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  • Articles  (356)
  • Molecular Sequence Data  (241)
  • *Ecosystem  (116)
  • American Association for the Advancement of Science (AAAS)  (356)
  • American Institute of Physics (AIP)
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  • Articles  (356)
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  • American Association for the Advancement of Science (AAAS)  (356)
  • American Institute of Physics (AIP)
  • American Society of Hematology
  • EMBO Press
  • Essen : Verl. Glückauf
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  • 2005-2009  (216)
  • 1995-1999  (140)
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  • 1
    Publication Date: 2007-09-29
    Description: The CCR5 co-receptor binds to the HIV-1 gp120 envelope glycoprotein and facilitates HIV-1 entry into cells. Its N terminus is tyrosine-sulfated, as are many antibodies that react with the co-receptor binding site on gp120. We applied nuclear magnetic resonance and crystallographic techniques to analyze the structure of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 and CD4. The conformations of tyrosine-sulfated regions of CCR5 (alpha-helix) and 412d (extended loop) are surprisingly different. Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2278242/" 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/PMC2278242/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Chih-Chin -- Lam, Son N -- Acharya, Priyamvada -- Tang, Min -- Xiang, Shi-Hua -- Hussan, Syed Shahzad-Ul -- Stanfield, Robyn L -- Robinson, James -- Sodroski, Joseph -- Wilson, Ian A -- Wyatt, Richard -- Bewley, Carole A -- Kwong, Peter D -- P30 AI060354/AI/NIAID NIH HHS/ -- U19 AI067854/AI/NIAID NIH HHS/ -- U19 AI067854-03/AI/NIAID NIH HHS/ -- Z99 AI999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1930-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901336" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD4/*chemistry/immunology ; Crystallography, X-Ray ; HIV Antibodies/*chemistry/immunology ; HIV Envelope Protein gp120/*chemistry/immunology/metabolism ; HIV-1/metabolism ; Humans ; Models, Molecular ; Molecular Mimicry ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Peptide Fragments/chemistry/metabolism ; Receptors, CCR5/*chemistry/metabolism ; Sulfates/metabolism ; Tyrosine/metabolism ; Virus Internalization
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  • 2
    Publication Date: 2007-04-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peng, Changhui -- Ouyang, Hua -- Gao, Qiong -- Jiang, Yuan -- Zhang, Feng -- Li, Jun -- Yu, Qiang -- New York, N.Y. -- Science. 2007 Apr 27;316(5824):546-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut des Sciences de L'Environnement, Departement des Sciences Biologiques, Universite du Quebec a Montreal, Montreal, QC, Canada, H3C 3P8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17463272" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Migration ; Animals ; China ; *Conservation of Natural Resources/legislation & jurisprudence ; *Ecosystem ; *Environment ; Fresh Water ; Plants ; *Railroads ; Refuse Disposal ; Temperature ; Travel
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  • 3
    Publication Date: 2007-02-03
    Description: The taxonomic composition of environmental communities is an important indicator of their ecology and function. We used a set of protein-coding marker genes, extracted from large-scale environmental shotgun sequencing data, to provide a more direct, quantitative, and accurate picture of community composition than that provided by traditional ribosomal RNA-based approaches depending on the polymerase chain reaction. Mapping marker genes from four diverse environmental data sets onto a reference species phylogeny shows that certain communities evolve faster than others. The method also enables determination of preferred habitats for entire microbial clades and provides evidence that such habitat preferences are often remarkably stable over time.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Mering, C -- Hugenholtz, P -- Raes, J -- Tringe, S G -- Doerks, T -- Jensen, L J -- Ward, N -- Bork, P -- New York, N.Y. -- Science. 2007 Feb 23;315(5815):1126-30. Epub 2007 Feb 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272687" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/*classification/genetics ; Biological Evolution ; Bone and Bones/microbiology ; *Ecosystem ; *Environmental Microbiology ; Genes, Bacterial ; Genes, rRNA ; Genetic Markers ; *Genomics ; Likelihood Functions ; Mining ; *Phylogeny ; Seawater/microbiology ; Soil Microbiology ; Water Microbiology ; Whales/microbiology
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  • 4
    Publication Date: 2007-08-04
    Description: In flowering plants, signaling between the male pollen tube and the synergid cells of the female gametophyte is required for fertilization. In the Arabidopsis thaliana mutant feronia (fer), fertilization is impaired; the pollen tube fails to arrest and thus continues to grow inside the female gametophyte. FER encodes a synergid-expressed, plasma membrane-localized receptor-like kinase. We found that the FER protein accumulates asymmetrically in the synergid membrane at the filiform apparatus. Interspecific crosses using pollen from Arabidopsis lyrata and Cardamine flexuosa on A. thaliana stigmas resulted in a fer-like phenotype that correlates with sequence divergence in the extracellular domain of FER. Our findings show that the female control of pollen tube reception is based on a FER-dependent signaling pathway, which may play a role in reproductive isolation barriers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Escobar-Restrepo, Juan-Miguel -- Huck, Norbert -- Kessler, Sharon -- Gagliardini, Valeria -- Gheyselinck, Jacqueline -- Yang, Wei-Cai -- Grossniklaus, Ueli -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):656-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Plant Biology and Zurich-Basel Plant Science Center, University of Zurich, Zollikerstrasse 107, CH-8008 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673660" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/enzymology/genetics/*physiology ; Arabidopsis Proteins/chemistry/*genetics/*metabolism ; Brassicaceae/genetics/physiology ; Cell Membrane/enzymology ; Crosses, Genetic ; Evolution, Molecular ; Flowers/cytology/enzymology/*physiology ; Gene Expression ; Genes, Plant ; Germination ; Ligands ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Phosphotransferases/chemistry/*genetics/*metabolism ; Plant Epidermis/enzymology ; Pollen Tube/growth & development/*physiology ; Recombinant Fusion Proteins/metabolism ; Reproduction ; Seeds/growth & development ; Signal Transduction ; Species Specificity
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  • 5
    Publication Date: 2007-10-06
    Description: The analytical power of environmental DNA sequences for modeling microbial ecosystems depends on accurate assessments of population structure, including diversity (richness) and relative abundance (evenness). We investigated both aspects of population structure for microbial communities at two neighboring hydrothermal vents by examining the sequences of more than 900,000 microbial small-subunit ribosomal RNA amplicons. The two vent communities have different population structures that reflect local geochemical regimes. Descriptions of archaeal diversity were nearly exhaustive, but despite collecting an unparalleled number of sequences, statistical analyses indicated additional bacterial diversity at every taxonomic level. We predict that hundreds of thousands of sequences will be necessary to capture the vast diversity of microbial communities, and that different patterns of evenness for both high- and low-abundance taxa may be important in defining microbial ecosystem dynamics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, Julie A -- Mark Welch, David B -- Morrison, Hilary G -- Huse, Susan M -- Neal, Phillip R -- Butterfield, David A -- Sogin, Mitchell L -- New York, N.Y. -- Science. 2007 Oct 5;318(5847):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Josephine Bay Paul Center, Marine Biological Laboratory, 7 MBL Street, Woods Hole, MA 02543, USA. jhuber@mbl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916733" target="_blank"〉PubMed〈/a〉
    Keywords: *Archaea/classification/genetics ; *Bacteria/classification/genetics ; *Biodiversity ; DNA, Archaeal/analysis ; DNA, Bacterial/analysis ; DNA, Ribosomal/analysis ; *Ecosystem ; Epsilonproteobacteria/classification/genetics ; Geologic Sediments/microbiology ; Pacific Ocean ; Polymerase Chain Reaction ; RNA, Ribosomal ; Seawater/*microbiology ; Sequence Analysis, DNA
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-02-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walther, Gian-Reto -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):606-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Ecology, University of Bayreuth, 95440 Bayreuth, Germany. gian-reto.walther@uni-bayreuth.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272708" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; California ; *Climate ; *Ecosystem ; *Invertebrates/physiology ; *Plant Development ; Poaceae/growth & development ; Population Dynamics ; Rain ; Research Design ; Seasons ; Time Factors
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  • 7
    Publication Date: 2007-08-04
    Description: BtuCD is an adenosine triphosphate-binding cassette (ABC) transporter that translocates vitamin B12 from the periplasmic binding protein BtuF into the cytoplasm of Escherichia coli. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF. The lobes of BtuF are spread apart, and B12 is displaced from the binding pocket. The transmembrane BtuC subunits reveal two distinct conformations, and the translocation pathway is closed to both sides of the membrane. Electron paramagnetic resonance spectra of spin-labeled cysteine mutants reconstituted in proteoliposomes are consistent with the conformation of BtuCD-F that was observed in the crystal structure. A comparison with BtuCD and the homologous HI1470/71 protein suggests that the structure of BtuCD-F may reflect a posttranslocation intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hvorup, Rikki N -- Goetz, Birke A -- Niederer, Martina -- Hollenstein, Kaspar -- Perozo, Eduardo -- Locher, Kaspar P -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1387-90. Epub 2007 Aug 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, HPK D14.3, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673622" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry ; Amino Acid Sequence ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Escherichia coli ; Escherichia coli Proteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Periplasmic Binding Proteins/*chemistry ; Protein Binding ; Protein Conformation ; Recombinant Fusion Proteins/chemistry
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  • 8
    Publication Date: 2007-10-27
    Description: We report the cloning of Style2.1, the major quantitative trait locus responsible for a key floral attribute (style length) associated with the evolution of self-pollination in cultivated tomatoes. The gene encodes a putative transcription factor that regulates cell elongation in developing styles. The transition from cross-pollination to self-pollination was accompanied, not by a change in the STYLE2.1 protein, but rather by a mutation in the Style2.1 promoter that results in a down-regulation of Style2.1 expression during flower development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Kai-Yi -- Cong, Bin -- Wing, Rod -- Vrebalov, Julia -- Tanksley, Steven D -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):643-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Breeding and Genetics, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962563" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Chromosome Mapping ; Cloning, Molecular ; Crosses, Genetic ; Down-Regulation ; Flowers/*anatomy & histology/genetics/growth & development ; Genes, Plant ; Genotype ; Helix-Loop-Helix Motifs ; Lycopersicon esculentum/anatomy & histology/*genetics/*physiology ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/metabolism ; Pollen/physiology ; Promoter Regions, Genetic ; Quantitative Trait Loci ; Reproduction ; Sequence Deletion ; Transcription Factors/chemistry/*genetics/metabolism ; Transformation, Genetic
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  • 9
    Publication Date: 2007-04-14
    Description: A systematic fluorescence in situ hybridization comparison of macaque and human synteny organization disclosed five additional macaque evolutionary new centromeres (ENCs) for a total of nine ENCs. To understand the dynamics of ENC formation and progression, we compared the ENC of macaque chromosome 4 with the human orthologous region, at 6q24.3, that conserves the ancestral genomic organization. A 250-kilobase segment was extensively duplicated around the macaque centromere. These duplications were strictly intrachromosomal. Our results suggest that novel centromeres may trigger only local duplication activity and that the absence of genes in the seeding region may have been important in ENC maintenance and progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ventura, Mario -- Antonacci, Francesca -- Cardone, Maria Francesca -- Stanyon, Roscoe -- D'Addabbo, Pietro -- Cellamare, Angelo -- Sprague, L James -- Eichler, Evan E -- Archidiacono, Nicoletta -- Rocchi, Mariano -- GM58815/GM/NIGMS NIH HHS/ -- HG002385/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Microbiology, University of Bari, 70126 Bari, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431171" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Centromere ; Chromosomes, Human, Pair 6 ; Dna ; *Evolution, Molecular ; Gene Duplication ; Humans ; Macaca mulatta/*genetics ; Molecular Sequence Data ; Sequence Tagged Sites ; Synteny
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  • 10
    Publication Date: 2007-03-24
    Description: Clustered regularly interspaced short palindromic repeats (CRISPR) are a distinctive feature of the genomes of most Bacteria and Archaea and are thought to be involved in resistance to bacteriophages. We found that, after viral challenge, bacteria integrated new spacers derived from phage genomic sequences. Removal or addition of particular spacers modified the phage-resistance phenotype of the cell. Thus, CRISPR, together with associated cas genes, provided resistance against phages, and resistance specificity is determined by spacer-phage sequence similarity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrangou, Rodolphe -- Fremaux, Christophe -- Deveau, Helene -- Richards, Melissa -- Boyaval, Patrick -- Moineau, Sylvain -- Romero, Dennis A -- Horvath, Philippe -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Danisco USA Inc., 3329 Agriculture Drive, Madison, WI 53716, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17379808" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Bacterial/genetics ; DNA, Intergenic/*genetics ; Evolution, Molecular ; *Genes, Bacterial ; Genome, Viral ; Molecular Sequence Data ; Mutation ; Polymorphism, Single Nucleotide ; *Repetitive Sequences, Nucleic Acid ; Streptococcus Phages/genetics/*physiology ; Streptococcus thermophilus/*genetics/*virology ; Viral Plaque Assay ; Virus Replication
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-05-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 May 4;316(5825):686-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17478697" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; Biodiversity ; *Biological Evolution ; *Ecosystem ; Gene Flow ; Geography ; Plants
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  • 12
    Publication Date: 2007-01-20
    Description: Litter decomposition provides the primary source of mineral nitrogen (N) for biological activity in most terrestrial ecosystems. A 10-year decomposition experiment in 21 sites from seven biomes found that net N release from leaf litter is dominantly driven by the initial tissue N concentration and mass remaining regardless of climate, edaphic conditions, or biota. Arid grasslands exposed to high ultraviolet radiation were an exception, where net N release was insensitive to initial N. Roots released N linearly with decomposition and exhibited little net N immobilization. We suggest that fundamental constraints on decomposer physiologies lead to predictable global-scale patterns in net N release during decomposition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parton, William -- Silver, Whendee L -- Burke, Ingrid C -- Grassens, Leo -- Harmon, Mark E -- Currie, William S -- King, Jennifer Y -- Adair, E Carol -- Brandt, Leslie A -- Hart, Stephen C -- Fasth, Becky -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Natural Resource Ecology Laboratory, Colorado State University, 200 West Lake, Campus Mail 1499, Fort Collins, CO 80523-1499, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17234944" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodegradation, Environmental ; Carbon/metabolism ; Climate ; *Ecosystem ; Humidity ; Mathematics ; Nitrogen/*metabolism ; Plant Leaves/metabolism ; Plant Roots/metabolism ; Plants/*metabolism ; Poaceae ; Regression Analysis ; Seasons ; Soil Microbiology ; Temperature ; Time Factors ; Trees
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-07-07
