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  • Molecular Sequence Data  (456)
  • Temperature  (299)
  • Cell & Developmental Biology
  • Ecology
  • Fisheries
  • Inorganic Chemistry
  • American Association for the Advancement of Science (AAAS)  (786)
  • North West Water Authority
  • 2000-2004  (786)
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  • 1
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    Temperatures, winds, and composition in the saturnian system (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-25
    Description: Stratospheric temperatures on Saturn imply a strong decay of the equatorial winds with altitude. If the decrease in winds reported from recent Hubble Space Telescope images is not a temporal change, then the features tracked must have been at least 130 kilometers higher than in earlier studies. Saturn's south polar stratosphere is warmer than predicted from simple radiative models. The C/H ratio on Saturn is seven times solar, twice Jupiter's. Saturn's ring temperatures have radial variations down to the smallest scale resolved (100 kilometers). Diurnal surface temperature variations on Phoebe suggest a more porous regolith than on the jovian satellites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flasar, F M -- Achterberg, R K -- Conrath, B J -- Pearl, J C -- Bjoraker, G L -- Jennings, D E -- Romani, P N -- Simon-Miller, A A -- Kunde, V G -- Nixon, C A -- Bezard, B -- Orton, G S -- Spilker, L J -- Spencer, J R -- Irwin, P G J -- Teanby, N A -- Owen, T C -- Brasunas, J -- Segura, M E -- Carlson, R C -- Mamoutkine, A -- Gierasch, P J -- Schinder, P J -- Showalter, M R -- Ferrari, C -- Barucci, A -- Courtin, R -- Coustenis, A -- Fouchet, T -- Gautier, D -- Lellouch, E -- Marten, A -- Prange, R -- Strobel, D F -- Calcutt, S B -- Read, P L -- Taylor, F W -- Bowles, N -- Samuelson, R E -- Abbas, M M -- Raulin, F -- Ade, P -- Edgington, S -- Pilorz, S -- Wallis, B -- Wishnow, E H -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1247-51. Epub 2004 Dec 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Aeronautics and Space Administration (NASA)/Goddard Space Flight Center, Code 693, Greenbelt, MD 20771, USA. f.m.flasar@nasa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618486" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Carbon ; Extraterrestrial Environment ; Hydrogen ; Methane ; *Saturn ; Spacecraft ; Spectrum Analysis ; Temperature ; Wind
    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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    No transcription-translation feedback in circadian rhythm of KaiC phosphorylation (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: An autoregulatory transcription-translation feedback loop is thought to be essential in generating circadian rhythms in any model organism. In the cyanobacterium Synechococcus elongatus, the essential clock protein KaiC is proposed to form this type of transcriptional negative feedback. Nevertheless, we demonstrate here temperature-compensated, robust circadian cycling of KaiC phosphorylation even without kaiBC messenger RNA accumulation under continuous dark conditions. This rhythm persisted in the presence of a transcription or translation inhibitor. Moreover, kinetic profiles in the ratio of KaiC autophosphorylation-dephosphorylation were also temperature compensated in vitro. Thus, the cyanobacterial clock can keep time independent of de novo transcription and translation processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomita, Jun -- Nakajima, Masato -- Kondo, Takao -- Iwasaki, Hideo -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):251-4. Epub 2004 Nov 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, and Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550625" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/biosynthesis/*metabolism ; *Circadian Rhythm ; Circadian Rhythm Signaling Peptides and Proteins ; Darkness ; Feedback, Physiological ; Light ; Mutation ; Operon ; Phosphorylation ; Protein Biosynthesis ; RNA, Bacterial/metabolism ; RNA, Messenger/metabolism ; Recombinant Proteins/metabolism ; Synechococcus/*genetics/*metabolism ; Temperature ; Transcription, Genetic
    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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  • 3
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    Crystal structure of the long-chain fatty acid transporter FadL (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-05
    Description: The mechanisms by which hydrophobic molecules, such as long-chain fatty acids, enter cells are poorly understood. In Gram-negative bacteria, the lipopolysaccharide layer in the outer membrane is an efficient barrier for fatty acids and aromatic hydrocarbons destined for biodegradation. We report crystal structures of the long-chain fatty acid transporter FadL from Escherichia coli at 2.6 and 2.8 angstrom resolution. FadL forms a 14-stranded beta barrel that is occluded by a central hatch domain. The structures suggest that hydrophobic compounds bind to multiple sites in FadL and use a transport mechanism that involves spontaneous conformational changes in the hatch.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van den Berg, Bert -- Black, Paul N -- Clemons, William M Jr -- Rapoport, Tom A -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1506-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. lvandenberg@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178802" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/metabolism ; Binding Sites ; Biological Transport ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/metabolism ; Fatty Acid Transport Proteins ; Fatty Acids/*metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
    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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    Ultraconserved elements in the human genome (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-08
    Description: There are 481 segments longer than 200 base pairs (bp) that are absolutely conserved (100% identity with no insertions or deletions) between orthologous regions of the human, rat, and mouse genomes. Nearly all of these segments are also conserved in the chicken and dog genomes, with an average of 95 and 99% identity, respectively. Many are also significantly conserved in fish. These ultraconserved elements of the human genome are most often located either overlapping exons in genes involved in RNA processing or in introns or nearby genes involved in the regulation of transcription and development. Along with more than 5000 sequences of over 100 bp that are absolutely conserved among the three sequenced mammals, these represent a class of genetic elements whose functions and evolutionary origins are yet to be determined, but which are more highly conserved between these species than are proteins and appear to be essential for the ontogeny of mammals and other vertebrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bejerano, Gill -- Pheasant, Michael -- Makunin, Igor -- Stephen, Stuart -- Kent, W James -- Mattick, John S -- Haussler, David -- 1P41HG02371/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2004 May 28;304(5675):1321-5. Epub 2004 May 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomolecular Engineering, University of California Santa Cruz, Santa Cruz, CA 95064, USA. jill@soe.ucsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131266" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Animals ; Base Sequence ; Chickens/genetics ; Computational Biology ; *Conserved Sequence ; DNA, Intergenic ; Dogs/genetics ; Evolution, Molecular ; Exons ; Gene Expression Regulation ; Genes ; Genome ; *Genome, Human ; Humans ; Introns ; Mice/genetics ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; RNA/chemistry/genetics/metabolism ; Rats/genetics ; Takifugu/genetics
    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
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    African origins of the domestic donkey (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beja-Pereira, Albano -- England, Phillip R -- Ferrand, Nuno -- Jordan, Steve -- Bakhiet, Amel O -- Abdalla, Mohammed A -- Mashkour, Marjan -- Jordana, Jordi -- Taberlet, Pierre -- Luikart, Gordon -- New York, N.Y. -- Science. 2004 Jun 18;304(5678):1781.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lab. d'Ecologie Alpine, UMR CNRS-UJF 5553, 38041 Grenoble, France. albano.beja-pereira@ujf-grenoble.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15205528" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animal Husbandry ; Animals ; *Animals, Domestic/classification/genetics ; Animals, Wild/genetics ; Archaeology ; Asia ; Cytochromes b/genetics ; DNA, Mitochondrial/genetics ; Equidae/classification/*genetics ; Haplotypes ; Molecular Sequence Data ; *Phylogeny ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
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  • 6
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    Planetary science. Alien weather at the poles of Mars (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Forget, Francois -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1298-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Meteorologie Dynamique, Institut Pierre Simon Laplace, Universite Paris 6, Paris cedex 5, France. francois.forget@lmd.jussieu.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550647" target="_blank"〉PubMed〈/a〉
    Keywords: *Argon ; Atmosphere ; *Carbon Dioxide ; *Dry Ice ; Extraterrestrial Environment ; Gases ; *Mars ; Seasons ; Spectrometry, Gamma ; Temperature ; Weather
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 7
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    Coordination of meiotic recombination, pairing, and synapsis by PHS1 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-06
    Description: Pairing, synapsis, and recombination are prerequisites for accurate chromosome segregation in meiosis. The phs1 gene in maize is required for pairing to occur between homologous chromosomes. In the phs1 mutant, homologous chromosome synapsis is completely replaced by synapsis between nonhomologous partners. The phs1 gene is also required for installation of the meiotic recombination machinery on chromosomes, as the mutant almost completely lacks chromosomal foci of the recombination protein RAD51. Thus, in the phs1 mutant, synapsis is uncoupled from recombination and pairing. The protein encoded by the phs1 gene likely acts in a multistep process to coordinate pairing, recombination, and synapsis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pawlowski, Wojciech P -- Golubovskaya, Inna N -- Timofejeva, Ljudmilla -- Meeley, Robert B -- Sheridan, William F -- Cande, W Zacheus -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):89-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. wpawlows@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704428" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Nucleus/metabolism ; *Chromosome Pairing ; Chromosomes, Plant/*physiology ; Cloning, Molecular ; Conserved Sequence ; DNA, Plant/metabolism ; DNA-Binding Proteins ; Genes, Plant ; In Situ Hybridization, Fluorescence ; In Situ Nick-End Labeling/methods ; *Meiosis ; Molecular Sequence Data ; Mutation ; Phenotype ; Plant Proteins/chemistry/genetics/*physiology ; RNA, Ribosomal, 5S/genetics ; Rad51 Recombinase ; *Recombination, Genetic ; Sequence Alignment ; Synaptonemal Complex/metabolism/ultrastructure ; Telomere/physiology ; Zea mays/*genetics/physiology
    Print ISSN: 0036-8075
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  • 8
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    Climate change. All downhill from here? (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krajick, Kevin -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1600-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15016975" target="_blank"〉PubMed〈/a〉
    Keywords: *Altitude ; Animals ; Biodiversity ; *Climate ; *Ecosystem ; Environment ; Environmental Pollutants/analysis ; Fishes/physiology ; Geography ; Lagomorpha/physiology ; *Plant Development ; Population Dynamics ; Temperature ; Trees/*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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  • 9
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    Environmental genome shotgun sequencing of the Sargasso Sea (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-07
    Description: We have applied "whole-genome shotgun sequencing" to microbial populations collected en masse on tangential flow and impact filters from seawater samples collected from the Sargasso Sea near Bermuda. A total of 1.045 billion base pairs of nonredundant sequence was generated, annotated, and analyzed to elucidate the gene content, diversity, and relative abundance of the organisms within these environmental samples. These data are estimated to derive from at least 1800 genomic species based on sequence relatedness, including 148 previously unknown bacterial phylotypes. We have identified over 1.2 million previously unknown genes represented in these samples, including more than 782 new rhodopsin-like photoreceptors. Variation in species present and stoichiometry suggests substantial oceanic microbial diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venter, J Craig -- Remington, Karin -- Heidelberg, John F -- Halpern, Aaron L -- Rusch, Doug -- Eisen, Jonathan A -- Wu, Dongying -- Paulsen, Ian -- Nelson, Karen E -- Nelson, William -- Fouts, Derrick E -- Levy, Samuel -- Knap, Anthony H -- Lomas, Michael W -- Nealson, Ken -- White, Owen -- Peterson, Jeremy -- Hoffman, Jeff -- Parsons, Rachel -- Baden-Tillson, Holly -- Pfannkoch, Cynthia -- Rogers, Yu-Hui -- Smith, Hamilton O -- New York, N.Y. -- Science. 2004 Apr 2;304(5667):66-74. Epub 2004 Mar 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biological Energy Alternatives, 1901 Research Boulevard, Rockville, MD 20850, USA. jcventer@tcag.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001713" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/*genetics ; Atlantic Ocean ; Bacteria/*genetics ; Bacteriophages/genetics ; Biodiversity ; Computational Biology ; Cyanobacteria/genetics/growth & development/metabolism ; *Ecosystem ; Eukaryotic Cells ; Genes, Archaeal ; Genes, Bacterial ; Genes, rRNA ; Genome, Archaeal ; *Genome, Bacterial ; *Genomics ; Molecular Sequence Data ; Photosynthesis ; Phylogeny ; Plasmids ; Rhodopsin/genetics ; Rhodopsins, Microbial ; Seawater/*microbiology ; *Sequence Analysis, DNA ; Water Microbiology
    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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  • 10
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    Local nanomechanical motion of the cell wall of Saccharomyces cerevisiae (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-25
    Description: We demonstrate that the cell wall of living Saccharomyces cerevisiae (baker's yeast) exhibits local temperature-dependent nanomechanical motion at characteristic frequencies. The periodic motions in the range of 0.8 to 1.6 kHz with amplitudes of approximately 3 nm were measured using the cantilever of an atomic force microscope (AFM). Exposure of the cells to a metabolic inhibitor causes the periodic motion to cease. From the strong frequency dependence on temperature, we derive an activation energy of 58 kJ/mol, which is consistent with the cell's metabolism involving molecular motors such as kinesin, dynein, and myosin. The magnitude of the forces observed ( approximately 10 nN) suggests concerted nanomechanical activity is operative in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelling, Andrew E -- Sehati, Sadaf -- Gralla, Edith B -- Valentine, Joan S -- Gimzewski, James K -- DK46828/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1147-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15326353" target="_blank"〉PubMed〈/a〉
    Keywords: Biomechanical Phenomena ; Cell Wall/*physiology/ultrastructure ; Fourier Analysis ; Microscopy, Atomic Force ; Motion ; Movement ; Saccharomyces cerevisiae/drug effects/*physiology/ultrastructure ; Sodium Azide/pharmacology ; Temperature
    Print ISSN: 0036-8075
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  • 11
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    RNAi-mediated targeting of heterochromatin by the RITS complex (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-06
    Description: RNA interference (RNAi) is a widespread silencing mechanism that acts at both the posttranscriptional and transcriptional levels. Here, we describe the purification of an RNAi effector complex termed RITS (RNA-induced initiation of transcriptional gene silencing) that is required for heterochromatin assembly in fission yeast. The RITS complex contains Ago1 (the fission yeast Argonaute homolog), Chp1 (a heterochromatin-associated chromodomain protein), and Tas3 (a novel protein). In addition, the complex contains small RNAs that require the Dicer ribonuclease for their production. These small RNAs are homologous to centromeric repeats and are required for the localization of RITS to heterochromatic domains. The results suggest a mechanism for the role of the RNAi machinery and small RNAs in targeting of heterochromatin complexes and epigenetic gene silencing at specific chromosomal loci.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3244756/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3244756/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verdel, Andre -- Jia, Songtao -- Gerber, Scott -- Sugiyama, Tomoyasu -- Gygi, Steven -- Grewal, Shiv I S -- Moazed, Danesh -- R01 GM072805/GM/NIGMS NIH HHS/ -- R01 GM072805-01/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):672-6. Epub 2004 Jan 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704433" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Argonaute Proteins ; Cell Cycle Proteins/chemistry/genetics/isolation & purification/*metabolism ; Centromere/metabolism ; Chromosomes, Fungal/metabolism ; Endoribonucleases/chemistry/genetics/isolation & purification/metabolism ; Genes, Reporter ; Heterochromatin/*metabolism ; Mass Spectrometry ; Models, Genetic ; Molecular Sequence Data ; Mutation ; Precipitin Tests ; Protein Binding ; *RNA Interference ; RNA, Fungal/metabolism ; RNA, Small Interfering/metabolism ; RNA-Binding Proteins ; Ribonuclease III/metabolism ; Schizosaccharomyces/*genetics/metabolism ; Schizosaccharomyces pombe Proteins/chemistry/genetics/isolation & ; purification/*metabolism
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  • 12
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    Jupiter's atmospheric composition from the Cassini thermal infrared spectroscopy experiment (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-21
    Description: The Composite Infrared Spectrometer observed Jupiter in the thermal infrared during the swing-by of the Cassini spacecraft. Results include the detection of two new stratospheric species, the methyl radical and diacetylene, gaseous species present in the north and south auroral infrared hot spots; determination of the variations with latitude of acetylene and ethane, the latter a tracer of atmospheric motion; observations of unexpected spatial distributions of carbon dioxide and hydrogen cyanide, both considered to be products of comet Shoemaker-Levy 9 impacts; characterization of the morphology of the auroral infrared hot spot acetylene emission; and a new evaluation of the energetics of the northern auroral infrared hot spot.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kunde, V G -- Flasar, F M -- Jennings, D E -- Bezard, B -- Strobel, D F -- Conrath, B J -- Nixon, C A -- Bjoraker, G L -- Romani, P N -- Achterberg, R K -- Simon-Miller, A A -- Irwin, P -- Brasunas, J C -- Pearl, J C -- Smith, M D -- Orton, G S -- Gierasch, P J -- Spilker, L J -- Carlson, R C -- Mamoutkine, A A -- Calcutt, S B -- Read, P L -- Taylor, F W -- Fouchet, T -- Parrish, P -- Barucci, A -- Courtin, R -- Coustenis, A -- Gautier, D -- Lellouch, E -- Marten, A -- Prange, R -- Biraud, Y -- Ferrari, C -- Owen, T C -- Abbas, M M -- Samuelson, R E -- Raulin, F -- Ade, P -- Cesarsky, C J -- Grossman, K U -- Coradini, A -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1582-6. Epub 2004 Aug 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy, University of Maryland, College Park, MD 20742, USA. Virgil.G.Kunde.1@gsfc.nasa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15319491" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylene ; Atmosphere ; *Carbon Dioxide ; Ethane ; Extraterrestrial Environment ; *Hydrocarbons ; *Hydrogen Cyanide ; *Jupiter ; Spacecraft ; Spectrum Analysis ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    The structure and receptor binding properties of the 1918 influenza hemagglutinin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: The 1918 influenza pandemic resulted in about 20 million deaths. This enormous impact, coupled with renewed interest in emerging infections, makes characterization of the virus involved a priority. Receptor binding, the initial event in virus infection, is a major determinant of virus transmissibility that, for influenza viruses, is mediated by the hemagglutinin (HA) membrane glycoprotein. We have determined the crystal structures of the HA from the 1918 virus and two closely related HAs in complex with receptor analogs. They explain how the 1918 HA, while retaining receptor binding site amino acids characteristic of an avian precursor HA, is able to bind human receptors and how, as a consequence, the virus was able to spread in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamblin, S J -- Haire, L F -- Russell, R J -- Stevens, D J -- Xiao, B -- Ha, Y -- Vasisht, N -- Steinhauer, D A -- Daniels, R S -- Elliot, A -- Wiley, D C -- Skehel, J J -- AI-13654/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1838-42. Epub 2004 Feb 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764886" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Birds ; Crystallography, X-Ray ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/*metabolism ; History, 20th Century ; Humans ; Hydrogen Bonding ; Influenza A virus/*immunology/metabolism/pathogenicity ; Influenza, Human/epidemiology/history/*virology ; Membrane Glycoproteins/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*metabolism ; Sequence Alignment ; Sialic Acids/metabolism ; Species Specificity ; Swine
