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  • Cell Research
    South Florida College of Medicine Tampa FL 33612 USA 3 College of Life Sciences Key Laboratory of Bioactive Materials of Ministry of Education Nankai University Tianjin 300071 China 4 Department of Biological Sciences Brock University Ontario Canada L2S 3A1 5 Department of Biomedical Informatics H Lee Moffitt Cancer Center Research Institute Tampa FL 33612 USA 6 Department of Obstetrics and Gynecology New York University Langone Medical Center New York 10016 USA Correspondence Lin Liu David L Keefe E mail liutelom yahoo com David Keefe nyumc org Telomerase and telomeres are important for indefinite replication of stem cells Recently telomeres of somatic cells were found to be reprogrammed to elongate in induced pluripotent stem cells iPSCs The role of telomeres in developmental pluripotency in vivo of embryonic stem cells ESCs or iPSCs however has not been directly addressed We show that ESCs with long telomeres exhibit authentic developmental pluripotency as evidenced by generation of complete ESC pups as well as germline competent chimeras the most stringent tests available in rodents ESCs with short telomeres show reduced teratoma formation and chimera production and fail to generate complete ESC pups Telomere lengths are highly correlated r 0 8 with the developmental pluripotency of

    Original URL path: http://www.cell-research.com/arts.asp?id=363 (2016-02-14)
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  • Cell Research
    Sciences 225 South Chongqing Road Shanghai 200025 China Correspondence Ke Lan Tel 86 21 63851321 E mail lanke sibs ac cn Type I interferon IFN signaling is the principal response mediating antiviral innate immunity IFN transcription is dependent upon the activation of transcription factors IRF3 IRF7 and NF κB Many viral proteins have been shown as being capable of interfering with IFN signaling to facilitate evasion from the host innate immune response Here we report that a viral miRNA miR K12 11 encoded by Kaposi s sarcoma associated herpesvirus KSHV is critical for the modulation of IFN signaling and acts through targeting I kappa B kinase epsilon IKK ε Ectopic expression of miR K12 11 resulted in decreased IKKε expression while inhibition of miR K12 11 was found to restore IKKε expression in KSHV infected cells Importantly expression of miR K12 11 attenuated IFN signaling by decreasing IKKε mediated IRF3 IRF7 phosphorylation and by inhibiting the activation of IKKε dependent IFN stimulating genes ISGs allowing miR K12 11 suppression of antiviral immunity Our data suggest that IKKε targeting by miR K12 11 is an important strategy utilized by KSHV to modulate IFN signaling during the KSHV lifecycle especially in latency

    Original URL path: http://www.cell-research.com/arts.asp?id=364 (2016-02-14)
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  • Cell Research
    China Normal University 500 Dongchuan Road Shanghai 200241 China 2 The James Hogg iCAPTURE Centre for Cardiovascular and Pulmonary Research University of British Columbia St Paul s Hospital 1081 Burrard Street Vancouver Canada V6Z 1Y6 3 Department of Molecular and Cellular Biology Baylor College of Medicine One Baylor Plaza Houston TX 77030 USA Correspondence Xiaotao Li Tel 713 7983817 E mail xiaotaol bcm edu Discovery of emerging REGγ regulated proteins has accentuated the REGγ proteasome as an important pathway in multiple biological processes including cell growth cell cycle regulation and apoptosis However little is known about the regulation of the REGγ proteasome pathway Here we demonstrate that REGγ can be SUMOylated in vitro and in vivo by SUMO 1 SUMO 2 and SUMO 3 The SUMO E3 protein inhibitor of activated STAT PIAS 1 physically associates with REGγ and promotes SUMOylation of REGγ SUMOylation of REGγ was found to occur at multiple sites including K6 K14 and K12 Mutation analysis indicated that these SUMO sites simultaneously contributed to the SUMOylation status of REGγ in cells Posttranslational modification of REGγ by SUMO conjugation was revealed to mediate cytosolic translocation of REGγ and to cause increased stability of this proteasome activator SUMOylation

