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  • *Ecosystem  (107)
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  • American Association for the Advancement of Science (AAAS)  (161)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-04-28
    Beschreibung: 〈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〉
    Schlagwort(e): Animal Migration ; Animals ; China ; *Conservation of Natural Resources/legislation & jurisprudence ; *Ecosystem ; *Environment ; Fresh Water ; Plants ; *Railroads ; Refuse Disposal ; Temperature ; Travel
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 2
    Publikationsdatum: 2007-12-22
    Beschreibung: Protein molecules have the ability to form a rich variety of natural and artificial structures and materials. We show that amyloid fibrils, ordered supramolecular nanostructures that are self-assembled from a wide range of polypeptide molecules, have rigidities varying over four orders of magnitude, and constitute a class of high-performance biomaterials. We elucidate the molecular origin of fibril material properties and show that the major contribution to their rigidity stems from a generic interbackbone hydrogen-bonding network that is modulated by variable side-chain interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knowles, Tuomas P -- Fitzpatrick, Anthony W -- Meehan, Sarah -- Mott, Helen R -- Vendruscolo, Michele -- Dobson, Christopher M -- Welland, Mark E -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1900-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nanoscience Centre, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0FF, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096801" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amyloid/*chemistry ; Amyloid beta-Peptides/chemistry ; Chemistry, Physical ; Elasticity ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Insulin/chemistry ; Lactalbumin/chemistry ; Lactoglobulins/chemistry ; Microscopy, Atomic Force ; Models, Molecular ; Muramidase/chemistry ; Nanostructures/*chemistry ; Peptide Termination Factors ; Peptides/*chemistry ; Physicochemical Phenomena ; Prealbumin/chemistry ; Prions/chemistry ; Protein Conformation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/chemistry ; Surface Tension ; alpha-Crystallin B Chain/chemistry
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 3
    Publikationsdatum: 2007-02-03
    Beschreibung: 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〉
    Schlagwort(e): 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
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 4
    Publikationsdatum: 2007-10-06
    Beschreibung: 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〉
    Schlagwort(e): *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
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-02-03
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Biodiversity ; California ; *Climate ; *Ecosystem ; *Invertebrates/physiology ; *Plant Development ; Poaceae/growth & development ; Population Dynamics ; Rain ; Research Design ; Seasons ; Time Factors
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 6
    Publikationsdatum: 2007-04-14
    Beschreibung: The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell development. In the 2.7 angstrom structure of a human pre-BCR Fab-like fragment, consisting of an antibody heavy chain (HC) paired with the surrogate light chain, the "unique regions" of VpreB and lambda5 replace the complementarity-determining region 3 (CDR3) loop of an antibody light chain and appear to "probe" the HC CDR3, potentially influencing the selection of the antibody repertoire. Biochemical analysis indicates that the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bankovich, Alexander J -- Raunser, Stefan -- Juo, Z Sean -- Walz, Thomas -- Davis, Mark M -- Garcia, K Christopher -- T32 AI007290/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431183" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Complementarity Determining Regions/chemistry/physiology ; Crystallography, X-Ray ; Humans ; Immunoglobulin Heavy Chains/chemistry/physiology ; Immunoglobulin Light Chains/chemistry/physiology ; Immunoglobulin Light Chains, Surrogate ; Membrane Glycoproteins/*chemistry/physiology/ultrastructure ; Mice ; Models, Molecular ; Pre-B Cell Receptors ; Protein Conformation ; Receptors, Antigen, B-Cell/*chemistry/physiology/ultrastructure ; Recombinant Proteins ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 7
    Publikationsdatum: 2007-08-04
    Beschreibung: 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〉
    Schlagwort(e): 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
    Print ISSN: 0036-8075
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-05-05
    Beschreibung: 〈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〉
    Schlagwort(e): Adaptation, Biological ; Animals ; Biodiversity ; *Biological Evolution ; *Ecosystem ; Gene Flow ; Geography ; Plants
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 9
    Publikationsdatum: 2007-01-20
    Beschreibung: 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〉
    Schlagwort(e): *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
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-08-19
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):884-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702918" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aldosterone/metabolism ; Animals ; Computer Simulation ; Crystallography, X-Ray ; Desoxycorticosterone/metabolism ; *Evolution, Molecular ; *Fishes ; Hydrocortisone/metabolism ; Models, Molecular ; Mutation ; Protein Conformation ; Receptors, Glucocorticoid/chemistry/*genetics/metabolism ; Receptors, Mineralocorticoid/chemistry/*genetics/metabolism ; Receptors, Steroid/chemistry/*genetics/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-07-07
    Beschreibung: 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〉
    Schlagwort(e): Animals ; *Biodiversity ; *Ecosystem ; Environment ; Extinction, Biological ; Models, Biological ; Population Dynamics
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-20
    Beschreibung: 〈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〉
    Schlagwort(e): 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
    Print ISSN: 0036-8075
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 13
    Publikationsdatum: 2007-01-27
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Jan 26;315(5811):456.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255491" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Biological Evolution ; Cephalopoda/chemistry/genetics ; Crystallins/*chemistry/genetics ; Decapodiformes/*chemistry/genetics/physiology ; *Evolution, Molecular ; Lens, Crystalline/chemistry/physiology ; Protein Conformation ; Protein Folding ; Sequence Analysis, DNA ; *Vision, Ocular
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-16
    Beschreibung: 〈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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-06-16
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fitzgerald, Katherine A -- Golenbock, Douglas T -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1574-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases and Immunology, University of Massachusetts Medical School, Worcester, MA 01605, USA. kate.fitzgerald@umassmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569850" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adaptor Proteins, Signal Transducing/metabolism ; Adaptor Proteins, Vesicular Transport/metabolism ; *Adjuvants, Immunologic ; Animals ; Crystallography, X-Ray ; Glycolipids/chemistry/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Lipid A/*analogs & derivatives/chemistry/immunology/metabolism ; Lymphocyte Activation ; Lymphocyte Antigen 96/*chemistry/metabolism ; Mice ; Phosphates/metabolism ; Protein Conformation ; Receptors, Interleukin/metabolism ; Signal Transduction ; T-Lymphocytes/immunology ; Toll-Like Receptor 4/chemistry/*immunology/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 16
