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  • *Ecosystem  (563)
  • Models, Molecular  (246)
  • Binding Sites
  • American Association for the Advancement of Science (AAAS)  (921)
  • American Chemical Society (ACS)
  • 2005-2009  (921)
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  • 1
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    Local DNA topography correlates with functional noncoding regions of the human genome (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-17
    Description: The three-dimensional molecular structure of DNA, specifically the shape of the backbone and grooves of genomic DNA, can be dramatically affected by nucleotide changes, which can cause differences in protein-binding affinity and phenotype. We developed an algorithm to measure constraint on the basis of similarity of DNA topography among multiple species, using hydroxyl radical cleavage patterns to interrogate the solvent-accessible surface area of DNA. This algorithm found that 12% of bases in the human genome are evolutionarily constrained-double the number detected by nucleotide sequence-based algorithms. Topography-informed constrained regions correlated with functional noncoding elements, including enhancers, better than did regions identified solely on the basis of nucleotide sequence. These results support the idea that the molecular shape of DNA is under selection and can identify evolutionary history.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2749491/" 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/PMC2749491/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parker, Stephen C J -- Hansen, Loren -- Abaan, Hatice Ozel -- Tullius, Thomas D -- Margulies, Elliott H -- R01 HG003541/HG/NHGRI NIH HHS/ -- R01 HG003541-03/HG/NHGRI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2009 Apr 17;324(5925):389-92. doi: 10.1126/science.1169050. Epub 2009 Mar 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bioinformatics Program, Boston University, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19286520" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Motifs ; Base Sequence ; Binding Sites ; Conserved Sequence ; DNA/*chemistry/genetics ; Deoxyribonuclease I/metabolism ; Early Growth Response Protein 1/genetics/metabolism ; Evolution, Molecular ; *Genome, Human ; Humans ; Mutant Proteins/metabolism ; Nucleic Acid Conformation ; Phenotype ; Polymorphism, Single Nucleotide ; Selection, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Coevolution of plants and their pathogens in natural habitats (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-09
    Description: Understanding of plant-pathogen coevolution in natural systems continues to develop as new theories at the population and species level are increasingly informed by studies unraveling the molecular basis of interactions between individual plants and their pathogens. The next challenge lies in further integration of these approaches to develop a comprehensive picture of how life history traits of both players interact with the environment to shape evolutionary trajectories.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2689373/" 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/PMC2689373/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burdon, Jeremy J -- Thrall, Peter H -- R01 GM074265-01A2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 May 8;324(5928):755-6. doi: 10.1126/science.1171663.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Commonwealth Scientific and Industrial Research Organization (CSIRO)-Plant Industry, Post Office Box 1600, Canberra, ACT 2601, Australia. Jeremy.Burdon@csiro.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19423818" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; *Ecosystem ; Fungal Proteins/genetics/metabolism ; Fungi/genetics/*pathogenicity/physiology ; *Host-Pathogen Interactions ; Immunity, Innate ; Plant Diseases/immunology/*microbiology ; Plant Proteins/genetics/metabolism ; Plants/genetics/immunology/metabolism/*microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Soil microbial communities and restoration ecology: facilitators or followers? (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: Microorganisms have critical roles in the functioning of soil in nutrient cycling, structural formation, and plant interactions, both positive and negative. These roles are important in reestablishing function and biodiversity in ecosystem restoration. Measurement of the community indicates the status of the system in relation to restoration targets and the effectiveness of management interventions, and manipulation of the community shows promise in the enhancement of the rate of recovery of degraded systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harris, Jim -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):573-4. doi: 10.1126/science.1172975.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Natural Resources, Cranfield University, Cranfield, Bedfordshire MK43 0AL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644111" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Physiological Phenomena ; Biodiversity ; *Conservation of Natural Resources ; *Ecosystem ; Fungi/*physiology ; Mycorrhizae/*physiology ; Plant Physiological Phenomena ; *Soil Microbiology ; Symbiosis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Restoration of ecosystem services for environmental markets (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: Ecological restoration is an activity that ideally results in the return of an ecosystem to an undisturbed state. Ecosystem services are the benefits humans derive from ecosystems. The two have been joined to support growing environmental markets with the goal of creating restoration-based credits that can be bought and sold. However, the allure of these markets may be overshadowing shortcomings in the science and practice of ecological restoration. Before making risky investments, we must understand why and when restoration efforts fall short of recovering the full suite of ecosystem services, what can be done to improve restoration success, and why direct measurement of the biophysical processes that support ecosystem services is the only way to guarantee the future success of these markets. Without new science and an oversight framework to protect the ecosystem service assets which people depend, markets could actually accelerate environmental degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palmer, Margaret A -- Filoso, Solange -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):575-6. doi: 10.1126/science.1172976.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chesapeake Biological Laboratory, University of Maryland Center for Environmental Science, Solomons, MD 20688, USA. mpalmer@umd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644112" target="_blank"〉PubMed〈/a〉
    Keywords: Biodiversity ; Biophysical Processes ; *Conservation of Natural Resources ; *Ecosystem ; *Environment ; Humans ; Wetlands
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Disruption of vertical motility by shear triggers formation of thin phytoplankton layers (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-02-21
    Description: Thin layers of phytoplankton are important hotspots of ecological activity that are found in the coastal ocean, meters beneath the surface, and contain cell concentrations up to two orders of magnitude above ambient concentrations. Current interpretations of their formation favor abiotic processes, yet many phytoplankton species found in these layers are motile. We demonstrated that layers formed when the vertical migration of phytoplankton was disrupted by hydrodynamic shear. This mechanism, which we call gyrotactic trapping, can be responsible for the thin layers of phytoplankton commonly observed in the ocean. These results reveal that the coupling between active microorganism motility and ambient fluid motion can shape the macroscopic features of the marine ecological landscape.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Durham, William M -- Kessler, John O -- Stocker, Roman -- New York, N.Y. -- Science. 2009 Feb 20;323(5917):1067-70. doi: 10.1126/science.1167334.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Civil and Environmental Engineering, Massachusetts Institute of Technology (MIT), Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19229037" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biomechanical Phenomena ; Cell Shape ; Chlamydomonas/cytology/*physiology ; *Ecosystem ; Flagella ; Gravitation ; Movement ; Phytoplankton/cytology/*physiology ; *Water ; *Water Movements
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Ecology. Seeing the big picture on microbe distribution (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-09-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patterson, David J -- New York, N.Y. -- Science. 2009 Sep 18;325(5947):1506-7. doi: 10.1126/science.1179690.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Encyclopedia of Life, Biodiversity Informatics, Marine Biological Laboratory, Woods Hole, MA 02543, USA. dpatterson@eol.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19762632" target="_blank"〉PubMed〈/a〉
    Keywords: Arctic Regions ; *Bacteria/classification ; Bacterial Physiological Phenomena ; Biodiversity ; *Diatoms ; *Ecosystem ; Geologic Sediments/*microbiology ; Seawater/*microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Basin-scale coherence in phenology of shrimps and phytoplankton in the North Atlantic Ocean (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-09