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  • 14
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    Mutations in a human ROBO gene disrupt hindbrain axon pathway crossing and morphogenesis (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-24
    Description: The mechanisms controlling axon guidance are of fundamental importance in understanding brain development. Growing corticospinal and somatosensory axons cross the midline in the medulla to reach their targets and thus form the basis of contralateral motor control and sensory input. The motor and sensory projections appeared uncrossed in patients with horizontal gaze palsy with progressive scoliosis (HGPPS). In patients affected with HGPPS, we identified mutations in the ROBO3 gene, which shares homology with roundabout genes important in axon guidance in developing Drosophila, zebrafish, and mouse. Like its murine homolog Rig1/Robo3, but unlike other Robo proteins, ROBO3 is required for hindbrain axon midline crossing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618874/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618874/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jen, Joanna C -- Chan, Wai-Man -- Bosley, Thomas M -- Wan, Jijun -- Carr, Janai R -- Rub, Udo -- Shattuck, David -- Salamon, Georges -- Kudo, Lili C -- Ou, Jing -- Lin, Doris D M -- Salih, Mustafa A M -- Kansu, Tulay -- Al Dhalaan, Hesham -- Al Zayed, Zayed -- MacDonald, David B -- Stigsby, Bent -- Plaitakis, Andreas -- Dretakis, Emmanuel K -- Gottlob, Irene -- Pieh, Christina -- Traboulsi, Elias I -- Wang, Qing -- Wang, Lejin -- Andrews, Caroline -- Yamada, Koki -- Demer, Joseph L -- Karim, Shaheen -- Alger, Jeffry R -- Geschwind, Daniel H -- Deller, Thomas -- Sicotte, Nancy L -- Nelson, Stanley F -- Baloh, Robert W -- Engle, Elizabeth C -- DC00162/DC/NIDCD NIH HHS/ -- DC05524/DC/NIDCD NIH HHS/ -- EY12498/EY/NEI NIH HHS/ -- EY13583/EY/NEI NIH HHS/ -- EY15298/EY/NEI NIH HHS/ -- EY15311/EY/NEI NIH HHS/ -- MH60233/MH/NIMH NIH HHS/ -- P30 HD 18655/HD/NICHD NIH HHS/ -- R01 EY008313/EY/NEI NIH HHS/ -- R01 EY008313-14/EY/NEI NIH HHS/ -- R01 HL066251/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1509-13. Epub 2004 Apr 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of California, Los Angeles, CA 90095, USA. jjen@ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15105459" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Alternative Splicing ; Amino Acid Motifs ; Amino Acid Sequence ; Axons/*physiology ; Evoked Potentials, Motor ; Evoked Potentials, Somatosensory ; Female ; Functional Laterality ; Genetic Linkage ; Humans ; In Situ Hybridization ; Magnetic Resonance Imaging ; Male ; Medulla Oblongata/growth & development/pathology ; Microsatellite Repeats ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Neural Pathways ; Ophthalmoplegia/*genetics/pathology/physiopathology ; Pedigree ; Protein Structure, Tertiary ; Receptors, Immunologic/chemistry/*genetics/*metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Rhombencephalon/*growth & development/pathology ; Scoliosis/*genetics/pathology/physiopathology ; Sequence Analysis, DNA ; Syndrome
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  • 15
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    Honey bee nest thermoregulation: diversity promotes stability (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-06-26
    Description: A honey bee colony is characterized by high genetic diversity among its workers, generated by high levels of multiple mating by its queen. Few clear benefits of this genetic diversity are known. Here we show that brood nest temperatures in genetically diverse colonies (i.e., those sired by several males) tend to be more stable than in genetically uniform ones (i.e., those sired by one male). One reason this increased stability arises is because genetically determined diversity in workers' temperature response thresholds modulates the hive-ventilating behavior of individual workers, preventing excessive colony-level responses to temperature fluctuations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Julia C -- Myerscough, Mary R -- Graham, Sonia -- Oldroyd, Benjamin P -- New York, N.Y. -- Science. 2004 Jul 16;305(5682):402-4. Epub 2004 Jun 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, Macleay Building A12, University of Sydney, NSW 2006, Australia. jjones@bio.usyd.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15218093" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bees/genetics/*physiology ; Behavior, Animal ; Biological Evolution ; Body Temperature Regulation ; Female ; *Genetic Variation ; Homeostasis ; Male ; Selection, Genetic ; Sexual Behavior, Animal ; Temperature
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    Use of CD134 as a primary receptor by the feline immunodeficiency virus (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-21
    Description: Feline immunodeficiency virus (FIV) induces a disease similar to acquired immunodeficiency syndrome (AIDS) in cats, yet in contrast to human immunodeficiency virus (HIV), CD4 is not the viral receptor. We identified a primary receptor for FIV as CD134 (OX40), a T cell activation antigen and costimulatory molecule. CD134 expression promotes viral binding and renders cells permissive for viral entry, productive infection, and syncytium formation. Infection is CXCR4-dependent, analogous to infection with X4 strains of HIV. Thus, despite the evolutionary divergence of the feline and human lentiviruses, both viruses use receptors that target the virus to a subset of cells that are pivotal to the acquired immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimojima, Masayuki -- Miyazawa, Takayuki -- Ikeda, Yasuhiro -- McMonagle, Elizabeth L -- Haining, Hayley -- Akashi, Hiroomi -- Takeuchi, Yasuhiro -- Hosie, Margaret J -- Willett, Brian J -- R01 AI49765-01A1/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1192-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterinary Microbiology, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CD4-Positive T-Lymphocytes/immunology/metabolism/virology ; Cats ; Cell Line ; Cell Line, Tumor ; DNA, Complementary ; Gene Library ; HIV/metabolism ; HeLa Cells ; Heterocyclic Compounds/pharmacology ; Humans ; Immunodeficiency Virus, Feline/*metabolism/pathogenicity ; Mice ; Molecular Sequence Data ; NIH 3T3 Cells ; Receptors, CXCR4/antagonists & inhibitors/metabolism ; Receptors, OX40 ; Receptors, Tumor Necrosis Factor/chemistry/genetics/immunology/*metabolism ; Receptors, Virus/chemistry/genetics/immunology/*metabolism ; Species Specificity ; Transduction, Genetic ; Transfection
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    Unification in the century of biology (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kafatos, Fotis C -- Eisner, Thomas -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1257.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14988521" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior ; Biological Evolution ; *Biological Science Disciplines ; Ecology ; Genetics ; Humans ; *Interdisciplinary Communication ; Molecular Biology
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  • 18
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    SOS response induction by beta-lactams and bacterial defense against antibiotic lethality (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-17
    Description: The SOS response aids bacterial propagation by inhibiting cell division during repair of DNA damage. We report that inactivation of the ftsI gene product, penicillin binding protein 3, by either beta-lactam antibiotics or genetic mutation induces SOS in Escherichia coli through the DpiBA two-component signal transduction system. This event, which requires the SOS-promoting recA and lexA genes as well as dpiA, transiently halts bacterial cell division, enabling survival to otherwise lethal antibiotic exposure. Our findings reveal defective cell wall synthesis as an unexpected initiator of the bacterial SOS response, indicate that beta-lactam antibiotics are extracellular stimuli of this response, and demonstrate a novel mechanism for mitigation of antimicrobial lethality.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Christine -- Thomsen, Line Elnif -- Gaggero, Carina -- Mosseri, Ronen -- Ingmer, Hanne -- Cohen, Stanley N -- R01 AI08619/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1629-31. Epub 2004 Aug 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15308764" target="_blank"〉PubMed〈/a〉
    Keywords: Ampicillin/*pharmacology ; Anti-Bacterial Agents/metabolism/*pharmacology ; Bacterial Proteins/genetics/metabolism ; Carrier Proteins/genetics/metabolism ; Cell Division ; Cell Wall/metabolism ; Escherichia coli/*drug effects/genetics/*metabolism ; Escherichia coli Proteins/genetics/metabolism ; Hexosyltransferases/genetics/metabolism ; Lac Operon ; Muramoylpentapeptide Carboxypeptidase/genetics/metabolism ; Mutation ; Operon ; Penicillin-Binding Proteins ; *Peptidoglycan Glycosyltransferase ; Peptidyl Transferases/genetics/metabolism ; Protein Kinases/genetics/metabolism ; *SOS Response (Genetics) ; Signal Transduction ; Temperature ; Transcription Factors/genetics/metabolism ; beta-Galactosidase/biosynthesis ; beta-Lactams/metabolism/*pharmacology
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    Reflectins: the unusual proteins of squid reflective tissues (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-01-13
    Description: A family of unusual proteins is deposited in flat, structural platelets in reflective tissues of the squid Euprymna scolopes. These proteins, which we have named reflectins, are encoded by at least six genes in three subfamilies and have no reported homologs outside of squids. Reflectins possess five repeating domains, which are highly conserved among members of the family. The proteins have a very unusual composition, with four relatively rare residues (tyrosine, methionine, arginine, and tryptophan) comprising approximately 57% of a reflectin, and several common residues (alanine, isoleucine, leucine, and lysine) occurring in none of the family members. These protein-based reflectors in squids provide a marked example of nanofabrication in animal systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crookes, Wendy J -- Ding, Lin-Lin -- Huang, Qing Ling -- Kimbell, Jennifer R -- Horwitz, Joseph -- McFall-Ngai, Margaret J -- NEI R01 EY3897/EY/NEI NIH HHS/ -- R01 A150661/PHS HHS/ -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):235-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kewalo Marine Laboratory, Pacific Biomedical Research Center, University of Hawaii-Manoa, 41 Ahui Street, Honolulu, HI 96813, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716016" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; DNA, Complementary ; Decapodiformes/anatomy & histology/*chemistry/genetics ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Immunohistochemistry ; *Light ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Proteins/*analysis/*chemistry/genetics/isolation & purification ; Sequence Alignment ; Solubility
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  • 20
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    Recruitment and spreading of the C. elegans dosage compensation complex along X chromosomes (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-21
    Description: To achieve X-chromosome dosage compensation, organisms must distinguish X chromosomes from autosomes. We identified multiple, cis-acting regions that recruit the Caenorhabditis elegans dosage compensation complex (DCC) through a search for regions of X that bind the complex when detached from X. The DCC normally assembles along the entire X chromosome, but not all detached regions recruit the complex, despite having genes known to be dosage compensated on the native X. Thus, the DCC binds first to recruitment sites, then spreads to neighboring X regions to accomplish chromosome-wide gene repression. From a large chromosomal domain, we defined a 793-base pair fragment that functions in vivo as an X-recognition element to recruit the DCC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Csankovszki, Gyorgyi -- McDonel, Patrick -- Meyer, Barbara J -- F32-GM065007/GM/NIGMS NIH HHS/ -- R37-GM30702/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1182-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3204, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976312" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Base Sequence ; Binding Sites ; Caenorhabditis elegans/*genetics/metabolism ; Caenorhabditis elegans Proteins/*metabolism ; Carrier Proteins/metabolism ; Chromosomes/metabolism ; Cosmids ; DNA-Binding Proteins/metabolism ; Disorders of Sex Development ; *Dosage Compensation, Genetic ; Female ; In Situ Hybridization, Fluorescence ; Male ; Models, Genetic ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Repetitive Sequences, Nucleic Acid ; X Chromosome/*metabolism
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    Bushmeat hunting, wildlife declines, and fish supply in West Africa (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-11-13
    Description: The multibillion-dollar trade in bushmeat is among the most immediate threats to the persistence of tropical vertebrates, but our understanding of its underlying drivers and effects on human welfare is limited by a lack of empirical data. We used 30 years of data from Ghana to link mammal declines to the bushmeat trade and to spatial and temporal changes in the availability of fish. We show that years of poor fish supply coincided with increased hunting in nature reserves and sharp declines in biomass of 41 wildlife species. Local market data provide evidence of a direct link between fish supply and subsequent bushmeat demand in villages and show bushmeat's role as a dietary staple in the region. Our results emphasize the urgent need to develop cheap protein alternatives to bushmeat and to improve fisheries management by foreign and domestic fleets to avert extinctions of tropical wildlife.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brashares, Justin S -- Arcese, Peter -- Sam, Moses K -- Coppolillo, Peter B -- Sinclair, A R E -- Balmford, Andrew -- New York, N.Y. -- Science. 2004 Nov 12;306(5699):1180-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Conservation Biology Group, Department of Zoology, University of Cambridge, Cambridge CB2 3EJ, UK. brashares@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539602" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture ; Animals ; *Animals, Wild ; Biodiversity ; Biomass ; Commerce ; Conservation of Natural Resources ; Fisheries ; *Fishes ; *Food Supply ; Ghana ; Humans ; *Mammals ; *Meat ; Population Density ; Population Dynamics
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  • 22
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    Atmospheric imaging results from the Mars exploration rovers: Spirit and Opportunity (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-12-04
    Description: A visible atmospheric optical depth of 0.9 was measured by the Spirit rover at Gusev crater and by the Opportunity rover at Meridiani Planum. Optical depth decreased by about 0.6 to 0.7% per sol through both 90-sol primary missions. The vertical distribution of atmospheric dust at Gusev crater was consistent with uniform mixing, with a measured scale height of 11.56 +/- 0.62 kilometers. The dust's cross section weighted mean radius was 1.47 +/- 0.21 micrometers (mm) at Gusev and 1.52 +/- 0.18 mm at Meridiani. Comparison of visible optical depths with 9-mm optical depths shows a visible-to-infrared optical depth ratio of 2.0 +/- 0.2 for comparison with previous monitoring of infrared optical depths.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lemmon, M T -- Wolff, M J -- Smith, M D -- Clancy, R T -- Banfield, D -- Landis, G A -- Ghosh, A -- Smith, P H -- Spanovich, N -- Whitney, B -- Whelley, P -- Greeley, R -- Thompson, S -- Bell, J F 3rd -- Squyres, S W -- New York, N.Y. -- Science. 2004 Dec 3;306(5702):1753-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Texas A&M University, College Station, TX 77843, USA. lemmon@tamu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15576613" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Atmosphere ; Carbon Dioxide ; Extraterrestrial Environment ; *Mars ; Solar System ; Spacecraft ; Temperature
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  • 23
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    Mars' south polar Ar enhancement: a tracer for south polar seasonal meridional mixing (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-10-09
    Description: The gamma ray spectrometer on the Mars Odyssey spacecraft measured an enhancement of atmospheric argon over southern high latitudes during autumn followed by dissipation during winter and spring. Argon does not freeze at temperatures normal for southern winter (approximately 145 kelvin) and is left in the atmosphere, enriched relative to carbon dioxide (CO2), as the southern seasonal cap of CO2 frost accumulates. Calculations of seasonal transport of argon into and out of southern high latitudes point to meridional (north-south) mixing throughout southern winter and spring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sprague, A L -- Boynton, W V -- Kerry, K E -- Janes, D M -- Hunten, D M -- Kim, K J -- Reedy, R C -- Metzger, A E -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1364-7. Epub 2004 Oct 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lunar and Planetary Laboratory, 1629 East University Boulevard, University of Arizona, Tucson, AZ 85721-0092, USA. sprague@lpl.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472041" target="_blank"〉PubMed〈/a〉
    Keywords: *Argon ; Atmosphere ; *Carbon Dioxide ; *Dry Ice ; Extraterrestrial Environment ; *Mars ; Mathematics ; Seasons ; Spectrometry, Gamma ; Sunlight ; Temperature ; Weather
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    Multiple Ebola virus transmission events and rapid decline of central African wildlife (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-17
    Description: Several human and animal Ebola outbreaks have occurred over the past 4 years in Gabon and the Republic of Congo. The human outbreaks consisted of multiple simultaneous epidemics caused by different viral strains, and each epidemic resulted from the handling of a distinct gorilla, chimpanzee, or duiker carcass. These animal populations declined markedly during human Ebola outbreaks, apparently as a result of Ebola infection. Recovered carcasses were infected by a variety of Ebola strains, suggesting that Ebola outbreaks in great apes result from multiple virus introductions from the natural host. Surveillance of animal mortality may help to predict and prevent human Ebola outbreaks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leroy, Eric M -- Rouquet, Pierre -- Formenty, Pierre -- Souquiere, Sandrine -- Kilbourne, Annelisa -- Froment, Jean-Marc -- Bermejo, Magdalena -- Smit, Sheilag -- Karesh, William -- Swanepoel, Robert -- Zaki, Sherif R -- Rollin, Pierre E -- New York, N.Y. -- Science. 2004 Jan 16;303(5656):387-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Recherche pour le Developpement, UR034, Centre International de Recherches Medicales de Franceville, BP 769 Franceville, Gabon. Eric.Leroy@ird.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14726594" target="_blank"〉PubMed〈/a〉