    Publikationsdatum: 2007-12-01
    Beschreibung: How chaperone interactions affect protein folding pathways is a central problem in biology. With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level. In the absence of SecB, we find that the MBP polypeptide first collapses into a molten globulelike compacted state and then folds into a stable core structure onto which several alpha helices are finally wrapped. Interactions with SecB completely prevent stable tertiary contacts in the core structure but have no detectable effect on the folding of the external alpha helices. It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bechtluft, Philipp -- van Leeuwen, Ruud G H -- Tyreman, Matthew -- Tomkiewicz, Danuta -- Nouwen, Nico -- Tepper, Harald L -- Driessen, Arnold J M -- Tans, Sander J -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1458-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Groningen Bio-molecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048690" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacterial Proteins/*metabolism ; Computer Simulation ; Escherichia coli Proteins/*chemistry/metabolism ; Models, Molecular ; Optical Tweezers ; Periplasmic Binding Proteins/*chemistry/metabolism ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 17
    Publikationsdatum: 2007-04-14
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 18
    Publikationsdatum: 2007-12-15
    Beschreibung: 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〉
    Schlagwort(e): *Amphibians/growth & development/physiology ; Animal Migration ; Animals ; *Biodiversity ; Brazil ; Conservation of Natural Resources ; *Ecosystem ; Larva/physiology ; Population Dynamics ; Trees ; Water
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 19
    Publikationsdatum: 2007-04-21
    Beschreibung: We report the structures of three intermediates in the O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2720167/" 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/PMC2720167/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kovaleva, Elena G -- Lipscomb, John D -- GM24689/GM/NIGMS NIH HHS/ -- R01 GM024689/GM/NIGMS NIH HHS/ -- R01 GM024689-27/GM/NIGMS NIH HHS/ -- R01 GM024689-28/GM/NIGMS NIH HHS/ -- R37 GM024689/GM/NIGMS NIH HHS/ -- R37 GM024689-26/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):453-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17446402" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Brevibacterium/*enzymology ; Catalysis ; Catechols/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Dioxygenases/*chemistry/*metabolism ; Ferric Compounds/*chemistry/metabolism ; Ferrous Compounds/chemistry ; Ligands ; Models, Chemical ; Models, Molecular ; Oxygen/chemistry/metabolism ; Protein Conformation ; Protein Subunits/chemistry/metabolism ; Superoxides/chemistry
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 20
    Publikationsdatum: 2007-06-02
    Beschreibung: 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〉
    Schlagwort(e): Animals ; *Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; *Fisheries ; *Fishes ; Forecasting ; Population Dynamics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 21
    Publikationsdatum: 2007-08-19
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 22
    Publikationsdatum: 2007-03-31
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-03-17
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; Arctic Regions ; Biodiversity ; *Cold Climate ; *Ecosystem ; Food Chain ; Ice Cover ; Invertebrates ; Plankton/growth & development ; Population Dynamics ; *Seawater ; Temperature
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 24
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-03-31
    Beschreibung: 〈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〉
    Schlagwort(e): *Agriculture ; *Animal Husbandry ; Animals ; Animals, Domestic ; *Behavior ; Biological Evolution ; *Ecosystem ; *Environment ; Humans
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 25
    Publikationsdatum: 2007-07-07
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 26
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-05-26
    Beschreibung: 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〉
    Schlagwort(e): Biodiversity ; Diatoms/*physiology ; *Ecosystem ; *Environmental Microbiology ; Europe ; Fresh Water ; Hydrogen-Ion Concentration ; Models, Biological ; North America ; Water Microbiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-12-15
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Anthozoa/microbiology/physiology ; Aspergillus ; Bacteria ; *Ecosystem ; Greenhouse Effect
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 28
    Publikationsdatum: 2007-06-26
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 29
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-04-21
    Beschreibung: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3097138/" 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/PMC3097138/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilmot, Carrie M -- R01 GM066569/GM/NIGMS NIH HHS/ -- R01 GM066569-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):379-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA. wilmo004@umn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17446378" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacteria/enzymology ; Binding Sites ; Catalysis ; Crystallization ; Dioxygenases/chemistry/*metabolism ; Ferric Compounds/chemistry/metabolism ; Ferrous Compounds/*metabolism ; Hydrogen Peroxide/metabolism ; Molecular Conformation ; Oxidation-Reduction ; Oxidoreductases/chemistry/*metabolism ; Oxygen/*metabolism ; Protein Conformation ; Protons ; Spectrum Analysis, Raman ; Superoxides/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-12-15
    Beschreibung: 〈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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 31
    Publikationsdatum: 2007-11-24
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Biological Evolution ; *Ecosystem ; *Fisheries/methods ; *Fishes/physiology ; Population Dynamics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-06
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-04-07
    Beschreibung: 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〉
    Schlagwort(e): 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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    Standort Signatur Erwartet Verfügbarkeit
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  • 34
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-09-18
    Beschreibung: 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〉
    Schlagwort(e): 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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  • 35
    Publikationsdatum: 2007-10-13
    Beschreibung: The catalytic (C) subunit of cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) is inhibited by two classes of regulatory subunits, RI and RII. The RII subunits are substrates as well as inhibitors and do not require adenosine triphosphate (ATP) to form holoenzyme, which distinguishes them from RI subunits. To understand the molecular basis for isoform diversity, we solved the crystal structure of an RIIalpha holoenzyme and compared it to the RIalpha holoenzyme. Unphosphorylated RIIalpha(90-400), a deletion mutant, undergoes major conformational changes as both of the cAMP-binding domains wrap around the C subunit's large lobe. The hallmark of this conformational reorganization is the helix switch in domain A. The C subunit is in an open conformation, and its carboxyl-terminal tail is disordered. This structure demonstrates the conserved and isoform-specific features of RI and RII and the importance of ATP, and also provides a new paradigm for designing isoform-specific activators or antagonists for PKA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4036697/" 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/PMC4036697/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Jian -- Brown, Simon H J -- von Daake, Sventja -- Taylor, Susan S -- GM34921/GM/NIGMS NIH HHS/ -- R01 GM034921/GM/NIGMS NIH HHS/ -- R01 GM034921-23/GM/NIGMS NIH HHS/ -- T32-CA009524/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):274-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932298" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Animals ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit ; Cyclic AMP-Dependent Protein Kinase RIalpha Subunit ; Cyclic AMP-Dependent Protein Kinases/*chemistry/genetics/metabolism ; Holoenzymes/chemistry ; Hydrophobic and Hydrophilic Interactions ; Isoenzymes/chemistry ; Mice ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Standort Signatur Erwartet Verfügbarkeit