    Description: Climate change could lead to mismatches between the reproductive cycles of marine organisms and their planktonic food. We tested this hypothesis by comparing shrimp (Pandalus borealis) egg hatching times and satellite-derived phytoplankton bloom dynamics throughout the North Atlantic. At large spatial and long temporal (10 years or longer) scales, hatching was correlated with the timing of the spring phytoplankton bloom. Annual egg development and hatching times were determined locally by bottom water temperature. We conclude that different populations of P. borealis have adapted to local temperatures and bloom timing, matching egg hatching to food availability under average conditions. This strategy is vulnerable to interannual oceanographic variability and long-term climatic changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koeller, P -- Fuentes-Yaco, C -- Platt, T -- Sathyendranath, S -- Richards, A -- Ouellet, P -- Orr, D -- Skuladottir, U -- Wieland, K -- Savard, L -- Aschan, M -- New York, N.Y. -- Science. 2009 May 8;324(5928):791-3. doi: 10.1126/science.1170987.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Fisheries and Oceans, Bedford Institute of Oceanography, Post Office Box 1006, Dartmouth, B2Y 4A2 Nova Scotia, Canada. koellerp@mar.dfo-mpo.gc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19423827" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atlantic Ocean ; Climate ; *Cold Temperature ; *Ecosystem ; Female ; Ovum/growth & development/physiology ; Pandalidae/*physiology ; Phytoplankton/*physiology ; Population Dynamics ; Reproduction ; Seasons ; *Seawater
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Oxygen-18 of O2 records the impact of abrupt climate change on the terrestrial biosphere (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-13
    Description: Photosynthesis and respiration occur widely on Earth's surface, and the 18O/16O ratio of the oxygen produced and consumed varies with climatic conditions. As a consequence, the history of climate is reflected in the deviation of the 18O/16O of air (delta18Oatm) from seawater delta18O (known as the Dole effect). We report variations in delta18Oatm over the past 60,000 years related to Heinrich and Dansgaard-Oeschger events, two modes of abrupt climate change observed during the last ice age. Correlations with cave records support the hypothesis that the Dole effect is primarily governed by the strength of the Asian and North African monsoons and confirm that widespread changes in low-latitude terrestrial rainfall accompanied abrupt climate change. The rapid delta18Oatm changes can also be used to synchronize ice records by providing global time markers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Severinghaus, Jeffrey P -- Beaudette, Ross -- Headly, Melissa A -- Taylor, Kendrick -- Brook, Edward J -- New York, N.Y. -- Science. 2009 Jun 12;324(5933):1431-4. doi: 10.1126/science.1169473.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Institution of Oceanography, University of California, San Diego, CA 92093-0244, USA. jseveringhaus@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19520957" target="_blank"〉PubMed〈/a〉
    Keywords: Antarctic Regions ; Atmosphere/*chemistry ; *Climatic Processes ; *Ecosystem ; Ice Cover/*chemistry ; Oxygen/*analysis ; Oxygen Isotopes/*analysis ; Photosynthesis ; Rain ; Seawater/chemistry ; Time
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: Simocyclinones are bifunctional antibiotics that inhibit bacterial DNA gyrase by preventing DNA binding to the enzyme. We report the crystal structure of the complex formed between the N-terminal domain of the Escherichia coli gyrase A subunit and simocyclinone D8, revealing two binding pockets that separately accommodate the aminocoumarin and polyketide moieties of the antibiotic. These are close to, but distinct from, the quinolone-binding site, consistent with our observations that several mutations in this region confer resistance to both agents. Biochemical studies show that the individual moieties of simocyclinone D8 are comparatively weak inhibitors of gyrase relative to the parent compound, but their combination generates a more potent inhibitor. Our results should facilitate the design of drug molecules that target these unexploited binding pockets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edwards, Marcus J -- Flatman, Ruth H -- Mitchenall, Lesley A -- Stevenson, Clare E M -- Le, Tung B K -- Clarke, Thomas A -- McKay, Adam R -- Fiedler, Hans-Peter -- Buttner, Mark J -- Lawson, David M -- Maxwell, Anthony -- Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2009 Dec 4;326(5958):1415-8. doi: 10.1126/science.1179123.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, John Innes Centre, Colney, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965760" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/chemistry/metabolism/pharmacology ; Binding Sites ; Coumarins/chemistry/metabolism/pharmacology ; Crystallography, X-Ray ; DNA Gyrase/*chemistry/genetics/*metabolism ; DNA, Bacterial/metabolism ; Drug Resistance, Bacterial ; Escherichia coli/drug effects/*enzymology/genetics ; Glycosides/chemistry/metabolism/pharmacology ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Site-Directed ; Mutation ; Protein Multimerization ; Protein Structure, Tertiary ; Topoisomerase II Inhibitors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Stability predicts genetic diversity in the Brazilian Atlantic forest hotspot (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-02-07
    Description: Biodiversity hotspots, representing regions with high species endemism and conservation threat, have been mapped globally. Yet, biodiversity distribution data from within hotspots are too sparse for effective conservation in the face of rapid environmental change. Using frogs as indicators, ecological niche models under paleoclimates, and simultaneous Bayesian analyses of multispecies molecular data, we compare alternative hypotheses of assemblage-scale response to late Quaternary climate change. This reveals a hotspot within the Brazilian Atlantic forest hotspot. We show that the southern Atlantic forest was climatically unstable relative to the central region, which served as a large climatic refugium for neotropical species in the late Pleistocene. This sets new priorities for conservation in Brazil and establishes a validated approach to biodiversity prediction in other understudied, species-rich regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carnaval, Ana Carolina -- Hickerson, Michael J -- Haddad, Celio F B -- Rodrigues, Miguel T -- Moritz, Craig -- New York, N.Y. -- Science. 2009 Feb 6;323(5915):785-9. doi: 10.1126/science.1166955.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Museum of Vertebrate Zoology, University of California, Berkeley, CA 94720-3160, USA. carnaval@berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19197066" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anura/classification/*genetics ; Bayes Theorem ; *Biodiversity ; Brazil ; Conservation of Natural Resources ; DNA, Mitochondrial/genetics ; Demography ; *Ecosystem ; Geography ; Molecular Sequence Data ; Mutation ; Phylogeny ; Population Dynamics ; Time ; *Trees ; *Tropical Climate
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
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    Unleashing an army to repair alien-ravaged ecosystems (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koenig, Robert -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):562-3. doi: 10.1126/science.325_562.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644106" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Conservation of Natural Resources/economics/methods ; *Ecosystem ; Insects ; Plant Development ; *Plants ; South Africa ; Water Supply
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 12
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    Structure and mechanism of a Na+-independent amino acid transporter (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-07-18
    Description: Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2851542/" 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/PMC2851542/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaffer, Paul L -- Goehring, April -- Shankaranarayanan, Aruna -- Gouaux, Eric -- R01 MH070039/MH/NIMH NIH HHS/ -- R01 MH070039-05/MH/NIMH NIH HHS/ -- T32 GM008281/GM/NIGMS NIH HHS/ -- T32 GM008281-17/GM/NIGMS NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54 GM075026-040002/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Aug 21;325(5943):1010-4. doi: 10.1126/science.1176088. Epub 2009 Jul 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health and Science University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97239, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19608859" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Transport Systems/*chemistry/*metabolism ; Amino Acids/metabolism ; Antiporters/chemistry ; Apoproteins/chemistry/metabolism ; Archaeal Proteins/*chemistry/*metabolism ; Crystallization ; Crystallography, X-Ray ; Escherichia coli Proteins/chemistry ; Methanococcus/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protons ; Sodium/metabolism ; Substrate Specificity
    Print ISSN: 0036-8075
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  • 13
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    Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-30