    Keywords: Africa, Central/epidemiology ; Animals ; Animals, Wild/*virology ; Ape Diseases/*epidemiology/virology ; Base Sequence ; *Disease Outbreaks/veterinary ; Disease Reservoirs ; Ebolavirus/classification/*genetics/isolation & purification ; Gabon/epidemiology ; Genes, Viral ; Gorilla gorilla/virology ; Hemorrhagic Fever, Ebola/*epidemiology/transmission/*veterinary/virology ; Humans ; Molecular Sequence Data ; Pan troglodytes/virology ; Population Density ; Population Surveillance ; Ruminants/virology ; Viral Envelope Proteins/genetics
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    Discovery of symbiotic nitrogen-fixing cyanobacteria in corals (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-18
    Description: Colonies of the Caribbean coral Montastraea cavernosa exhibit a solar-stimulated orange-red fluorescence that is spectrally similar to a variety of fluorescent proteins expressed by corals. The source of this fluorescence is phycoerythrin in unicellular, nonheterocystis, symbiotic cyanobacteria within the host cells of the coral. The cyanobacteria coexist with the symbiotic dinoflagellates (zooxanthellae) of the coral and express the nitrogen-fixing enzyme nitrogenase. The presence of this prokaryotic symbiont in a nitrogen-limited zooxanthellate coral suggests that nitrogen fixation may be an important source of this limiting element for the symbiotic association.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lesser, Michael P -- Mazel, Charles H -- Gorbunov, Maxim Y -- Falkowski, Paul G -- New York, N.Y. -- Science. 2004 Aug 13;305(5686):997-1000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology and Center for Marine Biology, University of New Hampshire, Durham, NH 03824, USA. mpl@cisunix.unh.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15310901" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/*microbiology/physiology ; Cyanobacteria/genetics/isolation & purification/*physiology/ultrastructure ; Dinoflagellida/isolation & purification/physiology ; Fluorescence ; Microscopy, Fluorescence ; Molecular Sequence Data ; *Nitrogen Fixation ; Nitrogenase/genetics/metabolism ; Organelles/ultrastructure ; Phycoerythrin/metabolism ; *Symbiosis ; Thylakoids/ultrastructure
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    Ecology. Sportfishers on the hook for dwindling U.S. fish stocks (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grimm, David -- New York, N.Y. -- Science. 2004 Aug 27;305(5688):1235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15333821" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Ecosystem ; Fisheries ; *Fishes ; Humans ; Population Density ; *Recreation ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The complete genome sequence of Propionibacterium acnes, a commensal of human skin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-03
    Description: Propionibacterium acnes is a major inhabitant of adult human skin, where it resides within sebaceous follicles, usually as a harmless commensal although it has been implicated in acne vulgaris formation. The entire genome sequence of this Gram-positive bacterium encodes 2333 putative genes and revealed numerous gene products involved in degrading host molecules, including sialidases, neuraminidases, endoglycoceramidases, lipases, and pore-forming factors. Surface-associated and other immunogenic factors have been identified, which might be involved in triggering acne inflammation and other P. acnes-associated diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bruggemann, Holger -- Henne, Anke -- Hoster, Frank -- Liesegang, Heiko -- Wiezer, Arnim -- Strittmatter, Axel -- Hujer, Sandra -- Durre, Peter -- Gottschalk, Gerhard -- New York, N.Y. -- Science. 2004 Jul 30;305(5684):671-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gottingen Genomics Laboratory, Institute of Microbiology and Genetics, Georg-August-University Gottingen, Grisebachstrasse 8, 37077 Gottingen, Germany. hbruegg@pasteur.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15286373" target="_blank"〉PubMed〈/a〉
    Keywords: Acne Vulgaris/immunology/microbiology ; Amino Acid Motifs ; Amino Acid Sequence ; Antigens, Bacterial/chemistry/genetics ; Bacterial Proteins/chemistry/genetics/immunology ; Base Sequence ; Chromosomes, Bacterial/genetics ; Computational Biology ; Energy Metabolism ; Esterases/genetics/metabolism ; Genes, Bacterial ; *Genome, Bacterial ; Heat-Shock Proteins/chemistry/genetics ; Humans ; Hydrolases/genetics/metabolism ; Lipase/genetics/metabolism ; Molecular Sequence Data ; Oxidative Phosphorylation ; Propionibacterium acnes/*genetics/immunology/physiology ; *Sequence Analysis, DNA ; Skin/*microbiology
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    Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-27
    Description: Heterosexual transmission accounts for the majority of human immunodeficiency virus-1 (HIV-1) infections worldwide, yet the viral properties that determine transmission fitness or outgrowth have not been elucidated. Here we show, for eight heterosexual transmission pairs, that recipient viruses were monophyletic, encoding compact, glycan-restricted envelope glycoproteins. These viruses were also uniquely sensitive to neutralization by antibody from the transmitting partner. Thus, the exposure of neutralizing epitopes, which are lost in chronic infection because of immune escape, appears to be favored in the newly infected host. This reveals characteristics of the envelope glycoprotein that influence HIV-1 transmission and may have implications for vaccine design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derdeyn, Cynthia A -- Decker, Julie M -- Bibollet-Ruche, Frederic -- Mokili, John L -- Muldoon, Mark -- Denham, Scott A -- Heil, Marintha L -- Kasolo, Francis -- Musonda, Rosemary -- Hahn, Beatrice H -- Shaw, George M -- Korber, Bette T -- Allen, Susan -- Hunter, Eric -- AI-40951/AI/NIAID NIH HHS/ -- AI-51231/AI/NIAID NIH HHS/ -- N01-85338/PHS HHS/ -- U01-AI-41530/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 26;303(5666):2019-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15044802" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; Amino Acid Sequence ; Cohort Studies ; Epitopes/immunology ; Female ; Genes, env ; Glycosylation ; HIV Antibodies/*immunology ; HIV Envelope Protein gp120/chemistry/genetics/*immunology ; HIV Infections/*immunology/*transmission/virology ; HIV-1/genetics/*immunology/physiology ; Heterosexuality ; Humans ; Likelihood Functions ; Male ; Molecular Sequence Data ; Neutralization Tests ; Prospective Studies ; Viral Load ; Zambia
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    Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: The 1918 "Spanish" influenza pandemic represents the largest recorded outbreak of any infectious disease. The crystal structure of the uncleaved precursor of the major surface antigen of the extinct 1918 virus was determined at 3.0 angstrom resolution after reassembly of the hemagglutinin gene from viral RNA fragments preserved in 1918 formalin-fixed lung tissues. A narrow avian-like receptor-binding site, two previously unobserved histidine patches, and a less exposed surface loop at the cleavage site that activates viral membrane fusion reveal structural features primarily found in avian viruses, which may have contributed to the extraordinarily high infectivity and mortality rates observed during 1918.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, James -- Corper, Adam L -- Basler, Christopher F -- Taubenberger, Jeffery K -- Palese, Peter -- Wilson, Ian A -- AI058113/AI/NIAID NIH HHS/ -- AI42266/AI/NIAID NIH HHS/ -- AI50619/AI/NIAID NIH HHS/ -- CA55896/CA/NCI NIH HHS/ -- P50-GM 62411/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1866-70. Epub 2004 Feb 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, 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/14764887" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Carbohydrate Conformation ; Cloning, Molecular ; Crystallography, X-Ray ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/metabolism ; Histidine/chemistry/metabolism ; History, 20th Century ; Humans ; Hydrogen Bonding ; Influenza A virus/classification/*immunology/pathogenicity ; Influenza, Human/epidemiology/history/virology ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Virus/metabolism ; Sialic Acids/metabolism
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    RNA-mediated metal-metal bond formation in the synthesis of hexagonal palladium nanoparticles (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: RNA sequences have been discovered that mediate the growth of hexagonal palladium nanoparticles. In vitro selection techniques were used to evolve an initial library of approximately 10(14) unique RNA sequences through eight cycles of selection to yield several active sequence families. Of the five families, all representative members could form crystalline hexagonal palladium platelets. The palladium particle growth occurred in aqueous solution at ambient temperature, without any endogenous reducing agent, and at low concentrations of metal precursor (100 micromolar). Relative to metal precursor, the RNA concentration was significantly lower (1 micromolar), yet micrometer-size crystalline hexagonal palladium particles were formed rapidly (7.5 to 1 minutes).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gugliotti, Lina A -- Feldheim, Daniel L -- Eaton, Bruce E -- New York, N.Y. -- Science. 2004 May 7;304(5672):850-2. Epub 2004 Apr 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, North Carolina State University, Raleigh, NC 27695, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087507" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chemistry, Physical ; Crystallization ; DNA, Complementary ; DNA-Directed RNA Polymerases/metabolism ; *Nanotubes ; Palladium/*chemistry ; Particle Size ; Physicochemical Phenomena ; Polymerase Chain Reaction ; RNA/*chemistry ; Temperature ; Transcription, Genetic ; Viral Proteins
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    The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-06
    Description: We have sequenced and annotated the genome of the filamentous ascomycete Ashbya gossypii. With a size of only 9.2 megabases, encoding 4718 protein-coding genes, it is the smallest genome of a free-living eukaryote yet characterized. More than 90% of A. gossypii genes show both homology and a particular pattern of synteny with Saccharomyces cerevisiae. Analysis of this pattern revealed 300 inversions and translocations that have occurred since divergence of these two species. It also provided compelling evidence that the evolution of S. cerevisiae included a whole genome duplication or fusion of two related species and showed, through inferred ancient gene orders, which of the duplicated genes lost one copy and which retained both copies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dietrich, Fred S -- Voegeli, Sylvia -- Brachat, Sophie -- Lerch, Anita -- Gates, Krista -- Steiner, Sabine -- Mohr, Christine -- Pohlmann, Rainer -- Luedi, Philippe -- Choi, Sangdun -- Wing, Rod A -- Flavier, Albert -- Gaffney, Thomas D -- Philippsen, Peter -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):304-7. Epub 2004 Mar 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum der Universitat Basel, Klingelbergstrasse 50, CH-4056 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001715" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Biological Evolution ; Centromere/genetics ; Chromosome Inversion ; *Chromosome Mapping ; Computational Biology ; Fungal Proteins/genetics ; Gene Duplication ; Gene Order ; Genes, Fungal ; *Genome, Fungal ; Molecular Sequence Data ; Open Reading Frames ; Saccharomyces cerevisiae/*genetics ; Saccharomycetales/*genetics ; Sequence Alignment ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Synteny ; Translocation, Genetic
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    Molecular evolution of the SARS coronavirus during the course of the SARS epidemic in China (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-31
    Description: Sixty-one SARS coronavirus genomic sequences derived from the early, middle, and late phases of the severe acute respiratory syndrome (SARS) epidemic were analyzed together with two viral sequences from palm civets. Genotypes characteristic of each phase were discovered, and the earliest genotypes were similar to the animal SARS-like coronaviruses. Major deletions were observed in the Orf8 region of the genome, both at the start and the end of the epidemic. The neutral mutation rate of the viral genome was constant but the amino acid substitution rate of the coding sequences slowed during the course of the epidemic. The spike protein showed the strongest initial responses to positive selection pressures, followed by subsequent purifying selection and eventual stabilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chinese SARS Molecular Epidemiology Consortium -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1666-9. Epub 2004 Jan 29.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752165" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Substitution ; Animals ; Base Sequence ; Carnivora/virology ; China/epidemiology ; Cluster Analysis ; Coronavirus/genetics/isolation & purification ; *Disease Outbreaks ; *Evolution, Molecular ; *Genome, Viral ; Genotype ; Humans ; Membrane Glycoproteins/genetics ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Open Reading Frames ; Phylogeny ; Point Mutation ; RNA, Viral/genetics ; SARS Virus/*genetics/isolation & purification/physiology ; Selection, Genetic ; Sequence Deletion ; Severe Acute Respiratory Syndrome/*epidemiology/*virology ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/genetics ; Viral Matrix Proteins/chemistry/genetics
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    The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-24
    Description: Jun N-terminal kinases (JNKs) are essential for neuronal microtubule assembly and apoptosis. Phosphorylation of the activating protein 1 (AP1) transcription factor c-Jun, at multiple sites within its transactivation domain, is required for JNK-induced neurotoxicity. We report that in neurons the stability of c-Jun is regulated by the E3 ligase SCF(Fbw7), which ubiquitinates phosphorylated c-Jun and facilitates c-Jun degradation. Fbw7 depletion resulted in accumulation of phosphorylated c-Jun, stimulation of AP1 activity, and neuronal apoptosis. SCF(Fbw7) therefore antagonizes the apoptotic c-Jun-dependent effector arm of JNK signaling, allowing neurons to tolerate potentially neurotoxic JNK activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nateri, Abdolrahman S -- Riera-Sans, Lluis -- Da Costa, Clive -- Behrens, Axel -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1374-8. Epub 2004 Jan 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mammalian Genetics Laboratory, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739463" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; Base Sequence ; Cell Cycle Proteins/genetics/*metabolism ; Cell Line ; F-Box Proteins/genetics/*metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Signaling System ; Mice ; Mitogen-Activated Protein Kinases/*metabolism ; Molecular Sequence Data ; Neurons/*physiology ; PC12 Cells ; Phosphorylation ; Proto-Oncogene Proteins c-jun/*metabolism ; RNA, Small Interfering/metabolism ; Rats ; Transcription Factor AP-1/metabolism ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/genetics/*metabolism
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    Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-31
    Description: The lantibiotic lacticin 481 is synthesized on ribosomes as a prepeptide (LctA) and posttranslationally modified to its mature form. These modifications include dehydration of serines and threonines, followed by intramolecular addition of cysteines to the unsaturated amino acids, which generates cyclic thioethers. This process breaks eight chemical bonds and forms six newbonds and is catalyzed by one enzyme, LctM. We have characterized the in vitro activity of LctM, which completely processed a series of LctA mutants, displaying a permissive substrate specificity that holds promise for antibiotic engineering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xie, Lili -- Miller, Leah M -- Chatterjee, Champak -- Averin, Olga -- Kelleher, Neil L -- van der Donk, Wilfred A -- GM 067725/GM/NIGMS NIH HHS/ -- GM58822/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):679-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Illinois at Urbana-Champaign, 600 S. Mathews Avenue, Urbana, IL61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752162" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*biosynthesis/genetics ; *Bacteriocins ; Cloning, Molecular ; Cysteine/metabolism ; Enzymes/chemistry/genetics/isolation & purification/*metabolism ; Escherichia coli/genetics ; Lactococcus lactis/enzymology/genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Protein Precursors/chemistry/metabolism ; Protein Processing, Post-Translational ; Serine/metabolism ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Substrate Specificity ; Threonine/metabolism
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    Climate impact on plankton ecosystems in the Northeast Atlantic (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-14
    Description: It is now widely accepted that global warming is occurring, yet its effects on the world's largest ecosystem, the marine pelagic realm, are largely unknown. We show that sea surface warming in the Northeast Atlantic is accompanied by increasing phytoplankton abundance in cooler regions and decreasing phytoplankton abundance in warmer regions. This impact propagates up the food web (bottom-up control) through copepod herbivores to zooplankton carnivores because of tight trophic coupling. Future warming is therefore likely to alter the spatial distribution of primary and secondary pelagic production, affecting ecosystem services and placing additional stress on already-depleted fish and mammal populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richardson, Anthony J -- Schoeman, David S -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1609-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sir Alister Hardy Foundation for Ocean Science, The Laboratory, Citadel Hill, Plymouth, PL1 2PB, UK. anr@sahfos.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15361622" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atlantic Ocean ; *Climate ; Copepoda/*growth & development ; *Ecosystem ; Fisheries ; Fishes ; *Food Chain ; Greenhouse Effect ; Meta-Analysis as Topic ; Phytoplankton/*growth & development ; Population Dynamics ; Seawater ; Temperature ; Zooplankton/*growth & development
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    GlyR alpha3: an essential target for spinal PGE2-mediated inflammatory pain sensitization (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-08
    Description: Prostaglandin E2 (PGE2) is a crucial mediator of inflammatory pain sensitization. Here, we demonstrate that inhibition of a specific glycine receptor subtype (GlyR alpha3) by PGE2-induced receptor phosphorylation underlies central inflammatory pain sensitization. We show that GlyR alpha3 is distinctly expressed in superficial layers of the spinal cord dorsal horn. Mice deficient in GlyR alpha3 not only lack the inhibition of glycinergic neurotransmission by PGE2 seen in wild-type mice but also show a reduction in pain sensitization induced by spinal PGE2 injection or peripheral inflammation. Thus, GlyR alpha3 may provide a previously unrecognized molecular target in pain therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harvey, Robert J -- Depner, Ulrike B -- Wassle, Heinz -- Ahmadi, Seifollah -- Heindl, Cornelia -- Reinold, Heiko -- Smart, Trevor G -- Harvey, Kirsten -- Schutz, Burkhard -- Abo-Salem, Osama M -- Zimmer, Andreas -- Poisbeau, Pierrick -- Welzl, Hans -- Wolfer, David P -- Betz, Heinrich -- Zeilhofer, Hanns Ulrich -- Muller, Ulrike -- New York, N.Y. -- Science. 2004 May 7;304(5672):884-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, The School of Pharmacy, London WC1N 1AX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131310" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dinoprostone/administration & dosage/*metabolism/pharmacology ; Female ; Freund's Adjuvant ; Glycine/metabolism ; Humans ; Inflammation/metabolism/*physiopathology ; Male ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Neurons/metabolism ; Pain/*physiopathology ; Patch-Clamp Techniques ; Phosphorylation ; Posterior Horn Cells/*metabolism ; Receptors, Glycine/chemistry/genetics/*metabolism ; Signal Transduction ; Spinal Cord/*metabolism ; Synaptic Transmission ; Transfection ; Zymosan