    Description: Understanding the relationship between diversity and stability requires a knowledge of how species interact with each other and how each is affected by the environment. The relationship is also complex, because the concept of stability is multifaceted; different types of stability describing different properties of ecosystems lead to multiple diversity-stability relationships. A growing number of empirical studies demonstrate positive diversity-stability relationships. These studies, however, have emphasized only a few types of stability, and they rarely uncover the mechanisms responsible for stability. Because anthropogenic changes often affect stability and diversity simultaneously, diversity-stability relationships cannot be understood outside the context of the environmental drivers affecting both. This shifts attention away from diversity-stability relationships toward the multiple factors, including diversity, that dictate the stability of ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ives, Anthony R -- Carpenter, Stephen R -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):58-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Wisconsin, Madison, WI 53706, USA. arives@wisc.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615333" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Ecosystem ; Environment ; Extinction, Biological ; Models, Biological ; Population Dynamics
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  • 14
    Publication Date: 2007-03-24
    Description: The nucleoporins Nup58 and Nup45 are part of the central transport channel of the nuclear pore complex, which is thought to have a flexible diameter. In the crystal structure of an alpha-helical region of mammalian Nup58/45, we identified distinct tetramers, each consisting of two antiparallel hairpin dimers. The intradimeric interface is hydrophobic, whereas dimer-dimer association occurs through large hydrophilic residues. These residues are laterally displaced in various tetramer conformations, which suggests an intermolecular sliding by 11 angstroms. We propose that circumferential sliding plays a role in adjusting the diameter of the central transport channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Melcak, Ivo -- Hoelz, Andre -- Blobel, Gunter -- R01 GM111461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1729-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17379812" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/chemistry ; Molecular Sequence Data ; Nuclear Pore Complex Proteins/*chemistry ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Rats ; Static Electricity
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  • 15
    Publication Date: 2007-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krajick, Kevin -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):322-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17234927" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea ; Bacteria ; Budgets ; *Ecosystem ; *Exobiology ; Hot Springs/*microbiology ; Jupiter ; Mexico ; Robotics/economics/*instrumentation ; Software ; United States ; United States National Aeronautics and Space Administration/economics ; *Water Microbiology
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fisher, Charles R -- Girguis, Peter -- New York, N.Y. -- Science. 2007 Jan 12;315(5809):198-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Pennsylvania State University, University Park, PA 16801, USA. cfisher@psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17218516" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/analysis/*metabolism ; Carbon/metabolism ; Carbon Isotopes/analysis ; Chemoautotrophic Growth ; Citric Acid Cycle ; *Ecosystem ; Gammaproteobacteria/*metabolism ; Metabolic Networks and Pathways ; Oxidation-Reduction ; Pacific Ocean ; Polychaeta/*microbiology/*physiology ; Proteome ; *Proteomics ; Reproduction ; Sulfides/metabolism ; *Symbiosis ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
    Publication Date: 2007-05-26
    Description: The advent of biotechnology-derived, herbicide-resistant crops has revolutionized farming practices in many countries. Facile, highly effective, environmentally sound, and profitable weed control methods have been rapidly adopted by crop producers who value the benefits associated with biotechnology-derived weed management traits. But a rapid rise in the populations of several troublesome weeds that are tolerant or resistant to herbicides currently used in conjunction with herbicide-resistant crops may signify that the useful lifetime of these economically important weed management traits will be cut short. We describe the development of soybean and other broadleaf plant species resistant to dicamba, a widely used, inexpensive, and environmentally safe herbicide. The dicamba resistance technology will augment current herbicide resistance technologies and extend their effective lifetime. Attributes of both nuclear- and chloroplast-encoded dicamba resistance genes that affect the potency and expected durability of the herbicide resistance trait are examined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Behrens, Mark R -- Mutlu, Nedim -- Chakraborty, Sarbani -- Dumitru, Razvan -- Jiang, Wen Zhi -- Lavallee, Bradley J -- Herman, Patricia L -- Clemente, Thomas E -- Weeks, Donald P -- New York, N.Y. -- Science. 2007 May 25;316(5828):1185-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525337" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture ; Arabidopsis/drug effects/genetics ; Chloroplasts/genetics ; Dicamba/*pharmacology ; Drug Resistance/genetics ; Genetic Engineering ; Genetic Vectors ; Herbicides/*pharmacology ; Lycopersicon esculentum/drug effects/genetics ; Mixed Function Oxygenases/*genetics/metabolism ; Molecular Sequence Data ; Oxidoreductases, O-Demethylating/metabolism ; Plants, Genetically Modified/drug effects/genetics ; Pseudomonas/enzymology/genetics ; Soybeans/*drug effects/genetics ; Tobacco/drug effects/genetics
    Print ISSN: 0036-8075
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  • 18
    Publication Date: 2007-10-13
    Description: Chlamydomonas reinhardtii is a unicellular green alga whose lineage diverged from land plants over 1 billion years ago. It is a model system for studying chloroplast-based photosynthesis, as well as the structure, assembly, and function of eukaryotic flagella (cilia), which were inherited from the common ancestor of plants and animals, but lost in land plants. We sequenced the approximately 120-megabase nuclear genome of Chlamydomonas and performed comparative phylogenomic analyses, identifying genes encoding uncharacterized proteins that are likely associated with the function and biogenesis of chloroplasts or eukaryotic flagella. Analyses of the Chlamydomonas genome advance our understanding of the ancestral eukaryotic cell, reveal previously unknown genes associated with photosynthetic and flagellar functions, and establish links between ciliopathy and the composition and function of flagella.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2875087/" 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/PMC2875087/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merchant, Sabeeha S -- Prochnik, Simon E -- Vallon, Olivier -- Harris, Elizabeth H -- Karpowicz, Steven J -- Witman, George B -- Terry, Astrid -- Salamov, Asaf -- Fritz-Laylin, Lillian K -- Marechal-Drouard, Laurence -- Marshall, Wallace F -- Qu, Liang-Hu -- Nelson, David R -- Sanderfoot, Anton A -- Spalding, Martin H -- Kapitonov, Vladimir V -- Ren, Qinghu -- Ferris, Patrick -- Lindquist, Erika -- Shapiro, Harris -- Lucas, Susan M -- Grimwood, Jane -- Schmutz, Jeremy -- Cardol, Pierre -- Cerutti, Heriberto -- Chanfreau, Guillaume -- Chen, Chun-Long -- Cognat, Valerie -- Croft, Martin T -- Dent, Rachel -- Dutcher, Susan -- Fernandez, Emilio -- Fukuzawa, Hideya -- Gonzalez-Ballester, David -- Gonzalez-Halphen, Diego -- Hallmann, Armin -- Hanikenne, Marc -- Hippler, Michael -- Inwood, William -- Jabbari, Kamel -- Kalanon, Ming -- Kuras, Richard -- Lefebvre, Paul A -- Lemaire, Stephane D -- Lobanov, Alexey V -- Lohr, Martin -- Manuell, Andrea -- Meier, Iris -- Mets, Laurens -- Mittag, Maria -- Mittelmeier, Telsa -- Moroney, James V -- Moseley, Jeffrey -- Napoli, Carolyn -- Nedelcu, Aurora M -- Niyogi, Krishna -- Novoselov, Sergey V -- Paulsen, Ian T -- Pazour, Greg -- Purton, Saul -- Ral, Jean-Philippe -- Riano-Pachon, Diego Mauricio -- Riekhof, Wayne -- Rymarquis, Linda -- Schroda, Michael -- Stern, David -- Umen, James -- Willows, Robert -- Wilson, Nedra -- Zimmer, Sara Lana -- Allmer, Jens -- Balk, Janneke -- Bisova, Katerina -- Chen, Chong-Jian -- Elias, Marek -- Gendler, Karla -- Hauser, Charles -- Lamb, Mary Rose -- Ledford, Heidi -- Long, Joanne C -- Minagawa, Jun -- Page, M Dudley -- Pan, Junmin -- Pootakham, Wirulda -- Roje, Sanja -- Rose, Annkatrin -- Stahlberg, Eric -- Terauchi, Aimee M -- Yang, Pinfen -- Ball, Steven -- Bowler, Chris -- Dieckmann, Carol L -- Gladyshev, Vadim N -- Green, Pamela -- Jorgensen, Richard -- Mayfield, Stephen -- Mueller-Roeber, Bernd -- Rajamani, Sathish -- Sayre, Richard T -- Brokstein, Peter -- Dubchak, Inna -- Goodstein, David -- Hornick, Leila -- Huang, Y Wayne -- Jhaveri, Jinal -- Luo, Yigong -- Martinez, Diego -- Ngau, Wing Chi Abby -- Otillar, Bobby -- Poliakov, Alexander -- Porter, Aaron -- Szajkowski, Lukasz -- Werner, Gregory -- Zhou, Kemin -- Grigoriev, Igor V -- Rokhsar, Daniel S -- Grossman, Arthur R -- GM07185/GM/NIGMS NIH HHS/ -- GM42143/GM/NIGMS NIH HHS/ -- R01 GM032843/GM/NIGMS NIH HHS/ -- R01 GM042143/GM/NIGMS NIH HHS/ -- R01 GM042143-09/GM/NIGMS NIH HHS/ -- R01 GM060992/GM/NIGMS NIH HHS/ -- R01 GM062915-06/GM/NIGMS NIH HHS/ -- R37 GM030626/GM/NIGMS NIH HHS/ -- R37 GM042143/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):245-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932292" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/*genetics/*physiology ; Animals ; *Biological Evolution ; Chlamydomonas reinhardtii/*genetics/physiology ; Chloroplasts/metabolism ; Computational Biology ; DNA, Algal/genetics ; Flagella/metabolism ; Genes ; *Genome ; Genomics ; Membrane Transport Proteins/genetics/physiology ; Molecular Sequence Data ; Multigene Family ; Photosynthesis/genetics ; Phylogeny ; Plants/genetics ; Proteome ; Sequence Analysis, DNA
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  • 19
    Publication Date: 2007-04-14
    Description: We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenni, Simon -- Leibundgut, Marc -- Boehringer, Daniel -- Frick, Christian -- Mikolasek, Bohdan -- Ban, Nenad -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):254-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, 8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431175" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/metabolism ; Acetyltransferases/metabolism ; Acyl Carrier Protein/chemistry/metabolism/ultrastructure ; Acyltransferases/metabolism ; Amino Acid Sequence ; Ascomycota/*enzymology ; Catalytic Domain ; Crystallography, X-Ray ; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)/metabolism ; Fatty Acid Synthases/*chemistry/metabolism ; Fungal Proteins/*chemistry/metabolism ; Hydro-Lyases/metabolism ; Models, Molecular ; Molecular Sequence Data ; NADP/chemistry ; Protein Conformation ; Protein Subunits/chemistry ; Substrate Specificity
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  • 20
    Publication Date: 2007-03-31
    Description: Plastid-to-nucleus retrograde signaling coordinates nuclear gene expression with chloroplast function and is essential for the photoautotrophic life-style of plants. Three retrograde signals have been described, but little is known of their signaling pathways. We show here that GUN1, a chloroplast-localized pentatricopeptide-repeat protein, and ABI4, an Apetala 2 (AP2)-type transcription factor, are common to all three pathways. ABI4 binds the promoter of a retrograde-regulated gene through a conserved motif found in close proximity to a light-regulatory element. We propose a model in which multiple indicators of aberrant plastid function in Arabidopsis are integrated upstream of GUN1 within plastids, which leads to ABI4-mediated repression of nuclear-encoded genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koussevitzky, Shai -- Nott, Ajit -- Mockler, Todd C -- Hong, Fangxin -- Sachetto-Martins, Gilberto -- Surpin, Marci -- Lim, Jason -- Mittler, Ron -- Chory, Joanne -- DRG-1865-05/PHS HHS/ -- F32 GM 18172/GM/NIGMS NIH HHS/ -- F32 GM 69090/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 4;316(5825):715-9. Epub 2007 Mar 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Salk Institute for Biological Studies, 10010 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/17395793" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid ; Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Cell Nucleus/*metabolism/*microbiology ; Chloroplasts/*metabolism ; DNA, Plant/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Electron Transport ; *Gene Expression Regulation, Plant ; Light-Harvesting Protein Complexes/genetics ; Lincomycin/pharmacology ; Models, Biological ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protoporphyrins/metabolism ; Pyridazines/pharmacology ; Signal Transduction ; Transcription Factors/*metabolism
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  • 21
    Publication Date: 2007-12-15
    Description: The worldwide decline in amphibians has been attributed to several causes, especially habitat loss and disease. We identified a further factor, namely "habitat split"-defined as human-induced disconnection between habitats used by different life history stages of a species-which forces forest-associated amphibians with aquatic larvae to make risky breeding migrations between suitable aquatic and terrestrial habitats. In the Brazilian Atlantic Forest, we found that habitat split negatively affects the richness of species with aquatic larvae but not the richness of species with terrestrial development (the latter can complete their life cycle inside forest remnants). This mechanism helps to explain why species with aquatic larvae have the highest incidence of population decline. These findings reinforce the need for the conservation and restoration of riparian vegetation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Becker, Carlos Guilherme -- Fonseca, Carlos Roberto -- Haddad, Celio Fernando Baptista -- Batista, Romulo Fernandes -- Prado, Paulo Inacio -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1775-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departamento de Zoologia, Universidade Estadual de Campinas, 13083-970 Campinas SP, Brazil.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079402" target="_blank"〉PubMed〈/a〉
    Keywords: *Amphibians/growth & development/physiology ; Animal Migration ; Animals ; *Biodiversity ; Brazil ; Conservation of Natural Resources ; *Ecosystem ; Larva/physiology ; Population Dynamics ; Trees ; Water
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  • 22
    Publication Date: 2007-06-02
    Description: Worm et al. (Research Articles, 3 November 2006, p. 787) reported an increasing proportion of fisheries in a "collapsed" state. We show that this may be an artifact of their definition of collapse as a fixed percentage of the maximum and that an increase in the number of managed fisheries could produce similar patterns as an increase in fisheries with catches below 10% of the maximum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilberg, Michael J -- Miller, Thomas J -- New York, N.Y. -- Science. 2007 Jun 1;316(5829):1285; author reply 1285.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chesapeake Biological Laboratory, University of Maryland Center for Environmental Science, P.O. Box 38, Solomons, MD 20688, USA. wilberg@cbl.umces.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540885" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; *Fisheries ; *Fishes ; Forecasting ; Population Dynamics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 23
    Publication Date: 2007-08-19
    Description: In Gram-negative bacteria and eukaryotic organelles, beta-barrel proteins of the outer membrane protein 85-two-partner secretion B (Omp85-TpsB) superfamily are essential components of protein transport machineries. The TpsB transporter FhaC mediates the secretion of Bordetella pertussis filamentous hemagglutinin (FHA). We report the 3.15 A crystal structure of FhaC. The transporter comprises a 16-stranded beta barrel that is occluded by an N-terminal alpha helix and an extracellular loop and a periplasmic module composed of two aligned polypeptide-transport-associated (POTRA) domains. Functional data reveal that FHA binds to the POTRA 1 domain via its N-terminal domain and likely translocates the adhesin-repeated motifs in an extended hairpin conformation, with folding occurring at the cell surface. General features of the mechanism obtained here are likely to apply throughout the superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clantin, Bernard -- Delattre, Anne-Sophie -- Rucktooa, Prakash -- Saint, Nathalie -- Meli, Albano C -- Locht, Camille -- Jacob-Dubuisson, Francoise -- Villeret, Vincent -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):957-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UMR8161 CNRS, Institut de Biologie de Lille, Universite de Lille 1, Universite de Lille 2, 1 rue du Prof. Calmette, F-59021 Lille cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702945" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/genetics/*metabolism ; Bordetella pertussis/*chemistry/metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/chemistry/metabolism ; Membrane Transport Proteins/chemistry/metabolism ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; Virulence Factors, Bordetella/chemistry/*metabolism
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  • 24
    Publication Date: 2007-03-31