    Description: Transcribing RNA polymerases oscillate between three stable states, two of which, pre- and posttranslocated, were previously subjected to x-ray crystal structure determination. We report here the crystal structure of RNA polymerase II in the third state, the reverse translocated, or "backtracked" state. The defining feature of the backtracked structure is a binding site for the first backtracked nucleotide. This binding site is occupied in case of nucleotide misincorporation in the RNA or damage to the DNA, and is termed the "P" site because it supports proofreading. The predominant mechanism of proofreading is the excision of a dinucleotide in the presence of the elongation factor SII (TFIIS). Structure determination of a cocrystal with TFIIS reveals a rearrangement whereby cleavage of the RNA may take place.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718261/" 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/PMC2718261/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Dong -- Bushnell, David A -- Huang, Xuhui -- Westover, Kenneth D -- Levitt, Michael -- Kornberg, Roger D -- GM036559/GM/NIGMS NIH HHS/ -- GM041455/GM/NIGMS NIH HHS/ -- GM049985/GM/NIGMS NIH HHS/ -- K99 GM085136/GM/NIGMS NIH HHS/ -- K99 GM085136-01/GM/NIGMS NIH HHS/ -- R00 GM085136/GM/NIGMS NIH HHS/ -- R01 GM036659/GM/NIGMS NIH HHS/ -- R01 GM041455/GM/NIGMS NIH HHS/ -- R01 GM049985/GM/NIGMS NIH HHS/ -- R01 GM049985-16/GM/NIGMS NIH HHS/ -- R37 GM036659/GM/NIGMS NIH HHS/ -- R37 GM036659-22/GM/NIGMS NIH HHS/ -- R37 GM041455/GM/NIGMS NIH HHS/ -- R37 GM041455-20/GM/NIGMS NIH HHS/ -- U54 GM072970/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 May 29;324(5931):1203-6. doi: 10.1126/science.1168729.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, 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/19478184" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pair Mismatch ; Crystallography, X-Ray ; Guanosine Monophosphate/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/chemistry/*metabolism ; RNA Polymerase II/*chemistry/*metabolism ; Saccharomyces cerevisiae/*enzymology ; *Transcription, Genetic ; Transcriptional Elongation Factors/chemistry/*metabolism
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  • 14
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    Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-17
    Description: Once all chromosomes are connected to the mitotic spindle (bioriented), anaphase is initiated by the protein ubiquitylation activity of the anaphase-promoting complex/cyclosome (APC/C) and its coactivator Cdc20 (APC/C(Cdc20)). Before chromosome biorientation, anaphase is delayed by a mitotic checkpoint complex (MCC) that inhibits APC/C(Cdc20). We used single-particle electron microscopy to obtain three-dimensional models of human APC/C in various functional states: bound to MCC, to Cdc20, or to neither (apo-APC/C). These experiments revealed that MCC associates with the Cdc20 binding site on APC/C, locks the otherwise flexible APC/C in a "closed" state, and prevents binding and ubiquitylation of a wide range of different APC/C substrates. These observations clarify the structural basis for the inhibition of APC/C by spindle checkpoint proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2989460/" 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/PMC2989460/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzog, Franz -- Primorac, Ivana -- Dube, Prakash -- Lenart, Peter -- Sander, Bjorn -- Mechtler, Karl -- Stark, Holger -- Peters, Jan-Michael -- F 3407/Austrian Science Fund FWF/Austria -- New York, N.Y. -- Science. 2009 Mar 13;323(5920):1477-81. doi: 10.1126/science.1163300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19286556" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cdc20 Proteins ; Cell Cycle Proteins/chemistry/metabolism ; HeLa Cells ; Humans ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Microscopy, Electron ; *Mitosis ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Spindle Apparatus/*metabolism ; Ubiquitin-Conjugating Enzymes/chemistry/metabolism ; Ubiquitin-Protein Ligase Complexes/*chemistry/*metabolism ; Ubiquitination
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  • 15
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    Physiology. What determines coral health? (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weis, Virginia M -- Allemand, Denis -- New York, N.Y. -- Science. 2009 May 29;324(5931):1153-5. doi: 10.1126/science.1172540.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, Oregon State University, Corvallis, OR 97331, USA. weisv@science.oregonstate.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19478172" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/genetics/*physiology ; *Calcification, Physiologic ; Dinoflagellida/physiology ; *Ecosystem ; Hydrogen-Ion Concentration ; Oceans and Seas ; Seawater/chemistry ; Stress, Physiological ; *Symbiosis
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  • 16
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    Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-13
    Description: Rotavirus outer-layer protein VP7 is a principal target of protective antibodies. Removal of free calcium ions (Ca2+) dissociates VP7 trimers into monomers, releasing VP7 from the virion, and initiates penetration-inducing conformational changes in the other outer-layer protein, VP4. We report the crystal structure at 3.4 angstrom resolution of VP7 bound with the Fab fragment of a neutralizing monoclonal antibody. The Fab binds across the outer surface of the intersubunit contact, which contains two Ca2+ sites. Mutations that escape neutralization by other antibodies suggest that the same region bears the epitopes of most neutralizing antibodies. The monovalent Fab is sufficient to neutralize infectivity. We propose that neutralizing antibodies against VP7 act by stabilizing the trimer, thereby inhibiting the uncoating trigger for VP4 rearrangement. A disulfide-linked trimer is a potential subunit immunogen.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2995306/" 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/PMC2995306/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aoki, Scott T -- Settembre, Ethan C -- Trask, Shane D -- Greenberg, Harry B -- Harrison, Stephen C -- Dormitzer, Philip R -- AI-21362/AI/NIAID NIH HHS/ -- CA-13202/CA/NCI NIH HHS/ -- DK-56339/DK/NIDDK NIH HHS/ -- R37 CA013202/CA/NCI NIH HHS/ -- R37 CA013202-38/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Jun 12;324(5933):1444-7. doi: 10.1126/science.1170481.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19520960" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/chemistry/immunology/metabolism ; Antibodies, Viral/chemistry/*immunology/metabolism ; Antigens, Viral/*chemistry/genetics/*immunology/metabolism ; Binding Sites ; Binding Sites, Antibody ; Calcium/metabolism ; Capsid Proteins/*chemistry/genetics/*immunology/metabolism ; Crystallography, X-Ray ; Epitopes/immunology ; Immunoglobulin Fab Fragments/chemistry/*immunology/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neutralization Tests ; Protein Folding ; Protein Multimerization ; Protein Structure, Tertiary ; Protein Subunits ; Recombinant Proteins/chemistry ; Rotavirus/*chemistry/immunology ; Serotyping
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  • 17
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    Serengeti birds maintain forests by inhibiting seed predators (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-07-04
    Description: Of fundamental interest in conservation ecology are the regulatory mechanisms that maintain communities. We document a mechanism that maintains forests in the Serengeti ecosystem, Tanzania, and the destabilization when disturbance opens forest canopy. Forest birds, by consuming seeds, protected them from beetle attack. Consumption increased the germination rate and the density of seedlings and recruits, which was sufficient to maintain the forest. Opening of the canopy resulted in loss of birds, increased beetle attack, and loss of germination. Thus, frugivorous birds are necessary for the maintenance of forests. Their absence could have resulted in the observed forest decline since 1966.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharam, Gregory J -- Sinclair, A R E -- Turkington, Roy -- New York, N.Y. -- Science. 2009 Jul 3;325(5936):51. doi: 10.1126/science.1173805.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biodiversity Research Center, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19574381" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Beetles ; *Birds ; *Ecosystem ; Feeding Behavior ; Germination ; Population Dynamics ; *Seeds/growth & development ; Tanzania ; *Trees/growth & development
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  • 18
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    Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-03-28
    Description: P-glycoprotein (P-gp) detoxifies cells by exporting hundreds of chemically unrelated toxins but has been implicated in multidrug resistance (MDR) in the treatment of cancers. Substrate promiscuity is a hallmark of P-gp activity, thus a structural description of poly-specific drug-binding is important for the rational design of anticancer drugs and MDR inhibitors. The x-ray structure of apo P-gp at 3.8 angstroms reveals an internal cavity of approximately 6000 angstroms cubed with a 30 angstrom separation of the two nucleotide-binding domains. Two additional P-gp structures with cyclic peptide inhibitors demonstrate distinct drug-binding sites in the internal cavity capable of stereoselectivity that is based on hydrophobic and aromatic interactions. Apo and drug-bound P-gp structures have portals open to the cytoplasm and the inner leaflet of the lipid bilayer for drug entry. The inward-facing conformation represents an initial stage of the transport cycle that is competent for drug binding.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2720052/" 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/PMC2720052/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aller, Stephen G -- Yu, Jodie -- Ward, Andrew -- Weng, Yue -- Chittaboina, Srinivas -- Zhuo, Rupeng -- Harrell, Patina M -- Trinh, Yenphuong T -- Zhang, Qinghai -- Urbatsch, Ina L -- Chang, Geoffrey -- F32 GM078914/GM/NIGMS NIH HHS/ -- F32 GM078914-03/GM/NIGMS NIH HHS/ -- GM073197/GM/NIGMS NIH HHS/ -- GM078914/GM/NIGMS NIH HHS/ -- GM61905/GM/NIGMS NIH HHS/ -- P50 GM073197/GM/NIGMS NIH HHS/ -- P50 GM073197-050002/GM/NIGMS NIH HHS/ -- R01 GM061905/GM/NIGMS NIH HHS/ -- R01 GM061905-09/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Mar 27;323(5922):1718-22. doi: 10.1126/science.1168750.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19325113" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Apoproteins/chemistry/metabolism ; Binding Sites ; Cell Membrane/chemistry ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/chemistry ; Mice ; Models, Molecular ; Molecular Sequence Data ; P-Glycoprotein/antagonists & inhibitors/*chemistry/*metabolism ; Peptides, Cyclic/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Stereoisomerism ; Verapamil/metabolism/pharmacology