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    A previously unknown maltose transporter essential for starch degradation in leaves (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-06
    Description: A previously unknown maltose transporter is essential for the conversion of starch to sucrose in Arabidopsis leaves at night. The transporter was identified by isolating two allelic mutants with high starch levels and very high maltose, an intermediate of starch breakdown. The mutations affect a gene of previously unknown function, MEX1. We show that MEX1is a maltose transporter that is unrelated to other sugar transporters. The severe mex1 phenotype demonstrates that MEX1is the predominant route of carbohydrate export from chloroplasts at night. Homologous genes in plants including rice and potato indicate that maltose export is of widespread significance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Niittyla, Totte -- Messerli, Gaelle -- Trevisan, Martine -- Chen, Jychian -- Smith, Alison M -- Zeeman, Samuel C -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):87-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Metabolic Biology, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704427" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Biological Transport ; Chloroplasts/metabolism ; Cloning, Molecular ; Crosses, Genetic ; DNA, Complementary ; Genes, Plant ; Glucose/metabolism ; Maltose/*metabolism ; Molecular Sequence Data ; Monosaccharide Transport Proteins/chemistry/genetics/*metabolism ; Mutation ; Phenotype ; Plant Leaves/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; Starch/*metabolism
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    ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: Mitochondrial dysfunction is a hallmark of beta-amyloid (Abeta)-induced neuronal toxicity in Alzheimer's disease (AD). Here, we demonstrate that Abeta-binding alcohol dehydrogenase (ABAD) is a direct molecular link from Abeta to mitochondrial toxicity. Abeta interacts with ABAD in the mitochondria of AD patients and transgenic mice. The crystal structure of Abeta-bound ABAD shows substantial deformation of the active site that prevents nicotinamide adenine dinucleotide (NAD) binding. An ABAD peptide specifically inhibits ABAD-Abeta interaction and suppresses Abeta-induced apoptosis and free-radical generation in neurons. Transgenic mice overexpressing ABAD in an Abeta-rich environment manifest exaggerated neuronal oxidative stress and impaired memory. These data suggest that the ABAD-Abeta interaction may be a therapeutic target in AD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lustbader, Joyce W -- Cirilli, Maurizio -- Lin, Chang -- Xu, Hong Wei -- Takuma, Kazuhiro -- Wang, Ning -- Caspersen, Casper -- Chen, Xi -- Pollak, Susan -- Chaney, Michael -- Trinchese, Fabrizio -- Liu, Shumin -- Gunn-Moore, Frank -- Lue, Lih-Fen -- Walker, Douglas G -- Kuppusamy, Periannan -- Zewier, Zay L -- Arancio, Ottavio -- Stern, David -- Yan, Shirley ShiDu -- Wu, Hao -- 1K07AG00959/AG/NIA NIH HHS/ -- AG16736/AG/NIA NIH HHS/ -- AG17490/AG/NIA NIH HHS/ -- NS42855/NS/NINDS NIH HHS/ -- P50AG08702/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):448-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Reproductive Sciences and Department of Obstetrics and Gynecology, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087549" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Hydroxyacyl CoA Dehydrogenases/chemistry/*metabolism ; Aged ; Aged, 80 and over ; Alzheimer Disease/*metabolism ; Amino Acid Sequence ; Amyloid beta-Peptides/chemistry/genetics/*metabolism ; Animals ; Binding Sites ; Brain/*metabolism ; Brain Chemistry ; Carrier Proteins/chemistry/*metabolism ; Cells, Cultured ; Cerebral Cortex/chemistry/metabolism ; Crystallization ; DNA Fragmentation ; Hippocampus/physiology ; Humans ; Learning ; Memory ; Mice ; Mice, Transgenic ; Microscopy, Confocal ; Microscopy, Immunoelectron ; Mitochondria/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; NAD/metabolism ; Neurons/metabolism ; Protein Binding ; Protein Conformation ; Reactive Oxygen Species/metabolism
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    Femtomolar sensitivity of a NO sensor from Clostridium botulinum (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-09
    Description: Nitric oxide (NO) is extremely toxic to Clostridium botulinum, but its molecular targets are unknown. Here, we identify a heme protein sensor (SONO) that displays femtomolar affinity for NO. The crystal structure of the SONO heme domain reveals a previously undescribed fold and a strategically placed tyrosine residue that modulates heme-nitrosyl coordination. Furthermore, the domain architecture of a SONO ortholog cloned from Chlamydomonas reinhardtii indicates that NO signaling through cyclic guanosine monophosphate arose before the origin of multicellular eukaryotes. Our findings have broad implications for understanding bacterial responses to NO, as well as for the activation of mammalian NO-sensitive guanylyl cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nioche, Pierre -- Berka, Vladimir -- Vipond, Julia -- Minton, Nigel -- Tsai, Ah-Lim -- Raman, C S -- AY343540/PHS HHS/ -- R01 AI054444/AI/NIAID NIH HHS/ -- R01 AI054444-05/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1550-3. Epub 2004 Oct 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Research Center and Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472039" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Bacterial Proteins/chemistry/metabolism ; Biological Evolution ; Carrier Proteins/*chemistry/genetics/*metabolism ; Chemotaxis ; Chlamydomonas reinhardtii/chemistry/genetics/metabolism ; Cloning, Molecular ; Clostridium botulinum/*chemistry/genetics/*metabolism ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Escherichia coli/genetics/growth & development ; Guanylate Cyclase ; Heme/chemistry/metabolism ; Hemeproteins/*chemistry/genetics/*metabolism ; Humans ; Hydrogen Bonding ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Nitric Oxide/*metabolism ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protoporphyrins/analysis/metabolism ; Receptors, Cytoplasmic and Nuclear/chemistry/metabolism ; Sequence Alignment ; Signal Transduction ; Static Electricity ; Thermoanaerobacter/chemistry
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    Breakthrough of the year. On Mars, a second chance for life (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2010-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604365" target="_blank"〉PubMed〈/a〉
    Keywords: Exobiology ; Ferric Compounds ; Geologic Sediments ; Life ; *Mars ; Robotics ; Salts ; Spacecraft ; Spectrum Analysis/instrumentation ; Temperature ; *Water
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    MicroRNA-directed cleavage of HOXB8 mRNA (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-24
    Description: MicroRNAs (miRNAs) are endogenous approximately 22-nucleotide RNAs, some of which are known to play important regulatory roles in animals by targeting the messages of protein-coding genes for translational repression. We find that miR-196, a miRNA encoded at three paralogous locations in the A, B, and C mammalian HOX clusters, has extensive, evolutionarily conserved complementarity to messages of HOXB8, HOXC8, and HOXD8. RNA fragments diagnostic of miR-196-directed cleavage of HOXB8 were detected in mouse embryos. Cell culture experiments demonstrated down-regulation of HOXB8, HOXC8, HOXD8, and HOXA7 and supported the cleavage mechanism for miR-196-directed repression of HOXB8. These results point to a miRNA-mediated mechanism for the posttranscriptional restriction of HOX gene expression during vertebrate development and demonstrate that metazoan miRNAs can repress expression of their natural targets through mRNA cleavage in addition to inhibiting productive translation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yekta, Soraya -- Shih, I-Hung -- Bartel, David P -- New York, N.Y. -- Science. 2004 Apr 23;304(5670):594-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15105502" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions ; Animals ; Base Sequence ; Down-Regulation ; *Genes, Homeobox ; Genes, Reporter ; HeLa Cells ; Homeodomain Proteins/*genetics ; Humans ; Mice ; MicroRNAs/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Neoplasm Proteins/genetics ; RNA, Messenger/chemistry/*genetics/*metabolism ; Sequence Alignment ; Transcription Factors/genetics ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular cloud origin for the oxygen isotope heterogeneity in the solar system (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-18
    Description: Meteorites and their components have anomalous oxygen isotopic compositions characterized by large variations in 18O/16O and 17O/16O ratios. On the basis of recent observations of star-forming regions and models of accreting protoplanetary disks, we suggest that these variations may originate in a parent molecular cloud by ultraviolet photodissociation processes. Materials with anomalous isotopic compositions were then transported into the solar nebula by icy dust grains during the collapse of the cloud. The icy dust grains drifted toward the Sun in the disk, and their subsequent evaporation resulted in the 17O- and 18O-enrichment of the inner disk gas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yurimoto, Hisayoshi -- Kuramoto, Kiyoshi -- New York, N.Y. -- Science. 2004 Sep 17;305(5691):1763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth and Planetary Sciences, Tokyo Institute of Technology, Meguro, Tokyo 152-8551, Japan. yuri@geo.titech.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15375265" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Isotopes ; Carbon Monoxide ; Cosmic Dust ; Ice ; *Oxygen Isotopes ; Photochemistry ; Photons ; *Solar System ; Temperature ; Ultraviolet Rays
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    Phosphorylation of proteins by inositol pyrophosphates (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: The inositol pyrophosphates IP7 and IP8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP7, we detected phosphorylation of multiple eukaryotic proteins. We also observed phosphorylation of endogenous proteins by endogenous IP7 in yeast. Phosphorylation by IP7 is nonenzymatic and may represent a novel intracellular signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saiardi, Adolfo -- Bhandari, Rashna -- Resnick, Adam C -- Snowman, Adele M -- Snyder, Solomon H -- DA00074/DA/NIDA NIH HHS/ -- MH068830-02/MH/NIMH NIH HHS/ -- MH18501/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2101-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604408" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Escherichia coli Proteins/metabolism ; Humans ; Inositol Phosphates/*metabolism ; Kinetics ; Magnesium/metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry/*metabolism ; Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Protein Kinases/genetics/metabolism ; Proteins/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Serine/metabolism ; Signal Transduction ; Temperature
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    A host-targeting signal in virulence proteins reveals a secretome in malarial infection (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-14
    Description: Malaria parasites secrete proteins across the vacuolar membrane into the erythrocyte, inducing modifications linked to disease and parasite survival. We identified an 11-amino acid signal required for the secretion of proteins from the Plasmodium falciparum vacuole to the human erythrocyte. Bioinformatics predicted a secretome of 〉320 proteins and conservation of the signal across parasite species. Functional studies indicated the predictive value of the signal and its role in targeting virulence proteins to the erythrocyte and implicated its recognition by a receptor/transporter. Erythrocyte modification by the parasite may involve plasmodial heat shock proteins and be vastly more complex than hitherto realized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hiller, N Luisa -- Bhattacharjee, Souvik -- van Ooij, Christiaan -- Liolios, Konstantinos -- Harrison, Travis -- Lopez-Estrano, Carlos -- Haldar, Kasturi -- AI39071/AI/NIAID NIH HHS/ -- HL69630/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1934-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Pathology and Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15591203" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Computational Biology ; Cytosol/metabolism ; Erythrocytes/*metabolism/parasitology ; Genes, Protozoan ; Humans ; Malaria, Falciparum/parasitology ; Membrane Proteins/chemistry/metabolism ; Molecular Sequence Data ; Plasmodium falciparum/genetics/growth & development/*metabolism/*pathogenicity ; *Protein Sorting Signals ; Protein Structure, Tertiary ; Protein Transport ; Protozoan Proteins/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transgenes ; Vacuoles/metabolism/parasitology ; Virulence Factors/chemistry/genetics/*metabolism
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    Initial results from the Mini-TES experiment in Gusev Crater from the Spirit Rover (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-07
    Description: The Miniature Thermal Emission Spectrometer (Mini-TES) on Spirit has studied the mineralogy and thermophysical properties at Gusev crater. Undisturbed soil spectra show evidence for minor carbonates and bound water. Rocks are olivinerich basalts with varying degrees of dust and other coatings. Dark-toned soils observed on disturbed surfaces may be derived from rocks and have derived mineralogy (+/-5 to 10%) of 45% pyroxene (20% Ca-rich pyroxene and 25% pigeonite), 40% sodic to intermediate plagioclase, and 15% olivine (forsterite 45% +/-5 to 10). Two spectrally distinct coatings are observed on rocks, a possible indicator of the interaction of water, rock, and airfall dust. Diurnal temperature data indicate particle sizes from 40 to 80 microm in hollows to approximately 0.5 to 3 mm in soils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christensen, P R -- Ruff, S W -- Fergason, R L -- Knudson, A T -- Anwar, S -- Arvidson, R E -- Bandfield, J L -- Blaney, D L -- Budney, C -- Calvin, W M -- Glotch, T D -- Golombek, M P -- Gorelick, N -- Graff, T G -- Hamilton, V E -- Hayes, A -- Johnson, J R -- McSween, H Y Jr -- Mehall, G L -- Mehall, L K -- Moersch, J E -- Morris, R V -- Rogers, A D -- Smith, M D -- Squyres, S W -- Wolff, M J -- Wyatt, M B -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):837-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geological Sciences, Arizona State University, Tempe, AZ 85287, USA. phil.christensen@asu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297667" target="_blank"〉PubMed〈/a〉
    Keywords: Carbonates ; Geologic Sediments ; Interferometry ; Iron Compounds ; Magnesium Compounds ; *Mars ; *Minerals ; Oxides ; Silicates ; Spectrum Analysis ; Temperature ; Water
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    Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-09-14
    Description: The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khademi, Shahram -- O'Connell, Joseph 3rd -- Remis, Jonathan -- Robles-Colmenares, Yaneth -- Miercke, Larry J W -- Stroud, Robert M -- GM24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1587-94.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, S412C Genentech Hall, University of California-San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15361618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ammonia/*metabolism ; Binding Sites ; Biological Transport ; Cation Transport Proteins/*chemistry/genetics/metabolism ; Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Liposomes ; Membrane Potentials ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Quaternary Ammonium Compounds/metabolism ; Rh-Hr Blood-Group System/chemistry/metabolism ; Sequence Alignment ; Water/chemistry/metabolism
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    Abiotic forcing of plankton evolution in the Cenozoic (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-01-13
    Description: We characterize the evolutionary radiation of planktic foraminifera by the test size distributions of entire assemblages in more than 500 Cenozoic marine sediment samples, including more than 1 million tests. Calibration of Holocene size patterns with environmental parameters and comparisons with Cenozoic paleoproxy data show a consistently positive correlation between test size and surface-water stratification intensity. We infer that the observed macroevolutionary increase in test size of planktic foraminifera through the Cenozoic was an adaptive response to intensifying surface-water stratification in low latitudes, which was driven by polar cooling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmidt, Daniela N -- Thierstein, Hans R -- Bollmann, Jorg -- Schiebel, Ralf -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):207-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, Eidgenossische Technische Hochschule (ETH) Zurich, and University of Zurich, ETH-Zentrum, CH-8092 Zurich, Switzerland. d.schmidt@gl.rhul.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Climate ; Ecosystem ; Eukaryota/chemistry/cytology ; Geography ; Oxygen Isotopes/analysis ; *Plankton/chemistry/cytology ; Seawater ; Temperature ; Time ; Zooplankton/chemistry/cytology
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    Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: Mobilization of fatty acids from triglyceride stores in adipose tissue requires lipolytic enzymes. Dysfunctional lipolysis affects energy homeostasis and may contribute to the pathogenesis of obesity and insulin resistance. Until now, hormone-sensitive lipase (HSL) was the only enzyme known to hydrolyze triglycerides in mammalian adipose tissue. Here, we report that a second enzyme, adipose triglyceride lipase (ATGL), catalyzes the initial step in triglyceride hydrolysis. It is interesting that ATGL contains a "patatin domain" common to plant acyl-hydrolases. ATGL is highly expressed in adipose tissue of mice and humans. It exhibits high substrate specificity for triacylglycerol and is associated with lipid droplets. Inhibition of ATGL markedly decreases total adipose acyl-hydrolase activity. Thus, ATGL and HSL coordinately catabolize stored triglycerides in adipose tissue of mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmermann, Robert -- Strauss, Juliane G -- Haemmerle, Guenter -- Schoiswohl, Gabriele -- Birner-Gruenberger, Ruth -- Riederer, Monika -- Lass, Achim -- Neuberger, Georg -- Eisenhaber, Frank -- Hermetter, Albin -- Zechner, Rudolf -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1383-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biosciences, University of Graz, Graz, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550674" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3-L1 Cells ; Adipocytes/enzymology/*metabolism ; Adipose Tissue/enzymology/*metabolism ; Adipose Tissue, Brown/enzymology/metabolism ; Amino Acid Sequence ; Animals ; COS Cells ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cytoplasm/enzymology ; DNA, Complementary ; Diglycerides/metabolism ; Fatty Acids/metabolism ; Gene Silencing ; Glycerol/metabolism ; Humans ; Isoproterenol/pharmacology ; *Lipid Mobilization ; Lipolysis ; Lipoprotein Lipase/chemistry/genetics/immunology/*metabolism ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Structure, Tertiary ; RNA, Messenger/genetics/metabolism ; Sterol Esterase/genetics/*metabolism ; Substrate Specificity ; Transfection ; Triglycerides/metabolism
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    Nervy links protein kinase a to plexin-mediated semaphorin repulsion (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-21