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-02-27
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Biodiversity ; Brazil ; *Conservation of Natural Resources/economics ; *Ecosystem ; Plant Development ; *Trees/growth & development
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-05-19
    Beschreibung: 〈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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 38
    Publikationsdatum: 2007-09-01
    Beschreibung: DNA replication in archaea and in eukaryotes share many similarities. We report the structure of an archaeal origin recognition complex protein, ORC1, bound to an origin recognition box, a DNA sequence that is found in multiple copies at replication origins. DNA binding is mediated principally by a C-terminal winged helix domain that inserts deeply into the major and minor grooves, widening them both. However, additional DNA contacts are made with the N-terminal AAA+ domain, which inserts into the minor groove at a characteristic G-rich sequence, inducing a 35 degrees bend in the duplex and providing directionality to the binding site. Both contact regions also induce substantial unwinding of the DNA. The structure provides insight into the initial step in assembly of a replication origin and recruitment of minichromosome maintenance (MCM) helicase to that origin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaudier, Martin -- Schuwirth, Barbara S -- Westcott, Sarah L -- Wigley, Dale B -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1213-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK Clare Hall Laboratories, London Research Institute, Blanche Lane, South Mimms, Potters Bar, Herts EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761880" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aeropyrum/*chemistry/metabolism ; Archaeal Proteins/*chemistry ; Binding Sites ; Crystallography, X-Ray ; DNA, Archaeal/*chemistry/metabolism ; Dimerization ; Models, Molecular ; Nucleic Acid Conformation ; Origin Recognition Complex/*chemistry ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Replication Origin
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  • 39
    Publikationsdatum: 2007-02-03
    Beschreibung: Quantum mechanical analysis of electron tunneling in nine thermally fluctuating cytochrome b562 derivatives reveals two distinct protein-mediated coupling limits. A structure-insensitive regime arises for redox partners coupled through dynamically averaged multiple-coupling pathways (in seven of the nine derivatives) where heme-edge coupling leads to the multiple-pathway regime. A structure-dependent limit governs redox partners coupled through a dominant pathway (in two of the nine derivatives) where axial-ligand coupling generates the single-pathway limit and slower rates. This two-regime paradigm provides a unified description of electron transfer rates in 26 ruthenium-modified heme and blue-copper proteins, as well as in numerous photosynthetic proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3523119/" 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/PMC3523119/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prytkova, Tatiana R -- Kurnikov, Igor V -- Beratan, David N -- R01 GM048043/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):622-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Chemistry and Biochemistry, Duke University, Durham, NC 27708, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272715" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Chemistry, Physical ; Computer Simulation ; Cytochrome b Group/*chemistry/*metabolism ; Cytochromes c/chemistry ; *Electron Transport ; Histidine/chemistry ; Hydrogen Bonding ; Ligands ; Mathematics ; Models, Chemical ; Models, Molecular ; Oxidation-Reduction ; Physicochemical Phenomena ; Protein Conformation ; Protein Folding ; Ruthenium
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    Standort Signatur Erwartet Verfügbarkeit
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  • 40
    facet.materialart.
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-09-01
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Georgescu, Roxana E -- O'Donnell, Mike -- GM38839/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1181-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of DNA Replication, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761872" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate/metabolism ; Aeropyrum/*chemistry/metabolism ; Archaeal Proteins/*chemistry/metabolism ; Binding Sites ; DNA, Archaeal/*chemistry/metabolism ; Dimerization ; Models, Molecular ; Nucleic Acid Conformation ; Origin Recognition Complex/*chemistry/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Replication Origin ; Sulfolobus solfataricus/*chemistry/metabolism
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    Standort Signatur Erwartet Verfügbarkeit
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-11-10
    Beschreibung: Prions are lethal mammalian pathogens composed of aggregated conformational isomers of a host-encoded glycoprotein and which appear to lack nucleic acids. Their unique biology, allied with the public-health risks posed by prion zoonoses such as bovine spongiform encephalopathy, has focused much attention on the molecular basis of prion propagation and the "species barrier" that controls cross-species transmission. Both are intimately linked to understanding how multiple prion "strains" are encoded by a protein-only agent. The underlying mechanisms are clearly of much wider importance, and analogous protein-based inheritance mechanisms are recognized in yeast and fungi. Recent advances suggest that prions themselves are not directly neurotoxic, but rather their propagation involves production of toxic species, which may be uncoupled from infectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collinge, John -- Clarke, Anthony R -- MC_U123160656/Medical Research Council/United Kingdom -- MC_U123192748/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):930-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Prion Unit, Department of Neurodegenerative Disease, UCL Institute of Neurology, London WC1N 3BG, UK. j.collinge@prion.ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991853" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Brain Chemistry ; Humans ; Models, Biological ; PrPC Proteins/chemistry/isolation & purification/metabolism ; PrPSc Proteins/*chemistry/isolation & purification/metabolism/*pathogenicity ; Prion Diseases/*metabolism/*transmission ; Prions/*chemistry/isolation & purification/*pathogenicity ; Protein Conformation ; Protein Folding ; Recombinant Proteins/chemistry ; Species Specificity
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    Standort Signatur Erwartet Verfügbarkeit
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  • 42
    Publikationsdatum: 2007-04-07
    Beschreibung: 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〉
    Schlagwort(e): 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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    Standort Signatur Erwartet Verfügbarkeit
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-09-29