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  • 19
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    DNA binding site sequence directs glucocorticoid receptor structure and activity (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-18
    Description: Genes are not simply turned on or off, but instead their expression is fine-tuned to meet the needs of a cell. How genes are modulated so precisely is not well understood. The glucocorticoid receptor (GR) regulates target genes by associating with specific DNA binding sites, the sequences of which differ between genes. Traditionally, these binding sites have been viewed only as docking sites. Using structural, biochemical, and cell-based assays, we show that GR binding sequences, differing by as little as a single base pair, differentially affect GR conformation and regulatory activity. We therefore propose that DNA is a sequence-specific allosteric ligand of GR that tailors the activity of the receptor toward specific target genes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2777810/" 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/PMC2777810/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meijsing, Sebastiaan H -- Pufall, Miles A -- So, Alex Y -- Bates, Darren L -- Chen, Lin -- Yamamoto, Keith R -- GM08537/GM/NIGMS NIH HHS/ -- R01 CA020535/CA/NCI NIH HHS/ -- R01 CA020535-31/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2009 Apr 17;324(5925):407-10. doi: 10.1126/science.1164265.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19372434" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Line, Tumor ; Crystallography, X-Ray ; DNA/*chemistry/*metabolism ; Humans ; Ligands ; Models, Molecular ; Mutation ; Protein Conformation ; Protein Isoforms/chemistry/metabolism ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Receptors, Glucocorticoid/chemistry/genetics/*metabolism ; Transcriptional Activation
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  • 20
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    Crystal structure of the catalytic core of an RNA-polymerase ribozyme (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-12-08
    Description: Primordial organisms of the putative RNA world would have required polymerase ribozymes able to replicate RNA. Known ribozymes with polymerase activity best approximating that needed for RNA replication contain at their catalytic core the class I RNA ligase, an artificial ribozyme with a catalytic rate among the fastest of known ribozymes. Here we present the 3.0 angstrom crystal structure of this ligase. The architecture resembles a tripod, its three legs converging near the ligation junction. Interacting with this tripod scaffold through a series of 10 minor-groove interactions (including two A-minor triads) is the unpaired segment that contributes to and organizes the active site. A cytosine nucleobase and two backbone phosphates abut the ligation junction; their location suggests a model for catalysis resembling that of proteinaceous polymerases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3978776/" 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/PMC3978776/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shechner, David M -- Grant, Robert A -- Bagby, Sarah C -- Koldobskaya, Yelena -- Piccirilli, Joseph A -- Bartel, David P -- GM61835/GM/NIGMS NIH HHS/ -- R01 GM061835/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Nov 27;326(5957):1271-5. doi: 10.1126/science.1174676.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research and Howard Hughes Medical Institute, 9 Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965478" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; Catalysis ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; DNA-Directed RNA Polymerases/chemistry/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Magnesium/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Polynucleotide Ligases/chemistry/metabolism ; RNA, Catalytic/*chemistry/metabolism ; Ribonucleotides/chemistry/metabolism
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  • 21
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    Shifts in lake N:P stoichiometry and nutrient limitation driven by atmospheric nitrogen deposition (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-11-07
    Description: Human activities have more than doubled the amount of nitrogen (N) circulating in the biosphere. One major pathway of this anthropogenic N input into ecosystems has been increased regional deposition from the atmosphere. Here we show that atmospheric N deposition increased the stoichiometric ratio of N and phosphorus (P) in lakes in Norway, Sweden, and Colorado, United States, and, as a result, patterns of ecological nutrient limitation were shifted. Under low N deposition, phytoplankton growth is generally N-limited; however, in high-N deposition lakes, phytoplankton growth is consistently P-limited. Continued anthropogenic amplification of the global N cycle will further alter ecological processes, such as biogeochemical cycling, trophic dynamics, and biological diversity, in the world's lakes, even in lakes far from direct human disturbance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elser, James J -- Andersen, Tom -- Baron, Jill S -- Bergstrom, Ann-Kristin -- Jansson, Mats -- Kyle, Marcia -- Nydick, Koren R -- Steger, Laura -- Hessen, Dag O -- New York, N.Y. -- Science. 2009 Nov 6;326(5954):835-7. doi: 10.1126/science.1176199.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Life Sciences, Arizona State University, Tempe, AZ 85287, USA. j.elser@asu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19892979" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere/*chemistry ; Biodiversity ; Biomass ; Colorado ; *Ecosystem ; Food Chain ; Fresh Water/*chemistry ; Human Activities ; Humans ; Nitrates/analysis ; Nitrogen/*analysis ; Norway ; Phosphorus/*analysis ; Phytoplankton/growth & development/*physiology ; Sweden ; Trees
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    Coral reefs. Calcification rates drop in Australian reefs (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-01-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2009 Jan 2;323(5910):27. doi: 10.1126/science.323.5910.27.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19119193" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/growth & development/*physiology ; Australia ; *Calcification, Physiologic ; Calcium Carbonate/analysis ; Carbon Dioxide ; *Ecosystem ; Hydrogen-Ion Concentration ; Oceans and Seas ; Seawater/*chemistry ; Temperature
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  • 23
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    Bone assemblages track animal community structure over 40 years in an African savanna ecosystem (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-05-23
    Description: Reconstructing ancient communities depends on how accurately fossil assemblages retain information about living populations. We report a high level of fidelity between modern bone assemblages and living populations based on a 40-year study of the Amboseli ecosystem in southern Kenya. Relative abundance of 15 herbivorous species recorded in the bone assemblage accurately tracks the living populations through major changes in community composition and habitat over intervals as short as 5 years. The aggregated bone sample provides an accurate record of community structure time-averaged over four decades. These results lay the groundwork for integrating paleobiological and contemporary ecological studies across evolutionary and ecological time scales. Bone surveys also provide a useful method of assessing population changes and community structure for modern vertebrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Western, David -- Behrensmeyer, Anna K -- New York, N.Y. -- Science. 2009 May 22;324(5930):1061-4. doi: 10.1126/science.1171155.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉African Conservation Center, Box 62844, Nairobi, Kenya. dwestern@africaonline.co.ke〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19461002" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Body Size ; *Bone and Bones ; *Ecosystem ; Fossils ; Kenya ; Population Dynamics ; Regression Analysis ; Statistics, Nonparametric ; *Vertebrates
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Biochemistry. Through a mirror, differently (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheps, Jonathan A -- New York, N.Y. -- Science. 2009 Mar 27;323(5922):1679-80. doi: 10.1126/science.1172428.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Genetics and Developmental Biology, BC Cancer Research Centre, British Columbia Cancer Agency, Vancouver, BC V5Z 1L3 Canada. jsheps@bccrc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19325102" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Biological Transport ; Crystallography, X-Ray ; Drug Design ; Lipid Bilayers/chemistry ; Models, Biological ; Oligopeptides/chemistry/metabolism ; P-Glycoprotein/*chemistry/*metabolism ; Peptides, Cyclic/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Stereoisomerism