    Description: Cyclic nucleotides regulate axonal responses to a number of guidance cues through unknown molecular events. We report here that Drosophila nervy, a member of the myeloid translocation gene family of A kinase anchoring proteins (AKAPs), regulates repulsive axon guidance by linking the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) to the Semaphorin 1a (Sema-1a) receptor Plexin A (PlexA). Nervy and PKA antagonize Sema-1a-PlexA-mediated repulsion, and the AKAP binding region of Nervy is critical for this effect. Thus, Nervy couples cAMP-PKA signaling to PlexA to regulate Sema-1a-mediated axonal repulsion, revealing a simple molecular mechanism that allows growing axons to integrate inputs from multiple guidance cues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Terman, Jonathan R -- Kolodkin, Alex L -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1204-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 1001 PCTB/725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976319" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Animals, Genetically Modified ; Axons/*physiology/ultrastructure ; Carrier Proteins/chemistry/*metabolism ; Central Nervous System/embryology ; Cues ; Cyclic AMP-Dependent Protein Kinases/*metabolism ; Drosophila/cytology/*embryology/genetics/metabolism ; Drosophila Proteins/chemistry/*metabolism ; Embryo, Nonmammalian/cytology/metabolism/physiology ; Molecular Sequence Data ; Motor Neurons/metabolism/*physiology/ultrastructure ; Muscles/embryology/innervation/metabolism ; Mutation ; Nerve Tissue Proteins/*metabolism ; Neural Pathways ; Phenotype ; Receptors, Cell Surface/*metabolism ; Semaphorins/*metabolism ; Signal Transduction ; Transgenes
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    A glycine-dependent riboswitch that uses cooperative binding to control gene expression (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-10-09
    Description: We identified a previously unknown riboswitch class in bacteria that is selectively triggered by glycine. A representative of these glycine-sensing RNAs from Bacillus subtilis operates as a rare genetic on switch for the gcvT operon, which codes for proteins that form the glycine cleavage system. Most glycine riboswitches integrate two ligand-binding domains that function cooperatively to more closely approximate a two-state genetic switch. This advanced form of riboswitch may have evolved to ensure that excess glycine is efficiently used to provide carbon flux through the citric acid cycle and maintain adequate amounts of the amino acid for protein synthesis. Thus, riboswitches perform key regulatory roles and exhibit complex performance characteristics that previously had been observed only with protein factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mandal, Maumita -- Lee, Mark -- Barrick, Jeffrey E -- Weinberg, Zasha -- Emilsson, Gail Mitchell -- Ruzzo, Walter L -- Breaker, Ronald R -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):275-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, Yale University, Post Office Box 208103, New Haven, CT 06520-8103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472076" target="_blank"〉PubMed〈/a〉
    Keywords: 5' Untranslated Regions/chemistry/*metabolism ; Allosteric Regulation ; Allosteric Site ; Bacillus subtilis/*genetics/metabolism ; Base Pairing ; Base Sequence ; Binding Sites ; *Gene Expression Regulation, Bacterial ; Glycine/*metabolism ; Ligands ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Operon ; RNA, Bacterial/chemistry/*metabolism ; RNA, Messenger/chemistry/*metabolism ; Transcription, Genetic ; Vibrio cholerae/*genetics/metabolism
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    Evidence for precipitation on Mars from dendritic valleys in the Valles Marineris area (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-07-03
    Description: Dendritic valleys on the plateau and canyons of the Valles Marineris region were identified from Thermal Emission Imaging System (THEMIS) images taken by Mars Odyssey. The geomorphic characteristics of these valleys, especially their high degree of branching, favor formation by atmospheric precipitation. The presence of inner channels and the maturity of the branched networks indicate sustained fluid flows over geologically long periods of time. These fluvial landforms occur within the Late Hesperian units (about 2.9 to 3.4 billion years old), when Mars was thought to have been cold. Our results suggest a period of warmer conditions conducive to hydrological activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mangold, Nicolas -- Quantin, Cathy -- Ansan, Veronique -- Delacourt, Christophe -- Allemand, Pascal -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):78-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire IDES, UMR CNRS and Universite Paris-Sud, Orsay Campus, 91405 Orsay, France. mangold@geol.u-psud.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232103" target="_blank"〉PubMed〈/a〉
    Keywords: Climate ; Extraterrestrial Environment ; *Mars ; *Rain ; Temperature ; *Water ; Weather
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    The duration of forest stages in southern Europe and interglacial climate variability (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-12-04
    Description: Foraminiferal oxygen isotope and pollen analyses from a deep-sea sequence off southwest Portugal show that the duration of temperate stages on land over the past 350,000 years varied considerably. The record shows forest contractions during intervals of low ice volume, coeval with declines in atmospheric methane, after which tree populations did not always recover. What emerges is that, although the broad timing of interglacials is consistent with orbital theory, their specific duration may be dictated by millennial variability. This complicates the prediction of the natural duration of interglacials, at least until the origin of this climate variability is understood.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tzedakis, P C -- Roucoux, K H -- de Abreu, L -- Shackleton, N J -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2231-5. Epub 2004 Dec 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Earth and Biosphere Institute, School of Geography, University of Leeds, Leeds, LS2 9JT, UK. P.C.Tzedakis@leeds.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15576573" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atmosphere ; *Climate ; Europe ; Ice ; Methane ; Olea ; Oxygen Isotopes ; Plankton ; Pollen ; Portugal ; Quercus ; Temperature ; Time ; *Trees
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    Origins of bilateral symmetry: Hox and dpp expression in a sea anemone (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-05-08
    Description: Over 99% of modern animals are members of the evolutionary lineage Bilateria. The evolutionary success of Bilateria is credited partly to the origin of bilateral symmetry. Although animals of the phylum Cnidaria are not within the Bilateria, some representatives, such as the sea anemone Nematostella vectensis, exhibit bilateral symmetry. We show that Nematostella uses homologous genes to achieve bilateral symmetry: Multiple Hox genes are expressed in a staggered fashion along its primary body axis, and the transforming growth factor-beta gene decapentaplegic (dpp) is expressed in an asymmetric fashion about its secondary body axis. These data suggest that bilateral symmetry arose before the evolutionary split of Cnidaria and Bilateria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finnerty, John R -- Pang, Kevin -- Burton, Pat -- Paulson, Dave -- Martindale, Mark Q -- New York, N.Y. -- Science. 2004 May 28;304(5675):1335-7. Epub 2004 May 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Boston University, 5 Cummington Street, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131263" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Body Patterning ; Endoderm/physiology ; Gene Duplication ; Gene Expression Profiling ; *Gene Expression Regulation, Developmental ; Genes ; *Genes, Homeobox ; In Situ Hybridization ; Larva/genetics/growth & development ; Molecular Sequence Data ; Phylogeny ; Sea Anemones/*anatomy & histology/embryology/*genetics/growth & development
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    Hereditary early-onset Parkinson's disease caused by mutations in PINK1 (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-04-17
    Description: Parkinson's disease (PD) is a neurodegenerative disorder characterized by degeneration of dopaminergic neurons in the substantia nigra. We previously mapped a locus for a rare familial form of PD to chromosome 1p36 (PARK6). Here we show that mutations in PINK1 (PTEN-induced kinase 1) are associated with PARK6. We have identified two homozygous mutations affecting the PINK1 kinase domain in three consanguineous PARK6 families: a truncating nonsense mutation and a missense mutation at a highly conserved amino acid. Cell culture studies suggest that PINK1 is mitochondrially located and may exert a protective effect on the cell that is abrogated by the mutations, resulting in increased susceptibility to cellular stress. These data provide a direct molecular link between mitochondria and the pathogenesis of PD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valente, Enza Maria -- Abou-Sleiman, Patrick M -- Caputo, Viviana -- Muqit, Miratul M K -- Harvey, Kirsten -- Gispert, Suzana -- Ali, Zeeshan -- Del Turco, Domenico -- Bentivoglio, Anna Rita -- Healy, Daniel G -- Albanese, Alberto -- Nussbaum, Robert -- Gonzalez-Maldonado, Rafael -- Deller, Thomas -- Salvi, Sergio -- Cortelli, Pietro -- Gilks, William P -- Latchman, David S -- Harvey, Robert J -- Dallapiccola, Bruno -- Auburger, Georg -- Wood, Nicholas W -- G-4029/Parkinson's UK/United Kingdom -- GGP02089/Telethon/Italy -- New York, N.Y. -- Science. 2004 May 21;304(5674):1158-60. Epub 2004 Apr 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSS IRCCS, Mendel Institute, viale Regina Margherita 261, 00198 Rome, Italy. e.valente@css-mendel.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087508" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apoptosis ; COS Cells ; Cell Line, Tumor ; Codon, Nonsense ; Exons ; Humans ; Leupeptins/pharmacology ; Membrane Potentials ; Mitochondria/enzymology/*metabolism ; Molecular Sequence Data ; *Mutation ; Mutation, Missense ; Neurons/metabolism/physiology ; Oxidative Stress ; Parkinson Disease/enzymology/*genetics/metabolism ; Protein Kinases/chemistry/*genetics/*metabolism ; Protein Structure, Tertiary ; Transfection
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    Carbon and nitrogen isotopic anomalies in an anhydrous interplanetary dust particle (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-28
    Description: Because hydrogen and nitrogen isotopic anomalies in interplanetary dust particles have been associated with carbonaceous material, the lack of similar anomalies in carbon has been a major conundrum. We report here the presence of a 13C depletion associated with a 15N enrichment in an anhydrous interplanetary dust particle. Our observations suggest that the anomalies are carried by heteroatomic organic compounds. Theoretical models indicate that low-temperature formation of organic compounds in cold interstellar molecular clouds can produce carbon and nitrogen fractionations, but it remains to be seen whether the specific effects observed here can be reproduced.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Floss, Christine -- Stadermann, Frank J -- Bradley, John -- Dai, Zu Rong -- Bajt, Sasa -- Graham, Giles -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Space Sciences, Washington University, St. Louis, MO 63130, USA. floss@wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14988560" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Isotopes/*analysis ; Cosmic Dust/*analysis ; Hydrocarbons/chemistry ; Mass Spectrometry ; Nitrogen Isotopes/*analysis ; Organic Chemicals/chemistry ; Spectrophotometry, Infrared ; Temperature
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    Structural basis of mitochondrial tethering by mitofusin complexes (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-08-07
    Description: Vesicle fusion involves vesicle tethering, docking, and membrane merger. We show that mitofusin, an integral mitochondrial membrane protein, is required on adjacent mitochondria to mediate fusion, which indicates that mitofusin complexes act in trans (that is, between adjacent mitochondria). A heptad repeat region (HR2) mediates mitofusin oligomerization by assembling a dimeric, antiparallel coiled coil. The transmembrane segments are located at opposite ends of the 95 angstrom coiled coil and provide a mechanism for organelle tethering. Consistent with this proposal, truncated mitofusin, in an HR2-dependent manner, causes mitochondria to become apposed with a uniform gap. Our results suggest that HR2 functions as a mitochondrial tether before fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshiba, Takumi -- Detmer, Scott A -- Kaiser, Jens T -- Chen, Hsiuchen -- McCaffery, J Michael -- Chan, David C -- R01 GM62967/GM/NIGMS NIH HHS/ -- S10 RR019409-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):858-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, 1200 East California Boulevard, MC114-96, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297672" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cell Line ; Crystallography, X-Ray ; Dimerization ; GTP Phosphohydrolases/*chemistry/*metabolism ; Humans ; Hybrid Cells ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes/physiology/ultrastructure ; Membrane Fusion ; Mice ; Mitochondria/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Hydrocarbons in hydrothermal vent fluids: the role of chromium-bearing catalysts (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-04-03
    Description: Fischer-Tropsch type (FTT) synthesis has long been proposed to account for the existence of hydrocarbons in hydrothermal fluids. We show that iron- and chromium-bearing minerals catalyze the abiotic formation of hydrocarbons. In addition to production of methane (CH4aq), we report abiotic generation of ethane (C2H6aq) and propane (C3H8aq) by mineral-catalyzed hydrothermal reactions at 390 degrees C and 400 bars. Results suggest that the chromium component in ultramafic rocks could be an important factor for FTT synthesis during water-rock interaction in mid-ocean ridge hydrothermal systems. This in turn could help to support microbial communities now recognized in the subsurface at deep-sea vents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foustoukos, Dionysis I -- Seyfried, William E Jr -- New York, N.Y. -- Science. 2004 May 14;304(5673):1002-5. Epub 2004 Apr 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology and Geophysics, University of Minnesota, Minneapolis, MN 55455, USA. fous0009@umn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15060286" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/growth & development ; Bacteria/growth & development ; Carbon Dioxide/chemistry ; Catalysis ; Chromium/*chemistry ; Chromium Compounds/chemistry ; Ecosystem ; Environment ; Ethane/chemical synthesis/chemistry ; Ferric Compounds/chemistry ; Geologic Sediments/*chemistry/microbiology ; Hydrocarbons/*chemical synthesis/chemistry ; Hydrogen/chemistry ; Hydrogen-Ion Concentration ; Methane/chemical synthesis/chemistry ; Pressure ; Propane/chemical synthesis/chemistry ; Temperature
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    Basis for structural diversity in homologous RNAs (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-10-02
    Description: Large RNA molecules, such as ribozymes, fold with well-defined tertiary structures that are important for their activity. There are many instances of ribozymes with identical function but differences in their secondary structures, suggesting alternative tertiary folds. Here, we report a crystal structure of the 161-nucleotide specificity domain of an A-type ribonuclease P that differs in secondary and tertiary structure from the specificity domain of a B-type molecule. Despite the differences, the cores of the domains have similar three-dimensional structure. Remarkably, the similar geometry of the cores is stabilized by a different set of interactions involving distinct auxiliary elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krasilnikov, Andrey S -- Xiao, Yinghua -- Pan, Tao -- Mondragon, Alfonso -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):104-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459389" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalytic Domain ; Conserved Sequence ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Phylogeny ; RNA Precursors/chemistry/metabolism ; RNA, Bacterial/*chemistry/metabolism ; RNA, Transfer/chemistry/metabolism ; Ribonuclease P/*chemistry/metabolism ; Ribonucleotides/chemistry/metabolism ; Thermus thermophilus/*chemistry/enzymology
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    Compensated deleterious mutations in insect genomes (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-10-23
    Description: Relatively little is known about the importance of amino acid interactions in protein and phenotypic evolution. Here we examine whether mutations that are pathogenic in Drosophila melanogaster become fixed via epistasis in other Dipteran genomes. Overall divergence at pathogenic amino acid sites is reduced. However, approximately 10% of the substitutions at these sites carry the exact same pathogenic amino acid found in D. melanogaster mutants. Hence compensatory mutation(s) must have evolved. Surprisingly, the fraction 10% is not affected by phylogenetic distance. These results support a selection-driven process that allows compensated amino acid substitutions to become rapidly fixed in taxa with large populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kulathinal, Rob J -- Bettencourt, Brian R -- Hartl, Daniel L -- GM068465/GM/NIGMS NIH HHS/ -- P41-HG00739/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1553-4. Epub 2004 Oct 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15498973" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Anopheles gambiae/*genetics ; Codon, Nonsense ; Drosophila/*genetics ; Drosophila melanogaster/*genetics ; Epistasis, Genetic ; *Evolution, Molecular ; Genes, Insect ; *Genome ; Insect Proteins/chemistry/*genetics ; Molecular Sequence Data ; *Mutation ; Mutation, Missense ; Phenotype ; Phylogeny ; Selection, Genetic ; Sequence Alignment
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    Oceanography. New dead zone off Oregon coast hints at sea change in currents (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-08-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1099.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15326328" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brachyura/*physiology ; *Ecosystem ; Fishes/*physiology ; Oceanography ; Oxygen/*analysis ; Pacific Ocean ; Phytoplankton/growth & development ; Seasons ; *Seawater ; Temperature ; Wind
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    Uses and abuses of mathematics in biology (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-07
    Description: In the physical sciences, mathematical theory and experimental investigation have always marched together. Mathematics has been less intrusive in the life sciences, possibly because they have until recently been largely descriptive, lacking the invariance principles and fundamental natural constants of physics. Increasingly in recent decades, however, mathematics has become pervasive in biology, taking many different forms: statistics in experimental design; pattern seeking in bioinformatics; models in evolution, ecology, and epidemiology; and much else. I offer an opinionated overview of such uses--and abuses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉May, Robert M -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):790-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoology Department, Oxford University, Oxford OX1 3PS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764866" target="_blank"〉PubMed〈/a〉
    Keywords: Allergy and Immunology ; Biological Evolution ; *Biological Science Disciplines ; Computational Biology ; Computer Simulation ; Creutzfeldt-Jakob Syndrome/prevention & control ; Ecology ; Genetics, Population ; HIV Infections/epidemiology/immunology/transmission ; Humans ; *Mathematics ; *Models, Biological ; Models, Statistical ; Nonlinear Dynamics ; Statistics as Topic
