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  • Cell Research
    Ecology and Biotechnology Institute of Hydrobiology Chinese Academy of Sciences Wuhan 430072 China 2College of Life Science Wuhan University Wuhan 430072 China Correspondence Zuo Yan ZHU Tel 86 27 6878 0628 E mail zyzhu ihb ac cn The integration pattern and adjacent host sequences of the inserted pMThGH transgene in the F4 hGH transgenic common carp were extensively studied Here we show that each F4 transgenic fish contained about 200 copies of the pMThGH transgene and the transgenes were integrated into the host genome generally with concatemers in a head to tail arrangement at 4 5 insertion sites By using a method of plasmid rescue four hundred copies of transgenes from two individuals of F4 transgenic fish A and B were recovered and clarified into 6 classes All classes of recovered transgenes contained either complete or partial pMThGH sequences The class I which comprised 83 and 84 5 respectively of the recovered transgene copies from fish A and B had maintained the original configuration indicating that most transgenes were faithfully inherited during the four generations of reproduction The other five classes were different from the original configuration in both molecular weight and restriction map indicating that a few transgenes had

    Original URL path: http://www.cell-research.com/arts.asp?id=1169 (2016-02-14)
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  • Cell Research
    and trafficked to cell surface by ER Golgi pathway and degraded by proteasomal or lysosomal pathways Li Qiang HE Fang CAI Yu LIU Mu Jun LIU Zhi Ping TAN Qian PAN Fai Yan FANG De Sheng LIANG Ling Qian WU Zhi Gao LONG He Ping DAI Kun XIA Jia Hui XIA Zhuo Hua ZHANG National Laboratory of Medical Genetics Central South University Changsha 410078 China Correspondence Kun XIA Tel 86

    Original URL path: http://www.cell-research.com/arts.asp?id=1170 (2016-02-14)
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  • Cell Research
    2 Department of Biochemistry and Molecular Biology College of Life Sciences Peking University Beijing 100871 China 3 Biocenter Oulu and Department of Biochemistry University of Oulu P O Box 3000 FIN 90014 University of Oulu Finland Correspondence Yu Xian ZHU Tel 86 10 6275 4427 E mail zhuyx water pku edu cn Genes encoding enzymes involved in biosynthesis of very long chain fatty acids were significantly up regulated during early cotton fiber development Two cDNAs GhKCR1 and GhKCR2 encoding putative cotton 3 ketoacyl CoA reductases that catalyze the second step in fatty acid elongation were isolated from developing cotton fibers GhKCR1 and 2 contain open reading frames of 963 bp and 924 bp encoding proteins of 320 and 307 amino acid residues respectively Quantatitive RT PCR analysis showed that both these genes were highly preferentially expressed during the cotton fiber elongation period with much lower levels recovered from roots stems and leaves GhKCR1 and 2 showed 30 32 identity to Saccharomyces cerevisiae Ybr159p at the deduced amino acid level These cotton cDNAs were cloned and expressed in yeast haploid ybr159wD mutant that was deficient in 3 ketoacyl CoA reductase activity Wild type growth rate was restored in ybr159wD cells that

    Original URL path: http://www.cell-research.com/arts.asp?id=1171 (2016-02-14)
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  • Cell Research
    Kunming 650223 China 2 Gradulate School of the Chinese Academy of Sciences Beijing 100039 China 3 Southwest Forestry College Kunming 650224 China 4 Capital University of Medical Sciences Beijing 100054 China Correspondence Jian Fan WEN Tel 86 871 5198682 E mail wenjf mail kiz ac cn The genes encoding type II DNA topoisomerases were investigated in Giardia lamblia genome and a type IIA gene GlTop 2 was identified It is a single copy gene with a 4476 bp long ORF without intron The deduced amino acid sequence shows strong homology to eukaryotic DNA Top 2 However some distortions were found such as six insertions in the ATPase domain and the central domain a 100 aa longer central domain a 200 aa shorter C terminal domain containing rich charged residues These features revealed by comparing with Top 2 of the host human might be helpful in exploiting drug selectivity for antigiardial therapy Phylogenetic analysis of eukaryotic enzymes showed that kinetoplastids plants fungi and animals were monophyletic groups and the animal and fungi lineages shared a more recent common ancestor than either did with the plant lineage microsporidia grouped with fungi However unlike many previous phylogenetic analyses the amitochondriate G lamblia was