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    Ecology. Phenology feedbacks on climate change (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Penuelas, Josep -- Rutishauser, This -- Filella, Iolanda -- New York, N.Y. -- Science. 2009 May 15;324(5929):887-8. doi: 10.1126/science.1173004.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Global Ecology Unit, Center for Ecological Research and Forestry Applications (CREAF-CEAB-CSIC), Universitat Autonoma de Barcelona, 08193 Bellaterra (Barcelona), Spain. josep.penuelas@uab.cat〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19443770" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere/chemistry ; Biophysical Phenomena ; Carbon Dioxide/analysis/metabolism ; *Climate ; *Ecosystem ; *Greenhouse Effect ; Organic Chemicals/analysis/metabolism ; *Plant Development ; Plant Leaves/*growth & development/metabolism ; Plants/metabolism ; *Seasons ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Diversity and complexity in DNA recognition by transcription factors (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-16
    Description: Sequence preferences of DNA binding proteins are a primary mechanism by which cells interpret the genome. Despite the central importance of these proteins in physiology, development, and evolution, comprehensive DNA binding specificities have been determined experimentally for only a few proteins. Here, we used microarrays containing all 10-base pair sequences to examine the binding specificities of 104 distinct mouse DNA binding proteins representing 22 structural classes. Our results reveal a complex landscape of binding, with virtually every protein analyzed possessing unique preferences. Roughly half of the proteins each recognized multiple distinctly different sequence motifs, challenging our molecular understanding of how proteins interact with their DNA binding sites. This complexity in DNA recognition may be important in gene regulation and in the evolution of transcriptional regulatory networks.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2905877/" 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/PMC2905877/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Badis, Gwenael -- Berger, Michael F -- Philippakis, Anthony A -- Talukder, Shaheynoor -- Gehrke, Andrew R -- Jaeger, Savina A -- Chan, Esther T -- Metzler, Genita -- Vedenko, Anastasia -- Chen, Xiaoyu -- Kuznetsov, Hanna -- Wang, Chi-Fong -- Coburn, David -- Newburger, Daniel E -- Morris, Quaid -- Hughes, Timothy R -- Bulyk, Martha L -- R01 HG003985/HG/NHGRI NIH HHS/ -- R01 HG003985-01/HG/NHGRI NIH HHS/ -- R01 HG003985-02/HG/NHGRI NIH HHS/ -- R01 HG003985-03/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2009 Jun 26;324(5935):1720-3. doi: 10.1126/science.1162327. Epub 2009 May 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Toronto, ON M5S 3E1, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19443739" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; DNA/chemistry/*metabolism ; Electrophoretic Mobility Shift Assay ; Gene Expression Regulation ; Gene Regulatory Networks ; Humans ; Mice ; Protein Array Analysis ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Transcription Factors/*chemistry/*metabolism
    Print ISSN: 0036-8075
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    Proteome organization in a genome-reduced bacterium (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: The genome of Mycoplasma pneumoniae is among the smallest found in self-replicating organisms. To study the basic principles of bacterial proteome organization, we used tandem affinity purification-mass spectrometry (TAP-MS) in a proteome-wide screen. The analysis revealed 62 homomultimeric and 116 heteromultimeric soluble protein complexes, of which the majority are novel. About a third of the heteromultimeric complexes show higher levels of proteome organization, including assembly into larger, multiprotein complex entities, suggesting sequential steps in biological processes, and extensive sharing of components, implying protein multifunctionality. Incorporation of structural models for 484 proteins, single-particle electron microscopy, and cellular electron tomograms provided supporting structural details for this proteome organization. The data set provides a blueprint of the minimal cellular machinery required for life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhner, Sebastian -- van Noort, Vera -- Betts, Matthew J -- Leo-Macias, Alejandra -- Batisse, Claire -- Rode, Michaela -- Yamada, Takuji -- Maier, Tobias -- Bader, Samuel -- Beltran-Alvarez, Pedro -- Castano-Diez, Daniel -- Chen, Wei-Hua -- Devos, Damien -- Guell, Marc -- Norambuena, Tomas -- Racke, Ines -- Rybin, Vladimir -- Schmidt, Alexander -- Yus, Eva -- Aebersold, Ruedi -- Herrmann, Richard -- Bottcher, Bettina -- Frangakis, Achilleas S -- Russell, Robert B -- Serrano, Luis -- Bork, Peer -- Gavin, Anne-Claude -- New York, N.Y. -- Science. 2009 Nov 27;326(5957):1235-40. doi: 10.1126/science.1176343.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965468" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*analysis/isolation & purification/metabolism ; Computational Biology ; *Genome, Bacterial ; Mass Spectrometry/methods ; Metabolic Networks and Pathways ; Microscopy, Electron ; Models, Biological ; Models, Molecular ; Multiprotein Complexes/*analysis/metabolism ; Mycoplasma pneumoniae/*chemistry/*genetics/metabolism/ultrastructure ; Pattern Recognition, Automated ; Protein Interaction Mapping ; *Proteome ; Systems Biology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    AAAS annual meeting. Will many endangered species recover? (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2009 Feb 20;323(5917):998-9. doi: 10.1126/science.323.5917.998b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19229008" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Birds ; *Conservation of Natural Resources ; *Ecosystem ; Extinction, Biological ; Population Dynamics ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Macrovertebrate paleontology and the Pliocene habitat of Ardipithecus ramidus (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-08
    Description: A diverse assemblage of large mammals is spatially and stratigraphically associated with Ardipithecus ramidus at Aramis. The most common species are tragelaphine antelope and colobine monkeys. Analyses of their postcranial remains situate them in a closed habitat. Assessment of dental mesowear, microwear, and stable isotopes from these and a wider range of abundant associated larger mammals indicates that the local habitat at Aramis was predominantly woodland. The Ar. ramidus enamel isotope values indicate a minimal C4 vegetation component in its diet (plants using the C4 photosynthetic pathway), which is consistent with predominantly forest/woodland feeding. Although the Early Pliocene Afar included a range of environments, and the local environment at Aramis and its vicinity ranged from forests to wooded grasslands, the integration of available physical and biological evidence establishes Ar. ramidus as a denizen of the closed habitats along this continuum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, Tim D -- Ambrose, Stanley H -- Suwa, Gen -- Su, Denise F -- DeGusta, David -- Bernor, Raymond L -- Boisserie, Jean-Renaud -- Brunet, Michel -- Delson, Eric -- Frost, Stephen -- Garcia, Nuria -- Giaourtsakis, Ioannis X -- Haile-Selassie, Yohannes -- Howell, F Clark -- Lehmann, Thomas -- Likius, Andossa -- Pehlevan, Cesur -- Saegusa, Haruo -- Semprebon, Gina -- Teaford, Mark -- Vrba, Elisabeth -- New York, N.Y. -- Science. 2009 Oct 2;326(5949):87-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Evolution Research Center and Department of Integrative Biology, 3101 Valley Life Sciences Building, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19810193" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Cercopithecidae/anatomy & histology ; Diet ; *Ecosystem ; Environment ; Ethiopia ; *Fossils ; *Hominidae/classification ; Mammals/anatomy & histology/classification ; Paleodontology ; Plants ; Population Density ; Tooth/anatomy & histology ; Trees
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structure of a type IV secretion system core complex (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-01-10
    Description: Type IV secretion systems (T4SSs) are important virulence factors used by Gram-negative bacterial pathogens to inject effectors into host cells or to spread plasmids harboring antibiotic resistance genes. We report the 15 angstrom resolution cryo-electron microscopy structure of the core complex of a T4SS. The core complex is composed of three proteins, each present in 14 copies and forming a approximately 1.1-megadalton two-chambered, double membrane-spanning channel. The structure is double-walled, with each component apparently spanning a large part of the channel. The complex is open on the cytoplasmic side and constricted on the extracellular side. Overall, the T4SS core complex structure is different in both architecture and composition from the other known double membrane-spanning secretion system that has been structurally characterized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fronzes, Remi -- Schafer, Eva -- Wang, Luchun -- Saibil, Helen R -- Orlova, Elena V -- Waksman, Gabriel -- 070776/Wellcome Trust/United Kingdom -- BB/C516144/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/C516179/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/F010281/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- Biotechnology and Biological Sciences Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Jan 9;323(5911):266-8. doi: 10.1126/science.1166101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Structural and Molecular Biology, School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19131631" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*chemistry/genetics/ultrastructure ; Bacterial Proteins/*chemistry/genetics/*ultrastructure ; Cloning, Molecular ; Cryoelectron Microscopy ; Gram-Negative Bacteria/*chemistry/genetics/pathogenicity ; Imaging, Three-Dimensional ; Models, Molecular ; Multiprotein Complexes/chemistry/ultrastructure ; *Plasmids ; Protein Conformation ; Protein Structure, Quaternary ; Virulence Factors/*chemistry/genetics