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    Robotic observations of enhanced carbon biomass and export at 55 degrees during SOFeX (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: Autonomous floats profiling in high-nitrate low-silicate waters of the Southern Ocean observed carbon biomass variability and carbon exported to depths of 100 m during the 2002 Southern Ocean Iron Experiment (SOFeX) to detect the effects of iron fertilization of surface water there. Control and "in-patch" measurements documented a greater than fourfold enhancement of carbon biomass in the iron-amended waters. Carbon export through 100 m increased two- to sixfold as the patch subducted below a front. The molar ratio of iron added to carbon exported ranged between 10(4) and 10(5). The biomass buildup and export were much higher than expected for iron-amended low-silicate waters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bishop, James K B -- Wood, Todd J -- Davis, Russ E -- Sherman, Jeffrey T -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):417-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Earth Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, MS 90-1116, Berkeley, CA 94720, USA. JKBishop@lbl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087544" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomass ; Carbon/*analysis/metabolism ; *Iron/metabolism ; Oceans and Seas ; Phytoplankton/*growth & development/metabolism ; Robotics ; *Seawater/chemistry ; Temperature
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    The genetic basis of singlet oxygen-induced stress responses of Arabidopsis thaliana (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-13
    Description: Plants under oxidative stress suffer from damages that have been interpreted as unavoidable consequences of injuries inflicted upon plants by toxic levels of reactive oxygen species (ROS). However, this paradigm needs to be modified. Inactivation of a single gene, EXECUTER1, is sufficient to abrogate stress responses of Arabidopsis thaliana caused by the release of singlet oxygen: External conditions under which these stress responses are observed and the amounts of ROS that accumulate in plants exposed to these environmental conditions do not directly cause damages. Instead, seedling lethality and growth inhibition of mature plants result from genetic programs that are activated after the release of singlet oxygen has been perceived by the plant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, Daniela -- Przybyla, Dominika -- Op den Camp, Roel -- Kim, Chanhong -- Landgraf, Frank -- Lee, Keun Pyo -- Wursch, Marco -- Laloi, Christophe -- Nater, Mena -- Hideg, Eva -- Apel, Klaus -- New York, N.Y. -- Science. 2004 Nov 12;306(5699):1183-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Plant Sciences, Plant Genetics, Swiss Federal Institute of Technology (ETH), CH-8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/cytology/*genetics/growth & development/*physiology ; Arabidopsis Proteins/chemistry/*genetics/*physiology ; Cell Death/drug effects ; Chromosome Mapping ; Cloning, Molecular ; Cosmids ; Darkness ; Diuron/pharmacology ; Gene Expression Regulation, Plant ; Genes, Plant ; Genetic Complementation Test ; Light ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; *Oxidative Stress ; Photosystem II Protein Complex/metabolism ; Plant Leaves/cytology/drug effects/metabolism ; Reactive Oxygen Species/metabolism ; Singlet Oxygen/*metabolism ; Transformation, Genetic
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    Plant cuticular lipid export requires an ABC transporter (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-23
    Description: A waxy protective cuticle coats all primary aerial plant tissues. Its synthesis requires extensive export of lipids from epidermal cells to the plant surface. Arabidopsis cer5 mutants had reduced stem cuticular wax loads and accumulated sheetlike inclusions in the cytoplasm of wax-secreting cells. These inclusions represented abnormal deposits of cuticular wax and resembled inclusions found in a human disorder caused by a defective peroxisomal adenosine triphosphate binding cassette (ABC) transporter. We found that the CER5 gene encodes an ABC transporter localized in the plasma membrane of epidermal cells and conclude that it is required for wax export to the cuticle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pighin, Jamie A -- Zheng, Huanquan -- Balakshin, Laura J -- Goodman, Ian P -- Western, Tamara L -- Jetter, Reinhard -- Kunst, Ljerka -- Samuels, A Lacey -- New York, N.Y. -- Science. 2004 Oct 22;306(5696):702-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, University of British Columbia (UBC), 6270 University Boulevard, Vancouver, BC V6T 1Z4, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15499022" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/chemistry/genetics/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/cytology/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Biological Transport, Active ; Cell Membrane/metabolism ; Cloning, Molecular ; Dimerization ; Genes, Plant ; Inclusion Bodies/ultrastructure ; *Lipid Metabolism ; Microscopy, Electron ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutation ; Plant Epidermis/cytology/*metabolism/ultrastructure ; Plant Stems/cytology/metabolism/ultrastructure ; Plants, Genetically Modified ; Recombinant Fusion Proteins/metabolism ; Vacuoles/ultrastructure ; Waxes/*metabolism
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    Mapping the antigenic and genetic evolution of influenza virus (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-26
    Description: The antigenic evolution of influenza A (H3N2) virus was quantified and visualized from its introduction into humans in 1968 to 2003. Although there was remarkable correspondence between antigenic and genetic evolution, significant differences were observed: Antigenic evolution was more punctuated than genetic evolution, and genetic change sometimes had a disproportionately large antigenic effect. The method readily allows monitoring of antigenic differences among vaccine and circulating strains and thus estimation of the effects of vaccination. Further, this approach offers a route to predicting the relative success of emerging strains, which could be achieved by quantifying the combined effects of population level immune escape and viral fitness on strain evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Derek J -- Lapedes, Alan S -- de Jong, Jan C -- Bestebroer, Theo M -- Rimmelzwaan, Guus F -- Osterhaus, Albert D M E -- Fouchier, Ron A M -- New York, N.Y. -- Science. 2004 Jul 16;305(5682):371-6. Epub 2004 Jun 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK. dsmith@zoo.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15218094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Antigenic Variation ; *Evolution, Molecular ; *Genes, Viral ; Genetic Drift ; Genetic Variation ; Hemagglutination Inhibition Tests ; *Hemagglutinins, Viral/chemistry/genetics/immunology ; Humans ; Influenza A virus/*genetics/*immunology ; Influenza, Human/epidemiology/virology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Seasons ; Virology/methods
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    Human PAD4 regulates histone arginine methylation levels via demethylimination (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-04
    Description: Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation. Although histone methyltransferases are known, enzymes that demethylate histones have not been identified. Here, we demonstrate that human peptidylarginine deiminase 4 (PAD4) regulates histone Arg methylation by converting methyl-Arg to citrulline and releasing methylamine. PAD4 targets multiple sites in histones H3 and H4, including those sites methylated by coactivators CARM1 (H3 Arg17) and PRMT1 (H4 Arg3). A decrease of histone Arg methylation, with a concomitant increase of citrullination, requires PAD4 activity in human HL-60 granulocytes. Moreover, PAD4 activity is linked with the transcriptional regulation of estrogen-responsive genes in MCF-7 cells. These data suggest that PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yanming -- Wysocka, Joanna -- Sayegh, Joyce -- Lee, Young-Ho -- Perlin, Julie R -- Leonelli, Lauriebeth -- Sonbuchner, Lakshmi S -- McDonald, Charles H -- Cook, Richard G -- Dou, Yali -- Roeder, Robert G -- Clarke, Steven -- Stallcup, Michael R -- Allis, C David -- Coonrod, Scott A -- DK55274/DK/NIDDK NIH HHS/ -- GM R01 26020/GM/NIGMS NIH HHS/ -- GM R01 50659/GM/NIGMS NIH HHS/ -- HD R01 38353/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):279-83. Epub 2004 Sep 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetic Medicine, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15345777" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/*metabolism ; Blotting, Western ; Calcimycin/pharmacology ; Cell Line, Tumor ; Citrulline/metabolism ; Gene Expression Regulation ; Genes, Reporter ; HL-60 Cells ; Histones/*metabolism ; Humans ; Hydrolases/*metabolism ; Ionophores/pharmacology ; Membrane Proteins/genetics ; Methylamines/metabolism ; Methylation ; Molecular Sequence Data ; Presenilin-2 ; Promoter Regions, Genetic ; Protein-Arginine N-Methyltransferases/metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    New EPA focus on sustainability (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilman, Paul -- New York, N.Y. -- Science. 2004 May 28;304(5675):1243-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166347" target="_blank"〉PubMed〈/a〉
    Keywords: *Conservation of Natural Resources ; Curriculum ; Ecology ; Education ; *Environment ; Research ; Rivers ; United States ; *United States Environmental Protection Agency
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    First Atmospheric Science Results from the Mars Exploration Rovers Mini-TES (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-04
    Description: Thermal infrared spectra of the martian atmosphere taken by the Miniature Thermal Emission Spectrometer (Mini-TES) were used to determine the atmospheric temperatures in the planetary boundary layer and the column-integrated optical depth of aerosols. Mini-TES observations show the diurnal variation of the martian boundary layer thermal structure, including a near-surface superadiabatic layer during the afternoon and an inversion layer at night. Upward-looking Mini-TES observations show warm and cool parcels of air moving through the Mini-TES field of view on a time scale of 30 seconds. The retrieved dust optical depth shows a downward trend at both sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Michael D -- Wolff, Michael J -- Lemmon, Mark T -- Spanovich, Nicole -- Banfield, Don -- Budney, Charles J -- Clancy, R Todd -- Ghosh, Amitabha -- Landis, Geoffrey A -- Smith, Peter -- Whitney, Barbara -- Christensen, Philip R -- Squyres, Steven W -- New York, N.Y. -- Science. 2004 Dec 3;306(5702):1750-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NASA Goddard Space Flight Center, Greenbelt, MD 20771, USA. Michael.D.Smith@nasa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15576612" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Atmosphere ; Carbon Dioxide ; Extraterrestrial Environment ; *Mars ; Seasons ; Spectrum Analysis ; Temperature ; Water
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    Local endemism within the Western Ghats-sri Lanka biodiversity hotspot (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-16
    Description: The apparent biotic affinities between the mainland and the island in the Western Ghats-Sri Lanka biodiversity hotspot have been interpreted as the result of frequent migrations during recent periods of low sea level. We show, using molecular phylogenies of two invertebrate and four vertebrate groups, that biotic interchange between these areas has been much more limited than hitherto assumed. Despite several extended periods of land connection during the past 500,000 years, Sri Lanka has maintained a fauna that is largely distinct from that of the Indian mainland. Future conservation programs for the subcontinent should take into account such patterns of local endemism at the finest scale at which they may occur.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bossuyt, Franky -- Meegaskumbura, Madhava -- Beenaerts, Natalie -- Gower, David J -- Pethiyagoda, Rohan -- Roelants, Kim -- Mannaert, An -- Wilkinson, Mark -- Bahir, Mohomed M -- Manamendra-Arachchi, Kelum -- Ng, Peter K L -- Schneider, Christopher J -- Oommen, Oommen V -- Milinkovitch, Michel C -- New York, N.Y. -- Science. 2004 Oct 15;306(5695):479-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Unit of Ecology and Systematics, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium. fbossuyt@vub.ac.be〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486298" target="_blank"〉PubMed〈/a〉
    Keywords: Amphibians/anatomy & histology/classification/genetics ; Animals ; *Biodiversity ; Biological Evolution ; Brachyura/anatomy & histology/classification/genetics ; Conservation of Natural Resources ; Cyprinidae/anatomy & histology/classification/genetics ; DNA, Mitochondrial ; Decapoda (Crustacea)/anatomy & histology/classification/genetics ; *Ecosystem ; Genes, rRNA ; India ; *Invertebrates/anatomy & histology/classification ; Molecular Sequence Data ; Phylogeny ; Population Density ; Ranidae/anatomy & histology/classification/genetics ; Snakes/anatomy & histology/classification/genetics ; Sri Lanka ; *Vertebrates/anatomy & histology/classification/genetics
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    Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-09
    Description: Very rare cases of human T cell acute lymphoblastic leukemia (T-ALL) harbor chromosomal translocations that involve NOTCH1, a gene encoding a transmembrane receptor that regulates normal T cell development. Here, we report that more than 50% of human T-ALLs, including tumors from all major molecular oncogenic subtypes, have activating mutations that involve the extracellular heterodimerization domain and/or the C-terminal PEST domain of NOTCH1. These findings greatly expand the role of activated NOTCH1 in the molecular pathogenesis of human T-ALL and provide a strong rationale for targeted therapies that interfere with NOTCH signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weng, Andrew P -- Ferrando, Adolfo A -- Lee, Woojoong -- Morris, John P 4th -- Silverman, Lewis B -- Sanchez-Irizarry, Cheryll -- Blacklow, Stephen C -- Look, A Thomas -- Aster, Jon C -- CA109901/CA/NCI NIH HHS/ -- CA21765/CA/NCI NIH HHS/ -- CA68484/CA/NCI NIH HHS/ -- CA82308/CA/NCI NIH HHS/ -- CA94233/CA/NCI NIH HHS/ -- CA98093/CA/NCI NIH HHS/ -- P01 CA109901/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):269-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472075" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Alleles ; Amino Acid Sequence ; Amyloid Precursor Protein Secretases ; Aspartic Acid Endopeptidases ; Cell Cycle ; Cell Line, Tumor ; Child ; Dimerization ; Endopeptidases/metabolism ; Frameshift Mutation ; Humans ; Leukemia-Lymphoma, Adult T-Cell/*genetics/metabolism ; Molecular Sequence Data ; *Mutation ; Mutation, Missense ; Point Mutation ; Protease Inhibitors/pharmacology ; Protein Structure, Tertiary ; Receptor, Notch1 ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; Sequence Deletion ; Signal Transduction ; Transcription Factors/chemistry/*genetics/metabolism
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    Ecology. Reproductive failure threatens bird colonies on North Sea coast (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Proffitt, Fiona -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1090.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15326320" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds/*physiology ; *Ecosystem ; *Eels ; Fisheries ; Food Chain ; North Sea ; Plankton ; Population Density ; *Reproduction ; Scotland ; Seawater ; Temperature
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    Carbonyl sulfide-mediated prebiotic formation of peptides (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-09
    Description: Almost all discussions of prebiotic chemistry assume that amino acids, nucleotides, and possibly other monomers were first formed on the Earth or brought to it in comets and meteorites, and then condensed nonenzymatically to form oligomeric products. However, attempts to demonstrate plausibly prebiotic polymerization reactions have met with limited success. We show that carbonyl sulfide (COS), a simple volcanic gas, brings about the formation of peptides from amino acids under mild conditions in aqueous solution. Depending on the reaction conditions and additives used, exposure of alpha-amino acids to COS generates peptides in yields of up to 80% in minutes to hours at room temperature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leman, Luke -- Orgel, Leslie -- Ghadiri, M Reza -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):283-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Skaggs Institute for Chemical Biology, 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/15472077" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*chemistry ; Anaerobiosis ; Cyclization ; Dipeptides/chemistry ; *Evolution, Chemical ; Magnetic Resonance Spectroscopy ; Oligopeptides/*chemistry ; Oxidation-Reduction ; Phenylalanine/chemistry ; Serine/chemistry ; Sulfur Oxides/*chemistry ; Temperature ; Thermodynamics ; Thiocarbamates/chemistry
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    A putative Ca2+ and calmodulin-dependent protein kinase required for bacterial and fungal symbioses (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-14
    Description: Legumes can enter into symbiotic relationships with both nitrogen-fixing bacteria (rhizobia) and mycorrhizal fungi. Nodulation by rhizobia results from a signal transduction pathway induced in legume roots by rhizobial Nod factors. DMI3, a Medicago truncatula gene that acts immediately downstream of calcium spiking in this signaling pathway and is required for both nodulation and mycorrhizal infection, has high sequence similarity to genes encoding calcium and calmodulin-dependent protein kinases (CCaMKs). This indicates that calcium spiking is likely an essential component of the signaling cascade leading to nodule development and mycorrhizal infection, and sheds light on the biological role of plant CCaMKs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, Julien -- Bres, Cecile -- Geurts, Rene -- Chalhoub, Boulos -- Kulikova, Olga -- Duc, Gerard -- Journet, Etienne-Pascal -- Ane, Jean-Michel -- Lauber, Emmanuelle -- Bisseling, Ton -- Denarie, Jean -- Rosenberg, Charles -- Debelle, Frederic -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1361-4. Epub 2004 Feb 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire des Interactions Plantes-Microorganismes INRA-CNRS, BP27, 31326 Castanet-Tolosan Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963335" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium/metabolism ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinases/chemistry/genetics/*metabolism ; Calmodulin/metabolism ; Chromosomes, Artificial, Bacterial ; Cloning, Molecular ; EF Hand Motifs ; Expressed Sequence Tags ; Gene Expression Regulation, Plant ; Genes, Plant ; Lipopolysaccharides/metabolism ; Medicago/*enzymology/genetics/microbiology ; Molecular Sequence Data ; Mutation ; Mycorrhizae/*physiology ; Peas/*enzymology/genetics/microbiology ; Plant Roots/enzymology/microbiology ; Protein Structure, Tertiary ; Rhizobium/genetics ; Sinorhizobium meliloti/*physiology ; *Symbiosis ; Transformation, Genetic
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    Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-24
    Description: Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing Cys-SO(2)H, thus reestablishing the antioxidant firewall. Sestrins contain a predicted redox-active domain homologous to AhpD, the enzyme catalyzing the reduction of a bacterial Prx, AhpC. Purified Hi95 (sestrin 2) protein supports adenosine triphosphate-dependent reduction of overoxidized PrxI in vitro, indicating that unlike AhpD, which is a disulfide reductase, sestrins are cysteine sulfinyl reductases. As modulators of peroxide signaling and antioxidant defense, sestrins constitute potential therapeutic targets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Budanov, Andrei V -- Sablina, Anna A -- Feinstein, Elena -- Koonin, Eugene V -- Chumakov, Peter M -- New York, N.Y. -- Science. 2004 Apr 23;304(5670):596-600.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15105503" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Cell Division ; Cell Line, Tumor ; Cell Survival ; Cells, Cultured ; Heat-Shock Proteins/chemistry/genetics/*metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry/genetics/*metabolism ; Oxidation-Reduction ; Oxidoreductases/genetics/metabolism ; Peroxidases/*chemistry/*metabolism ; Peroxiredoxins ; RNA, Small Interfering ; Reactive Oxygen Species/metabolism ; Recombinant Proteins/metabolism ; Tumor Suppressor Protein p53/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Impact of nitrogen deposition on the species richness of grasslands (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-20