    Original URL path: http://www.cell-research.com/arts.asp?id=1172 (2016-02-14)
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  • Cell Research

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    Original URL path: /artsmore1.asp?id=97 (2016-02-14)


  • Cell Research
    with its binding partners Yao Jiong WU 1 3 David P LA PIERRE 1 3 Jin WU 2 Albert J YEE 1 Burton B YANG 1 3 1 Sunnybrook Women s College Health Sciences Centre 2075 Bayview Avenue Toronto M4N 3M5 Canada 2 School of Chinese Medicine The University of Hong Kong Hong Kong SAR China 3 Department of Laboratory Medicine and Pathobiology University of Toronto Canada Correspondence Burton B YANG Tel 416 480 5874 E mail Burton Yang sw ca Versican belongs to the family of the large aggregating chondroitin sulfate proteoglycans located primarily within the extracellular matrix ECM Versican like other members of its family has unique N and C terminal globular regions each with multiple motifs A large glycosaminoglycan binding region lies between them This review will begin by outlining these structures in the context of ECM proteoglycans The diverse binding partners afforded to versican by virtue of its modular design will then be examined These include ECM components such as hyaluronan type I collagen tenascin R fibulin 1 and 2 fibrillin 1 fibronectin P and L selectins and chemokines Versican also binds to the cell surface proteins CD44 integrin b1 epidermal growth factor receptor and P

    Original URL path: http://www.cell-research.com/arts.asp?id=1158 (2016-02-14)
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  • Cell Research
    postcommitment stages Ana GARCÍA SACRISTÁN María J FERNÁNDEZ NESTOSA Pablo HERNÁNDEZ Jorge B SCHVARTZMAN Dora B KRIMER Department of Cell and Developmental Biology Centro de Investigaciones Biológicas Consejo Superior de Investigaciones Científicas Ramiro de Maeztu 9 Madrid 28040 Spain Present address Institute of Molecular Medicine 1649 028 Lisbon Medical School Lisbon Portugal Correspondence Dora B KRIMER Tel 34 918 373 112 4238 E mail dbkrimer cib csic es Clk STY is a LAMMER protein kinase capable to phosphorylate serine arginine rich SR proteins that modulate pre mRNA splicing Clk STY alternative splicing generates transcripts encoding a full length kinase and a truncated catalytically inactive protein Here we showed that clk STY as well as other members of the family e g clk2 clk3 and clk4 are up regulated during HMBA induced erythroleukemia cell differentiation mRNAs coding for the full length and the truncated forms were responsible for the overall increased expression In clk STY however a switch was observed for the ratio of the two alternative spliced products In undifferentiated cells the full length transcript was more abundant whereas the transcript encoding for the truncated form predominated at latter stages of differentiation Surprisingly overexpression of clk STY did not alter

    Original URL path: http://www.cell-research.com/arts.asp?id=1159 (2016-02-14)
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  • Cell Research
    Top 10 VOLUME 15 ISSUE 7 7 2005 504 510 Identification of novel nuclear localization signal within the ErbB 2 protein Qiao Qiao CHEN Xiao Ying CHEN Yun Yun JIANG Jing LIU School of Life Science University of Science and Technology of China Hefei 230027 China Correspondence Jing LIU Tel 86 551 3606294 E mail jliu ustc edu cn ErbB2 a member of the receptor tyrosine kinase family is frequently over expressed in breast cancer Proteolysis of the extracellular domain of ErbB2 results in constitutive activation of ErbB2 kinase Recent study reported that ErbB2 is found in the nucleus Here we showed that ErbB2 is imported into the nucleus through a nuclear localization signal NLS mediated mechanism The NLS sequence KRRQQKIRKYTMRR aa655 668 contains three clusters of basic amino acids and it is sufficient to target GFP into the nucleus However mutation in any basic amino acid cluster of this NLS sequence significantly affects its nuclear localization Furthermore it was found that this NLS is essential for the nuclear localization of ErbB2 since the intracellular domain of Erb2 lacking NLS completely abrogates its nuclear translocation Taken together our study identified a novel nuclear localization signal and reveals a novel mechanism

    Original URL path: http://www.cell-research.com/arts.asp?id=1160 (2016-02-14)
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