    Print ISSN: 0036-8075
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    Eutrophication: time to adjust expectations (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacoby, Charles A -- Frazer, Thomas K -- New York, N.Y. -- Science. 2009 May 8;324(5928):723-4; author reply 724-5. doi: 10.1126/science.324_723b.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Forest Resources and Conservation, University of Florida, Gainesville, FL 32653, USA. cajacoby@ufl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19423801" target="_blank"〉PubMed〈/a〉
    Keywords: *Ecosystem ; *Eutrophication ; *Fresh Water/chemistry ; *Nitrogen/analysis ; *Phosphorus/analysis
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    S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-04
    Description: Mitochondria continuously undergo two opposing processes, fission and fusion. The disruption of this dynamic equilibrium may herald cell injury or death and may contribute to developmental and neurodegenerative disorders. Nitric oxide functions as a signaling molecule, but in excess it mediates neuronal injury, in part via mitochondrial fission or fragmentation. However, the underlying mechanism for nitric oxide-induced pathological fission remains unclear. We found that nitric oxide produced in response to beta-amyloid protein, thought to be a key mediator of Alzheimer's disease, triggered mitochondrial fission, synaptic loss, and neuronal damage, in part via S-nitrosylation of dynamin-related protein 1 (forming SNO-Drp1). Preventing nitrosylation of Drp1 by cysteine mutation abrogated these neurotoxic events. SNO-Drp1 is increased in brains of human Alzheimer's disease patients and may thus contribute to the pathogenesis of neurodegeneration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2823371/" 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/PMC2823371/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Dong-Hyung -- Nakamura, Tomohiro -- Fang, Jianguo -- Cieplak, Piotr -- Godzik, Adam -- Gu, Zezong -- Lipton, Stuart A -- P01 ES016738/ES/NIEHS NIH HHS/ -- P01 ES016738-01/ES/NIEHS NIH HHS/ -- P01 ES016738-010003/ES/NIEHS NIH HHS/ -- P01 ES016738-02/ES/NIEHS NIH HHS/ -- P01 ES016738-020003/ES/NIEHS NIH HHS/ -- P01 HD029587/HD/NICHD NIH HHS/ -- P01 HD029587-16/HD/NICHD NIH HHS/ -- P01 HD29587/HD/NICHD NIH HHS/ -- P30 NS057096/NS/NINDS NIH HHS/ -- P30 NS057096-04/NS/NINDS NIH HHS/ -- R01 EY005477/EY/NEI NIH HHS/ -- R01 EY005477-25/EY/NEI NIH HHS/ -- R01 EY05477/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2009 Apr 3;324(5923):102-5. doi: 10.1126/science.1171091.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neuroscience, Aging, and Stem Cell Research, Burnham Institute for Medical Research, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19342591" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism/pathology ; Amino Acid Motifs ; Amyloid beta-Peptides/*metabolism/pharmacology ; Animals ; Cell Line ; Cell Line, Tumor ; Cerebral Cortex/cytology ; Cysteine/analogs & derivatives/genetics/metabolism/pharmacology ; Female ; GTP Phosphohydrolases/chemistry/*metabolism ; Humans ; Male ; Mice ; Mice, Transgenic ; Microtubule-Associated Proteins/chemistry/*metabolism ; Mitochondria/drug effects/physiology/*ultrastructure ; Mitochondrial Proteins/chemistry/*metabolism ; Models, Molecular ; Mutation ; Neurons/drug effects/*ultrastructure ; Nitric Oxide/*metabolism ; Peptide Fragments/metabolism/pharmacology ; Protein Multimerization ; Protein Structure, Tertiary ; S-Nitrosothiols/pharmacology
    Print ISSN: 0036-8075
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    Microbiology. No place too cold (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laybourn-Parry, Johanna -- New York, N.Y. -- Science. 2009 Jun 19;324(5934):1521-2. doi: 10.1126/science.1173645.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Antarctic and Southern Ocean Studies, University of Tasmania, Hobart, Tasmania 7001, Australia. Jo.Laybourn-Parry@utas.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19541982" target="_blank"〉PubMed〈/a〉
    Keywords: Antarctic Regions ; Arctic Regions ; Biodiversity ; Carbon/metabolism ; *Cold Temperature ; *Ecosystem ; *Water Microbiology
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    Where are the parasites? (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kutz, Susan J -- Dobson, Andy P -- Hoberg, Eric P -- New York, N.Y. -- Science. 2009 Nov 27;326(5957):1187-8. doi: 10.1126/science.326.5957.1187-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965449" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arctic Regions/epidemiology ; *Climate Change ; *Ecosystem ; Host-Parasite Interactions ; Parasites/growth & development/*physiology ; Parasitic Diseases, Animal/epidemiology/parasitology/transmission ; Population Dynamics
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    Drought sensitivity of the Amazon rainforest (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-07
    Description: Amazon forests are a key but poorly understood component of the global carbon cycle. If, as anticipated, they dry this century, they might accelerate climate change through carbon losses and changed surface energy balances. We used records from multiple long-term monitoring plots across Amazonia to assess forest responses to the intense 2005 drought, a possible analog of future events. Affected forest lost biomass, reversing a large long-term carbon sink, with the greatest impacts observed where the dry season was unusually intense. Relative to pre-2005 conditions, forest subjected to a 100-millimeter increase in water deficit lost 5.3 megagrams of aboveground biomass of carbon per hectare. The drought had a total biomass carbon impact of 1.2 to 1.6 petagrams (1.2 x 10(15) to 1.6 x 10(15) grams). Amazon forests therefore appear vulnerable to increasing moisture stress, with the potential for large carbon losses to exert feedback on climate change.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phillips, Oliver L -- Aragao, Luiz E O C -- Lewis, Simon L -- Fisher, Joshua B -- Lloyd, Jon -- Lopez-Gonzalez, Gabriela -- Malhi, Yadvinder -- Monteagudo, Abel -- Peacock, Julie -- Quesada, Carlos A -- van der Heijden, Geertje -- Almeida, Samuel -- Amaral, Ieda -- Arroyo, Luzmila -- Aymard, Gerardo -- Baker, Tim R -- Banki, Olaf -- Blanc, Lilian -- Bonal, Damien -- Brando, Paulo -- Chave, Jerome -- de Oliveira, Atila Cristina Alves -- Cardozo, Nallaret Davila -- Czimczik, Claudia I -- Feldpausch, Ted R -- Freitas, Maria Aparecida -- Gloor, Emanuel -- Higuchi, Niro -- Jimenez, Eliana -- Lloyd, Gareth -- Meir, Patrick -- Mendoza, Casimiro -- Morel, Alexandra -- Neill, David A -- Nepstad, Daniel -- Patino, Sandra -- Penuela, Maria Cristina -- Prieto, Adriana -- Ramirez, Fredy -- Schwarz, Michael -- Silva, Javier -- Silveira, Marcos -- Thomas, Anne Sota -- Steege, Hans Ter -- Stropp, Juliana -- Vasquez, Rodolfo -- Zelazowski, Przemyslaw -- Alvarez Davila, Esteban -- Andelman, Sandy -- Andrade, Ana -- Chao, Kuo-Jung -- Erwin, Terry -- Di Fiore, Anthony -- Honorio C, Euridice -- Keeling, Helen -- Killeen, Tim J -- Laurance, William F -- Pena Cruz, Antonio -- Pitman, Nigel C A -- Nunez Vargas, Percy -- Ramirez-Angulo, Hirma -- Rudas, Agustin -- Salamao, Rafael -- Silva, Natalino -- Terborgh, John -- Torres-Lezama, Armando -- New York, N.Y. -- Science. 2009 Mar 6;323(5919):1344-7. doi: 10.1126/science.1164033.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ecology and Global Change, School of Geography, University of Leeds, Leeds LS2 9JT, UK. o.phillips@leeds.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19265020" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Biomass ; Brazil ; Carbon ; Carbon Dioxide ; Climate ; *Droughts ; *Ecosystem ; South America ; *Trees/growth & development ; Tropical Climate
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    Microbiology. Fantastic fixers (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fulweiler, Robinson W -- New York, N.Y. -- Science. 2009 Oct 16;326(5951):377-8. doi: 10.1126/science.1181129.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, Boston University, Boston, MA 02215, USA. rwf@bu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19833949" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/growth & development/*metabolism ; Bacteria, Anaerobic/growth & development/*metabolism ; Cold Temperature ; Deltaproteobacteria/growth & development/*metabolism ; *Ecosystem ; Geologic Sediments/*microbiology ; Mass Spectrometry/methods ; Methane/metabolism ; *Nitrogen Fixation ; Nitrogen Isotopes/metabolism ; Oxidation-Reduction ; *Seawater/microbiology ; Sulfates/metabolism ; Symbiosis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A cytidine deaminase edits C to U in transfer RNAs in Archaea (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-02