    Description: A transect of 68 acid grasslands across Great Britain, covering the lower range of ambient annual nitrogen deposition in the industrialized world (5 to 35 kg Nha-1 year-1), indicates that long-term, chronic nitrogen deposition has significantly reduced plant species richness. Species richness declines as a linear function of the rate of inorganic nitrogen deposition, with a reduction of one species per 4-m2 quadrat for every 2.5 kg Nha-1 year-1 of chronic nitrogen deposition. Species adapted to infertile conditions are systematically reduced at high nitrogen deposition. At the mean chronic nitrogen deposition rate of central Europe (17 kg Nha-1 year-1), there is a 23% species reduction compared with grasslands receiving the lowest levels of nitrogen deposition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, Carly J -- Dise, Nancy B -- Mountford, J Owen -- Gowing, David J -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1876-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, The Open University, Milton Keynes MK7 6AA, UK. c.j.stevens@open.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15031507" target="_blank"〉PubMed〈/a〉
    Keywords: Air Pollution ; Altitude ; Atmosphere ; *Biodiversity ; Carbon/analysis ; *Ecosystem ; Great Britain ; Hydrogen-Ion Concentration ; *Nitrogen/analysis ; *Plant Development ; Poaceae/*growth & development ; Soil/analysis ; Temperature ; Weather
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    The 1.2-megabase genome sequence of Mimivirus (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-16
    Description: We recently reported the discovery and preliminary characterization of Mimivirus, the largest known virus, with a 400-nanometer particle size comparable to mycoplasma. Mimivirus is a double-stranded DNA virus growing in amoebae. We now present its 1,181,404-base pair genome sequence, consisting of 1262 putative open reading frames, 10% of which exhibit a similarity to proteins of known functions. In addition to exceptional genome size, Mimivirus exhibits many features that distinguish it from other nucleocytoplasmic large DNA viruses. The most unexpected is the presence of numerous genes encoding central protein-translation components, including four amino-acyl transfer RNA synthetases, peptide release factor 1, translation elongation factor EF-TU, and translation initiation factor 1. The genome also exhibits six tRNAs. Other notable features include the presence of both type I and type II topoisomerases, components of all DNA repair pathways, many polysaccharide synthesis enzymes, and one intein-containing gene. The size and complexity of the Mimivirus genome challenge the established frontier between viruses and parasitic cellular organisms. This new sequence data might help shed a new light on the origin of DNA viruses and their role in the early evolution of eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raoult, Didier -- Audic, Stephane -- Robert, Catherine -- Abergel, Chantal -- Renesto, Patricia -- Ogata, Hiroyuki -- La Scola, Bernard -- Suzan, Marie -- Claverie, Jean-Michel -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1344-50. Epub 2004 Oct 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite des Rickettsies, Faculte de Medecine, CNRS UMR6020, Universite de la Mediterranee, 13385 Marseille Cedex 05, France. Didier.Raoult@medecine.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486256" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthamoeba/virology ; Animals ; Base Composition ; Computational Biology ; DNA Repair/genetics ; DNA Topoisomerases/genetics ; DNA Viruses/classification/*genetics/metabolism ; DNA, Viral/chemistry/genetics ; Enzymes/genetics/metabolism ; Genes, Viral ; *Genome, Viral ; Inteins ; Introns ; Molecular Sequence Data ; Open Reading Frames ; Phylogeny ; Protein Biosynthesis ; Protein Folding ; Proteome ; RNA, Transfer/analysis ; RNA, Viral/analysis ; Sequence Analysis, DNA ; Viral Proteins/chemistry/genetics/metabolism
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    Ecology and conservation. Space--the final frontier for economists and elephants (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bulte, Erwin -- Damania, Richard -- Lindsey, Gillson -- Lindsay, Keith -- New York, N.Y. -- Science. 2004 Oct 15;306(5695):420-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Economics, Tilburg University, Post Office Box 90153, 5000 LE Tilburg, Netherlands. e.h.bulte@uvt.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486280" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Commerce ; *Conservation of Natural Resources/economics ; Ecology ; *Ecosystem ; *Elephants ; Environment ; Models, Economic ; Population Dynamics ; Population Growth
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    Cofolding organizes alfalfa mosaic virus RNA and coat protein for replication (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-12-18
    Description: Alfalfa mosaic virus genomic RNAs are infectious only when the viral coat protein binds to the RNA 3' termini. The crystal structure of an alfalfa mosaic virus RNA-peptide complex reveals that conserved AUGC repeats and Pro-Thr-x-Arg-Ser-x-x-Tyr coat protein amino acids cofold upon interacting. Alternating AUGC residues have opposite orientation, and they base pair in different adjacent duplexes. Localized RNA backbone reversals stabilized by arginine-guanine interactions place the adenosines and guanines in reverse order in the duplex. The results suggest that a uniform, organized 3' conformation, similar to that found on viral RNAs with transfer RNA-like ends, may be essential for replication.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1500904/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1500904/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guogas, Laura M -- Filman, David J -- Hogle, James M -- Gehrke, Lee -- AI20566/AI/NIAID NIH HHS/ -- GM42504/GM/NIGMS NIH HHS/ -- R01 AI020566/AI/NIAID NIH HHS/ -- R01 GM042504/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604410" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions ; Alfalfa mosaic virus/*chemistry/*physiology ; Amino Acid Sequence ; Base Pairing ; Base Sequence ; Binding Sites ; Capsid Proteins/*chemistry/metabolism ; Crystallization ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA, Viral/*chemistry/metabolism ; Repetitive Sequences, Nucleic Acid ; *Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Missing OH reactivity in a forest: evidence for unknown reactive biogenic VOCs (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-05-01
    Description: Forest emissions of biogenic volatile organic compounds (BVOCs), such as isoprene and other terpenes, play a role in the production of tropospheric ozone and aerosols. In a northern Michigan forest, the direct measurement of total OH reactivity, which is the inverse of the OH lifetime, was significantly greater than expected. The difference between measured and expected OH reactivity, called the missing OH reactivity, increased with temperature, as did emission rates for terpenes and other BVOCs. These measurements are consistent with the hypothesis that unknown reactive BVOCs, perhaps terpenes, provide the missing OH reactivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Di Carlo, Piero -- Brune, William H -- Martinez, Monica -- Harder, Hartwig -- Lesher, Robert -- Ren, Xinrong -- Thornberry, Troy -- Carroll, Mary Anne -- Young, Valerie -- Shepson, Paul B -- Riemer, Daniel -- Apel, Eric -- Campbell, Colleen -- New York, N.Y. -- Science. 2004 Apr 30;304(5671):722-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Meteorology, Pennsylvania State University, University Park, PA 16802, USA. piero.dicarlo@aquila.infn.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15118159" target="_blank"〉PubMed〈/a〉
    Keywords: Aerosols ; *Atmosphere ; Butadienes/analysis ; Hemiterpenes/analysis ; Hydroxyl Radical/analysis/*chemistry ; Michigan ; Organic Chemicals/analysis/*chemistry ; Ozone/analysis/chemistry ; Pentanes/analysis ; Sunlight ; Temperature ; Terpenes ; *Trees
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    48,000 years of climate and forest change in a biodiversity hot spot (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-07
    Description: A continuous 48,000-year-long paleoecological record from Neotropical lower montane forest reveals a consistent forest presence and an ice-age cooling of approximately 5 degrees to 9 degrees C. After 30,000 years of compositional stability, a steady turnover of species marks the 8000-year-long transition from ice-age to Holocene conditions. Although the changes were directional, the rates of community change were no different during this transitional period than in the preceding 30,000-year period of community stability. The warming rate of about 1 degrees C per millennium during the Pleistocene-Holocene transition was an order of magnitude less than the projected changes for the 21st century.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bush, Mark B -- Silman, Miles R -- Urrego, Dunia H -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):827-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Florida Institute of Technology, 150 West University Boulevard, Melbourne, FL 32901-6975, USA. mbush@fit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764876" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Climate ; *Ecosystem ; Environment ; Fossils ; Fresh Water ; Geography ; Geologic Sediments ; Peru ; *Plant Development ; Pollen ; Temperature ; Time ; Trees/*growth & development ; Tropical Climate
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    Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-14
    Description: The structure of the general transcription factor IIB (TFIIB) in a complex with RNA polymerase II reveals three features crucial for transcription initiation: an N-terminal zinc ribbon domain of TFIIB that contacts the "dock" domain of the polymerase, near the path of RNA exit from a transcribing enzyme; a "finger" domain of TFIIB that is inserted into the polymerase active center; and a C-terminal domain, whose interaction with both the polymerase and with a TATA box-binding protein (TBP)-promoter DNA complex orients the DNA for unwinding and transcription. TFIIB stabilizes an early initiation complex, containing an incomplete RNA-DNA hybrid region. It may interact with the template strand, which sets the location of the transcription start site, and may interfere with RNA exit, which leads to abortive initiation or promoter escape. The trajectory of promoter DNA determined by the C-terminal domain of TFIIB traverses sites of interaction with TFIIE, TFIIF, and TFIIH, serving to define their roles in the transcription initiation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bushnell, David A -- Westover, Kenneth D -- Davis, Ralph E -- Kornberg, Roger D -- AI21144/AI/NIAID NIH HHS/ -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):983-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963322" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Nucleic Acid Hybridization ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/chemistry/metabolism ; RNA Polymerase II/*chemistry/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; TATA Box ; TATA-Box Binding Protein/chemistry/metabolism ; Templates, Genetic ; Transcription Factor TFIIB/*chemistry/metabolism ; Transcription Factors, TFII/chemistry/metabolism ; *Transcription, Genetic ; Zinc/chemistry
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    Argonaute2 is the catalytic engine of mammalian RNAi (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-31
    Description: Gene silencing through RNA interference (RNAi) is carried out by RISC, the RNA-induced silencing complex. RISC contains two signature components, small interfering RNAs (siRNAs) and Argonaute family proteins. Here, we show that the multiple Argonaute proteins present in mammals are both biologically and biochemically distinct, with a single mammalian family member, Argonaute2, being responsible for messenger RNA cleavage activity. This protein is essential for mouse development, and cells lacking Argonaute2 are unable to mount an experimental response to siRNAs. Mutations within a cryptic ribonuclease H domain within Argonaute2, as identified by comparison with the structure of an archeal Argonaute protein, inactivate RISC. Thus, our evidence supports a model in which Argonaute contributes "Slicer" activity to RISC, providing the catalytic engine for RNAi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Jidong -- Carmell, Michelle A -- Rivas, Fabiola V -- Marsden, Carolyn G -- Thomson, J Michael -- Song, Ji-Joon -- Hammond, Scott M -- Joshua-Tor, Leemor -- Hannon, Gregory J -- New York, N.Y. -- Science. 2004 Sep 3;305(5689):1437-41. Epub 2004 Jul 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Watson School of Biological Sciences, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15284456" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Argonaute Proteins ; Catalysis ; Cell Line ; Cells, Cultured ; Central Nervous System/embryology ; Embryonic and Fetal Development ; Eukaryotic Initiation Factor-2 ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Humans ; In Situ Hybridization ; Mice ; MicroRNAs/metabolism ; Molecular Sequence Data ; Mutagenesis, Insertional ; Oligonucleotide Array Sequence Analysis ; Peptide Initiation Factors/chemistry/*metabolism ; Point Mutation ; *RNA Interference ; RNA, Double-Stranded ; RNA, Messenger/*metabolism ; RNA, Small Interfering/metabolism ; RNA-Induced Silencing Complex/chemistry/*metabolism
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    Complete genome sequence of the apicomplexan, Cryptosporidium parvum (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-27
    Description: The apicomplexan Cryptosporidium parvum is an intestinal parasite that affects healthy humans and animals, and causes an unrelenting infection in immunocompromised individuals such as AIDS patients. We report the complete genome sequence of C. parvum, type II isolate. Genome analysis identifies extremely streamlined metabolic pathways and a reliance on the host for nutrients. In contrast to Plasmodium and Toxoplasma, the parasite lacks an apicoplast and its genome, and possesses a degenerate mitochondrion that has lost its genome. Several novel classes of cell-surface and secreted proteins with a potential role in host interactions and pathogenesis were also detected. Elucidation of the core metabolism, including enzymes with high similarities to bacterial and plant counterparts, opens new avenues for drug development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abrahamsen, Mitchell S -- Templeton, Thomas J -- Enomoto, Shinichiro -- Abrahante, Juan E -- Zhu, Guan -- Lancto, Cheryl A -- Deng, Mingqi -- Liu, Chang -- Widmer, Giovanni -- Tzipori, Saul -- Buck, Gregory A -- Xu, Ping -- Bankier, Alan T -- Dear, Paul H -- Konfortov, Bernard A -- Spriggs, Helen F -- Iyer, Lakshminarayan -- Anantharaman, Vivek -- Aravind, L -- Kapur, Vivek -- U01 AI 46397/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):441-5. Epub 2004 Mar 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterinary and Biomedical Science, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, USA. abe@umn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15044751" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiprotozoal Agents/pharmacology ; Carbohydrate Metabolism ; Cryptosporidium parvum/*genetics/*metabolism/pathogenicity/physiology ; DNA, Protozoan/genetics ; Drug Resistance/genetics ; Enzymes/genetics/*metabolism ; Ethanol/metabolism ; Genes, Protozoan ; *Genome, Protozoan ; Glycolysis ; Introns ; Mitochondria/genetics ; Molecular Sequence Data ; Multigene Family ; Open Reading Frames ; Organelles/genetics ; Protozoan Proteins/chemistry/genetics/*metabolism ; Purines/metabolism ; Sequence Analysis, DNA ; Transcription, Genetic
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    Creating a sustainable future? (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-06-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wright, Bruce A -- Okey, Thomas A -- New York, N.Y. -- Science. 2004 Jun 25;304(5679):1903.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15218125" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Conservation of Natural Resources ; *Ecosystem ; *Environment ; Fisheries ; Humans ; Information Dissemination ; Population Growth ; Public Policy
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    How unique is the rice transcriptome? (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wyrwicz, Lucjan S -- von Grotthuss, Marcin -- Pas, Jakub -- Rychlewski, Leszek -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):168; author reply 168.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14715990" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Computational Biology ; DNA, Complementary ; Databases, Nucleic Acid ; Databases, Protein ; *Genome, Plant ; Molecular Sequence Data ; Oryza/*genetics ; Plant Proteins/chemistry/*genetics ; Sequence Homology, Amino Acid ; *Transcription, Genetic
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    A linear, O-coordinated eta1-CO2 bound to uranium (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-09-18
    Description: The electron-rich, six-coordinate tris-aryloxide uranium(III) complex [((AdArO)3tacn)U(III)] [where (AdArOH)3tacn = 1,4,7-tris(3-adamantyl-5-tert-butyl-2-hydroxybenzyl)1,4,7-triazacyclononane] reacts rapidly with CO2 to yield [((AdArO)3tacn)U(IV)(CO2)], a complex in which the CO(2) ligand is linearly coordinated to the metal through its oxygen atom (eta1-OCO). The latter complex has been crystallographically and spectroscopically characterized. The inequivalent O-C-O bond lengths [1.122 angstroms (A) for the O-C bond adjacent to uranium and 1.277 A for the other], considered together with magnetization data and electronic and vibrational spectra, support the following bonding model: U(IV)=O=C*-O- 〈--〉 U(IV)-OC-O-. In these charge-separated resonance structures, the uranium center is oxidized to uranium(IV) and the CO2 ligand reduced by one electron.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castro-Rodriguez, Ingrid -- Nakai, Hidetaka -- Zakharov, Lev N -- Rheingold, Arnold L -- Meyer, Karsten -- 3 T32 DK07233-2651/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 17;305(5691):1757-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, MC 0358, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15375263" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Dioxide/*chemistry ; Crystallography ; Electrons ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Magnetics ; Models, Molecular ; Molecular Structure ; Oxidation-Reduction ; Oxygen/*chemistry ; Spectrum Analysis ; Temperature ; Uranium/*chemistry ; X-Rays
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    A draft sequence for the genome of the domesticated silkworm (Bombyx mori) (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 88
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    Discovery and directed evolution of a glyphosate tolerance gene (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: The herbicide glyphosate is effectively detoxified by N-acetylation. We screened a collection of microbial isolates and discovered enzymes exhibiting glyphosate N-acetyltransferase (GAT) activity. Kinetic properties of the discovered enzymes were insufficient to confer glyphosate tolerance to transgenic organisms. Eleven iterations of DNA shuffling improved enzyme efficiency by nearly four orders of magnitude from 0.87 mM-1 min-1 to 8320 mM-1 min-1. From the fifth iteration and beyond, GAT enzymes conferred increasing glyphosate tolerance to Escherichia coli, Arabidopsis, tobacco, and maize. Glyphosate acetylation provides an alternative strategy for supporting glyphosate use on crops.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castle, Linda A -- Siehl, Daniel L -- Gorton, Rebecca -- Patten, Phillip A -- Chen, Yong Hong -- Bertain, Sean -- Cho, Hyeon-Je -- Duck, Nicholas -- Wong, James -- Liu, Donglong -- Lassner, Michael W -- New York, N.Y. -- Science. 2004 May 21;304(5674):1151-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verdia, Inc. Redwood City, CA 94063, USA. linda.castle@verdiainc.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155947" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Bacillus/enzymology ; Catalysis ; *DNA Shuffling ; *Directed Molecular Evolution ; Drug Resistance ; Escherichia coli/genetics ; Gene Library ; Genetic Variation ; Glycine/*analogs & derivatives/metabolism/*toxicity ; Herbicides/metabolism/*toxicity ; Kinetics ; Molecular Sequence Data ; Mutagenesis ; *Plants, Genetically Modified/drug effects/genetics ; Recombinant Proteins/metabolism ; Recombination, Genetic ; Tobacco/drug effects/genetics/growth & development ; Transformation, Genetic ; Zea mays/drug effects/genetics/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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    The wheat VRN2 gene is a flowering repressor down-regulated by vernalization (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-16