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; Antarctic Regions ; *Biodiversity ; *Ecosystem ; *Eukaryota ; Fossils ; *Ice Cover ; *Invertebrates ; Lichens ; Time
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  • 44
    Publikationsdatum: 2007-08-11
    Beschreibung: 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〉
    Schlagwort(e): 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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  • 45
    Publikationsdatum: 2007-12-08
    Beschreibung: 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〉
    Schlagwort(e): 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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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-11-24
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ranganathan, Rama -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1253-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Green Center for Systems Biology and Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. rama.ranganathan@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18033872" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adrenergic beta-Agonists/chemistry/metabolism ; Adrenergic beta-Antagonists/chemistry/metabolism/pharmacology ; Bacteriophage T4/enzymology ; Binding Sites ; Cell Membrane/chemistry/metabolism ; Immunoglobulin Fab Fragments/metabolism ; Ligands ; Muramidase/chemistry/metabolism ; Propanolamines/chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Adrenergic, beta-2/*chemistry/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Rhodopsin/chemistry/metabolism ; Signal Transduction
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  • 47
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-12-15
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; Australia ; China ; *Ecosystem ; Female ; Hemiptera/classification/genetics/*physiology ; Male ; Population Dynamics ; Reproduction ; *Sexual Behavior, Animal
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 48
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-06
    Beschreibung: 〈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〉
    Schlagwort(e): *Agriculture ; Animals ; *Animals, Domestic ; Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; Environment ; *Plants ; Policy Making ; Population Density ; Rain ; Systems Theory
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 49
    Publikationsdatum: 2007-04-14
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 50
    Publikationsdatum: 2007-05-19
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 51
    Publikationsdatum: 2007-01-06
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 52
    Publikationsdatum: 2007-05-15
    Beschreibung: 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〉
    Schlagwort(e): Animals ; Biodiversity ; *Desert Climate ; Ecology ; *Ecosystem ; *Environment ; Humans ; Public Policy ; Soil
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 53
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-04-14
    Beschreibung: 〈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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-03-17
    Beschreibung: 〈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〉
    Schlagwort(e): Antarctic Regions ; Arctic Regions ; *Cold Climate ; *Ecosystem ; Geological Phenomena ; Geology ; Ice Cover ; Interdisciplinary Communication ; International Cooperation ; *Science
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-09-22
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nies, Dietrich H -- New York, N.Y. -- Science. 2007 Sep 21;317(5845):1695-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Microbiology, Martin-Luther-University Halle-Wittenberg, 06099 Halle/Saale, Germany. d.nies@mikrobiologie.uni-halle.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17885121" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry/*metabolism ; Homeostasis ; Membrane Transport Proteins/chemistry/*metabolism ; Protein Conformation ; Zinc/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 56
    Publikationsdatum: 2007-03-10
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 57
    Publikationsdatum: 2007-04-28
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-08-25
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 59
    Publikationsdatum: 2007-03-10
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 60
    Publikationsdatum: 2007-09-18
    Beschreibung: 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〉
    Schlagwort(e): 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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  • 61
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-12-08
    Beschreibung: 〈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〉
    Schlagwort(e): Biological Evolution ; Crops, Agricultural/genetics/*growth & development ; *Ecosystem ; *Plant Development ; Plant Roots/genetics/growth & development/*physiology ; Plants/genetics ; Selection, Genetic
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  • 62
    Publikationsdatum: 2007-06-16
    Beschreibung: 〈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〉
    Schlagwort(e): *Agriculture ; Animals ; *Animals, Domestic ; *Biodiversity ; *Ecosystem ; Population Density
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 63
    Publikationsdatum: 2007-06-16
    Beschreibung: Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4. Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively. MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined. The phosphorylated glucosamine moieties are located at the entrance to the cavity. These structures suggest that MD-2 plays a principal role in endotoxin recognition and provide a basis for antiseptic drug development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohto, Umeharu -- Fukase, Koichi -- Miyake, Kensuke -- Satow, Yoshinori -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1632-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569869" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Crystallography, X-Ray ; Fatty Acids/chemistry ; Glycolipids/*chemistry/metabolism ; Glycosylation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Lipid A/*analogs & derivatives/chemistry/metabolism ; Lymphocyte Antigen 96/*chemistry/metabolism ; Models, Molecular ; Phosphorylation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary
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  • 64
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-09-18
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Anthozoa ; Conservation of Natural Resources ; *Diving ; *Ecosystem ; Travel
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 65
    Publikationsdatum: 2007-08-11
    Beschreibung: Na+/H+ antiporters are central to cellular salt and pH homeostasis. The structure of Escherichia coli NhaA was recently determined, but its mechanisms of transport and pH regulation remain elusive. We performed molecular dynamics simulations of NhaA that, with existing experimental data, enabled us to propose an atomically detailed model of antiporter function. Three conserved aspartates are key to our proposed mechanism: Asp164 (D164) is the Na+-binding site, D163 controls the alternating accessibility of this binding site to the cytoplasm or periplasm, and D133 is crucial for pH regulation. Consistent with experimental stoichiometry, two protons are required to transport a single Na+ ion: D163 protonates to reveal the Na+-binding site to the periplasm, and subsequent protonation of D164 releases Na+. Additional mutagenesis experiments further validated the model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arkin, Isaiah T -- Xu, Huafeng -- Jensen, Morten O -- Arbely, Eyal -- Bennett, Estelle R -- Bowers, Kevin J -- Chow, Edmond -- Dror, Ron O -- Eastwood, Michael P -- Flitman-Tene, Ravenna -- Gregersen, Brent A -- Klepeis, John L -- Kolossvary, Istvan -- Shan, Yibing -- Shaw, David E -- New York, N.Y. -- Science. 2007 Aug 10;317(5839):799-803.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉D. E. Shaw Research, New York, NY 10036, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17690293" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aspartic Acid/metabolism ; Binding Sites ; Computer Simulation ; Crystallization ; Cytoplasm/metabolism ; Escherichia coli/growth & development/*metabolism ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Ion Transport ; *Models, Biological ; Models, Molecular ; Mutagenesis ; Periplasm/metabolism ; Protein Conformation ; Protein Structure, Secondary ; *Protons ; Sodium/*metabolism ; Sodium-Hydrogen Antiporter/*chemistry/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 66
