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  • 1
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    Anomalously metal-rich fluids form hydrothermal ore deposits (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-02-07
    Description: Hydrothermal ore deposits form when metals, often as sulfides, precipitate in abundance from aqueous solutions in Earth's crust. Much of our knowledge of the fluids involved comes from studies of fluid inclusions trapped in silicates or carbonates that are believed to represent aliquots of the same solutions that precipitated the ores. We used laser ablation inductively coupled plasma mass spectrometry to test this paradigm by analysis of fluid inclusions in sphalerite from two contrasting zinc-lead ore systems. Metal contents in these inclusions are up to two orders of magnitude greater than those in quartz-hosted inclusions and are much higher than previously thought, suggesting that ore formation is linked to influx of anomalously metal-rich fluids into systems dominated by barren fluids for much of their life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkinson, Jamie J -- Stoffell, Barry -- Wilkinson, Clara C -- Jeffries, Teresa E -- Appold, Martin S -- New York, N.Y. -- Science. 2009 Feb 6;323(5915):764-7. doi: 10.1126/science.1164436.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Science and Engineering, Imperial College London, South Kensington Campus, Exhibition Road, London SW7 2AZ, UK. j.wilkinson@imperial.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19197059" 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
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    Fungal diversity regulates plant-soil feedbacks in temperate grassland (2018)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2018
    Description: 〈p〉Feedbacks between plants and soil microbial communities play an important role in vegetation dynamics, but the underlying mechanisms remain unresolved. Here, we show that the diversity of putative pathogenic, mycorrhizal, and saprotrophic fungi is a primary regulator of plant-soil feedbacks across a broad range of temperate grassland plant species. We show that plant species with resource-acquisitive traits, such as high shoot nitrogen concentrations and thin roots, attract diverse communities of putative fungal pathogens and specialist saprotrophs, and a lower diversity of mycorrhizal fungi, resulting in strong plant growth suppression on soil occupied by the same species. Moreover, soil properties modulate feedbacks with fertile soils, promoting antagonistic relationships between soil fungi and plants. This study advances our capacity to predict plant-soil feedbacks and vegetation dynamics by revealing fundamental links between soil properties, plant resource acquisition strategies, and the diversity of fungal guilds in soil.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Mechanism of 5' splice site transfer for human spliceosome activation (2019)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2019
    Description: 〈p〉The prespliceosome, comprising U1 and U2 small nuclear ribonucleoproteins (snRNPs) bound to the precursor messenger RNA 5' splice site (5'SS) and branch point sequence, associates with the U4/U6.U5 tri-snRNP to form the fully assembled precatalytic pre–B spliceosome. Here, we report cryo–electron microscopy structures of the human pre–B complex captured before U1 snRNP dissociation at 3.3-angstrom core resolution and the human tri-snRNP at 2.9-angstrom resolution. U1 snRNP inserts the 5'SS–U1 snRNA helix between the two RecA domains of the Prp28 DEAD-box helicase. Adenosine 5'-triphosphate–dependent closure of the Prp28 RecA domains releases the 5'SS to pair with the nearby U6 ACAGAGA-box sequence presented as a mobile loop. The structures suggest that formation of the 5'SS-ACAGAGA helix triggers remodeling of an intricate protein-RNA network to induce Brr2 helicase relocation to its loading sequence in U4 snRNA, enabling Brr2 to unwind the U4/U6 snRNA duplex to allow U6 snRNA to form the catalytic center of the spliceosome.〈/p〉
    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
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    A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation (2019)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉During exon ligation, the 〈i〉S. cerevisiae〈/i〉 spliceosome recognizes the 3'-splice site (3'SS) of precursor mRNA through non-Watson-Crick pairing with the 5'SS and the branch adenosine, in a conformation stabilized by Prp18 and Prp8. Here we present the 3.3 Å cryoEM structure of a human post-catalytic spliceosome just after exon ligation. The 3'SS docks at the active site through conserved RNA interactions in the absence of Prp18. Unexpectedly, the metazoan-specific FAM32A directly bridges the 5'-exon and intron 3'SS of pre-mRNA and promotes exon-ligation, as shown by functional assays. CACTIN, SDE2, and NKAP – factors implicated in alternative splicing – further stabilize the catalytic conformation of the spliceosome during exon ligation. Together these four proteins act as exon ligation factors. Our study reveals how the human spliceosome has co-opted additional proteins to modulate a conserved RNA-based mechanism for 3'-splice site selection and to potentially fine-tune alternative splicing at the exon ligation stage.〈/p〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Natural Sciences in General
