desired protein To address this issue we established a mutant mouse model harboring a FEN1 point mutation F343A F344A FFAA which specifically abolishes the FEN1 PCNA interaction We show that the FFAA mutation causes defects in RNA primer removal and long patch base excision repair even in the heterozygous state resulting in numerous DNA breaks These breaks activate the G2 M checkpoint protein Chk1 and induce

    Original URL path: http://www.cell-research.com/arts.asp?id=330 (2016-02-14)
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  • Cell Research
    Medicine University of California Los Angeles Los Angeles CA 90095 USA 2 Division of Dermatology Department of Medicine David Geffen School of Medicine University of California Los Angeles Los Angeles CA 90095 USA 3 Molecular Biology Institute University of California Los Angeles Los Angeles CA 90095 USA 4 Jonsson Comprehensive Cancer Center University of California Los Angeles Los Angeles CA 90095 USA 5 Current address Cynvenio Biosystems LLC Westlake Village CA 91361 USA Correspondence Genhong Cheng Tel 310 825 8896 E mail gcheng mednet ucla edu Monocytes are mobilized to sites of infection via interaction between the chemokine MCP 1 and its receptor CCR2 at which point they differentiate into macrophages that mediate potent antimicrobial effects In this study we investigated the mechanisms by which monocytes are mobilized in response to systemic challenge with the intracellular bacterium Francisella tularensis We found that mice deficient in MyD88 interferon γ IFNγ R or CCR2 all had defects in the expansion of splenic monocyte populations upon F tularensis challenge and in control of F tularensis infection Interestingly MyD88 deficient mice were defective in production of IFNγ and IFNγR deficient mice exhibited defective production of MCP 1 the ligand for CCR2 Transplantation of IFNγR

    Original URL path: http://www.cell-research.com/arts.asp?id=331 (2016-02-14)
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  • Cell Research
    CA 90095 USA 3 Liu Hua Qiao Hospital Guangzhou 510010 China Correspondence Shuo Lin Tel 1 310 267 4970 E mail shuolin ucla edu Blood vessels normally maintain stereotyped lumen diameters and their stable structures are crucial for vascular function However very little is known about the molecular mechanisms controlling the maintenance of vessel diameters and the integrity of endothelial cells We investigated this issue in zebrafish embryos by a chemical genetics approach Small molecule libraries were screened using live Tg kdrl GRCFP zn1 transgenic embryos in which endothelial cells are specifically labeled with GFP By analyzing the effects of compounds on the morphology and function of embryonic blood vessels after lumen formation PP1 a putative Src kinase inhibitor was identified as capable of specifically reducing vascular lumen size by interrupting endothelial cell integrity The inhibitory effect is not due to Src or general VEGF signaling inhibition because another Src inhibitor and Src morpholino as well as several VEGFR inhibitors failed to produce a similar phenotype After profiling a panel of 22 representative mammalian kinases and surveying published data we selected a few possible new candidates Combinational analysis of these candidate kinase inhibitors established that PP1 induced endothelial collapse by

    Original URL path: http://www.cell-research.com/arts.asp?id=332 (2016-02-14)
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