    Description: A marine ecosystem model seeded with many phytoplankton types, whose physiological traits were randomly assigned from ranges defined by field and laboratory data, generated an emergent community structure and biogeography consistent with observed global phytoplankton distributions. The modeled organisms included types analogous to the marine cyanobacterium Prochlorococcus. Their emergent global distributions and physiological properties simultaneously correspond to observations. This flexible representation of community structure can be used to explore relations between ecosystems, biogeochemical cycles, and climate change.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Follows, Michael J -- Dutkiewicz, Stephanie -- Grant, Scott -- Chisholm, Sallie W -- New York, N.Y. -- Science. 2007 Mar 30;315(5820):1843-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth, Atmospheric and Planetary Sciences, Massachusetts Institute of Technology, 54-1514 MIT, Cambridge, MA 02139, USA. mick@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395828" target="_blank"〉PubMed〈/a〉
    Keywords: Biomass ; Computer Simulation ; *Ecosystem ; Geography ; Light ; Mathematics ; Models, Biological ; Oceans and Seas ; Phytoplankton/growth & development/*physiology ; Prochlorococcus/growth & development/*physiology ; Seawater/*microbiology ; Temperature
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  • 25
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krajick, Kevin -- New York, N.Y. -- Science. 2007 Mar 16;315(5818):1527.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17363662" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arctic Regions ; Biodiversity ; *Cold Climate ; *Ecosystem ; Food Chain ; Ice Cover ; Invertebrates ; Plankton/growth & development ; Population Dynamics ; *Seawater ; Temperature
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  • 26
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Bruce D -- New York, N.Y. -- Science. 2007 Mar 30;315(5820):1797-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Archaeobiology Program, National Museum of Natural History, Smithsonian Institution, Washington, DC 20560, USA. smithb@si.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395815" target="_blank"〉PubMed〈/a〉
    Keywords: *Agriculture ; *Animal Husbandry ; Animals ; Animals, Domestic ; *Behavior ; Biological Evolution ; *Ecosystem ; *Environment ; Humans
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  • 27
    Publication Date: 2007-12-15
    Description: The assimilation of carbon dioxide (CO2) into organic material is quantitatively the most important biosynthetic process. We discovered that an autotrophic member of the archaeal order Sulfolobales, Metallosphaera sedula, fixed CO2 with acetyl-coenzyme A (acetyl-CoA)/propionyl-CoA carboxylase as the key carboxylating enzyme. In this system, one acetyl-CoA and two bicarbonate molecules were reductively converted via 3-hydroxypropionate to succinyl-CoA. This intermediate was reduced to 4-hydroxybutyrate and converted into two acetyl-CoA molecules via 4-hydroxybutyryl-CoA dehydratase. The key genes of this pathway were found not only in Metallosphaera but also in Sulfolobus, Archaeoglobus, and Cenarchaeum species. Moreover, the Global Ocean Sampling database contains half as many 4-hydroxybutyryl-CoA dehydratase sequences as compared with those found for another key photosynthetic CO2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase-oxygenase. This indicates the importance of this enzyme in global carbon cycling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Ivan A -- Kockelkorn, Daniel -- Buckel, Wolfgang -- Fuchs, Georg -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mikrobiologie, Fakultat Biologie, Universitat Freiburg, Schanzlestrasse 1, D-79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079405" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetyl-CoA Carboxylase/metabolism ; Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Anaerobiosis ; Archaea/genetics/metabolism ; Autotrophic Processes ; Bicarbonates/metabolism ; Carbon Dioxide/*metabolism ; Genes, Archaeal ; Hydro-Lyases/genetics/metabolism ; Hydroxybutyrates/*metabolism ; Kinetics ; Lactic Acid/*analogs & derivatives/metabolism ; Metabolic Networks and Pathways ; Molecular Sequence Data ; Oxidation-Reduction ; Photosynthesis ; Phylogeny ; Sulfolobaceae/genetics/*metabolism
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  • 28
    Publication Date: 2007-07-07
    Description: It is difficult to obtain fossil data from the 10% of Earth's terrestrial surface that is covered by thick glaciers and ice sheets, and hence, knowledge of the paleoenvironments of these regions has remained limited. We show that DNA and amino acids from buried organisms can be recovered from the basal sections of deep ice cores, enabling reconstructions of past flora and fauna. We show that high-altitude southern Greenland, currently lying below more than 2 kilometers of ice, was inhabited by a diverse array of conifer trees and insects within the past million years. The results provide direct evidence in support of a forested southern Greenland and suggest that many deep ice cores may contain genetic records of paleoenvironments in their basal sections.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2694912/" 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/PMC2694912/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willerslev, Eske -- Cappellini, Enrico -- Boomsma, Wouter -- Nielsen, Rasmus -- Hebsgaard, Martin B -- Brand, Tina B -- Hofreiter, Michael -- Bunce, Michael -- Poinar, Hendrik N -- Dahl-Jensen, Dorthe -- Johnsen, Sigfus -- Steffensen, Jorgen Peder -- Bennike, Ole -- Schwenninger, Jean-Luc -- Nathan, Roger -- Armitage, Simon -- de Hoog, Cees-Jan -- Alfimov, Vasily -- Christl, Marcus -- Beer, Juerg -- Muscheler, Raimund -- Barker, Joel -- Sharp, Martin -- Penkman, Kirsty E H -- Haile, James -- Taberlet, Pierre -- Gilbert, M Thomas P -- Casoli, Antonella -- Campani, Elisa -- Collins, Matthew J -- 076905/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):111-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Ancient Genetics, University of Copenhagen, Denmark. ewillerslev@bi.ku.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615355" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*analysis/history/isolation & purification ; Animals ; Bayes Theorem ; Climate ; DNA/*analysis/history/isolation & purification ; *Ecosystem ; Fossils ; Geography ; Greenland ; History, Ancient ; Ice Cover/*chemistry ; *Invertebrates/classification/genetics ; *Plants/classification/genetics ; Polymerase Chain Reaction ; Time ; *Trees
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  • 29
    Publication Date: 2007-11-10
    Description: Liu et al. (Reports, 23 March 2007, p. 1712) reported that the Arabidopsis thaliana gene GCR2 encodes a seven-transmembrane, G protein-coupled receptor for abscisic acid. We argue that GCR2 is not likely to be a transmembrane protein nor a G protein-coupled receptor. Instead, GCR2 is most likely a plant homolog of bacterial lanthionine synthetases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnston, Christopher A -- Temple, Brenda R -- Chen, Jin-Gui -- Gao, Yajun -- Moriyama, Etsuko N -- Jones, Alan M -- Siderovski, David P -- Willard, Francis S -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):914; author reply 914.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991845" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*metabolism ; Algorithms ; Amino Acid Sequence ; Arabidopsis/chemistry/*metabolism ; Arabidopsis Proteins/*chemistry/isolation & purification/*metabolism ; GTP-Binding Protein alpha Subunits/metabolism ; Hydro-Lyases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Plant Growth Regulators/*metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, G-Protein-Coupled/*chemistry/isolation & purification/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Sequence Alignment
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  • 30
    Publication Date: 2007-05-26
    Description: Telford et al. (Brevia, 19 May 2006, p. 1015) reported that freshwater diatoms exhibit regional-scale richness-pH relationships that depend substantially on regional habitat availability. On this basis, the authors argued that, despite their microscopic size, diatoms are not ubiquitously dispersed. Here, I describe my demonstration that their primary evidence against the ubiquitous dispersal hypothesis is spurious.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pither, Jason -- New York, N.Y. -- Science. 2007 May 25;316(5828):1124; author reply 1124.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, University of Arizona, BSW 310, 1041 East Lowell Street, Tucson, AZ 85721, USA. pitherj@email.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525319" target="_blank"〉PubMed〈/a〉
    Keywords: Biodiversity ; Diatoms/*physiology ; *Ecosystem ; *Environmental Microbiology ; Europe ; Fresh Water ; Hydrogen-Ion Concentration ; Models, Biological ; North America ; Water Microbiology
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Cheryl -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1716.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079379" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa/microbiology/physiology ; Aspergillus ; Bacteria ; *Ecosystem ; Greenhouse Effect
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  • 32
    Publication Date: 2007-06-26
    Description: The proliferation of icebergs from Antarctica over the past decade has raised questions about their potential impact on the surrounding pelagic ecosystem. Two free-drifting icebergs, 0.1 and 30.8 square kilometers in aerial surface area, and the surrounding waters were sampled in the northwest Weddell Sea during austral spring 2005. There was substantial enrichment of terrigenous material, and there were high concentrations of chlorophyll, krill, and seabirds surrounding each iceberg, extending out to a radial distance of approximately 3.7 kilometers. Extrapolating these results to all icebergs in the same size range, with the use of iceberg population estimates from satellite surveys, indicates that they similarly affect 39% of the surface ocean in this region. These results suggest that free-drifting icebergs can substantially affect the pelagic ecosystem of the Southern Ocean and can serve as areas of enhanced production and sequestration of organic carbon to the deep sea.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Kenneth L Jr -- Robison, Bruce H -- Helly, John J -- Kaufmann, Ronald S -- Ruhl, Henry A -- Shaw, Timothy J -- Twining, Benjamin S -- Vernet, Maria -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):478-82. Epub 2007 Jun 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monterey Bay Aquarium Research Institute (MBARI), 7700 Sandholdt Road, Moss Landing, CA 95039, USA. ksmith@mbari.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17588896" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antarctic Regions ; *Birds ; Chlorophyll/analysis ; *Ecosystem ; *Ice Cover ; Oceans and Seas ; *Phytoplankton/growth & development ; Sodium Chloride/analysis ; Trace Elements/analysis ; Water Movements ; *Zooplankton/growth & development
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Cheryl -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1715.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079378" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/genetics/growth & development/*physiology ; *Ecosystem ; Eukaryota/physiology ; Gene Expression ; Greenhouse Effect ; Hydrogen-Ion Concentration ; Larva/growth & development ; Reproduction ; Seawater ; Symbiosis
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  • 34
    Publication Date: 2007-09-29
    Description: The SAX-3/roundabout (Robo) receptor has SLT-1/Slit-dependent and -independent functions in guiding cell and axon migrations. We identified enhancer of ventral-axon guidance defects of unc-40 mutants (EVA-1) as a Caenorhabditis elegans transmembrane receptor for SLT-1. EVA-1 has two predicted galactose-binding ectodomains, acts cell-autonomously for SLT-1/Slit-dependent axon migration functions of SAX-3/Robo, binds to SLT-1 and SAX-3, colocalizes with SAX-3 on cells, and provides cell specificity to the activation of SAX-3 signaling by SLT-1. Double mutants of eva-1 or slt-1 with sax-3 mutations suggest that SAX-3 can (when slt-1 or eva-1 function is reduced) inhibit a parallel-acting guidance mechanism, which involves UNC-40/deleted in colorectal cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujisawa, Kazuko -- Wrana, Jeffrey L -- Culotti, Joseph G -- NS41397/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1934-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute of Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901337" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Axons/*physiology ; Caenorhabditis elegans/cytology/genetics/growth & development/*physiology ; Caenorhabditis elegans Proteins/*chemistry/genetics/*metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cell Movement ; Cloning, Molecular ; Humans ; Molecular Sequence Data ; Mutation ; Nerve Tissue Proteins/*metabolism ; Nervous System/growth & development/metabolism ; Neurons/physiology ; Protein Structure, Tertiary ; Receptors, Immunologic/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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  • 35
    Publication Date: 2007-05-26
    Description: Mutations affecting the BRCT domains of the breast cancer-associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs). The molecular structures at DSBs recognized by BRCA1 are presently unknown. We report the interaction of the BRCA1 BRCT domain with RAP80, a ubiquitin-binding protein. RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-gammaH2AX-dependent lysine(6)- and lysine(63)-linked ubiquitin polymers at DSBs. These events are required for cell cycle checkpoint and repair responses to ionizing radiation, implicating ubiquitin chain recognition and turnover in the BRCA1-mediated repair of DSBs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2706583/" 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/PMC2706583/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sobhian, Bijan -- Shao, Genze -- Lilli, Dana R -- Culhane, Aedin C -- Moreau, Lisa A -- Xia, Bing -- Livingston, David M -- Greenberg, Roger A -- K08 CA106597/CA/NCI NIH HHS/ -- K08 CA106597-01A2/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 May 25;316(5828):1198-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Department of Genetics and Department of Medicine, Harvard Medical School, 44 Binney Street, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525341" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; BRCA1 Protein/*metabolism ; Binding Sites ; Carrier Proteins/*metabolism ; Cell Line ; DNA/*metabolism ; *DNA Breaks, Double-Stranded ; DNA Repair/physiology ; HeLa Cells ; Humans ; Mice ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Nucleic Acid Conformation ; Protein Structure, Tertiary ; Tumor Suppressor Proteins/metabolism ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligases/metabolism
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  • 36
    Publication Date: 2007-10-27
    Description: The melanocortin 1 receptor (MC1R) regulates pigmentation in humans and other vertebrates. Variants of MC1R with reduced function are associated with pale skin color and red hair in humans of primarily European origin. We amplified and sequenced a fragment of the MC1R gene (mc1r) from two Neanderthal remains. Both specimens have a mutation that was not found in approximately 3700 modern humans analyzed. Functional analyses show that this variant reduces MC1R activity to a level that alters hair and/or skin pigmentation in humans. The impaired activity of this variant suggests that Neanderthals varied in pigmentation levels, potentially on the scale observed in modern humans. Our data suggest that inactive MC1R variants evolved independently in both modern humans and Neanderthals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lalueza-Fox, Carles -- Rompler, Holger -- Caramelli, David -- Staubert, Claudia -- Catalano, Giulio -- Hughes, David -- Rohland, Nadin -- Pilli, Elena -- Longo, Laura -- Condemi, Silvana -- de la Rasilla, Marco -- Fortea, Javier -- Rosas, Antonio -- Stoneking, Mark -- Schoneberg, Torsten -- Bertranpetit, Jaume -- Hofreiter, Michael -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1453-5. Epub 2007 Oct 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departament de Biologia Animal, Universitat de Barcelona, Spain. clalueza@ub.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962522" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Substitution ; Animals ; Biological Evolution ; Cell Line ; DNA/genetics ; *Fossils ; Hair Color/*genetics ; Hominidae/*genetics ; Humans ; Molecular Sequence Data ; *Mutation ; Polymerase Chain Reaction ; Receptor, Melanocortin, Type 1/chemistry/*genetics/metabolism ; Sequence Analysis, DNA ; Skin Pigmentation/*genetics
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  • 37
    Publication Date: 2007-11-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jorgensen, Christian -- Enberg, Katja -- Dunlop, Erin S -- Arlinghaus, Robert -- Boukal, David S -- Brander, Keith -- Ernande, Bruno -- Gardmark, Anna -- Johnston, Fiona -- Matsumura, Shuichi -- Pardoe, Heidi -- Raab, Kristina -- Silva, Alexandra -- Vainikka, Anssi -- Dieckmann, Ulf -- Heino, Mikko -- Rijnsdorp, Adriaan D -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1247-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Bergen, N-5020 Bergen. christian.jorgensen@bio.uib.no〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18033868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Ecosystem ; *Fisheries/methods ; *Fishes/physiology ; Population Dynamics
