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  • 2000-2004  (611)
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  • 1
    Publication Date: 2003-11-01
    Description: Using high-resolution transmission electron microscopy, we obtained structure images of strontium titanate (SrTiO3) with a clearly resolved oxygen sublattice along different crystallographic directions in the bulklattice and for a Sigma3 tilt grain boundary. Comparison with image simulations showed that the grain boundary contains oxygen vacancies. Measurements of atom displacements near the grain boundary revealed close correspondence with theoretical calculations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Zaoli -- Sigle, Wilfried -- Phillipp, Fritz -- Ruhle, Manfred -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):846-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Metallforschung, Heisenbergstrasse 3, D-70569 Stuttgart, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593173" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2000-12-16
    Description: The completion of the Arabidopsis thaliana genome sequence allows a comparative analysis of transcriptional regulators across the three eukaryotic kingdoms. Arabidopsis dedicates over 5% of its genome to code for more than 1500 transcription factors, about 45% of which are from families specific to plants. Arabidopsis transcription factors that belong to families common to all eukaryotes do not share significant similarity with those of the other kingdoms beyond the conserved DNA binding domains, many of which have been arranged in combinations specific to each lineage. The genome-wide comparison reveals the evolutionary generation of diversity in the regulation of transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riechmann, J L -- Heard, J -- Martin, G -- Reuber, L -- Jiang, C -- Keddie, J -- Adam, L -- Pineda, O -- Ratcliffe, O J -- Samaha, R R -- Creelman, R -- Pilgrim, M -- Broun, P -- Zhang, J Z -- Ghandehari, D -- Sherman, B K -- Yu, G -- New York, N.Y. -- Science. 2000 Dec 15;290(5499):2105-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mendel Biotechnology, 21375 Cabot Boulevard, Hayward, CA 94545, USA. jriechmann@mendelbio.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11118137" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Arabidopsis/chemistry/*genetics ; Caenorhabditis elegans/chemistry/*genetics ; DNA/metabolism ; Drosophila melanogaster/chemistry/*genetics ; Eukaryotic Cells ; Evolution, Molecular ; Gene Duplication ; *Genome ; Genome, Plant ; Protein Binding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/chemistry/*genetics ; Transcription Factors/chemistry/*genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2001-10-20
    Description: Global Positioning System (GPS) measurements in China indicate that crustal shortening accommodates most of India's penetration into Eurasia. Deformation within the Tibetan Plateau and its margins, the Himalaya, the Altyn Tagh, and the Qilian Shan, absorbs more than 90% of the relative motion between the Indian and Eurasian plates. Internal shortening of the Tibetan plateau itself accounts for more than one-third of the total convergence. However, the Tibetan plateau south of the Kunlun and Ganzi-Mani faults is moving eastward relative to both India and Eurasia. This movement is accommodated through rotation of material around the eastern Syntaxis. The North China and South China blocks, east of the Tibetan Plateau, move coherently east-southeastward at rates of 2 to 8 millimeters per year and 6 to 11 millimeters per year, respectively, with respect to the stable Eurasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Q -- Zhang, P Z -- Freymueller, J T -- Bilham, R -- Larson, K M -- Lai, X -- You, X -- Niu, Z -- Wu, J -- Li, Y -- Liu, J -- Yang, Z -- Chen, Q -- New York, N.Y. -- Science. 2001 Oct 19;294(5542):574-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Seismology, China Seismological Bureau, Wuhan 430071, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11641493" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2000-02-11
    Description: The roles of phosphoinositide 3-kinase (PI3K) and phospholipase C (PLC) in chemoattractant-elicited responses were studied in mice lacking these key enzymes. PI3Kgamma was required for chemoattractant-induced production of phosphatidylinositol 3,4,5-trisphosphate [PtdIns (3,4,5)P3] and has an important role in chemoattractant-induced superoxide production and chemotaxis in mouse neutrophils and in production of T cell-independent antigen-specific antibodies composed of the immunoglobulin lambda light chain (TI-IglambdaL). The study of the mice lacking PLC-beta2 and -beta3 revealed that the PLC pathways have an important role in chemoattractant-mediated production of superoxide and regulation of protein kinases, but not chemotaxis. The PLC pathways also appear to inhibit the chemotactic activity induced by certain chemoattractants and to suppress TI-IglambdaL production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Z -- Jiang, H -- Xie, W -- Zhang, Z -- Smrcka, A V -- Wu, D -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1046-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Rochester, Rochester, NY 14642, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669417" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Chemokine CCL4 ; Chemotactic Factors/*pharmacology ; Chemotaxis, Leukocyte/*physiology ; Immunoglobulin lambda-Chains/biosynthesis ; Isoenzymes/*metabolism ; Macrophage Inflammatory Proteins/pharmacology ; Mice ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophil Infiltration ; Neutrophils/metabolism/*physiology ; Peritonitis/immunology ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase C beta ; Phosphorylation ; *Signal Transduction ; Skin Ulcer/pathology ; Superoxides/metabolism ; Type C Phospholipases/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2001-03-10