    Publikationsdatum: 2007-04-07
    Beschreibung: Kinesin-1 is a two-headed molecular motor that walks along microtubules, with each step gated by adenosine triphosphate (ATP) binding. Existing models for the gating mechanism propose a role for the microtubule lattice. We show that unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate (ADP). With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable ATP analog, each kinesin-1 dimer binds two tubulin heterodimers. The data reveal an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of a steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2504013/" 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/PMC2504013/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alonso, Maria C -- Drummond, Douglas R -- Kain, Susan -- Hoeng, Julia -- Amos, Linda -- Cross, Robert A -- G0200542/Medical Research Council/United Kingdom -- G0200542(63814)/Medical Research Council/United Kingdom -- MC_U105184313/Medical Research Council/United Kingdom -- U.1051.04.002(78842)/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Motors Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412962" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/*metabolism ; Adenylyl Imidodiphosphate/metabolism ; Animals ; Binding Sites ; Dimerization ; Kinesin/chemistry/*metabolism ; Microtubules/*metabolism ; Models, Biological ; Molecular Motor Proteins/*metabolism ; Neurospora ; Protein Conformation ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Schizosaccharomyces ; Tubulin/chemistry/*metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 67
    Publikationsdatum: 2007-06-16
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 68
    Publikationsdatum: 2007-11-10
    Beschreibung: DNA polymerase eta (Pol eta) is a eukaryotic lesion bypass polymerase that helps organisms to survive exposure to ultraviolet (UV) radiation, and tumor cells to gain resistance against cisplatin-based chemotherapy. It allows cells to replicate across cross-link lesions such as 1,2-d(GpG) cisplatin adducts (Pt-GG) and UV-induced cis-syn thymine dimers. We present structural and biochemical analysis of how Pol eta copies Pt-GG-containing DNA. The damaged DNA is bound in an open DNA binding rim. Nucleotidyl transfer requires the DNA to rotate into an active conformation, driven by hydrogen bonding of the templating base to the dNTP. For the 3'dG of the Pt-GG, this step is accomplished by a Watson-Crick base pair to dCTP and is biochemically efficient and accurate. In contrast, bypass of the 5'dG of the Pt-GG is less efficient and promiscuous for dCTP and dATP as a result of the presence of the rigid Pt cross-link. Our analysis reveals the set of structural features that enable Pol eta to replicate across strongly distorting DNA lesions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alt, Aaron -- Lammens, Katja -- Chiocchini, Claudia -- Lammens, Alfred -- Pieck, J Carsten -- Kuch, David -- Hopfner, Karl-Peter -- Carell, Thomas -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):967-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Munich Center for Integrated Protein Science (CiPS), Ludwig Maximilians University, D-81377 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991862" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Antineoplastic Agents/metabolism/*pharmacology ; Base Pairing ; Binding Sites ; Cisplatin/analogs & derivatives/chemistry/metabolism/*pharmacology ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Adducts/chemistry/*metabolism ; *DNA Damage ; DNA Replication ; DNA-Directed DNA Polymerase/chemistry/genetics/*metabolism ; Deoxycytosine Nucleotides/chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Tertiary ; Templates, Genetic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 69
    Publikationsdatum: 2007-12-15
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 70
    Publikationsdatum: 2007-08-19
    Beschreibung: 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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 71
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-05-19
    Beschreibung: 〈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〉
    Schlagwort(e): 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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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 72
    Publikationsdatum: 2007-08-25
    Beschreibung: 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〉
    Schlagwort(e): Atmosphere ; *Ecosystem ; Iron/*analysis ; Oceans and Seas ; Oxygen/analysis ; Phytoplankton/*growth & development ; Seasons ; *Seawater/chemistry ; *Wind
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  • 73
    Publikationsdatum: 2007-07-07
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; *Rhizophoraceae ; *Trees
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 74
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-12-15
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Anthozoa ; *Ecosystem ; *Fishes/physiology ; *Food Chain ; Pacific Islands ; Population Dynamics ; Predatory Behavior
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 75
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-05-05
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Anthozoa/physiology ; *Conservation of Natural Resources ; *Ecosystem ; Pacific Ocean ; Palau ; Temperature
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 76
    facet.materialart.
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-06
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seringhaus, Michael -- Gerstein, Mark -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):40-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204626" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bibliometrics ; Chemical Phenomena ; *Chemistry ; Crystallography ; Molecular Structure ; *Nobel Prize ; Protein Conformation ; PubMed
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-08-19
    Beschreibung: 〈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〉
    Schlagwort(e): Biomass ; *Cellulose ; *Ecosystem ; *Energy-Generating Resources ; *Plant Physiological Phenomena
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 78
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-12-01
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kintisch, Eli -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1368-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048662" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Carbon Dioxide/metabolism ; *Ecosystem ; Eukaryota/*growth & development/metabolism ; *Eutrophication ; Food Chain ; Greenhouse Effect ; *Iron/metabolism ; Nitrous Oxide/metabolism ; Oceanography/*methods ; Phytoplankton/growth & development/metabolism ; *Seawater
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  • 79
    Publikationsdatum: 2007-12-15