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  • 38
    Publication Date: 2007-01-06
    Description: A cause-and-effect understanding of climate influences on ecosystems requires evaluation of thermal limits of member species and of their ability to cope with changing temperatures. Laboratory data available for marine fish and invertebrates from various climatic regions led to the hypothesis that, as a unifying principle, a mismatch between the demand for oxygen and the capacity of oxygen supply to tissues is the first mechanism to restrict whole-animal tolerance to thermal extremes. We show in the eelpout, Zoarces viviparus, a bioindicator fish species for environmental monitoring from North and Baltic Seas (Helcom), that thermally limited oxygen delivery closely matches environmental temperatures beyond which growth performance and abundance decrease. Decrements in aerobic performance in warming seas will thus be the first process to cause extinction or relocation to cooler waters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Portner, Hans O -- Knust, Rainer -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):95-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Alfred Wegener Institute for Polar and Marine Research, Animal Ecophysiology, Postfach 12 01 61, 27515 Bremerhaven, Germany. hpoertner@awi-bremerhaven.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204649" target="_blank"〉PubMed〈/a〉
    Keywords: Acclimatization ; Aerobiosis ; Animals ; Blood Circulation ; Body Size ; *Climate ; *Ecosystem ; North Sea ; Oxygen/analysis/blood/*metabolism ; Oxygen Consumption ; Perciformes/growth & development/*physiology ; Population Dynamics ; Population Growth ; Seasons ; Seawater/chemistry ; Temperature
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  • 39
    Publication Date: 2007-10-20
    Description: A computational analysis of the nuclear genome of a red alga, Cyanidioschyzon merolae, identified 11 transfer RNA (tRNA) genes in which the 3' half of the tRNA lies upstream of the 5' half in the genome. We verified that these genes are expressed and produce mature tRNAs that are aminoacylated. Analysis of tRNA-processing intermediates for these genes indicates an unusual processing pathway in which the termini of the tRNA precursor are ligated, resulting in formation of a characteristic circular RNA intermediate that is then processed at the acceptor stem to generate the correct termini.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soma, Akiko -- Onodera, Akinori -- Sugahara, Junichi -- Kanai, Akio -- Yachie, Nozomu -- Tomita, Masaru -- Kawamura, Fujio -- Sekine, Yasuhiko -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):450-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Life Science, College of Science, Rikkyo (St. Paul's) University, Toshima, Tokyo 171-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947580" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Algal/chemistry/genetics ; *Genes ; Methionine-tRNA Ligase/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/chemistry/genetics/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Algal/*genetics/metabolism ; RNA, Transfer/*genetics/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Rhodophyta/*genetics/metabolism ; Transcription, Genetic
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  • 40
    Publication Date: 2007-10-13
    Description: Theory suggests it should be difficult for asexual organisms to adapt to a changing environment because genetic diversity can only arise from mutations accumulating within direct antecedents and not through sexual exchange. In an asexual microinvertebrate, the bdelloid rotifer, we have observed a mechanism by which such organisms could acquire the diversity needed for adaptation. Gene copies most likely representing former alleles have diverged in function so that the proteins they encode play complementary roles in survival of dry conditions. One protein prevents desiccation-sensitive enzymes from aggregating during drying, whereas its counterpart does not have this activity, but is able to associate with phospholipid bilayers and is potentially involved in maintenance of membrane integrity. The functional divergence of former alleles observed here suggests that adoption of asexual reproduction could itself be an evolutionary mechanism for the generation of diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pouchkina-Stantcheva, Natalia N -- McGee, Brian M -- Boschetti, Chiara -- Tolleter, Dimitri -- Chakrabortee, Sohini -- Popova, Antoaneta V -- Meersman, Filip -- Macherel, David -- Hincha, Dirk K -- Tunnacliffe, Alan -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932297" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; *Alleles ; Amino Acid Sequence ; Animals ; Biological Evolution ; Chromosomes/genetics ; DNA, Complementary ; Dehydration ; Gene Dosage ; *Genes, Helminth ; *Genetic Variation ; Helminth Proteins/chemistry/genetics/*physiology ; Lipid Bilayers ; Molecular Sequence Data ; Protein Structure, Secondary ; *Reproduction, Asexual ; Rotifera/*genetics/*physiology
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  • 41
    Publication Date: 2007-04-07
    Description: Information on responses of higher organisms to climate change is dominated by events in spring. Far less is known about autumnal events and virtually nothing about communities of microorganisms. We analyzed autumnal fruiting patterns of macrofungi over the past 56 years and found that average first fruiting date of 315 species is earlier, while last fruiting date is later. Fruiting of mycorrhizal species that associate with both deciduous and coniferous trees is delayed in deciduous, but not in coniferous, forests. Many species are now fruiting twice a year, indicating increased mycelial activity and possibly greater decay rates in ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gange, A C -- Gange, E G -- Sparks, T H -- Boddy, L -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, Royal Holloway, University of London, Egham, Surrey TW20 0EX, UK. a.gange@rhul.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412949" target="_blank"〉PubMed〈/a〉
    Keywords: Coniferophyta/microbiology ; *Ecosystem ; England ; Fruiting Bodies, Fungal/*growth & development ; Fungi/*growth & development ; Mycorrhizae/*growth & development ; Seasons ; Temperature ; Time Factors ; Trees/microbiology
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  • 42
    Publication Date: 2007-09-18
    Description: The forces that maintain genetic diversity among individuals and diversity among species are usually studied separately. Nevertheless, diversity at one of these levels may depend on the diversity at the other. We have combined observations of natural populations, quantitative genetics, and field experiments to show that genetic variation in the concentration of an allelopathic secondary compound in Brassica nigra is necessary for the coexistence of B. nigra and its competitor species. In addition, the diversity of competing species was required for the maintenance of genetic variation in the trait within B. nigra. Thus, conservation of species diversity may also necessitate maintenance of the processes that sustain the genetic diversity of each individual species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lankau, Richard A -- Strauss, Sharon Y -- New York, N.Y. -- Science. 2007 Sep 14;317(5844):1561-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Evolution and Ecology, University of California- Davis, One Shields Avenue, Davis, CA 95616, USA. ralankau@gmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17872447" target="_blank"〉PubMed〈/a〉
    Keywords: Amsinckia/growth & development ; Biodiversity ; *Ecosystem ; Genes, Plant ; *Genetic Variation ; Genotype ; Glucosinolates/genetics/*metabolism ; Malva/growth & development ; Mustard Plant/*genetics/growth & development/*metabolism ; Mycorrhizae/growth & development ; Selection, Genetic ; Soil Microbiology ; Sonchus/growth & development ; Species Specificity
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-02-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wuethrich, Bernice -- New York, N.Y. -- Science. 2007 Feb 23;315(5815):1070-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17322040" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Brazil ; *Conservation of Natural Resources/economics ; *Ecosystem ; Plant Development ; *Trees/growth & development
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-05-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Michaels, Anthony F -- New York, N.Y. -- Science. 2007 May 18;316(5827):992-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA. tony@usc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510353" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Ecosystem ; Geologic Sediments ; Oceanography ; Oceans and Seas ; Oxygen/analysis ; Photosynthesis ; Plankton/*growth & development/physiology ; *Seawater/chemistry ; Silicon Dioxide/analysis ; *Water Movements
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  • 45
    Publication Date: 2007-06-30
    Description: As a step toward propagation of synthetic genomes, we completely replaced the genome of a bacterial cell with one from another species by transplanting a whole genome as naked DNA. Intact genomic DNA from Mycoplasma mycoides large colony (LC), virtually free of protein, was transplanted into Mycoplasma capricolum cells by polyethylene glycol-mediated transformation. Cells selected for tetracycline resistance, carried by the M. mycoides LC chromosome, contain the complete donor genome and are free of detectable recipient genomic sequences. These cells that result from genome transplantation are phenotypically identical to the M. mycoides LC donor strain as judged by several criteria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lartigue, Carole -- Glass, John I -- Alperovich, Nina -- Pieper, Rembert -- Parmar, Prashanth P -- Hutchison, Clyde A 3rd -- Smith, Hamilton O -- Venter, J Craig -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):632-8. Epub 2007 Jun 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉J. Craig Venter Institute, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600181" target="_blank"〉PubMed〈/a〉
    Keywords: Acetate Kinase/chemistry/genetics ; Amino Acid Sequence ; DNA, Bacterial/*genetics/isolation & purification ; *Genome, Bacterial ; Genotype ; Molecular Sequence Data ; Mycoplasma/chemistry/*genetics ; Mycoplasma mycoides/chemistry/*genetics ; Phenotype ; Polyethylene Glycols ; Proteome/analysis ; Recombination, Genetic ; Sequence Analysis, DNA ; *Transformation, Bacterial
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  • 46
    Publication Date: 2007-07-14
    Description: Many human cancers involve up-regulation of the phosphoinositide 3-kinase PI3Kalpha, with oncogenic mutations identified in both the p110alpha catalytic and the p85alpha regulatory subunits. We used crystallographic and biochemical approaches to gain insight into activating mutations in two noncatalytic p110alpha domains-the adaptor-binding and the helical domains. A structure of the adaptor-binding domain of p110alpha in a complex with the p85alpha inter-Src homology 2 (inter-SH2) domain shows that oncogenic mutations in the adaptor-binding domain are not at the inter-SH2 interface but in a polar surface patch that is a plausible docking site for other domains in the holo p110/p85 complex. We also examined helical domain mutations and found that the Glu545 to Lys545 (E545K) oncogenic mutant disrupts an inhibitory charge-charge interaction with the p85 N-terminal SH2 domain. These studies extend our understanding of the architecture of PI3Ks and provide insight into how two classes of mutations that cause a gain in function can lead to cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miled, Nabil -- Yan, Ying -- Hon, Wai-Ching -- Perisic, Olga -- Zvelebil, Marketa -- Inbar, Yuval -- Schneidman-Duhovny, Dina -- Wolfson, Haim J -- Backer, Jonathan M -- Williams, Roger L -- GM55692/GM/NIGMS NIH HHS/ -- MC_U105184308/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Jul 13;317(5835):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17626883" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; *Catalytic Domain ; Cattle ; Cell Line ; Cell Transformation, Neoplastic ; Crystallography, X-Ray ; Dimerization ; Humans ; Models, Molecular ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Phosphatidylinositol 3-Kinases/antagonists & ; inhibitors/chemistry/*genetics/*metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; src Homology Domains
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  • 47
    Publication Date: 2007-03-31
    Description: Telomerase is a ribonucleoprotein enzyme complex that adds 5'-TTAGGG-3' repeats onto the ends of human chromosomes, providing a telomere maintenance mechanism for approximately 90% of human cancers. We have purified human telomerase approximately 10(8)-fold, with the final elution dependent on the enzyme's ability to catalyze nucleotide addition onto a DNA oligonucleotide of telomeric sequence, thereby providing specificity for catalytically active telomerase. Mass spectrometric sequencing of the protein components and molecular size determination indicated an enzyme composition of two molecules each of telomerase reverse transcriptase, telomerase RNA, and dyskerin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Scott B -- Graham, Mark E -- Lovrecz, George O -- Bache, Nicolai -- Robinson, Phillip J -- Reddel, Roger R -- New York, N.Y. -- Science. 2007 Mar 30;315(5820):1850-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Unit, Children's Medical Research Institute, 214 Hawkesbury Road, Westmead NSW 2145, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395830" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Cycle Proteins/*chemistry/isolation & purification ; Cell Line ; Cell Line, Tumor ; Centrifugation, Density Gradient ; Humans ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes/chemistry ; Nuclear Proteins/*chemistry/isolation & purification ; RNA/*chemistry/isolation & purification ; Tandem Mass Spectrometry ; Telomerase/*chemistry/isolation & purification/metabolism
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  • 48
    Publication Date: 2007-04-07
    Description: Freeman and Byers (Reports, 11 August 2006, p. 831) presented evidence for the rapid evolution of antipredator defenses in the mussel Mytilus edulis. However, their analysis is confounded by three issues. Samples from some sites are likely to have included a second species, M. trossulus; their manipulation of chemical cues does not preclude other interpretations; and they failed to establish an adaptive significance to shell thickening.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rawson, Paul D -- Yund, Philip O -- Lindsay, Sara M -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):53; author reply 53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Marine Sciences, 5751 Murray Hall, University of Maine, Orono, ME 04469-5751, USA. prawson@maine.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412940" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Atlantic Ocean ; Biological Evolution ; *Brachyura ; Cues ; *Ecosystem ; Mytilus/anatomy & histology/classification/*physiology ; Mytilus edulis/anatomy & histology/*physiology ; New England ; *Predatory Behavior ; *Selection, Genetic ; Species Specificity
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Convey, Peter -- Stevens, Mark I -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1877-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉British Antarctic Survey, Natural Environment Research Council, High Cross, Madingley Road, Cambridge CB3 0ET, UK. p.convey@bas.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901323" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antarctic Regions ; *Biodiversity ; *Ecosystem ; *Eukaryota ; Fossils ; *Ice Cover ; *Invertebrates ; Lichens ; Time
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  • 50
    Publication Date: 2007-08-11
    Description: Tricyclic antidepressants exert their pharmacological effect-inhibiting the reuptake of serotonin, norepinephrine, and dopamine-by directly blocking neurotransmitter transporters (SERT, NET, and DAT, respectively) in the presynaptic membrane. The drug-binding site and the mechanism of this inhibition are poorly understood. We determined the crystal structure at 2.9 angstroms of the bacterial leucine transporter (LeuT), a homolog of SERT, NET, and DAT, in complex with leucine and the antidepressant desipramine. Desipramine binds at the inner end of the extracellular cavity of the transporter and is held in place by a hairpin loop and by a salt bridge. This binding site is separated from the leucine-binding site by the extracellular gate of the transporter. By directly locking the gate, desipramine prevents conformational changes and blocks substrate transport. Mutagenesis experiments on human SERT and DAT indicate that both the desipramine-binding site and its inhibition mechanism are probably conserved in the human neurotransmitter transporters.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711652/" 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/PMC3711652/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Zheng -- Zhen, Juan -- Karpowich, Nathan K -- Goetz, Regina M -- Law, Christopher J -- Reith, Maarten E A -- Wang, Da-Neng -- DA013261/DA/NIDA NIH HHS/ -- DA019676/DA/NIDA NIH HHS/ -- GM075026/GM/NIGMS NIH HHS/ -- GM075936/GM/NIGMS NIH HHS/ -- R01 DA013261/DA/NIDA NIH HHS/ -- R01 DA019676/DA/NIDA NIH HHS/ -- R01 DK053973/DK/NIDDK NIH HHS/ -- R21 DK060841/DK/NIDDK NIH HHS/ -- R21 GM075936/GM/NIGMS NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54 GM095315/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1390-3. Epub 2007 Aug 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17690258" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antidepressive Agents, Tricyclic/chemistry/*metabolism ; Bacterial Proteins/chemistry/*metabolism ; Binding Sites ; Caenorhabditis elegans Proteins/chemistry/metabolism ; Cell Line ; Conserved Sequence ; Crystallography, X-Ray ; Desipramine/chemistry/*metabolism ; Dopamine/chemistry/metabolism ; Dopamine Uptake Inhibitors/chemistry/metabolism ; Drosophila Proteins/chemistry/metabolism ; Humans ; Leucine/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Neurotransmitter Uptake Inhibitors/chemistry/*metabolism ; Norepinephrine/chemistry/metabolism ; Norepinephrine Plasma Membrane Transport Proteins/antagonists & ; inhibitors/chemistry/metabolism ; Plasma Membrane Neurotransmitter Transport Proteins/chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Sequence Homology, Amino Acid ; Serotonin/chemistry/metabolism ; Serotonin Uptake Inhibitors/chemistry/metabolism