    Description: Plants with a winter growth habit flower earlier when exposed for several weeks to cold temperatures, a process called vernalization. We report here the positional cloning of the wheat vernalization gene VRN2, a dominant repressor of flowering that is down-regulated by vernalization. Loss of function of VRN2, whether by natural mutations or deletions, resulted in spring lines, which do not require vernalization to flower. Reduction of the RNA level of VRN2 by RNA interference accelerated the flowering time of transgenic winter-wheat plants by more than a month.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4737501/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4737501/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, Liuling -- Loukoianov, Artem -- Blechl, Ann -- Tranquilli, Gabriela -- Ramakrishna, Wusirika -- SanMiguel, Phillip -- Bennetzen, Jeffrey L -- Echenique, Viviana -- Dubcovsky, Jorge -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1640-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Agronomy and Range Science, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15016992" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/genetics/growth & development ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; *Cold Temperature ; Down-Regulation ; Epistasis, Genetic ; Evolution, Molecular ; Flowers/*growth & development ; Gene Deletion ; *Gene Expression Regulation, Plant ; Genes, Plant ; Genetic Variation ; Hordeum/genetics ; Molecular Sequence Data ; Mutation ; Plant Proteins/chemistry/genetics/physiology ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; RNA Interference ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Seasons ; Transcription, Genetic ; Triticum/*genetics/*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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  • 90
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    Another group at high risk for HIV (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allison, Edward H -- Seeley, Janet A -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15326332" target="_blank"〉PubMed〈/a〉
    Keywords: Asia/epidemiology ; Female ; Fisheries ; HIV Infections/*epidemiology/transmission ; Humans ; Male ; Occupations ; Prevalence ; Sexual Partners ; *Transients and Migrants
    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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  • 91
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    RNA branching and debranching in the yeast retrovirus-like element Ty1 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-13
    Description: Ty elements of Saccharomyces cerevisiae are long terminal repeat (LTR) retroelements related to retroviruses. Normal levels of Ty1 transposition require Dbr1p, a cellular enzyme that cleaves 2'-5' RNA bonds. We show that Ty1 RNAs lacking identifiable 5' ends accumulate in virus-like particles (VLPs) in dbr1 mutants. Debranching this RNA in vitro with Dbr1p creates an uncapped version of the normal Ty1 RNA 5' end. We show that the 5' nucleotide (nt) of Ty1 RNA forms a 2'-5' bond with a nt near the 3' end of the same RNA, creating a lariat. The properties of the lariat suggest it forms by a novel mechanism and that branching and debranching may play roles in Ty1 reverse transcription at the minus-strand transfer step.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, Zhi -- Menees, Thomas M -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):240-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716018" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; Blotting, Northern ; DNA, Complementary/metabolism ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; RNA Caps ; RNA Nucleotidyltransferases/genetics/metabolism ; RNA, Fungal/*chemistry/genetics/*metabolism ; RNA, Messenger/chemistry/genetics/metabolism ; RNA-Directed DNA Polymerase/metabolism ; Retroelements/genetics/*physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Ribonuclease H/metabolism ; Saccharomyces cerevisiae/*genetics ; Terminal Repeat Sequences ; Transcription, Genetic
    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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  • 92
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    Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: The observation of the regulation of fast protein dynamics in a cellular context requires the development of reliable technologies. Here, a signal regulation cascade reliant on the stimulus-dependent acceleration of the bidirectional flow of mitogen-activated protein kinase (extracellular signal-regulated kinase) across the nuclear envelope was visualized by reversible protein highlighting. Light-induced conversion between the bright and dark states of a monomeric fluorescent protein engineered from a novel coral protein was employed. Because of its photochromic properties, the protein could be highlighted, erased, and highlighted again in a nondestructive manner, allowing direct observation of regulated fast nucleocytoplasmic shuttling of key signaling molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ando, Ryoko -- Mizuno, Hideaki -- Miyawaki, Atsushi -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Function and Dynamics, Advanced Technology Development Group, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako-city, Saitama, 351-0198, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550670" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Sequence ; Animals ; Anthozoa ; COS Cells ; Cell Nucleus/*metabolism ; Cytoplasm/*metabolism ; Epidermal Growth Factor/pharmacology ; Fluorescence ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Light ; Luminescent Proteins/chemistry/*metabolism ; MAP Kinase Signaling System ; Microscopy, Confocal ; Mitogen-Activated Protein Kinase 3/*metabolism ; Molecular Sequence Data ; Nuclear Envelope/*metabolism ; Phosphorylation ; Protein Transport ; Recombinant Proteins/chemistry/metabolism ; Transfection ; beta Karyopherins/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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  • 93
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    TAF1 activates transcription by phosphorylation of serine 33 in histone H2B (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-15
    Description: Dynamic changes in chromatin structure, induced by posttranslational modification of histones, play a fundamental role in regulating eukaryotic transcription. Here we report that histone H2B is phosphorylated at evolutionarily conserved Ser33 (H2B-S33) by the carboxyl-terminal kinase domain (CTK) of the Drosophila TFIID subunit TAF1. Phosphorylation of H2B-S33 at the promoter of the cell cycle regulatory gene string and the segmentation gene giant coincides with transcriptional activation. Elimination of TAF1 CTK activity in Drosophila cells and embryos reduces transcriptional activation and phosphorylation of H2B-S33. These data reveal that H2B-S33 is a physiological substrate for the TAF1 CTK and that H2B-S33 phosphorylation is essential for transcriptional activation events that promote cell cycle progression and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maile, Tobias -- Kwoczynski, Simona -- Katzenberger, Rebeccah J -- Wassarman, David A -- Sauer, Frank -- GM066204-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 May 14;304(5673):1010-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California-Riverside, Riverside, CA 95121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15143281" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cell Cycle ; Cell Cycle Proteins ; DNA-Binding Proteins/genetics ; Drosophila/embryology/*genetics/metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Embryo, Nonmammalian/physiology ; Genes, Insect ; Histone Acetyltransferases ; Histones/chemistry/*metabolism ; Homeodomain Proteins/genetics ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Phosphoserine/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/genetics ; RNA Interference ; Recombinant Proteins/chemistry/metabolism ; Repressor Proteins/genetics ; TATA-Binding Protein Associated Factors ; Transcription Factor TFIID/chemistry/genetics/*metabolism ; Transcription Factors ; *Transcription, Genetic ; *Transcriptional Activation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and metabolism (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-02
    Description: Diatoms are unicellular algae with plastids acquired by secondary endosymbiosis. They are responsible for approximately 20% of global carbon fixation. We report the 34 million-base pair draft nuclear genome of the marine diatom Thalassiosira pseudonana and its 129 thousand-base pair plastid and 44 thousand-base pair mitochondrial genomes. Sequence and optical restriction mapping revealed 24 diploid nuclear chromosomes. We identified novel genes for silicic acid transport and formation of silica-based cell walls, high-affinity iron uptake, biosynthetic enzymes for several types of polyunsaturated fatty acids, use of a range of nitrogenous compounds, and a complete urea cycle, all attributes that allow diatoms to prosper in aquatic environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Armbrust, E Virginia -- Berges, John A -- Bowler, Chris -- Green, Beverley R -- Martinez, Diego -- Putnam, Nicholas H -- Zhou, Shiguo -- Allen, Andrew E -- Apt, Kirk E -- Bechner, Michael -- Brzezinski, Mark A -- Chaal, Balbir K -- Chiovitti, Anthony -- Davis, Aubrey K -- Demarest, Mark S -- Detter, J Chris -- Glavina, Tijana -- Goodstein, David -- Hadi, Masood Z -- Hellsten, Uffe -- Hildebrand, Mark -- Jenkins, Bethany D -- Jurka, Jerzy -- Kapitonov, Vladimir V -- Kroger, Nils -- Lau, Winnie W Y -- Lane, Todd W -- Larimer, Frank W -- Lippmeier, J Casey -- Lucas, Susan -- Medina, Monica -- Montsant, Anton -- Obornik, Miroslav -- Parker, Micaela Schnitzler -- Palenik, Brian -- Pazour, Gregory J -- Richardson, Paul M -- Rynearson, Tatiana A -- Saito, Mak A -- Schwartz, David C -- Thamatrakoln, Kimberlee -- Valentin, Klaus -- Vardi, Assaf -- Wilkerson, Frances P -- Rokhsar, Daniel S -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):79-86.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Oceanography, University of Washington, Seattle, WA 98195, USA. armbrust@ocean.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459382" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Algal Proteins/chemistry/genetics/physiology ; Animals ; *Biological Evolution ; Cell Nucleus/genetics ; Chromosomes ; DNA/genetics ; Diatoms/chemistry/cytology/*genetics/metabolism ; *Ecosystem ; Energy Metabolism ; *Genome ; Iron/metabolism ; Light ; Light-Harvesting Protein Complexes/chemistry/genetics/metabolism ; Mitochondria/genetics ; Molecular Sequence Data ; Nitrogen/metabolism ; Photosynthesis ; Plastids/genetics ; Restriction Mapping ; Sequence Alignment ; *Sequence Analysis, DNA ; Silicic Acid/metabolism ; Symbiosis ; Urea/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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  • 95
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    Planetary science. A wet early Mars seen in salty deposits (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2004 Mar 5;303(5663):1450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001747" target="_blank"〉PubMed〈/a〉
    Keywords: Extraterrestrial Environment ; Ferric Compounds/analysis ; Geologic Sediments/chemistry ; Magnesium Sulfate/analysis ; *Mars ; Temperature ; *Water
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    The sudden death of a coral reef (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoeksema, Bert W -- Cleary, Daniel F R -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1293-4; author reply 1293-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14988535" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/*growth & development ; *Dinoflagellida ; *Ecosystem ; *Fires ; Fishes ; Indian Ocean ; Indonesia ; Iron ; Temperature
    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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  • 97
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    Zebrafish Dpr2 inhibits mesoderm induction by promoting degradation of nodal receptors (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-02
    Description: Nodal proteins, members of the transforming growth factor-beta (TGFbeta) superfamily, have been identified as key endogenous mesoderm inducers in vertebrates. Precise control of Nodal signaling is essential for normal development of embryos. Here, we report that zebrafish dapper2 (dpr2) is expressed in mesoderm precursors during early embryogenesis and is positively regulated by Nodal signals. In vivo functional studies in zebrafish suggest that Dpr2 suppresses mesoderm induction activities of Nodal signaling. Dpr2 is localized in late endosomes, binds to the TGFbeta receptors ALK5 and ALK4, and accelerates lysosomal degradation of these receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Lixia -- Zhou, Hu -- Su, Ying -- Sun, Zhihui -- Zhang, Haiwen -- Zhang, Long -- Zhang, Yu -- Ning, Yuanheng -- Chen, Ye-Guang -- Meng, Anming -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Biology, Ministry of Education (MOE), Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459392" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/*metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Embryo, Nonmammalian/embryology/*metabolism ; *Embryonic Induction ; Endosomes/metabolism ; Fluorescent Antibody Technique ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Humans ; In Situ Hybridization ; Intracellular Signaling Peptides and Proteins ; Lysosomes/metabolism ; Mesoderm/*physiology ; Molecular Sequence Data ; Mutation ; Nodal Signaling Ligands ; Oligonucleotides, Antisense ; Protein-Serine-Threonine Kinases ; Proteins/metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Signal Transduction ; Transforming Growth Factor beta/genetics/metabolism ; Zebrafish/*embryology/genetics/metabolism ; Zebrafish Proteins/chemistry/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Diversification of Ig superfamily genes in an invertebrate (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-13
    Description: The freshwater snail Biomphalaria glabrata possesses a diverse family of fibrinogen-related proteins (FREPs), hemolymph polypeptides that consist of one or two amino-terminal immunoglobulin superfamily (IgSF) domains and a carboxyl-terminal fibrinogen domain. Here, we show that the IgSF1 domain of the FREP3 subfamily is diversified at the genomic level at higher rates than those recorded for control genes. All sequence variants are derived from a small set of nine source sequences by point mutation and recombinatorial processes. Diverse FREP3 transcripts are also produced. We hypothesize a mechanism present in snails that is capable of diversifying molecules involved in internal defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Si-Ming -- Adema, Coen M -- Kepler, Thomas B -- Loker, Eric S -- R01AI24340/AI/NIAID NIH HHS/ -- R01AI52363/AI/NIAID NIH HHS/ -- RR-1P20RR18754/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 9;305(5681):251-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of New Mexico, Albuquerque, NM 87131, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15247481" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Biomphalaria/embryology/*genetics/immunology ; Blotting, Southern ; Computational Biology ; DNA, Complementary ; Disorders of Sex Development ; Genes, Immunoglobulin ; *Genetic Variation ; Hemocytes ; Immunoglobulins/chemistry/*genetics ; Molecular Sequence Data ; Point Mutation ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Recombination, Genetic
    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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  • 99
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    Functional adaptation of BabA, the H. pylori ABO blood group antigen binding adhesin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-27
    Description: Adherence by Helicobacter pylori increases the risk of gastric disease. Here, we report that more than 95% of strains that bind fucosylated blood group antigen bind A, B, and O antigens (generalists), whereas 60% of adherent South American Amerindian strains bind blood group O antigens best (specialists). This specialization coincides with the unique predominance of blood group O in these Amerindians. Strains differed about 1500-fold in binding affinities, and diversifying selection was evident in babA sequences. We propose that cycles of selection for increased and decreased bacterial adherence contribute to babA diversity and that these cycles have led to gradual replacement of generalist binding by specialist binding in blood group O-dominant human populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aspholm-Hurtig, Marina -- Dailide, Giedrius -- Lahmann, Martina -- Kalia, Awdhesh -- Ilver, Dag -- Roche, Niamh -- Vikstrom, Susanne -- Sjostrom, Rolf -- Linden, Sara -- Backstrom, Anna -- Lundberg, Carina -- Arnqvist, Anna -- Mahdavi, Jafar -- Nilsson, Ulf J -- Velapatino, Billie -- Gilman, Robert H -- Gerhard, Markus -- Alarcon, Teresa -- Lopez-Brea, Manuel -- Nakazawa, Teruko -- Fox, James G -- Correa, Pelayo -- Dominguez-Bello, Maria Gloria -- Perez-Perez, Guillermo I -- Blaser, Martin J -- Normark, Staffan -- Carlstedt, Ingemar -- Oscarson, Stefan -- Teneberg, Susann -- Berg, Douglas E -- Boren, Thomas -- P30 DK52574/DK/NIDDK NIH HHS/ -- R01 AI38166/AI/NIAID NIH HHS/ -- R01 DK53727/DK/NIDDK NIH HHS/ -- R01 DK63041/DK/NIDDK NIH HHS/ -- R03 AI49161/AI/NIAID NIH HHS/ -- R0IGM62370/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 23;305(5683):519-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Odontology, section of Oral Microbiology, Umea University, SE-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15273394" target="_blank"〉PubMed〈/a〉
    Keywords: ABO Blood-Group System/*metabolism ; Adaptation, Biological ; Adhesins, Bacterial/chemistry/*genetics/immunology/*metabolism ; Alleles ; *Bacterial Adhesion ; Base Sequence ; Binding Sites ; Evolution, Molecular ; Fucose/metabolism ; Gastric Mucosa/microbiology ; Helicobacter Infections/microbiology ; Helicobacter pylori/genetics/immunology/*physiology ; Humans ; Indians, South American ; Lewis Blood-Group System/metabolism ; Molecular Sequence Data ; Mutation ; Peru ; Phenotype ; Phylogeny ; Protein Binding ; Selection, Genetic ; Transformation, Bacterial
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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    Detection of a deep 3-microm absorption feature in the spectrum of Amalthea (JV) (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-25
    Description: Near-infrared spectra of Jupiter's small inner satellites Amalthea and Thebe are similar to those of D-type asteroids in the 0.8- to 2.5-micrometer wavelength range. A deep absorption feature is detected at 3 micrometers in the spectra of the trailing side of Amalthea, which is similar to that of the non-ice components of Callisto and can be attributed to hydrous minerals. These surface materials cannot be explained if the satellite formed at its present orbit by accreting from a circumjovian nebula. Amalthea and Thebe may be the remnants of Jupiter's inflowing building blocks that formed in the outer part or outside of the circumjovian nebula.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takato, Naruhisa -- Bus, Schelte J -- Terada, Hiroshi -- Pyo, Tae-Soo -- Kobayashi, Naoto -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Subaru Telescope, National Astronomical Observatory of Japan, 650 North Aohoku Place, Hilo, Hawaii 96720, USA. takato@naoj.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618511" target="_blank"〉PubMed〈/a〉
    Keywords: Ice ; *Jupiter ; *Minerals ; Spectroscopy, Near-Infrared ; Temperature ; *Water
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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