    Beschreibung: PIK3CA, one of the two most frequently mutated oncogenes in human tumors, codes for p110alpha, the catalytic subunit of a phosphatidylinositol 3-kinase, isoform alpha (PI3Kalpha, p110alpha/p85). Here, we report a 3.0 angstrom resolution structure of a complex between p110alpha and a polypeptide containing the p110alpha-binding domains of p85alpha, a protein required for its enzymatic activity. The structure shows that many of the mutations occur at residues lying at the interfaces between p110alpha and p85alpha or between the kinase domain of p110alpha and other domains within the catalytic subunit. Disruptions of these interactions are likely to affect the regulation of kinase activity by p85 or the catalytic activity of the enzyme, respectively. In addition to providing new insights about the structure of PI3Kalpha, these results suggest specific mechanisms for the effect of oncogenic mutations in p110alpha and p85alpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Chuan-Hsiang -- Mandelker, Diana -- Schmidt-Kittler, Oleg -- Samuels, Yardena -- Velculescu, Victor E -- Kinzler, Kenneth W -- Vogelstein, Bert -- Gabelli, Sandra B -- Amzel, L Mario -- CA 43460/CA/NCI NIH HHS/ -- GM 07184/GM/NIGMS NIH HHS/ -- GM066895/GM/NIGMS NIH HHS/ -- GM07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1744-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079394" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Triphosphate ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Phosphatidylinositol 3-Kinases/*chemistry/genetics/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/genetics/metabolism ; src Homology Domains
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 80
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-12-15
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1712-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079377" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Anthozoa/growth & development/*physiology ; Biodiversity ; Cues ; *Ecosystem ; Eukaryota/physiology ; Larva/growth & development ; Reproduction ; Seasons ; Seawater ; Symbiosis ; Temperature
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 81
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-04-14
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCauley, Douglas J -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):200-1; author reply 200-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431154" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Biomass ; Conservation of Natural Resources ; *Ecosystem ; Fisheries ; Pacific Ocean ; Population Dynamics ; Predatory Behavior ; *Sharks ; *Tuna
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 82
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-03-03
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Settele, Josef -- Kuhn, Ingolf -- Klotz, Stefan -- Hammen, Volker -- Spangenberg, Joachim -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1220.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17332393" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Biodiversity ; Economics ; *Ecosystem ; Environment ; *European Union ; *Interdisciplinary Communication ; *Research
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 83
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-03-10
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koenig, Robert -- New York, N.Y. -- Science. 2007 Mar 9;315(5817):1349.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17347418" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Behavior, Animal ; *Ecosystem ; *Elephants ; Population Control ; Population Density ; Population Growth ; South Africa
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-06
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Tobias -- Overgaard, Johannes -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):49-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoophysiology, Aarhus University, 8000 Aarhus, Denmark. tobias.wang@biology.au.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204631" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acclimatization ; Aerobiosis ; Animals ; Cardiac Output ; *Ecosystem ; *Greenhouse Effect ; Heart/*physiology ; Oceans and Seas ; Oxygen/analysis/blood/*metabolism ; Oxygen Consumption ; Perciformes/*physiology ; Population Density ; Population Dynamics ; Seasons ; Seawater/chemistry ; Temperature
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 85
    facet.materialart.
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-03-03
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shea, Katriona -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1231-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and the Intercollege Graduate Degree Program in Ecology, Pennsylvania State University, 208 Mueller Laboratory, University Park, PA 16802, USA. k-shea@psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17332401" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Birds ; *Ecosystem ; Feces ; Fruit ; *Gene Flow ; Genes, Plant ; *Mammals ; Movement ; Pollen ; Prunus/*genetics ; Seeds/*genetics ; Trees/*genetics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 86
    Publikationsdatum: 2007-12-08
    Beschreibung: Regulated intramembrane proteolysis by members of the site-2 protease (S2P) family is an important signaling mechanism conserved from bacteria to humans. Here we report the crystal structure of the transmembrane core domain of an S2P metalloprotease from Methanocaldococcus jannaschii. The protease consists of six transmembrane segments, with the catalytic zinc atom coordinated by two histidine residues and one aspartate residue approximately 14 angstroms into the lipid membrane surface. The protease exhibits two distinct conformations in the crystals. In the closed conformation, the active site is surrounded by transmembrane helices and is impermeable to substrate peptide; water molecules gain access to zinc through a polar, central channel that opens to the cytosolic side. In the open conformation, transmembrane helices alpha1 and alpha6 separate from each other by 10 to 12 angstroms, exposing the active site to substrate entry. The structure reveals how zinc embedded in an integral membrane protein can catalyze peptide cleavage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Liang -- Yan, Hanchi -- Wu, Zhuoru -- Yan, Nieng -- Wang, Zhe -- Jeffrey, Philip D -- Shi, Yigong -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1608-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063795" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Archaeal Proteins/chemistry/metabolism ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Catalysis ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Membrane Proteins/*chemistry/metabolism ; Metalloendopeptidases/*chemistry/metabolism ; Methanococcus/*enzymology ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Water ; Zinc/chemistry
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 87
    Publikationsdatum: 2007-05-19
    Beschreibung: Episodic eddy-driven upwelling may supply a significant fraction of the nutrients required to sustain primary productivity of the subtropical ocean. New observations in the northwest Atlantic reveal that, although plankton blooms occur in both cyclones and mode-water eddies, the biological responses differ. Mode-water eddies can generate extraordinary diatom biomass and primary production at depth, relative to the time series near Bermuda. These blooms are sustained by eddy/wind interactions, which amplify the eddy-induced upwelling. In contrast, eddy/wind interactions dampen eddy-induced upwelling in cyclones. Carbon export inferred from oxygen anomalies in eddy cores is one to three times as much as annual new production for the region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGillicuddy, Dennis J Jr -- Anderson, Laurence A -- Bates, Nicholas R -- Bibby, Thomas -- Buesseler, Ken O -- Carlson, Craig A -- Davis, Cabell S -- Ewart, Courtney -- Falkowski, Paul G -- Goldthwait, Sarah A -- Hansell, Dennis A -- Jenkins, William J -- Johnson, Rodney -- Kosnyrev, Valery K -- Ledwell, James R -- Li, Qian P -- Siegel, David A -- Steinberg, Deborah K -- New York, N.Y. -- Science. 2007 May 18;316(5827):1021-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Woods Hole Oceanographic Institution, Woods Hole, MA 02543-1541, USA. dmcgillicuddy@whoi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510363" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Atlantic Ocean ; Biomass ; Carbon/analysis ; Chlorophyll/analysis ; Cyanobacteria/growth & development/physiology ; Diatoms/growth & development ; *Ecosystem ; Geologic Sediments ; Oxygen/analysis ; Photosynthesis ; Phytoplankton/growth & development/physiology ; Plankton/*growth & development/physiology ; Seasons ; *Seawater/chemistry ; *Water Movements ; *Wind ; Zooplankton/growth & development/physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-02-10