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  • 51
    Publication Date: 2007-09-29
    Description: Although the application of sequencing-by-synthesis techniques to DNA extracted from bones has revolutionized the study of ancient DNA, it has been plagued by large fractions of contaminating environmental DNA. The genetic analyses of hair shafts could be a solution: We present 10 previously unexamined Siberian mammoth (Mammuthus primigenius) mitochondrial genomes, sequenced with up to 48-fold coverage. The observed levels of damage-derived sequencing errors were lower than those observed in previously published frozen bone samples, even though one of the specimens was 〉50,000 14C years old and another had been stored for 200 years at room temperature. The method therefore sets the stage for molecular-genetic analysis of museum collections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilbert, M Thomas P -- Tomsho, Lynn P -- Rendulic, Snjezana -- Packard, Michael -- Drautz, Daniela I -- Sher, Andrei -- Tikhonov, Alexei -- Dalen, Love -- Kuznetsova, Tatyana -- Kosintsev, Pavel -- Campos, Paula F -- Higham, Thomas -- Collins, Matthew J -- Wilson, Andrew S -- Shidlovskiy, Fyodor -- Buigues, Bernard -- Ericson, Per G P -- Germonpre, Mietje -- Gotherstrom, Anders -- Iacumin, Paola -- Nikolaev, Vladimir -- Nowak-Kemp, Malgosia -- Willerslev, Eske -- Knight, James R -- Irzyk, Gerard P -- Perbost, Clotilde S -- Fredrikson, Karin M -- Harkins, Timothy T -- Sheridan, Sharon -- Miller, Webb -- Schuster, Stephan C -- HG002238/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1927-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Ancient Genetics, University of Copenhagen, Universitetsparken 15, DK-2100 Copenhagen, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901335" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone and Bones/chemistry ; DNA Damage ; DNA, Mitochondrial/chemistry/genetics/*history ; Elephants/*genetics ; Genes, Mitochondrial ; *Genome ; *Hair/chemistry/ultrastructure ; History, Ancient ; Mitochondria/*genetics ; Molecular Sequence Data ; Preservation, Biological ; *Sequence Analysis, DNA ; Siberia ; Temperature
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  • 52
    Publication Date: 2007-12-08
    Description: Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-beta domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, Hae Joo -- Coulibaly, Fasseli -- Clow, Fiona -- Proft, Thomas -- Baker, Edward N -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1625-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland 1010, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063798" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Asparagine/chemistry ; Chemistry, Physical ; Crystallography, X-Ray ; Fimbriae Proteins/*chemistry ; Fimbriae, Bacterial/*chemistry/ultrastructure ; Hydrogen Bonding ; Lysine/chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Streptococcus pyogenes/*chemistry/metabolism/*ultrastructure
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reitz, Stuart R -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1733-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Agricultural Research Service, U.S. Department of Agriculture, Tallahassee, FL 32308, USA. stuart.reitz@ars.usda.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079389" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Australia ; China ; *Ecosystem ; Female ; Hemiptera/classification/genetics/*physiology ; Male ; Population Dynamics ; Reproduction ; *Sexual Behavior, Animal
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  • 54
    Publication Date: 2007-01-27
    Description: Vitamin A has diverse biological functions. It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. We identified in bovine retinal pigment epithelium cells STRA6, a multitransmembrane domain protein, as a specific membrane receptor for RBP. STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. It is widely expressed in embryonic development and in adult organ systems. The RBP receptor represents a major physiological mediator of cellular vitamin A uptake.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, Riki -- Yu, Jiamei -- Honda, Jane -- Hu, Jane -- Whitelegge, Julian -- Ping, Peipei -- Wiita, Patrick -- Bok, Dean -- Sun, Hui -- 5T32EY07026/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):820-5. Epub 2007 Jan 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255476" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Blood-Retinal Barrier ; COS Cells ; Cattle ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cercopithecus aethiops ; Embryonic Development ; Endocytosis ; Humans ; Molecular Sequence Data ; Mutation, Missense ; Pigment Epithelium of Eye/*metabolism ; Placenta/metabolism ; Receptors, Cell Surface/*metabolism ; Retinal Vessels/metabolism ; Retinol-Binding Proteins/*metabolism ; Spleen/metabolism ; Transfection ; Vitamin A/*metabolism
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gillson, Lindsey -- Hoffman, M Timm -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):53-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Plant Conservation, Botany Department, University of Cape Town, Rondebosch 7701, South Africa. lindsey.gillson@uct.ac.za〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204634" target="_blank"〉PubMed〈/a〉
    Keywords: *Agriculture ; Animals ; *Animals, Domestic ; Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; Environment ; *Plants ; Policy Making ; Population Density ; Rain ; Systems Theory
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  • 56
    Publication Date: 2007-10-27
    Description: Pathogenicity of many Gram-negative bacteria relies on the injection of effector proteins by type III secretion into eukaryotic cells, where they modulate host signaling pathways to the pathogen's benefit. One such effector protein injected by Xanthomonas into plants is AvrBs3, which localizes to the plant cell nucleus and causes hypertrophy of plant mesophyll cells. We show that AvrBs3 induces the expression of a master regulator of cell size, upa20, which encodes a transcription factor containing a basic helix-loop-helix domain. AvrBs3 binds to a conserved element in the upa20 promoter via its central repeat region and induces gene expression through its activation domain. Thus, AvrBs3 and likely other members of this family provoke developmental reprogramming of host cells by mimicking eukaryotic transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kay, Sabine -- Hahn, Simone -- Marois, Eric -- Hause, Gerd -- Bonas, Ulla -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):648-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biology, Department of Genetics, Martin-Luther-University Halle-Wittenberg, Weinbergweg 10, D-06120 Halle (Saale), Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962565" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/*physiology ; Basic Helix-Loop-Helix Transcription Factors/chemistry/genetics/*physiology ; Capsicum/cytology/*genetics/*microbiology ; Cell Enlargement ; Cell Size ; Chromatin Immunoprecipitation ; Gene Expression Regulation, Plant ; Gene Silencing ; Molecular Sequence Data ; Plant Leaves/cytology/genetics/metabolism ; Plant Proteins/chemistry/genetics/metabolism/*physiology ; Promoter Regions, Genetic ; Tobacco/genetics ; Transcription, Genetic ; Xanthomonas campestris/genetics/*metabolism/pathogenicity
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  • 57
    Publication Date: 2007-04-14
    Description: In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leibundgut, Marc -- Jenni, Simon -- Frick, Christian -- Ban, Nenad -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):288-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, 8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431182" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Carrier Protein/*chemistry/metabolism ; Acyltransferases/metabolism ; Amino Acid Sequence ; Catalytic Domain ; Crystallography, X-Ray ; Fatty Acid Synthases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/*chemistry/metabolism
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  • 58
    Publication Date: 2007-06-02
    Description: Leguminous plants (such as peas and soybeans) and rhizobial soil bacteria are symbiotic partners that communicate through molecular signaling pathways, resulting in the formation of nodules on legume roots and occasionally stems that house nitrogen-fixing bacteria. Nodule formation has been assumed to be exclusively initiated by the binding of bacterial, host-specific lipochito-oligosaccharidic Nod factors, encoded by the nodABC genes, to kinase-like receptors of the plant. Here we show by complete genome sequencing of two symbiotic, photosynthetic, Bradyrhizobium strains, BTAi1 and ORS278, that canonical nodABC genes and typical lipochito-oligosaccharidic Nod factors are not required for symbiosis in some legumes. Mutational analyses indicated that these unique rhizobia use an alternative pathway to initiate symbioses, where a purine derivative may play a key role in triggering nodule formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giraud, Eric -- Moulin, Lionel -- Vallenet, David -- Barbe, Valerie -- Cytryn, Eddie -- Avarre, Jean-Christophe -- Jaubert, Marianne -- Simon, Damien -- Cartieaux, Fabienne -- Prin, Yves -- Bena, Gilles -- Hannibal, Laure -- Fardoux, Joel -- Kojadinovic, Mila -- Vuillet, Laurie -- Lajus, Aurelie -- Cruveiller, Stephane -- Rouy, Zoe -- Mangenot, Sophie -- Segurens, Beatrice -- Dossat, Carole -- Franck, William L -- Chang, Woo-Suk -- Saunders, Elizabeth -- Bruce, David -- Richardson, Paul -- Normand, Philippe -- Dreyfus, Bernard -- Pignol, David -- Stacey, Gary -- Emerich, David -- Vermeglio, Andre -- Medigue, Claudine -- Sadowsky, Michael -- New York, N.Y. -- Science. 2007 Jun 1;316(5829):1307-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Recherche pour le Developpement, Centre de Cooperation International en Recherche Agronomique pour le Developpement, Institut National de la Recherche Agronomique, Universite Montpellier 2, France. giraud@mpl.ird.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540897" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/genetics/metabolism ; Amidohydrolases/genetics/metabolism ; Bacterial Proteins/genetics/metabolism ; Bradyrhizobium/*genetics/growth & development/*physiology ; Cytokinins/metabolism ; Fabaceae/*microbiology ; Genes, Bacterial ; Genome, Bacterial ; Genomics ; Lipopolysaccharides/metabolism ; Molecular Sequence Data ; Mutation ; N-Acetylglucosaminyltransferases/genetics/metabolism ; Photosynthesis ; Plant Roots/microbiology ; Plant Stems/*microbiology ; Purines/biosynthesis ; Root Nodules, Plant/microbiology/*physiology ; Signal Transduction ; *Symbiosis
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  • 59
    Publication Date: 2007-05-19
    Description: The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1).〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3682417/" 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/PMC3682417/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zoltowski, Brian D -- Schwerdtfeger, Carsten -- Widom, Joanne -- Loros, Jennifer J -- Bilwes, Alexandrine M -- Dunlap, Jay C -- Crane, Brian R -- GM079879-01/GM/NIGMS NIH HHS/ -- MH44651/MH/NIMH NIH HHS/ -- P01 GM068087/GM/NIGMS NIH HHS/ -- R01 GM034985/GM/NIGMS NIH HHS/ -- R01 GM034985-24/GM/NIGMS NIH HHS/ -- R37GM34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 18;316(5827):1054-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510367" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites ; Crystallography, X-Ray ; Darkness ; Dimerization ; Flavin-Adenine Dinucleotide/chemistry ; Fungal Proteins/*chemistry/genetics/metabolism ; Light ; Molecular Sequence Data ; Mutagenesis ; Neurospora crassa/*chemistry ; Protein Conformation ; Protein Structure, Tertiary
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  • 60
    Publication Date: 2007-11-10
    Description: Production of type I interferon (IFN-I) is a critical host defense triggered by pattern-recognition receptors (PRRs) of the innate immune system. Deubiquitinating enzyme A (DUBA), an ovarian tumor domain-containing deubiquitinating enzyme, was discovered in a small interfering RNA-based screen as a regulator of IFN-I production. Reduction of DUBA augmented the PRR-induced IFN-I response, whereas ectopic expression of DUBA had the converse effect. DUBA bound tumor necrosis factor receptor-associated factor 3 (TRAF3), an adaptor protein essential for the IFN-I response. TRAF3 is an E3 ubiquitin ligase that preferentially assembled lysine-63-linked polyubiquitin chains. DUBA selectively cleaved the lysine-63-linked polyubiquitin chains on TRAF3, resulting in its dissociation from the downstream signaling complex containing TANK-binding kinase 1. A discrete ubiquitin interaction motif within DUBA was required for efficient deubiquitination of TRAF3 and optimal suppression of IFN-I. Our data identify DUBA as a negative regulator of innate immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kayagaki, Nobuhiko -- Phung, Qui -- Chan, Salina -- Chaudhari, Ruchir -- Quan, Casey -- O'Rourke, Karen M -- Eby, Michael -- Pietras, Eric -- Cheng, Genhong -- Bazan, J Fernando -- Zhang, Zemin -- Arnott, David -- Dixit, Vishva M -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1628-32. Epub 2007 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry, Genentech, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991829" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Line ; Endopeptidases/*metabolism ; Humans ; Interferon Type I/*biosynthesis/genetics ; Interferon-alpha/genetics ; Molecular Sequence Data ; NF-kappa B/metabolism ; Protein Structure, Tertiary ; RNA, Small Interfering ; Signal Transduction ; TNF Receptor-Associated Factor 3/metabolism ; Toll-Like Receptor 3/metabolism ; Ubiquitin/metabolism ; Ubiquitination
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  • 61
    Publication Date: 2007-01-06
    Description: The late Paleozoic deglaciation is the vegetated Earth's only recorded icehouse-to-greenhouse transition, yet the climate dynamics remain enigmatic. By using the stable isotopic compositions of soil-formed minerals, fossil-plant matter, and shallow-water brachiopods, we estimated atmospheric partial pressure of carbon dioxide (pCO2) and tropical marine surface temperatures during this climate transition. Comparison to southern Gondwanan glacial records documents covariance between inferred shifts in pCO2, temperature, and ice volume consistent with greenhouse gas forcing of climate. Major restructuring of paleotropical flora in western Euramerica occurred in step with climate and pCO2 shifts, illustrating the biotic impact associated with past CO2-forced turnover to a permanent ice-free world.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montanez, Isabel P -- Tabor, Neil J -- Niemeier, Deb -- Dimichele, William A -- Frank, Tracy D -- Fielding, Christopher R -- Isbell, John L -- Birgenheier, Lauren P -- Rygel, Michael C -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):87-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology, University of California, Davis, CA 95616, USA. montanez@geology.ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204648" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atmosphere ; Biodiversity ; Calcium Carbonate/analysis ; *Carbon Dioxide ; Carbon Isotopes ; *Climate ; *Ecosystem ; Fossils ; Greenhouse Effect ; Ice Cover ; Invertebrates/chemistry ; *Plants ; Seasons ; Soil/analysis ; Temperature ; Time
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  • 62
    Publication Date: 2007-05-15