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  • 5
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    A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation (2019)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2019
    Description: 〈p〉During exon ligation, the 〈i〉Saccharomyces cerevisiae〈/i〉 spliceosome recognizes the 3'-splice site (3'SS) of precursor messenger RNA (pre-mRNA) through non–Watson-Crick pairing with the 5'SS and the branch adenosine, in a conformation stabilized by Prp18 and Prp8. Here we present the 3.3-angstrom cryo–electron microscopy structure of a human postcatalytic spliceosome just after exon ligation. The 3'SS docks at the active site through conserved RNA interactions in the absence of Prp18. Unexpectedly, the metazoan-specific FAM32A directly bridges the 5'-exon and intron 3'SS of pre-mRNA and promotes exon ligation, as shown by functional assays. CACTIN, SDE2, and NKAP—factors implicated in alternative splicing—further stabilize the catalytic conformation of the spliceosome during exon ligation. Together these four proteins act as exon ligation factors. Our study reveals how the human spliceosome has co-opted additional proteins to modulate a conserved RNA-based mechanism for 3'SS selection and to potentially fine-tune alternative splicing at the exon ligation stage.〈/p〉
    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
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    Testing the genetics of behavior in mice (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dawson, G R -- Flint, J -- Wilkinson, L S -- New York, N.Y. -- Science. 1999 Sep 24;285(5436):2068; author reply 2069-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10523201" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Laboratory/genetics ; *Behavior, Animal ; Confounding Factors (Epidemiology) ; Genetics, Behavioral/*methods ; Handling (Psychology) ; Mice ; Reproducibility of Results
    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
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    Surface expression of HLA-E, an inhibitor of natural killer cells, enhanced by human cytomegalovirus gpUL40 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-11
    Description: The nonclassical major histocompatibility complex (MHC) class I molecule HLA-E inhibits natural killer (NK) cell-mediated lysis by interacting with CD94/NKG2A receptors. Surface expression of HLA-E depends on binding of conserved peptides derived from MHC class I molecules. The same peptide is present in the leader sequence of the human cytomegalovirus (HCMV) glycoprotein UL40 (gpUL40). It is shown that, independently of the transporter associated with antigen processing, gpUL40 can up-regulate expression of HLA-E, which protects targets from NK cell lysis. While classical MHC class I molecules are down-regulated, HLA-E is up-regulated by HCMV. Induction of HLA-E surface expression by gpUL40 may represent an escape route for HCMV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomasec, P -- Braud, V M -- Rickards, C -- Powell, M B -- McSharry, B P -- Gadola, S -- Cerundolo, V -- Borysiewicz, L K -- McMichael, A J -- Wilkinson, G W -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1031.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Wales College of Medicine, Cardiff CF14 4XN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669413" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; *Antigens, CD ; Cell Line ; Cell Membrane/immunology ; Cells, Cultured ; Conserved Sequence ; Cytomegalovirus/genetics/immunology/*metabolism ; Cytotoxicity, Immunologic ; Down-Regulation ; HLA Antigens/immunology/*metabolism ; Histocompatibility Antigens Class I/immunology/*metabolism ; Humans ; Killer Cells, Natural/*immunology ; Molecular Sequence Data ; Open Reading Frames ; Protein Sorting Signals/chemistry/*metabolism ; Receptors, Immunologic/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection ; Up-Regulation ; Viral Proteins/chemistry/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 8
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    Role of a ubiquitin-like modification in polarized morphogenesis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-30