    Original URL path: http://www.cell-research.com/arts.asp?id=365 (2016-02-14)
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  • Cell Research
    dong Dongdaemoon gu Seoul 130 701 Korea 2 MRC Mitochondrial Biology Unit Hills Road Cambridge CB2 0XY UK Correspondence Sung Soo Kim Tel 82 2 961 0524 E mail sgskim khu ac kr Mitochondrial reactive oxygen species mROS have been considered detrimental to cells However their physiological roles as signaling mediators have not been thoroughly explored Here we investigated whether mROS generated from mitochondrial electron transport chain mETC complex I stimulated muscle differentiation Our results showed that the quantity of mROS was increased and that manganese superoxide dismutase MnSOD was induced via NF κB activation during muscle differentiation Mitochondria targeted antioxidants MitoQ and MitoTEMPOL and mitochondria targeted catalase decreased mROS quantity and suppressed muscle differentiation without affecting the amount of ATP Mitochondrial alterations including the induction of mitochondrial transcription factor A and an increase in the number and size of mitochondria and functional activations were observed during muscle differentiation In particular increased expression levels of mETC complex I subunits and a higher activity of complex I than other complexes were observed Rotenone an inhibitor of mETC complex I decreased the mitochondrial NADH NAD ratio and mROS levels during muscle differentiation The inhibition of complex I using small interfering RNAs and

    Original URL path: http://www.cell-research.com/arts.asp?id=366 (2016-02-14)
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  • Cell Research
    2 Bizeng Mao 1 Yiwen Deng 2 Huijuan Zhang 1 Longjun Zeng 2 Fengming Song 1 and Zuhua He 1 2 1 National Key Laboratory for Rice Biology Institute of Biotechnology Zhejiang University Hangzhou 310029 China 2 National Key Laboratory of Plant Molecular Genetics Institute of Plant Physiology and Ecology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Shanghai 200032 China Correspondence Zuhua He Fengming Song Tel 86 21 5492 4121 86 571 8697 1207 E mail zhhe sibs ac cn fmsong zju edu cn Emerging evidence suggests that E3 ligases play critical roles in diverse biological processes including innate immune responses in plants However the mechanism of the E3 ligase involvement in plant innate immunity is unclear We report that a rice gene OsBBI1 encoding a RING finger protein with E3 ligase activity mediates broad spectrum disease resistance The expression of OsBBI1 was induced by rice blast fungus Magnaporthe oryzae as well as chemical inducers benzothiadiazole and salicylic acid Biochemical analysis revealed that OsBBI1 protein possesses E3 ubiquitin ligase activity in vitro Genetic analysis revealed that the loss of OsBBI1 function in a Tos17 insertion line increased susceptibility while the overexpression of OsBBI1 in transgenic plants conferred enhanced resistance to multiple races of M oryzae This indicates that OsBBI1 modulates broad spectrum resistance against the blast fungus The OsBBI1 overexpressing plants showed higher levels of H 2 O 2 accumulation in cells and higher levels of phenolic compounds and cross linking of proteins in cell walls at infection sites by M oryzae compared with wild type WT plants The cell walls were thicker in the OsBBI1 overexpressing plants and thinner in the mutant plants than in the WT plants Our results suggest that OsBBI1 modulates broad spectrum resistance to blast fungus by modifying cell wall defence responses The

    Original URL path: http://www.cell-research.com/arts.asp?id=367 (2016-02-14)
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  • Cell Research
    6 Hakchol Ri 2 and Lei Xiao 1 4 1 Laboratory of Molecular Cell Biology Institute of Biochemistry and Cell Biology Cell Bank Stem Cell Bank Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Shanghai 200031 China 2 Cloning Center Biology Branch Academy of Sciences Korea DPR 3 Xiangtan Central Hospital Xiangtan 411100 China 4 College of Animal Sciences Zhejiang University Hangzhou 310058 China 5 Department of Animal Toxinology

    Original URL path: http://www.cell-research.com/arts.asp?id=368 (2016-02-14)
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  • Cell Research
    2 3 and Jinsong Li 1 1 Laboratory of Molecular Cell Biology Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences 320 Yueyang Road Shanghai 200031 China 2 State Key Laboratory of Molecular Biology Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences 320 Yueyang Road Shanghai 200031 China 3 Shanghai Key Laboratory of Molecular Andrology Institute of

    Original URL path: http://www.cell-research.com/arts.asp?id=369 (2016-02-14)
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  • Cell Research

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    Original URL path: /artsmore1.asp?id=25 (2016-02-14)




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