    Description: In this millennium, global drylands face a myriad of problems that present tough research, management, and policy challenges. Recent advances in dryland development, however, together with the integrative approaches of global change and sustainability science, suggest that concerns about land degradation, poverty, safeguarding biodiversity, and protecting the culture of 2.5 billion people can be confronted with renewed optimism. We review recent lessons about the functioning of dryland ecosystems and the livelihood systems of their human residents and introduce a new synthetic framework, the Drylands Development Paradigm (DDP). The DDP, supported by a growing and well-documented set of tools for policy and management action, helps navigate the inherent complexity of desertification and dryland development, identifying and synthesizing those factors important to research, management, and policy communities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reynolds, James F -- Smith, D Mark Stafford -- Lambin, Eric F -- Turner, B L 2nd -- Mortimore, Michael -- Batterbury, Simon P J -- Downing, Thomas E -- Dowlatabadi, Hadi -- Fernandez, Roberto J -- Herrick, Jeffrey E -- Huber-Sannwald, Elisabeth -- Jiang, Hong -- Leemans, Rik -- Lynam, Tim -- Maestre, Fernando T -- Ayarza, Miguel -- Walker, Brian -- New York, N.Y. -- Science. 2007 May 11;316(5826):847-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nicholas School of the Environment and Earth Sciences and Department of Biology, Post Office Box 90328, Duke University, Durham, NC 27708, USA. james.f.reynolds@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17495163" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Desert Climate ; Ecology ; *Ecosystem ; *Environment ; Humans ; Public Policy ; Soil
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  • 63
    Publication Date: 2007-04-28
    Description: By screening N-ethyl-N-nitrosourea-mutagenized animals for alterations in rhythms of wheel-running activity, we identified a mouse mutation, after hours (Afh). The mutation, a Cys(358)Ser substitution in Fbxl3, an F-box protein with leucine-rich repeats, results in long free-running rhythms of about 27 hours in homozygotes. Circadian transcriptional and translational oscillations are attenuated in Afh mice. The Afh allele significantly affected Per2 expression and delayed the rate of Cry protein degradation in Per2::Luciferase tissue slices. Our in vivo and in vitro studies reveal a central role for Fbxl3 in mammalian circadian timekeeping.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Godinho, Sofia I H -- Maywood, Elizabeth S -- Shaw, Linda -- Tucci, Valter -- Barnard, Alun R -- Busino, Luca -- Pagano, Michele -- Kendall, Rachel -- Quwailid, Mohamed M -- Romero, M Rosario -- O'neill, John -- Chesham, Johanna E -- Brooker, Debra -- Lalanne, Zuzanna -- Hastings, Michael H -- Nolan, Patrick M -- MC_U105170643/Medical Research Council/United Kingdom -- MC_U142684172/Medical Research Council/United Kingdom -- MC_U142684173/Medical Research Council/United Kingdom -- MC_U142684175/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 May 11;316(5826):897-900. Epub 2007 Apr 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) Mammalian Genetics Unit, Harwell, Oxfordshire OX11 0RD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17463252" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Basic Helix-Loop-Helix Transcription Factors/genetics/metabolism ; CLOCK Proteins ; COS Cells ; Cell Cycle Proteins/genetics/metabolism ; Cercopithecus aethiops ; *Circadian Rhythm/genetics ; Crosses, Genetic ; Cryptochromes ; F-Box Proteins/*genetics/*physiology ; Female ; Flavoproteins/genetics/metabolism ; Gene Expression Regulation ; Liver/metabolism ; Lung/metabolism ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Molecular Sequence Data ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; *Point Mutation ; Suprachiasmatic Nucleus/metabolism ; Trans-Activators/genetics/metabolism ; Transcription Factors/genetics/metabolism ; Transcription, Genetic
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  • 64
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-04-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerdau, Manuel -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):212-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Blandy Experimental Farm, Department of Environmental Sciences, University of Virginia, Charlottesville, VA 22904, USA. mlerdau@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431162" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere/*chemistry ; Butadienes/*chemistry/metabolism ; *Ecosystem ; Feedback, Physiological ; *Fossil Fuels ; Hemiterpenes/*chemistry/metabolism ; Humans ; Nitrogen Oxides/chemistry ; Oxidative Stress ; Ozone/chemistry ; Pentanes/*chemistry/metabolism ; Plants/*metabolism ; Trees
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  • 65
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leshner, Alan I -- New York, N.Y. -- Science. 2007 Mar 16;315(5818):1465.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17363632" target="_blank"〉PubMed〈/a〉
    Keywords: Antarctic Regions ; Arctic Regions ; *Cold Climate ; *Ecosystem ; Geological Phenomena ; Geology ; Ice Cover ; Interdisciplinary Communication ; International Cooperation ; *Science
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  • 66
    Publication Date: 2007-02-17
    Description: Chemoautotrophic endosymbionts are the metabolic cornerstone of hydrothermal vent communities, providing invertebrate hosts with nearly all of their nutrition. The Calyptogena magnifica (Bivalvia: Vesicomyidae) symbiont, Candidatus Ruthia magnifica, is the first intracellular sulfur-oxidizing endosymbiont to have its genome sequenced, revealing a suite of metabolic capabilities. The genome encodes major chemoautotrophic pathways as well as pathways for biosynthesis of vitamins, cofactors, and all 20 amino acids required by the clam.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newton, I L G -- Woyke, T -- Auchtung, T A -- Dilly, G F -- Dutton, R J -- Fisher, M C -- Fontanez, K M -- Lau, E -- Stewart, F J -- Richardson, P M -- Barry, K W -- Saunders, E -- Detter, J C -- Wu, D -- Eisen, J A -- Cavanaugh, C M -- New York, N.Y. -- Science. 2007 Feb 16;315(5814):998-1000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harvard University, 16 Divinity Avenue, Biolabs 4080, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17303757" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bivalvia/*microbiology ; Carbon/metabolism ; Chemoautotrophic Growth ; Gammaproteobacteria/*genetics/isolation & purification/metabolism/ultrastructure ; *Genome, Bacterial ; Molecular Sequence Data ; Photosynthesis ; *Symbiosis
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  • 67
    Publication Date: 2007-03-10
    Description: Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovering, Andrew L -- de Castro, Liza H -- Lim, Daniel -- Strynadka, Natalie C J -- New York, N.Y. -- Science. 2007 Mar 9;315(5817):1402-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, and Center for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17347437" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Aminoacyltransferases/*chemistry/metabolism ; Anti-Bacterial Agents/chemistry/metabolism ; Apoenzymes/chemistry ; Binding Sites ; Carbohydrate Conformation ; Carbohydrate Sequence ; Catalytic Domain ; Cell Wall/*metabolism ; Crystallography, X-Ray ; Enzyme Inhibitors/chemistry/metabolism/pharmacology ; Glycosylation ; Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/chemistry/metabolism ; Oligosaccharides/chemistry/metabolism/pharmacology ; Penicillin-Binding Proteins/*chemistry/metabolism ; Peptidoglycan/*biosynthesis ; Peptidoglycan Glycosyltransferase/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Staphylococcus aureus/*enzymology/metabolism
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  • 68
    Publication Date: 2007-02-03
    Description: Acetylation of histone H3 lysine 56 (H3-K56) occurs in S phase, and cells lacking H3-K56 acetylation are sensitive to DNA-damaging agents. However, the histone acetyltransferase (HAT) that catalyzes global H3-K56 acetylation has not been found. Here we show that regulation of Ty1 transposition gene product 109 (Rtt109) is an H3-K56 HAT. Cells lacking Rtt109 or expressing rtt109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit increased sensitivity toward genotoxic agents, as well as elevated levels of spontaneous chromosome breaks. Thus, Rtt109, which shares no sequence homology with any other known HATs, is a unique HAT that acetylates H3-K56.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, Junhong -- Zhou, Hui -- Horazdovsky, Bruce -- Zhang, Kangling -- Xu, Rui-Ming -- Zhang, Zhiguo -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):653-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272723" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Camptothecin/pharmacology ; Catalytic Domain ; Chromosome Breakage ; DNA Damage ; *DNA Replication ; Histone Acetyltransferases/chemistry/genetics/*metabolism ; Histones/*metabolism ; Hydroxyurea/pharmacology ; Lysine/*metabolism ; Methyl Methanesulfonate/pharmacology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutagens/pharmacology ; Mutation ; Recombinant Proteins/metabolism ; S Phase ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Sequence Homology, Amino Acid
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  • 69
    Publication Date: 2007-04-28
    Description: The oceanic biological pump drives sequestration of carbon dioxide in the deep sea via sinking particles. Rapid biological consumption and remineralization of carbon in the "twilight zone" (depths between the euphotic zone and 1000 meters) reduce the efficiency of sequestration. By using neutrally buoyant sediment traps to sample this chronically understudied realm, we measured a transfer efficiency of sinking particulate organic carbon between 150 and 500 meters of 20 and 50% at two contrasting sites. This large variability in transfer efficiency is poorly represented in biogeochemical models. If applied globally, this is equivalent to a difference in carbon sequestration of more than 3 petagrams of carbon per year.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buesseler, Ken O -- Lamborg, Carl H -- Boyd, Philip W -- Lam, Phoebe J -- Trull, Thomas W -- Bidigare, Robert R -- Bishop, James K B -- Casciotti, Karen L -- Dehairs, Frank -- Elskens, Marc -- Honda, Makio -- Karl, David M -- Siegel, David A -- Silver, Mary W -- Steinberg, Deborah K -- Valdes, Jim -- Van Mooy, Benjamin -- Wilson, Stephanie -- New York, N.Y. -- Science. 2007 Apr 27;316(5824):567-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Marine Chemistry and Geochemistry, Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA. kbuesseler@whoi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17463282" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carbon/metabolism ; Carbon Dioxide ; Copepoda/physiology ; *Ecosystem ; Food Chain ; Geologic Sediments/chemistry ; Hydrogen-Ion Concentration ; Pacific Ocean ; Phytoplankton/physiology ; *Seawater/chemistry ; Zooplankton/physiology
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-25
    Description: YiiP is a membrane transporter that catalyzes Zn2+/H+ exchange across the inner membrane of Escherichia coli. Mammalian homologs of YiiP play critical roles in zinc homeostasis and cell signaling. Here, we report the x-ray structure of YiiP in complex with zinc at 3.8 angstrom resolution. YiiP is a homodimer held together in a parallel orientation through four Zn2+ ions at the interface of the cytoplasmic domains, whereas the two transmembrane domains swing out to yield a Y-shaped structure. In each protomer, the cytoplasmic domain adopts a metallochaperone-like protein fold; the transmembrane domain features a bundle of six transmembrane helices and a tetrahedral Zn2+ binding site located in a cavity that is open to both the membrane outer leaflet and the periplasm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Min -- Fu, Dax -- R01 GM065137/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 21;317(5845):1746-8. Epub 2007 Aug 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brookhaven National Laboratory, Upton, NY 11973, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17717154" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Escherichia coli/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/metabolism ; Membrane Transport Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Sequence Alignment ; Zinc/*chemistry/metabolism
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  • 71
    Publication Date: 2007-03-10
    Description: Examples of sympatric speciation in nature are rare and hotly debated. We describe the parallel speciation of finches on two small islands in the Tristan da Cunha archipelago in the South Atlantic Ocean. Nesospiza buntings are a classic example of a simple adaptive radiation, with two species on each island: an abundant small-billed dietary generalist and a scarce large-billed specialist. Their morphological diversity closely matches the available spectrum of seed sizes, and genetic evidence suggests that they evolved independently on each island. Speciation is complete on the smaller island, where there is a single habitat with strongly bimodal seed size abundance, but is incomplete on the larger island, where a greater diversity of habitats has resulted in three lineages. Our study suggests that the buntings have undergone parallel ecological speciation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ryan, Peter G -- Bloomer, Paulette -- Moloney, Coleen L -- Grant, Tyron J -- Delport, Wayne -- New York, N.Y. -- Science. 2007 Mar 9;315(5817):1420-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Percy Fitz Patrick Institute, Department of Science and Technology/National Research Foundation Centre of Excellence, University of Cape Town, Rondebosch 7701, South Africa. Peter.Ryan@uct.ac.za〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17347442" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; Atlantic Islands ; Beak/anatomy & histology ; Biological Evolution ; Body Size ; DNA, Mitochondrial/analysis/genetics ; *Ecosystem ; *Finches/anatomy & histology/genetics ; *Genetic Speciation ; Geography ; Microsatellite Repeats ; Seeds ; Selection, Genetic
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  • 72
    Publication Date: 2007-07-14
    Description: The temporal and spatial regulation of gene expression in mammalian development is linked to the establishment of functional chromatin domains. Here, we report that tissue-specific transcription of a retrotransposon repeat in the murine growth hormone locus is required for gene activation. This repeat serves as a boundary to block the influence of repressive chromatin modifications. The repeat element is able to generate short, overlapping Pol II-and Pol III-driven transcripts, both of which are necessary and sufficient to enable a restructuring of the regulated locus into nuclear compartments. These data suggest that transcription of interspersed repetitive sequences may represent a developmental strategy for the establishment of functionally distinct domains within the mammalian genome to control gene activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lunyak, Victoria V -- Prefontaine, Gratien G -- Nunez, Esperanza -- Cramer, Thorsten -- Ju, Bong-Gun -- Ohgi, Kenneth A -- Hutt, Kasey -- Roy, Rosa -- Garcia-Diaz, Angel -- Zhu, Xiaoyan -- Yung, Yun -- Montoliu, Lluis -- Glass, Christopher K -- Rosenfeld, Michael G -- New York, N.Y. -- Science. 2007 Jul 13;317(5835):248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, School of Medicine, University of California, San Diego, 9500 Gilman Drive, Room 345, La Jolla, CA 92093-0648, USA. vlunyak@uscd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17626886" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromatin Immunoprecipitation ; DNA Polymerase II/metabolism ; DNA Polymerase III/metabolism ; *Gene Expression Regulation, Developmental ; Growth Hormone/*genetics ; Histones/metabolism ; *Insulator Elements ; Methylation ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Organogenesis ; Pituitary Gland/*embryology/metabolism ; *Short Interspersed Nucleotide Elements ; *Transcription, Genetic ; Transcriptional Activation
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  • 73
    Publication Date: 2007-09-18
    Description: Membrane attack is important for mammalian immune defense against invading microorganisms and infected host cells. Proteins of the complement membrane attack complex (MAC) and the protein perforin share a common MACPF domain that is responsible for membrane insertion and pore formation. We determined the crystal structure of the MACPF domain of complement component C8alpha at 2.5 angstrom resolution and show that it is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins. The structure displays two regions that (in the bacterial cytolysins) refold into transmembrane beta hairpins, forming the lining of a barrel pore. Local hydrophobicity explains why C8alpha is the first complement protein to insert into the membrane. The size of the MACPF domain is consistent with known C9 pore sizes. These data imply that these mammalian and bacterial cytolytic proteins share a common mechanism of membrane insertion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hadders, Michael A -- Beringer, Dennis X -- Gros, Piet -- New York, N.Y. -- Science. 2007 Sep 14;317(5844):1552-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17872444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Membrane/immunology/metabolism ; Complement C8/*chemistry/immunology/*metabolism ; Complement Membrane Attack Complex/*chemistry/immunology/*metabolism ; Crystallography, X-Ray ; Cytotoxins/chemistry/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Perforin ; Pore Forming Cytotoxic Proteins/chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; *Protein Structure, Tertiary
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  • 74
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Kroon, Hans -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1562-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Plant Ecology, Institute for Water and Wetland Research, Radboud University, 6525 ED Nijmegen, the Netherlands. H.deKroon@science.ru.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063777" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Crops, Agricultural/genetics/*growth & development ; *Ecosystem ; *Plant Development ; Plant Roots/genetics/growth & development/*physiology ; Plants/genetics ; Selection, Genetic