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barber, Richard T -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):777-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289968" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Biomass ; Carbon/*metabolism ; *Ecosystem ; *Food Chain ; Models, Biological ; Oceans and Seas ; Pacific Ocean ; Phytoplankton/growth & development/*physiology ; *Seawater ; Urochordata/physiology ; Zooplankton/growth & development/*physiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 89
    Publikationsdatum: 2007-06-30
    Beschreibung: Leukotrienes are proinflammatory products of arachidonic acid oxidation by 5-lipoxygenase that have been shown to be involved in respiratory and cardiovascular diseases. The integral membrane protein FLAP is essential for leukotriene biosynthesis. We describe the x-ray crystal structures of human FLAP in complex with two leukotriene biosynthesis inhibitors at 4.0 and 4.2 angstrom resolution, respectively. The structures show that inhibitors bind in membrane-embedded pockets of FLAP, which suggests how these inhibitors prevent arachidonic acid from binding to FLAP and subsequently being transferred to 5-lipoxygenase, thereby preventing leukotriene biosynthesis. This structural information provides a platform for the development of therapeutics for respiratory and cardiovascular diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, Andrew D -- McKeever, Brian M -- Xu, Shihua -- Wisniewski, Douglas -- Miller, Douglas K -- Yamin, Ting-Ting -- Spencer, Robert H -- Chu, Lin -- Ujjainwalla, Feroze -- Cunningham, Barry R -- Evans, Jilly F -- Becker, Joseph W -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):510-2. Epub 2007 Jun 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicinal Chemistry, Merck Research Laboratories, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600184" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 5-Lipoxygenase-Activating Proteins ; Arachidonate 5-Lipoxygenase/metabolism ; Arachidonic Acid/metabolism ; Binding Sites ; Carrier Proteins/antagonists & inhibitors/*chemistry/genetics/metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Cytosol/chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Indoles/*chemistry/metabolism/pharmacology ; Membrane Proteins/antagonists & inhibitors/*chemistry/genetics/metabolism ; Models, Molecular ; Mutagenesis ; Nuclear Envelope/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Quinolines/*chemistry/metabolism/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-07-07
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inman, Mason -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):35-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615316" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Antarctic Regions ; Bacteria/classification/*isolation & purification ; Bacterial Physiological Phenomena ; Colony Count, Microbial ; *Ecosystem ; Fresh Water ; Geologic Sediments/*microbiology ; Ice ; Ice Cover/*microbiology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 91
    Publikationsdatum: 2007-01-16
    Beschreibung: As compared with extensive contiguous areas, small isolated habitat patches lack many species. Some species disappear after isolation; others are rarely found in any small patch, regardless of isolation. We used a 13-year data set of bird captures from a large landscape-manipulation experiment in a Brazilian Amazon forest to model the extinction-colonization dynamics of 55 species and tested basic predictions of island biogeography and metapopulation theory. From our models, we derived two metrics of species vulnerability to changes in isolation and patch area. We found a strong effect of area and a variable effect of isolation on the predicted patch occupancy by birds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferraz, Goncalo -- Nichols, James D -- Hines, James E -- Stouffer, Philip C -- Bierregaard, Richard O Jr -- Lovejoy, Thomas E -- New York, N.Y. -- Science. 2007 Jan 12;315(5809):238-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Dynamics of Forest Fragments Project, Instituto Nacional de Pesquisas da Amazonia, 69011 Manaus AM, Brazil. gferraz@inpa.gov.br〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17218527" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Birds ; Brazil ; *Conservation of Natural Resources ; *Ecosystem ; Extinction, Biological ; Likelihood Functions ; Models, Biological ; Models, Statistical ; Population Dynamics ; *Trees/growth & development
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  • 92
    Publikationsdatum: 2007-06-02
    Beschreibung: Worm et al. (Research Articles, 3 November 2006, p. 787) investigated the importance of biodiversity to marine ecosystem services across temporal and spatial scales. In projecting the extent of future fisheries collapse, we argue that the authors inappropriately extrapolated beyond their available observations and used data on marine reserves and fishery closures that are not representative of global fisheries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holker, Franz -- Beare, Doug -- Dorner, Hendrik -- di Natale, Antonio -- Ratz, Hans-Joachim -- Temming, Axel -- Casey, John -- New York, N.Y. -- Science. 2007 Jun 1;316(5829):1285; author reply 1285.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Commission, Directorate General Joint Research Centre, Institute for the Protection and Security of the Citizen, Agriculture and Fisheries Unit, TP 051, 21020, Italy. franz.hoelker@jrc.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540886" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; *Fisheries ; *Fishes ; Forecasting ; Oceans and Seas ; Population Dynamics
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
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  • 93
    Publikationsdatum: 2007-10-27
    Beschreibung: Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors constitute the largest family of eukaryotic signal transduction proteins that communicate across the membrane. We report the crystal structure of a human beta2-adrenergic receptor-T4 lysozyme fusion protein bound to the partial inverse agonist carazolol at 2.4 angstrom resolution. The structure provides a high-resolution view of a human G protein-coupled receptor bound to a diffusible ligand. Ligand-binding site accessibility is enabled by the second extracellular loop, which is held out of the binding cavity by a pair of closely spaced disulfide bridges and a short helical segment within the loop. Cholesterol, a necessary component for crystallization, mediates an intriguing parallel association of receptor molecules in the crystal lattice. Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopsin as a template model for this large receptor family.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2583103/" 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/PMC2583103/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cherezov, Vadim -- Rosenbaum, Daniel M -- Hanson, Michael A -- Rasmussen, Soren G F -- Thian, Foon Sun -- Kobilka, Tong Sun -- Choi, Hee-Jung -- Kuhn, Peter -- Weis, William I -- Kobilka, Brian K -- Stevens, Raymond C -- F32 GM082028/GM/NIGMS NIH HHS/ -- GM075915/GM/NIGMS NIH HHS/ -- NS028471/NS/NINDS NIH HHS/ -- P50 GM062411/GM/NIGMS NIH HHS/ -- P50 GM073197/GM/NIGMS NIH HHS/ -- P50 GM073197-04/GM/NIGMS NIH HHS/ -- R01 GM056169/GM/NIGMS NIH HHS/ -- R01 GM089857/GM/NIGMS NIH HHS/ -- R21 GM075811/GM/NIGMS NIH HHS/ -- U54 GM074961/GM/NIGMS NIH HHS/ -- U54 GM074961-030001/GM/NIGMS NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1258-65. Epub 2007 Oct 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962520" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacteriophage T4/enzymology ; Binding Sites ; Cell Membrane/chemistry/metabolism ; Cholesterol/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Drug Inverse Agonism ; Humans ; Ligands ; Models, Molecular ; Muramidase/chemistry/metabolism ; Propanolamines/chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Adrenergic, beta-2/*chemistry/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Rhodopsin/chemistry/metabolism ; Static Electricity