    Description: beta-Lactamase and penicillin-binding protein 2a mediate staphylococcal resistance to beta-lactam antibiotics, which are otherwise highly clinically effective. Production of these inducible proteins is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which autoactivates, and the repressor, which is inactivated, unblocking gene transcription. Compounds that disrupt this regulatory pathway could restore the activity of beta-lactam antibiotics against drug-resistant strains of staphylococci.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, H Z -- Hackbarth, C J -- Chansky, K M -- Chambers, H F -- AI4005804/AI/NIAID NIH HHS/ -- AI46610/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1962-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases, San Francisco General Hospital, Department of Medicine, University of California at San Francisco, 1001 Potrero Avenue, San Francisco, CA 94110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11239156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Anti-Bacterial Agents/metabolism/pharmacology ; Bacterial Proteins/chemistry/metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Catalysis ; Cell Membrane/metabolism ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/metabolism ; Genes, Regulator ; Metalloendopeptidases/chemistry/metabolism ; Mutagenesis, Site-Directed ; *Penicillin-Binding Proteins ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/chemistry/genetics/*metabolism ; *Signal Transduction ; Staphylococcus aureus/*drug effects/genetics/*metabolism ; Transformation, Bacterial ; *beta-Lactam Resistance ; beta-Lactamases/*biosynthesis ; beta-Lactams
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2003-08-16
    Description: We describe a general and rapid route for the addition of unnatural amino acids to the genetic code of Saccharomyces cerevisiae. Five amino acids have been incorporated into proteins efficiently and with high fidelity in response to the nonsense codon TAG. The side chains of these amino acids contain a keto group, which can be uniquely modified in vitro and in vivo with a wide range of chemical probes and reagents; a heavy atom-containing amino acid for structural studies; and photocrosslinkers for cellular studies of protein interactions. This methodology not only removes the constraints imposed by the genetic code on our ability to manipulate protein structure and function in yeast, it provides a gateway to the systematic expansion of the genetic codes of multicellular eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chin, Jason W -- Cropp, T Ashton -- Anderson, J Christopher -- Mukherji, Mridul -- Zhang, Zhiwen -- Schultz, Peter G -- GM 62159/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 15;301(5635):964-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12920298" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*genetics/metabolism ; Anticodon ; Azides/metabolism ; *Codon, Nonsense ; Escherichia coli/enzymology/genetics ; *Genetic Code ; Humans ; Methyltyrosines/*genetics/metabolism ; Mutation ; Phenylalanine/*analogs & derivatives/genetics/metabolism ; Protein Biosynthesis ; RNA, Transfer/genetics/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; Superoxide Dismutase/chemistry/genetics/metabolism ; Tyrosine-tRNA Ligase/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2004-12-14
    Description: We report a draft sequence for the genome of the domesticated silkworm (Bombyx mori), covering 90.9% of all known silkworm genes. Our estimated gene count is 18,510, which exceeds the 13,379 genes reported for Drosophila melanogaster. Comparative analyses to fruitfly, mosquito, spider, and butterfly reveal both similarities and differences in gene content.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xia, Qingyou -- Zhou, Zeyang -- Lu, Cheng -- Cheng, Daojun -- Dai, Fangyin -- Li, Bin -- Zhao, Ping -- Zha, Xingfu -- Cheng, Tingcai -- Chai, Chunli -- Pan, Guoqing -- Xu, Jinshan -- Liu, Chun -- Lin, Ying -- Qian, Jifeng -- Hou, Yong -- Wu, Zhengli -- Li, Guanrong -- Pan, Minhui -- Li, Chunfeng -- Shen, Yihong -- Lan, Xiqian -- Yuan, Lianwei -- Li, Tian -- Xu, Hanfu -- Yang, Guangwei -- Wan, Yongji -- Zhu, Yong -- Yu, Maode -- Shen, Weide -- Wu, Dayang -- Xiang, Zhonghuai -- Yu, Jun -- Wang, Jun -- Li, Ruiqiang -- Shi, Jianping -- Li, Heng -- Li, Guangyuan -- Su, Jianning -- Wang, Xiaoling -- Li, Guoqing -- Zhang, Zengjin -- Wu, Qingfa -- Li, Jun -- Zhang, Qingpeng -- Wei, Ning -- Xu, Jianzhe -- Sun, Haibo -- Dong, Le -- Liu, Dongyuan -- Zhao, Shengli -- Zhao, Xiaolan -- Meng, Qingshun -- Lan, Fengdi -- Huang, Xiangang -- Li, Yuanzhe -- Fang, Lin -- Li, Changfeng -- Li, Dawei -- Sun, Yongqiao -- Zhang, Zhenpeng -- Yang, Zheng -- Huang, Yanqing -- Xi, Yan -- Qi, Qiuhui -- He, Dandan -- Huang, Haiyan -- Zhang, Xiaowei -- Wang, Zhiqiang -- Li, Wenjie -- Cao, Yuzhu -- Yu, Yingpu -- Yu, Hong -- Li, Jinhong -- Ye, Jiehua -- Chen, Huan -- Zhou, Yan -- Liu, Bin -- Wang, Jing -- Ye, Jia -- Ji, Hai -- Li, Shengting -- Ni, Peixiang -- Zhang, Jianguo -- Zhang, Yong -- Zheng, Hongkun -- Mao, Bingyu -- Wang, Wen -- Ye, Chen -- Li, Songgang -- Wang, Jian -- Wong, Gane Ka-Shu -- Yang, Huanming -- Biology Analysis Group -- 1 P50 HG02351/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1937-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Southwest Agricultural University, Chongqing Beibei, 400716, China. xiaqy@swau.cq.cn〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15591204" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Anopheles/genetics ; Body Patterning/genetics ; Bombyx/*genetics/growth & development/metabolism ; Butterflies/genetics ; Computational Biology ; DNA Transposable Elements ; Drosophila melanogaster/genetics ; Exocrine Glands/metabolism ; Expressed Sequence Tags ; Female ; Genes, Homeobox ; *Genes, Insect ; *Genome ; Immunity, Innate/genetics ; Insect Hormones/genetics ; Insect Proteins/genetics ; Male ; Molecular Sequence Data ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Sex Determination Processes ; Spiders/genetics ; Wings, Animal/growth & development
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2004-01-24
    Description: Arabidopsis thaliana De-etiolated-1 (AtDET1) is a highly conserved protein, with orthologs in vertebrate and invertebrate organisms. AtDET1 negatively regulates photomorphogenesis, but its biochemical mechanism and function in other species are unknown. We report that human DET1 (hDET1) promotes ubiquitination and degradation of the proto-oncogenic transcription factor c-Jun by assembling a multisubunit ubiquitin ligase containing DNA Damage Binding Protein-1 (DDB1), cullin 4A (CUL4A), Regulator of Cullins-1 (ROC1), and constitutively photomorphogenic-1. Ablation of any subunit by RNA interference stabilized c-Jun and increased c-Jun-activated transcription. These findings characterize a c-Jun ubiquitin ligase and define a specific function for hDET1 in mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wertz, Ingrid E -- O'Rourke, Karen M -- Zhang, Zemin -- Dornan, David -- Arnott, David -- Deshaies, Raymond J -- Dixit, Vishva M -- GM065997/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1371-4. Epub 2004 Jan 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, Inc., South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739464" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cloning, Molecular ; Cullin Proteins/genetics/*metabolism ; DNA-Binding Proteins/metabolism ; Genes, jun ; Humans ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/metabolism ; Protein Binding ; Proteomics ; Proto-Oncogene Proteins c-jun/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Small Interfering/metabolism ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/chemistry/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2004-01-17
    Description: Posttranslational modifications of proteins regulate many biological processes, including metabolism, signal transduction, and gene expression. The synthetic challenges associated with generating homogeneous populations of selectively modified proteins, however, have hindered detailed studies of the effects of these modifications on protein structure and function. Here, we report an approach to the cotranslational synthesis of selectively glycosylated proteins in which the modified amino acid is genetically encoded. We show that myoglobin containing beta-N-acetylglucosamine (GlcNAc)-serine at a defined position can be expressed in Escherichia coli in good yield and with high fidelity. The beta-GlcNAc moiety can be recognized by a saccharide-binding protein, or subsequently modified with a galactosyltransferase to build more complex carbohydrates. This approach should be generally applicable to other posttranslational modifications such as protein phosphorylation, acetylation, and methylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Zhiwen -- Gildersleeve, Jeff -- Yang, Yu-Ying -- Xu, Ran -- Loo, Joseph A -- Uryu, Sean -- Wong, Chi-Huey -- Schultz, Peter G -- 5 F32 AI10419/AI/NIAID NIH HHS/ -- GM66494/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 16;303(5656):371-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14726590" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetylglucosamine/*metabolism ; Codon ; Directed Molecular Evolution ; Escherichia coli/genetics/metabolism ; Glycoproteins/*biosynthesis/chemistry ; Glycosylation ; Lectins/metabolism ; Mutation ; Myoglobin/*biosynthesis/chemistry/genetics ; *Protein Engineering ; Protein Processing, Post-Translational ; RNA, Transfer, Tyr/metabolism ; Serine/*metabolism ; Suppression, Genetic ; Tyrosine-tRNA Ligase/genetics/metabolism ; Uridine Diphosphate Galactose/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2004-04-02
    Print ISSN: 1550-7998
    Electronic ISSN: 1550-2368
    Topics: Physics
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