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  • 75
    Publication Date: 2007-04-07
    Description: The carbon skeletons of over 55,000 naturally occurring isoprenoid compounds are constructed from four fundamental coupling reactions: chain elongation, cyclopropanation, branching, and cyclobutanation. Enzymes that catalyze chain elongation and cyclopropanation are well studied, whereas those that catalyze branching and cyclobutanation are unknown. We have catalyzed the four reactions with chimeric proteins generated by replacing segments of a chain-elongation enzyme with corresponding sequences from a cyclopropanation enzyme. Stereochemical and mechanistic considerations suggest that the four coupling enzymes could have evolved from a common ancestor through relatively small changes in the catalytic site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thulasiram, Hirekodathakallu V -- Erickson, Hans K -- Poulter, C Dale -- GM 21328/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):73-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Utah, 315 South 1400 East, Room 2020, Salt Lake City, UT 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412950" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Artemisia/enzymology ; Catalysis ; Catalytic Domain ; Chrysanthemum cinerariifolium/enzymology ; Cyclopropanes/chemistry ; Evolution, Molecular ; Geranyltranstransferase/chemistry/genetics/*metabolism ; Kinetics ; Molecular Conformation ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Recombinant Fusion Proteins/chemistry/metabolism ; Stereoisomerism ; Terpenes/chemistry/*metabolism
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  • 76
    Publication Date: 2007-07-28
    Description: Only five bacterial phyla with members capable of chlorophyll (Chl)-based phototrophy are presently known. Metagenomic data from the phototrophic microbial mats of alkaline siliceous hot springs in Yellowstone National Park revealed the existence of a distinctive bacteriochlorophyll (BChl)-synthesizing, phototrophic bacterium. A highly enriched culture of this bacterium grew photoheterotrophically, synthesized BChls a and c under oxic conditions, and had chlorosomes and type 1 reaction centers. "Candidatus Chloracidobacterium thermophilum" is a BChl-producing member of the poorly characterized phylum Acidobacteria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bryant, Donald A -- Costas, Amaya M Garcia -- Maresca, Julia A -- Chew, Aline Gomez Maqueo -- Klatt, Christian G -- Bateson, Mary M -- Tallon, Luke J -- Hostetler, Jessica -- Nelson, William C -- Heidelberg, John F -- Ward, David M -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):523-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA. dab14@psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17656724" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria, Aerobic/*classification/*isolation & ; purification/physiology/ultrastructure ; Bacterial Chromatophores/ultrastructure ; Bacteriochlorophylls/biosynthesis ; Computational Biology ; Ecosystem ; Genome, Bacterial ; Genomics ; Hot Springs/*microbiology ; Molecular Sequence Data ; Photosystem I Protein Complex/analysis ; *Phototrophic Processes ; RNA, Ribosomal, 16S/genetics ; Temperature ; Wyoming
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  • 77
    Publication Date: 2007-06-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hambler, Clive -- Canney, Susan M -- Coe, Malcolm J -- Henderson, Peter A -- Illius, Andrew W -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1564-7; author reply 1564-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569844" target="_blank"〉PubMed〈/a〉
    Keywords: *Agriculture ; Animals ; *Animals, Domestic ; *Biodiversity ; *Ecosystem ; Population Density
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  • 78
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macpherson, Rick -- New York, N.Y. -- Science. 2007 Sep 14;317(5844):1498-500.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17872426" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa ; Conservation of Natural Resources ; *Diving ; *Ecosystem ; Travel
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  • 79
    Publication Date: 2007-09-01
    Description: Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions. Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length. These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aricescu, A Radu -- Siebold, Christian -- Choudhuri, Kaushik -- Chang, Veronica T -- Lu, Weixian -- Davis, Simon J -- van der Merwe, P Anton -- Jones, E Yvonne -- 081894/Wellcome Trust/United Kingdom -- G9722488/Medical Research Council/United Kingdom -- G9900061/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1217-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK Receptor Structure Research Group, University of Oxford, Henry Wellcome Building of Genomic Medicine, Division of Structural Biology, Roosevelt Drive, Oxford OX3 7BN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761881" target="_blank"〉PubMed〈/a〉
    Keywords: Adherens Junctions/chemistry/*physiology/ultrastructure ; Amino Acid Sequence ; Cell Adhesion ; Cell Adhesion Molecules/*chemistry/metabolism ; Cell Membrane/chemistry/enzymology ; Conserved Sequence ; Dimerization ; Fibronectins/chemistry ; Humans ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Immunoglobulins/chemistry ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/*chemistry/genetics/*metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class 2
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  • 80
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-10-20
    Description: Arginine methylation occurs on a number of proteins involved in a variety of cellular functions. Histone tails are known to be mono- and dimethylated on multiple arginine residues where they influence chromatin remodeling and gene expression. To date, no enzyme has been shown to reverse these regulatory modifications. We demonstrate that the Jumonji domain-containing 6 protein (JMJD6) is a JmjC-containing iron- and 2-oxoglutarate-dependent dioxygenase that demethylates histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) in both biochemical and cell-based assays. These findings may help explain the many developmental defects observed in the JMJD6(-/-) knockout mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Bingsheng -- Chen, Yue -- Zhao, Yingming -- Bruick, Richard K -- C06-RR15437-01/RR/NCRR NIH HHS/ -- CA107943/CA/NCI NIH HHS/ -- CA115962/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):444-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947579" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/*metabolism ; HeLa Cells ; Histones/*metabolism ; Humans ; Jumonji Domain-Containing Histone Demethylases ; Methylation ; Molecular Sequence Data ; Oxidation-Reduction ; Protein Processing, Post-Translational ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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  • 81
    Publication Date: 2007-05-26
    Description: Mutations in the breast cancer susceptibility gene 1 (BRCA1) are associated with an increased risk of breast and ovarian cancers. BRCA1 participates in the cellular DNA damage response. We report the identification of receptor-associated protein 80 (RAP80) as a BRCA1-interacting protein in humans. RAP80 contains a tandem ubiquitin-interacting motif domain, which is required for its binding with ubiquitin in vitro and its damage-induced foci formation in vivo. Moreover, RAP80 specifically recruits BRCA1 to DNA damage sites and functions with BRCA1 in G2/M checkpoint control. Together, these results suggest the existence of a ubiquitination-dependent signaling pathway involved in the DNA damage response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Hongtae -- Chen, Junjie -- Yu, Xiaochun -- R01CA089239/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 May 25;316(5828):1202-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Therapeutic Radiology, Yale University School of Medicine, Post Office Box 208040, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; BRCA1 Protein/*metabolism ; Carrier Proteins/*metabolism ; Cell Cycle ; Cell Line, Tumor ; DNA/*metabolism/radiation effects ; *DNA Damage ; DNA Repair/*physiology ; HeLa Cells ; Humans ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; RNA, Small Interfering ; Radiation, Ionizing ; Ubiquitin/*metabolism
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  • 82
    Publication Date: 2007-06-16
    Description: The ability of species to track their ecological niche after climate change is a major source of uncertainty in predicting their future distribution. By analyzing DNA fingerprinting (amplified fragment-length polymorphism) of nine plant species, we show that long-distance colonization of a remote arctic archipelago, Svalbard, has occurred repeatedly and from several source regions. Propagules are likely carried by wind and drifting sea ice. The genetic effect of restricted colonization was strongly correlated with the temperature requirements of the species, indicating that establishment limits distribution more than dispersal. Thus, it may be appropriate to assume unlimited dispersal when predicting long-term range shifts in the Arctic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alsos, Inger Greve -- Eidesen, Pernille Bronken -- Ehrich, Dorothee -- Skrede, Inger -- Westergaard, Kristine -- Jacobsen, Gro Hilde -- Landvik, Jon Y -- Taberlet, Pierre -- Brochmann, Christian -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1606-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Centre for Biosystematics, Natural History Museum, University of Oslo, Post Office Box 1172 Blindern, NO-0318 Oslo, Norway. ingera@unis.no〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569861" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Angiosperms/genetics/*growth & development/physiology ; Arabis/genetics/growth & development/physiology ; Arctic Regions ; Betula/genetics/growth & development/physiology ; *Cold Climate ; DNA Fingerprinting ; *Ecosystem ; Ericaceae/genetics/growth & development/physiology ; Genetic Variation ; Geography ; Ice Cover ; Polymerase Chain Reaction ; Rosales/genetics/growth & development/physiology ; Salix/genetics/growth & development/physiology ; Wind
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  • 83
    Publication Date: 2007-02-03
    Description: Dimethyl sulfide (DMS) is a key compound in global sulfur and carbon cycles. DMS oxidation products cause cloud nucleation and may affect weather and climate. DMS is generated largely by bacterial catabolism of dimethylsulfoniopropionate (DMSP), a secondary metabolite made by marine algae. We demonstrate that the bacterial gene dddD is required for this process and that its transcription is induced by the DMSP substrate. Cloned dddD from the marine bacterium Marinomonas and from two bacterial strains that associate with higher plants, the N(2)-fixing symbiont Rhizobium NGR234 and the root-colonizing Burkholderia cepacia AMMD, conferred to Escherichia coli the ability to make DMS from DMSP. The inferred enzymatic mechanism for DMS liberation involves an initial step in which DMSP is modified by addition of acyl coenzyme A, rather than the immediate release of DMS by a DMSP lyase, the previously suggested mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Todd, Jonathan D -- Rogers, Rachel -- Li, You Guo -- Wexler, Margaret -- Bond, Philip L -- Sun, Lei -- Curson, Andrew R J -- Malin, Gill -- Steinke, Michael -- Johnston, Andrew W B -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):666-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272727" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/genetics/*metabolism ; Burkholderia cepacia/genetics/growth & development/metabolism ; Cloning, Molecular ; Coenzyme A-Transferases/genetics/*metabolism ; DNA Transposable Elements ; Escherichia coli/genetics/metabolism ; *Genes, Bacterial ; *Genes, Regulator ; Marinomonas/*genetics/growth & development/*metabolism ; Molecular Sequence Data ; Operon ; Oxidation-Reduction ; Phenotype ; Poaceae/microbiology ; Promoter Regions, Genetic ; Rhizobium/genetics/growth & development/metabolism ; Sulfides/*metabolism ; Sulfonium Compounds/metabolism ; Transformation, Bacterial
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  • 84
    Publication Date: 2007-06-30
    Description: HIV-1 integrates into the host chromosome and persists as a provirus flanked by long terminal repeats (LTRs). To date, treatment regimens primarily target the virus enzymes or virus-cell fusion, but not the integrated provirus. We report here the substrate-linked protein evolution of a tailored recombinase that recognizes an asymmetric sequence within an HIV-1 LTR. This evolved recombinase efficiently excised integrated HIV proviral DNA from the genome of infected cells. Although a long way from use in the clinic, we speculate that this type of technology might be adapted in future antiretroviral therapies, among other possible uses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sarkar, Indrani -- Hauber, Ilona -- Hauber, Joachim -- Buchholz, Frank -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1912-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, D-01307 Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600219" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Shuffling ; DNA, Viral/*metabolism ; *Directed Molecular Evolution ; Escherichia coli/genetics ; Gene Library ; Genome, Human ; *HIV Long Terminal Repeat ; HIV-1/*metabolism ; HeLa Cells ; Humans ; Integrases/*genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Proviruses/metabolism ; Recombination, Genetic ; *Virus Integration
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  • 85
    Publication Date: 2007-07-14
    Description: The ratio of males to females in a species is often considered to be relatively constant, at least over ecological time. Hamilton noted that the spread of "selfish" sex ratio-distorting elements could be rapid and produce a switch to highly biased population sex ratios. Selection against a highly skewed sex ratio should promote the spread of mutations that suppress the sex ratio distortion. We show that in the butterfly Hypolimnas bolina the suppression of sex biases occurs extremely fast, with a switch from a 100:1 population sex ratio to 1:1 occurring in fewer than 10 generations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Charlat, Sylvain -- Hornett, Emily A -- Fullard, James H -- Davies, Neil -- Roderick, George K -- Wedell, Nina -- Hurst, Gregory D D -- New York, N.Y. -- Science. 2007 Jul 13;317(5835):214.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University College London, 4 Stephenson Way, London NW1 2HE, UK. s.charlat@ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17626876" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Butterflies/genetics/*microbiology/*physiology ; Female ; Genes, Insect ; Male ; Molecular Sequence Data ; Reproduction ; Samoa ; Selection, Genetic ; *Sex Ratio ; Wolbachia/genetics/*physiology
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  • 86
    Publication Date: 2007-12-15
    Description: Atmospheric carbon dioxide concentration is expected to exceed 500 parts per million and global temperatures to rise by at least 2 degrees C by 2050 to 2100, values that significantly exceed those of at least the past 420,000 years during which most extant marine organisms evolved. Under conditions expected in the 21st century, global warming and ocean acidification will compromise carbonate accretion, with corals becoming increasingly rare on reef systems. The result will be less diverse reef communities and carbonate reef structures that fail to be maintained. Climate change also exacerbates local stresses from declining water quality and overexploitation of key species, driving reefs increasingly toward the tipping point for functional collapse. This review presents future scenarios for coral reefs that predict increasingly serious consequences for reef-associated fisheries, tourism, coastal protection, and people. As the International Year of the Reef 2008 begins, scaled-up management intervention and decisive action on global emissions are required if the loss of coral-dominated ecosystems is to be avoided.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoegh-Guldberg, O -- Mumby, P J -- Hooten, A J -- Steneck, R S -- Greenfield, P -- Gomez, E -- Harvell, C D -- Sale, P F -- Edwards, A J -- Caldeira, K -- Knowlton, N -- Eakin, C M -- Iglesias-Prieto, R -- Muthiga, N -- Bradbury, R H -- Dubi, A -- Hatziolos, M E -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1737-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Marine Studies, University of Queensland, St. Lucia, 4072 Queensland, Australia. oveh@uq.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079392" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa/growth & development/physiology ; Atmosphere ; Carbon Dioxide ; *Climate ; Dinoflagellida/physiology ; *Ecosystem ; Eukaryota/physiology ; Fishes ; Forecasting ; *Greenhouse Effect ; Hydrogen-Ion Concentration ; Oceans and Seas ; Seawater/*chemistry ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 87