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 94
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-03-31
    Beschreibung: Anthropogenic-driven accumulation of carbon dioxide in the atmosphere and projected ocean acidification have raised concerns regarding the eventual impact on coral reefs. This study demonstrates that skeleton-producing corals grown in acidified experimental conditions are able to sustain basic life functions, including reproductive ability, in a sea anemone-like form and will resume skeleton building when reintroduced to normal modern marine conditions. These results support the existence of physiological refugia, allowing corals to alternate between nonfossilizing soft-body ecophenotypes and fossilizing skeletal forms in response to changes in ocean chemistry. This refugia, however, does not undermine the threats to reef ecosystems in a high carbon dioxide world.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fine, Maoz -- Tchernov, Dan -- New York, N.Y. -- Science. 2007 Mar 30;315(5820):1811.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, 52900, Israel. finema@mail.biu.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395821" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Anthozoa/*anatomy & histology/*physiology ; Biomass ; Calcification, Physiologic ; Calcium Carbonate/analysis ; Carbon Dioxide ; *Ecosystem ; Eukaryota/physiology ; Hydrogen-Ion Concentration ; Seawater/chemistry ; Symbiosis
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 95
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-07-28
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):442-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17656696" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; California ; *Conservation of Natural Resources ; *Ecosystem ; Fishes ; *Fresh Water ; Population Dynamics ; *Rivers ; *Salmoniformes ; Water Supply
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    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 96
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-16
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pedros-Alio, Carlos -- New York, N.Y. -- Science. 2007 Jan 12;315(5809):192-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Marine Biology and Oceanography, Institut de Ciencies del Mar, CMIMA-CSIC, Barcelona E-08003, Spain. cpedros@icm.csic.es〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17218512" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Bacteria/classification/genetics/growth & development/isolation & purification ; *Biodiversity ; *Ecosystem ; Eukaryota/classification/isolation & purification ; Gene Library ; Genes, Bacterial ; Genes, rRNA ; Oceans and Seas ; Polymerase Chain Reaction ; Seawater/*microbiology ; Sequence Analysis, DNA
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 97
    Publikationsdatum: 2007-11-03
    Beschreibung: Quinoxalinedione compounds such as 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX) are the most commonly used alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor antagonists. However, we find that in the presence of transmembrane AMPA receptor regulatory proteins (TARPs), which are AMPA receptor auxiliary subunits, CNQX acts as a partial agonist. CNQX induced small depolarizing currents in neurons of the central nervous system, and reconstitution of this agonist activity required coexpression of TARPs. A crystal structure of CNQX bound to the TARP-less AMPA receptor ligand-binding domain showed that, although CNQX induces partial domain closure, this movement is not transduced into linker separation, suggesting that TARPs may increase agonist efficacy by strengthening the coupling between domain closure and channel opening. Our results demonstrate that the presence of an auxiliary subunit can determine whether a compound functions as an agonist or antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Menuz, Karen -- Stroud, Robert M -- Nicoll, Roger A -- Hays, Franklin A -- GM078754/GM/NIGMS NIH HHS/ -- P50 GM73210/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):815-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California at San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17975069" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 6-Cyano-7-nitroquinoxaline-2,3-dione/chemistry/*pharmacology ; Animals ; Benzodiazepines/pharmacology ; Binding, Competitive ; Cell Line ; Cerebellum/cytology ; Crystallography, X-Ray ; *Drug Partial Agonism ; Hippocampus/cytology ; Humans ; In Vitro Techniques ; Interneurons/drug effects ; Mice ; Models, Molecular ; Patch-Clamp Techniques ; Protein Conformation ; Protein Subunits/*physiology ; Pyramidal Cells/drug effects/metabolism ; Quinoxalines/pharmacology ; Receptors, AMPA/*agonists/*antagonists & inhibitors ; Structure-Activity Relationship ; Synaptic Transmission/drug effects ; Trichlormethiazide/pharmacology
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 98
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-01-06
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204613" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Arctic Regions ; Biodiversity ; *Ecosystem ; Extinction, Biological ; *Greenhouse Effect ; *Ice Cover ; Population Density ; United States ; United States Government Agencies ; *Ursidae
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 99
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2007-05-15
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, Douglas -- New York, N.Y. -- Science. 2007 May 11;316(5826):823-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17495151" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Biodiversity ; *Climate ; *Ecosystem ; *Forecasting ; Models, Theoretical ; North America ; Trees ; Tropical Climate
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 100
    Publikationsdatum: 2007-12-01
    Beschreibung: Anaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO2 at a complex Ni-, Fe-, and S-containing metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO2 supplied in solution is bound and reductively activated by cluster C. In the intermediate structure, CO2 acts as a bridging ligand between Ni and the asymmetrically coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidation and CO2 reduction at the Ni-Fe site of cluster C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeoung, Jae-Hun -- Dobbek, Holger -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1461-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratorium Proteinkristallographie and Forschungszentrum fur Bio-Makromolekule, Universitat Bayreuth, D-95440 Bayreuth, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048691" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aldehyde Oxidoreductases/chemistry/isolation & purification/*metabolism ; Anaerobiosis ; Binding Sites ; Carbon Dioxide/*metabolism ; Carbon Monoxide/metabolism ; Crystallization ; Crystallography, X-Ray ; Iron/chemistry/metabolism ; Ligands ; Multienzyme Complexes/chemistry/isolation & purification/*metabolism ; Nickel/chemistry/metabolism ; Peptococcaceae/*enzymology ; Protein Conformation ; Recombinant Proteins/chemistry/isolation & purification/metabolism
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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