    Description: Type I ubiquitin-like proteins constitute a family of protein modifiers. Here we report the identification of a posttranslational protein modifier from Saccharomyces cerevisiae, Hub1. Overexpression of Hub1 resulted in enhanced conjugate formation when its carboxyl-terminal residue was deleted, suggesting that mature Hub1 may be produced by proteolytic processing. In vivo targets of Hub1 conjugation included cell polarity factors Sph1 and Hbt1. In the hub1Delta mutant, the subcellular localization of both Hbt1 and Sph1 was disrupted, and cell polarization during the formation of mating projections was defective. Consistent with these polarization defects, the hub1Delta mutant was deficient in mating.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dittmar, Gunnar A G -- Wilkinson, Caroline R M -- Jedrzejewski, Paul T -- Finley, Daniel -- GM58223/GM/NIGMS NIH HHS/ -- GM62663/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2442-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923536" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Evolution ; *Cell Polarity ; Electrophoresis, Gel, Two-Dimensional ; Gene Deletion ; Genes, Fungal ; Humans ; Ligases/chemistry/genetics/*metabolism ; Mass Spectrometry ; *Microfilament Proteins ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Peptides/pharmacology ; Phenotype ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*physiology ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Schizosaccharomyces/genetics ; Sequence Alignment ; Subcellular Fractions/metabolism ; Ubiquitin/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 9
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    Alternatively spliced TCR mRNA induced by disruption of reading frame (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-06
    Description: Nonsense codons that prematurely terminate translation generate potentially deleterious truncated proteins. Here, we show that the T cell receptor-beta (TCRbeta) gene, which acquires in-frame nonsense codons at high frequency during normal lymphocyte development, gives rise to an alternatively spliced transcript [alternative messenger RNA (alt-mRNA)] that skips the offending mutations that generate such nonsense codons. This alt-mRNA is up-regulated by a transfer RNA-dependent scanning mechanism that responds specifically to mutations that disrupt the reading frame. The finding that translation signals regulate the levels of alternatively spliced mRNAs generated in the nucleus may alter the current view of how gene expression is controlled in eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Jun -- Hamilton, John I -- Carter, Mark S -- Li, Shulin -- Wilkinson, Miles F -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):108-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, The University of Texas M. D. Anderson Cancer Center, Box 180, 1515 Holcombe Boulevard, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12098701" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Animals ; Cell Nucleus/genetics/metabolism ; *Codon, Nonsense ; Enhancer Elements, Genetic ; Exons ; Frameshift Mutation ; HeLa Cells ; Humans ; Introns ; Mice ; Mutation, Missense ; Protein Biosynthesis ; RNA, Messenger/genetics/metabolism ; *Reading Frames ; Receptors, Antigen, T-Cell, alpha-beta/*genetics ; Up-Regulation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 10
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    Plasma insulin-like growth factor-I and prostate cancer risk: a prospective study (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: Insulin-like growth factor-I (IGF-I) is a mitogen for prostate epithelial cells. To investigate associations between plasma IGF levels and prostate cancer risk, a nested case-control study within the Physicians' Health Study was conducted on prospectively collected plasma from 152 cases and 152 controls. A strong positive association was observed between IGF-I levels and prostate cancer risk. Men in the highest quartile of IGF-I levels had a relative risk of 4.3 (95 percent confidence interval 1.8 to 10.6) compared with men in the lowest quartile. This association was independent of baseline prostate-specific antigen levels. Identification of plasma IGF-I as a predictor of prostate cancer risk may have implications for risk reduction and treatment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, J M -- Stampfer, M J -- Giovannucci, E -- Gann, P H -- Ma, J -- Wilkinson, P -- Hennekens, C H -- Pollak, M -- CA-42182/CA/NCI NIH HHS/ -- CA-58684/CA/NCI NIH HHS/ -- T32 CA 09001-20/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):563-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Epidemiology, Harvard School of Public Health, 677 Huntington Avenue, Boston, MA 02115, USA. jmlchan@hsph.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438850" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Aged, 80 and over ; Analysis of Variance ; Case-Control Studies ; Confidence Intervals ; Disease Susceptibility ; Humans ; Insulin-Like Growth Factor Binding Protein 3/blood ; Insulin-Like Growth Factor I/*analysis ; Insulin-Like Growth Factor II/analysis ; Male ; Middle Aged ; Odds Ratio ; Prospective Studies ; Prostate-Specific Antigen/blood ; Prostatic Neoplasms/*etiology ; Reference Values ; Regression Analysis ; Risk ; Risk Factors
    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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