    Publication Date: 2007-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Asara, John M -- Garavelli, John S -- Slatter, David A -- Schweitzer, Mary H -- Freimark, Lisa M -- Phillips, Matthew -- Cantley, Lewis C -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1324-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17823333" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone and Bones/chemistry ; Collagen/*chemistry ; *Dinosaurs ; *Elephants ; *Fossils ; Glycine/chemistry ; Mass Spectrometry ; Molecular Sequence Data ; Proline/chemistry ; Tandem Mass Spectrometry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 88
    Publication Date: 2007-04-14
    Description: Fossilized bones from extinct taxa harbor the potential for obtaining protein or DNA sequences that could reveal evolutionary links to extant species. We used mass spectrometry to obtain protein sequences from bones of a 160,000- to 600,000-year-old extinct mastodon (Mammut americanum) and a 68-million-year-old dinosaur (Tyrannosaurus rex). The presence of T. rex sequences indicates that their peptide bonds were remarkably stable. Mass spectrometry can thus be used to determine unique sequences from ancient organisms from peptide fragmentation patterns, a valuable tool to study the evolution and adaptation of ancient taxa from which genomic sequences are unlikely to be obtained.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Asara, John M -- Schweitzer, Mary H -- Freimark, Lisa M -- Phillips, Matthew -- Cantley, Lewis C -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):280-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Beth Israel Deaconess Medical Center, Boston, MA 02115, USA. jasara@bidmc.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone and Bones/*chemistry ; Collagen/chemistry ; *Dinosaurs ; *Elephants ; Evolution, Molecular ; *Fossils ; Humans ; *Mass Spectrometry ; Molecular Sequence Data ; Proteins/analysis/*chemistry ; Reptilian Proteins/analysis/*chemistry ; Sequence Alignment ; Sequence Analysis, Protein ; Struthioniformes
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  • 89
    Publication Date: 2007-01-16
    Description: We describe the genome sequence of the protist Trichomonas vaginalis, a sexually transmitted human pathogen. Repeats and transposable elements comprise about two-thirds of the approximately 160-megabase genome, reflecting a recent massive expansion of genetic material. This expansion, in conjunction with the shaping of metabolic pathways that likely transpired through lateral gene transfer from bacteria, and amplification of specific gene families implicated in pathogenesis and phagocytosis of host proteins may exemplify adaptations of the parasite during its transition to a urogenital environment. The genome sequence predicts previously unknown functions for the hydrogenosome, which support a common evolutionary origin of this unusual organelle with mitochondria.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080659/" 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/PMC2080659/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carlton, Jane M -- Hirt, Robert P -- Silva, Joana C -- Delcher, Arthur L -- Schatz, Michael -- Zhao, Qi -- Wortman, Jennifer R -- Bidwell, Shelby L -- Alsmark, U Cecilia M -- Besteiro, Sebastien -- Sicheritz-Ponten, Thomas -- Noel, Christophe J -- Dacks, Joel B -- Foster, Peter G -- Simillion, Cedric -- Van de Peer, Yves -- Miranda-Saavedra, Diego -- Barton, Geoffrey J -- Westrop, Gareth D -- Muller, Sylke -- Dessi, Daniele -- Fiori, Pier Luigi -- Ren, Qinghu -- Paulsen, Ian -- Zhang, Hanbang -- Bastida-Corcuera, Felix D -- Simoes-Barbosa, Augusto -- Brown, Mark T -- Hayes, Richard D -- Mukherjee, Mandira -- Okumura, Cheryl Y -- Schneider, Rachel -- Smith, Alias J -- Vanacova, Stepanka -- Villalvazo, Maria -- Haas, Brian J -- Pertea, Mihaela -- Feldblyum, Tamara V -- Utterback, Terry R -- Shu, Chung-Li -- Osoegawa, Kazutoyo -- de Jong, Pieter J -- Hrdy, Ivan -- Horvathova, Lenka -- Zubacova, Zuzana -- Dolezal, Pavel -- Malik, Shehre-Banoo -- Logsdon, John M Jr -- Henze, Katrin -- Gupta, Arti -- Wang, Ching C -- Dunne, Rebecca L -- Upcroft, Jacqueline A -- Upcroft, Peter -- White, Owen -- Salzberg, Steven L -- Tang, Petrus -- Chiu, Cheng-Hsun -- Lee, Ying-Shiung -- Embley, T Martin -- Coombs, Graham H -- Mottram, Jeremy C -- Tachezy, Jan -- Fraser-Liggett, Claire M -- Johnson, Patricia J -- 072031/Wellcome Trust/United Kingdom -- G0000508/Medical Research Council/United Kingdom -- G0000508(56841)/Medical Research Council/United Kingdom -- G9722968/Medical Research Council/United Kingdom -- G9722968(65078)/Medical Research Council/United Kingdom -- R01 LM006845/LM/NLM NIH HHS/ -- R01 LM006845-08/LM/NLM NIH HHS/ -- R01 LM007938/LM/NLM NIH HHS/ -- R01 LM007938-04/LM/NLM NIH HHS/ -- U01 AI050913/AI/NIAID NIH HHS/ -- U01 AI050913-01A1/AI/NIAID NIH HHS/ -- U01 AI050913-02/AI/NIAID NIH HHS/ -- UO1 AI50913-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Jan 12;315(5809):207-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, 9712 Medical Research Drive, Rockville, MD 20850, USA. jane.carlton@med.nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17218520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport/genetics ; DNA Transposable Elements ; DNA, Protozoan/genetics ; Gene Transfer, Horizontal ; Genes, Protozoan ; *Genome, Protozoan ; Humans ; Hydrogen/metabolism ; Metabolic Networks and Pathways/genetics ; Molecular Sequence Data ; Multigene Family ; Organelles/metabolism ; Oxidative Stress/genetics ; Peptide Hydrolases/genetics/metabolism ; Protozoan Proteins/genetics/physiology ; RNA Processing, Post-Transcriptional ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA ; Sexually Transmitted Diseases/parasitology ; Trichomonas Infections/parasitology/transmission ; Trichomonas vaginalis/cytology/*genetics/metabolism/pathogenicity
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  • 90
    Publication Date: 2007-01-16
    Description: Environmental sequencing has revealed unimagined diversity among eukaryotic picoplankton. A distinct picoplanktonic algal group, initially detected from 18S ribosomal DNA (rDNA) sequences, was hybridized with rRNA-targeted probes, detected by tyramide signal amplification-fluorescent in situ hybridization, and showed an organelle-like body with orange fluorescence indicative of phycobilins. Using this fluorescence signal, cells were sorted by flow cytometry and probed. Hybridized cells contained a 4',6'-diamidino-2-phenylindole-stained organelle resembling a plastid with a nucleomorph. This suggests that they may be secondary endosymbiotic algae. Pending the isolation of living cells and their formal description, these algae have been termed picobiliphytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Not, Fabrice -- Valentin, Klaus -- Romari, Khadidja -- Lovejoy, Connie -- Massana, Ramon -- Tobe, Kerstin -- Vaulot, Daniel -- Medlin, Linda K -- New York, N.Y. -- Science. 2007 Jan 12;315(5809):253-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Station Biologique de Roscoff, UMR 7144 CNRS and Universite Pierre et Marie Curie, Boite Postale 74, 29682 Roscoff Cedex, France. not@icm.csic.es〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17218530" target="_blank"〉PubMed〈/a〉
    Keywords: Bayes Theorem ; DNA, Ribosomal/genetics ; *Eukaryota/classification/cytology/genetics/isolation & purification ; Flow Cytometry ; Fluorescence ; In Situ Hybridization, Fluorescence ; Molecular Sequence Data ; Organelles/ultrastructure ; Phycobiliproteins/analysis ; Phylogeny ; *Phytoplankton/classification/cytology/genetics/isolation & purification ; Seasons ; Seawater/*microbiology ; Symbiosis
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  • 91
    Publication Date: 2007-08-19
    Description: Integral beta-barrel proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. The machine that assembles these proteins contains an integral membrane protein, called YaeT in Escherichia coli, which has one or more polypeptide transport-associated (POTRA) domains. The crystal structure of a periplasmic fragment of YaeT reveals the POTRA domain fold and suggests a model for how POTRA domains can bind different peptide sequences, as required for a machine that handles numerous beta-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Seokhee -- Malinverni, Juliana C -- Sliz, Piotr -- Silhavy, Thomas J -- Harrison, Stephen C -- Kahne, Daniel -- GM34821/GM/NIGMS NIH HHS/ -- GM66174/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):961-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702946" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/genetics/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Dimerization ; Escherichia coli/*chemistry/*metabolism ; Escherichia coli Proteins/*chemistry/genetics/*metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Lipoproteins/chemistry/metabolism ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport
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  • 92
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-05-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kintisch, Eli -- New York, N.Y. -- Science. 2007 May 18;316(5827):969.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510335" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Budgets ; *Ecology ; *Ecosystem ; Financing, Government ; Georgia ; Laboratories/economics ; *Radioactive Waste ; *Research Support as Topic ; *Rivers ; United States ; *United States Government Agencies
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  • 93
    Publication Date: 2007-08-25
    Description: Biogeochemical rate processes in the Southern Ocean have an important impact on the global environment. Here, we summarize an extensive set of published and new data that establishes the pattern of gross primary production and net community production over large areas of the Southern Ocean. We compare these rates with model estimates of dissolved iron that is added to surface waters by aerosols. This comparison shows that net community production, which is comparable to export production, is proportional to modeled input of soluble iron in aerosols. Our results strengthen the evidence that the addition of aerosol iron fertilizes export production in the Southern Ocean. The data also show that aerosol iron input particularly enhances gross primary production over the large area of the Southern Ocean downwind of dry continental areas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cassar, Nicolas -- Bender, Michael L -- Barnett, Bruce A -- Fan, Songmiao -- Moxim, Walter J -- Levy, Hiram 2nd -- Tilbrook, Bronte -- New York, N.Y. -- Science. 2007 Aug 24;317(5841):1067-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geosciences, Princeton University, Princeton, NJ 08544, USA. ncassar@princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17717181" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Ecosystem ; Iron/*analysis ; Oceans and Seas ; Oxygen/analysis ; Phytoplankton/*growth & development ; Seasons ; *Seawater/chemistry ; *Wind
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  • 94
    Publication Date: 2007-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duke, N C -- Meynecke, J-O -- Dittmann, S -- Ellison, A M -- Anger, K -- Berger, U -- Cannicci, S -- Diele, K -- Ewel, K C -- Field, C D -- Koedam, N -- Lee, S Y -- Marchand, C -- Nordhaus, I -- Dahdouh-Guebas, F -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):41-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615322" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; *Rhizophoraceae ; *Trees
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  • 95
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pala, Christopher -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1719.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079380" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa ; *Ecosystem ; *Fishes/physiology ; *Food Chain ; Pacific Islands ; Population Dynamics ; Predatory Behavior
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  • 96
    Publication Date: 2007-02-10
    Description: The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 and 2.6 A resolution for ATP- and AMP-bound forms of a core alphabetagamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the gamma subunit, with their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, ATP binds without counterions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Townley, Robert -- Shapiro, Lawrence -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1726-9. Epub 2007 Feb 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289942" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases ; Adenosine Monophosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Binding, Competitive ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Protein Kinases/*chemistry/metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Protein-Serine-Threonine Kinases/*chemistry/metabolism ; Schizosaccharomyces/*enzymology
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  • 97
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-05-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pala, Christopher -- New York, N.Y. -- Science. 2007 May 4;316(5825):680-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17478694" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa/physiology ; *Conservation of Natural Resources ; *Ecosystem ; Pacific Ocean ; Palau ; Temperature
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  • 98
    Publication Date: 2007-10-06
    Description: Telomeres, the DNA-protein complexes located at the end of linear eukaryotic chromosomes, are essential for chromosome stability. Until now, telomeres have been considered to be transcriptionally silent. We demonstrate that mammalian telomeres are transcribed into telomeric repeat-containing RNA (TERRA). TERRA molecules are heterogeneous in length, are transcribed from several subtelomeric loci toward chromosome ends, and localize to telomeres. We also show that suppressors with morphogenetic defects in genitalia (SMG) proteins, which are effectors of nonsense-mediated messenger RNA decay, are enriched at telomeres in vivo, negatively regulate TERRA association with chromatin, and protect chromosome ends from telomere loss. Thus, telomeres are actively transcribed into TERRA, and SMG factors represent a molecular link between TERRA regulation and the maintenance of telomere integrity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Azzalin, Claus M -- Reichenbach, Patrick -- Khoriauli, Lela -- Giulotto, Elena -- Lingner, Joachim -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):798-801. Epub 2007 Oct 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Institute for Experimental Cancer Research (ISREC), CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916692" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Cells, Cultured ; Chromosomes, Human ; Chromosomes, Mammalian ; HeLa Cells ; Humans ; In Situ Hybridization, Fluorescence ; Mice ; Molecular Sequence Data ; Proteins/metabolism ; RNA/*genetics ; Repetitive Sequences, Nucleic Acid ; Telomerase/physiology ; Telomere/*genetics ; Transcription, Genetic ; Tumor Cells, Cultured
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  • 99
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palmer, Michael W -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):897-8; author reply 987-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702924" target="_blank"〉PubMed〈/a〉
    Keywords: Biomass ; *Cellulose ; *Ecosystem ; *Energy-Generating Resources ; *Plant Physiological Phenomena
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  • 100
    Publication Date: 2007-09-01
    Description: Although common among bacteria, lateral gene transfer-the movement of genes between distantly related organisms-is thought to occur only rarely between bacteria and multicellular eukaryotes. However, the presence of endosymbionts, such as Wolbachia pipientis, within some eukaryotic germlines may facilitate bacterial gene transfers to eukaryotic host genomes. We therefore examined host genomes for evidence of gene transfer events from Wolbachia bacteria to their hosts. We found and confirmed transfers into the genomes of four insect and four nematode species that range from nearly the entire Wolbachia genome (〉1 megabase) to short (〈500 base pairs) insertions. Potential Wolbachia-to-host transfers were also detected computationally in three additional sequenced insect genomes. We also show that some of these inserted Wolbachia genes are transcribed within eukaryotic cells lacking endosymbionts. Therefore, heritable lateral gene transfer occurs into eukaryotic hosts from their prokaryote symbionts, potentially providing a mechanism for acquisition of new genes and functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunning Hotopp, Julie C -- Clark, Michael E -- Oliveira, Deodoro C S G -- Foster, Jeremy M -- Fischer, Peter -- Munoz Torres, Monica C -- Giebel, Jonathan D -- Kumar, Nikhil -- Ishmael, Nadeeza -- Wang, Shiliang -- Ingram, Jessica -- Nene, Rahul V -- Shepard, Jessica -- Tomkins, Jeffrey -- Richards, Stephen -- Spiro, David J -- Ghedin, Elodie -- Slatko, Barton E -- Tettelin, Herve -- Werren, John H -- New York, N.Y. -- Science. 2007 Sep 21;317(5845):1753-6. Epub 2007 Aug 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, J. Craig Venter Institute, 9712 Medical Center Drive, Rockville, MD 20850, USA. jhotopp@som.umaryland.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; Crosses, Genetic ; DNA, Bacterial ; Drosophila/genetics/microbiology ; Female ; *Gene Transfer, Horizontal ; Genes, Bacterial ; In Situ Hybridization, Fluorescence ; Insects/*genetics/microbiology ; Male ; Molecular Sequence Data ; Nematoda/*genetics/microbiology ; Retroelements ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, DNA ; Symbiosis ; Wolbachia/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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