    Description: All canonical transfer RNAs (tRNAs) have a uridine at position 8, involved in maintaining tRNA tertiary structure. However, the hyperthermophilic archaeon Methanopyrus kandleri harbors 30 (out of 34) tRNA genes with cytidine at position 8. Here, we demonstrate C-to-U editing at this location in the tRNA's tertiary core, and present the crystal structure of a tRNA-specific cytidine deaminase, CDAT8, which has the cytidine deaminase domain linked to a tRNA-binding THUMP domain. CDAT8 is specific for C deamination at position 8, requires only the acceptor stem hairpin for activity, and belongs to a unique family within the "cytidine deaminase-like" superfamily. The presence of this C-to-U editing enzyme guarantees the proper folding and functionality of all M. kandleri tRNAs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2857566/" 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/PMC2857566/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Randau, Lennart -- Stanley, Bradford J -- Kohlway, Andrew -- Mechta, Sarah -- Xiong, Yong -- Soll, Dieter -- AI078831/AI/NIAID NIH HHS/ -- GM22854/GM/NIGMS NIH HHS/ -- R01 GM022854/GM/NIGMS NIH HHS/ -- R01 GM022854-33/GM/NIGMS NIH HHS/ -- R33 AI078831/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2009 May 1;324(5927):657-9. doi: 10.1126/science.1170123.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. lennart.randau@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19407206" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Catalytic Domain ; Crystallography, X-Ray ; Cytidine Deaminase/*chemistry/*metabolism ; Deamination ; Euryarchaeota/enzymology/genetics/*metabolism ; Genes, Archaeal ; Models, Chemical ; Models, Molecular ; Nucleic Acid Conformation ; Protein Multimerization ; Protein Structure, Tertiary ; *RNA Editing ; RNA, Archaeal/chemistry/genetics/*metabolism ; RNA, Transfer/chemistry/genetics/*metabolism
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    Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-25
    Description: Polyphosphate (polyP) occurs ubiquitously in cells, but its functions are poorly understood and its synthesis has only been characterized in bacteria. Using x-ray crystallography, we identified a eukaryotic polyphosphate polymerase within the membrane-integral vacuolar transporter chaperone (VTC) complex. A 2.6 angstrom crystal structure of the catalytic domain grown in the presence of adenosine triphosphate (ATP) reveals polyP winding through a tunnel-shaped pocket. Nucleotide- and phosphate-bound structures suggest that the enzyme functions by metal-assisted cleavage of the ATP gamma-phosphate, which is then in-line transferred to an acceptor phosphate to form polyP chains. Mutational analysis of the transmembrane domain indicates that VTC may integrate cytoplasmic polymer synthesis with polyP membrane translocation. Identification of the polyP-synthesizing enzyme opens the way to determine the functions of polyP in lower eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hothorn, Michael -- Neumann, Heinz -- Lenherr, Esther D -- Wehner, Mark -- Rybin, Vladimir -- Hassa, Paul O -- Uttenweiler, Andreas -- Reinhardt, Monique -- Schmidt, Andrea -- Seiler, Jeanette -- Ladurner, Andreas G -- Herrmann, Christian -- Scheffzek, Klaus -- Mayer, Andreas -- G0500367/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2009 Apr 24;324(5926):513-6. doi: 10.1126/science.1168120.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19390046" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Catalysis ; Catalytic Domain ; Crystallography, X-Ray ; Membrane Proteins/*chemistry/metabolism ; Models, Molecular ; Phosphotransferases/*chemistry/metabolism ; Polyphosphates/*chemistry/metabolism ; Protein Conformation ; Saccharomyces cerevisiae/enzymology/metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/metabolism
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    Symbiotic nitrogen fixation in the fungus gardens of leaf-cutter ants (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: Bacteria-mediated acquisition of atmospheric N2 serves as a critical source of nitrogen in terrestrial ecosystems. Here we reveal that symbiotic nitrogen fixation facilitates the cultivation of specialized fungal crops by leaf-cutter ants. By using acetylene reduction and stable isotope experiments, we demonstrated that N2 fixation occurred in the fungus gardens of eight leaf-cutter ant species and, further, that this fixed nitrogen was incorporated into ant biomass. Symbiotic N2-fixing bacteria were consistently isolated from the fungus gardens of 80 leaf-cutter ant colonies collected in Argentina, Costa Rica, and Panama. The discovery of N2 fixation within the leaf-cutter ant-microbe symbiosis reveals a previously unrecognized nitrogen source in neotropical ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pinto-Tomas, Adrian A -- Anderson, Mark A -- Suen, Garret -- Stevenson, David M -- Chu, Fiona S T -- Cleland, W Wallace -- Weimer, Paul J -- Currie, Cameron R -- GM 18938/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Nov 20;326(5956):1120-3. doi: 10.1126/science.1173036.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin-Madison, 1550 Linden Drive, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965433" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylene/metabolism ; Animals ; Ants/metabolism/microbiology/*physiology ; Argentina ; Costa Rica ; *Ecosystem ; Fungi/growth & development/*physiology ; Klebsiella/isolation & purification/*metabolism ; Molecular Sequence Data ; Nitrogen/analysis/metabolism ; *Nitrogen Fixation ; Oxidation-Reduction ; Panama ; Pantoea/isolation & purification/*metabolism ; Phylogeny ; Plant Leaves/chemistry ; *Symbiosis
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    Ecology. Biodiversity and climate change (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-11-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willis, Kathy J -- Bhagwat, Shonil A -- New York, N.Y. -- Science. 2009 Nov 6;326(5954):806-7. doi: 10.1126/science.1178838.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Long-Term Ecology Laboratory, Oxford University Centre for the Environment, South Parks Road, Oxford, OX1 3QY, UK. kathy.willis@ouce.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19892969" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; *Biodiversity ; Birds ; Butterflies ; *Climate Change ; Conservation of Natural Resources ; *Ecosystem ; Extinction, Biological ; Plants ; Population Dynamics ; South America ; Trees ; Tropical Climate
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    Nursing China's ailing forests back to health (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, Richard -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):556-8. doi: 10.1126/science.325_556.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644103" target="_blank"〉PubMed〈/a〉
    Keywords: China ; Conservation of Natural Resources ; *Ecosystem ; *Forestry/economics/methods ; Government Regulation ; Public Policy ; *Trees
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  • 42
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    The structure of the ribosome with elongation factor G trapped in the posttranslocational state (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-17
    Description: Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during translation by the ribosome. We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid. Fusidic acid traps EF-G in a conformation intermediate between the guanosine triphosphate and guanosine diphosphate forms. The interaction of EF-G with ribosomal elements implicated in stimulating catalysis, such as the L10-L12 stalk and the L11 region, and of domain IV of EF-G with the tRNA at the peptidyl-tRNA binding site (P site) and with mRNA shed light on the role of these elements in EF-G function. The stabilization of the mobile stalks of the ribosome also results in a more complete description of its structure.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3763468/" 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/PMC3763468/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Yong-Gui -- Selmer, Maria -- Dunham, Christine M -- Weixlbaumer, Albert -- Kelley, Ann C -- Ramakrishnan, V -- 082086/Wellcome Trust/United Kingdom -- MC_U105184332/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Oct 30;326(5953):694-9. doi: 10.1126/science.1179709.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19833919" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry ; Catalysis ; Crystallography, X-Ray ; Fusidic Acid/chemistry/pharmacology ; Models, Molecular ; Peptide Elongation Factor G/*chemistry ; Protein Biosynthesis ; Protein Conformation ; Protein Structure, Tertiary ; Protein Synthesis Inhibitors/chemistry/pharmacology ; RNA, Bacterial/chemistry ; RNA, Messenger/chemistry ; RNA, Transfer/chemistry ; Ribosomes/*chemistry ; Thermus thermophilus
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    Structure and mechanism of an amino acid antiporter (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-30
    Description: Virulent enteric pathogens such as Escherichia coli strain O157:H7 rely on acid-resistance (AR) systems to survive the acidic environment in the stomach. A major component of AR is an arginine-dependent arginine:agmatine antiporter that expels intracellular protons. Here, we report the crystal structure of AdiC, the arginine:agmatine antiporter from E. coli O157:H7 and a member of the amino acid/polyamine/organocation (APC) superfamily of transporters at 3.6 A resolution. The overall fold is similar to that of several Na+-coupled symporters. AdiC contains 12 transmembrane segments, forms a homodimer, and exists in an outward-facing, open conformation in the crystals. A conserved, acidic pocket opens to the periplasm. Structural and biochemical analysis reveals the essential ligand-binding residues, defines the transport route, and suggests a conserved mechanism for the antiporter activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Xiang -- Lu, Feiran -- Zhou, Lijun -- Dang, Shangyu -- Sun, Linfeng -- Li, Xiaochun -- Wang, Jiawei -- Shi, Yigong -- New York, N.Y. -- Science. 2009 Jun 19;324(5934):1565-8. doi: 10.1126/science.1173654. Epub 2009 May 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉State Key Laboratory of Bio-membrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19478139" target="_blank"〉PubMed〈/a〉
    Keywords: Agmatine/metabolism ; Amino Acid Sequence ; Amino Acid Transport Systems/*chemistry/genetics/metabolism/physiology ; Antiporters/*chemistry/genetics/metabolism/physiology ; Arginine/metabolism ; Conserved Sequence ; Crystallography, X-Ray ; Escherichia coli O157/*chemistry/genetics/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism/physiology ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation
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    Elevated CO2 reduces losses of plant diversity caused by nitrogen deposition (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-12-08
    Description: The interactive effects of rising atmospheric carbon dioxide (CO2) concentrations and elevated nitrogen (N) deposition on plant diversity are not well understood. This is of concern because both factors are important components of global environmental change and because each might suppress diversity, with their combined effects possibly additive or synergistic. In a long-term open-air experiment, grassland assemblages planted with 16 species were grown under all combinations of ambient and elevated CO2 and ambient and elevated N. Over 10 years, elevated N reduced species richness by 16% at ambient CO2 but by just 8% at elevated CO2. This resulted from multiple effects of CO2 and N on plant traits and soil resources that altered competitive interactions among species. Elevated CO2 thus ameliorated the negative effects of N enrichment on species richness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reich, Peter B -- New York, N.Y. -- Science. 2009 Dec 4;326(5958):1399-402. doi: 10.1126/science.1178820.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Forest Resources, University of Minnesota, 1530 Cleveland Avenue North, St. Paul, MN 55108, USA. preich@umn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965757" target="_blank"〉PubMed〈/a〉
    Keywords: Anemone/growth & development/metabolism ; Asclepias/genetics/metabolism ; Asteraceae/growth & development/metabolism ; *Atmosphere ; *Biodiversity ; Biomass ; *Carbon Dioxide ; *Ecosystem ; Fabaceae/growth & development/metabolism ; Light ; Minnesota ; *Nitrogen/metabolism ; Nitrogen Fixation ; Plant Development ; *Plants/metabolism ; Poaceae/growth & development/metabolism ; Soil/analysis ; Water/analysis
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    Public trust doctrine: in need of integration (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Portman, Michelle E -- New York, N.Y. -- Science. 2009 Oct 2;326(5949):45; author reply 45-6. doi: 10.1126/science.326_45a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Marine Policy Center of the Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA. mportman@whoi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19797643" target="_blank"〉PubMed〈/a〉
    Keywords: *Ecosystem ; *Government Regulation ; Legislation as Topic ; Oceans and Seas ; *Public Policy ; United States ; United States Government Agencies
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  • 46
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    Rebuilding global fisheries (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: After a long history of overexploitation, increasing efforts to restore marine ecosystems and rebuild fisheries are under way. Here, we analyze current trends from a fisheries and conservation perspective. In 5 of 10 well-studied ecosystems, the average exploitation rate has recently declined and is now at or below the rate predicted to achieve maximum sustainable yield for seven systems. Yet 63% of assessed fish stocks worldwide still require rebuilding, and even lower exploitation rates are needed to reverse the collapse of vulnerable species. Combined fisheries and conservation objectives can be achieved by merging diverse management actions, including catch restrictions, gear modification, and closed areas, depending on local context. Impacts of international fleets and the lack of alternatives to fishing complicate prospects for rebuilding fisheries in many poorer regions, highlighting the need for a global perspective on rebuilding marine resources.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worm, Boris -- Hilborn, Ray -- Baum, Julia K -- Branch, Trevor A -- Collie, Jeremy S -- Costello, Christopher -- Fogarty, Michael J -- Fulton, Elizabeth A -- Hutchings, Jeffrey A -- Jennings, Simon -- Jensen, Olaf P -- Lotze, Heike K -- Mace, Pamela M -- McClanahan, Tim R -- Minto, Coilin -- Palumbi, Stephen R -- Parma, Ana M -- Ricard, Daniel -- Rosenberg, Andrew A -- Watson, Reg -- Zeller, Dirk -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):578-85. doi: 10.1126/science.1173146.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Dalhousie University, Halifax, NS B3H 4J1, Canada. bworm@dal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644114" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Biomass ; *Conservation of Natural Resources ; *Ecosystem ; *Fisheries/methods ; *Fishes/anatomy & histology ; Internationality ; Marine Biology ; Models, Biological ; Oceans and Seas ; Population Dynamics
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    Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-11-07
    Description: The LKB1 tumor suppressor is a protein kinase that controls the activity of adenosine monophosphate-activated protein kinase (AMPK). LKB1 activity is regulated by the pseudokinase STRADalpha and the scaffolding protein MO25alpha through an unknown, phosphorylation-independent, mechanism. We describe the structure of the core heterotrimeric LKB1-STRADalpha-MO25alpha complex, revealing an unusual allosteric mechanism of LKB1 activation. STRADalpha adopts a closed conformation typical of active protein kinases and binds LKB1 as a pseudosubstrate. STRADalpha and MO25alpha promote the active conformation of LKB1, which is stabilized by MO25alpha interacting with the LKB1 activation loop. This previously undescribed mechanism of kinase activation may be relevant to understanding the evolution of other pseudokinases. The structure also reveals how mutations found in Peutz-Jeghers syndrome and in various sporadic cancers impair LKB1 function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3518268/" 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/PMC3518268/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zeqiraj, Elton -- Filippi, Beatrice Maria -- Deak, Maria -- Alessi, Dario R -- van Aalten, Daan M F -- 087590/Wellcome Trust/United Kingdom -- C33794/A10969/Cancer Research UK/United Kingdom -- G0900138/Medical Research Council/United Kingdom -- MC_U127070193/Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Dec 18;326(5960):1707-11. doi: 10.1126/science.1178377. Epub 2009 Nov 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19892943" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases/metabolism ; Adaptor Proteins, Vesicular Transport/*chemistry/metabolism ; Allosteric Regulation ; Amino Acid Sequence ; Binding Sites ; Calcium-Binding Proteins/*chemistry/metabolism ; Crystallography, X-Ray ; Enzyme Activation ; Humans ; Models, Molecular ; Molecular Sequence Data ; Multiprotein Complexes/chemistry/metabolism ; Mutant Proteins/chemistry/metabolism ; Mutation ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/*chemistry/metabolism
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    Biochemistry. Force signaling in biology (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-06-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gebhardt, J Christof M -- Rief, Matthias -- New York, N.Y. -- Science. 2009 Jun 5;324(5932):1278-80. doi: 10.1126/science.1175874.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physik Department E22, Technische Universitat Munchen, James-Franck-Strasse, 85748 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19498156" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins/*metabolism ; Binding Sites ; Blood Coagulation/physiology ; Hemostasis/*physiology ; Humans ; *Mechanical Phenomena ; Optical Tweezers ; Protein Conformation ; Protein Folding ; Protein Multimerization ; Protein Structure, Tertiary ; Stress, Mechanical ; von Willebrand Factor/*chemistry/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Recent changes in phytoplankton communities associated with rapid regional climate change along the western Antarctic Peninsula (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-17
    Description: The climate of the western shelf of the Antarctic Peninsula (WAP) is undergoing a transition from a cold-dry polar-type climate to a warm-humid sub-Antarctic-type climate. Using three decades of satellite and field data, we document that ocean biological productivity, inferred from chlorophyll a concentration (Chl a), has significantly changed along the WAP shelf. Summertime surface Chl a (summer integrated Chl a approximately 63% of annually integrated Chl a) declined by 12% along the WAP over the past 30 years, with the largest decreases equatorward of 63 degrees S and with substantial increases in Chl a occurring farther south. The latitudinal variation in Chl a trends reflects shifting patterns of ice cover, cloud formation, and windiness affecting water-column mixing. Regional changes in phytoplankton coincide with observed changes in krill (Euphausia superba) and penguin populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montes-Hugo, Martin -- Doney, Scott C -- Ducklow, Hugh W -- Fraser, William -- Martinson, Douglas -- Stammerjohn, Sharon E -- Schofield, Oscar -- New York, N.Y. -- Science. 2009 Mar 13;323(5920):1470-3. doi: 10.1126/science.1164533.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Coastal Ocean Observation Lab, Institute of Marine and Coastal Sciences, School of Environmental and Biological Sciences, Rutgers University, New Brunswick, NJ 08901, USA. montes@marine.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19286554" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antarctic Regions ; Biomass ; Chlorophyll/*analysis ; *Cold Climate ; *Ecosystem ; Euphausiacea ; Geography ; Ice Cover ; Oceans and Seas ; Phytoplankton/cytology/*growth & development ; Population Dynamics ; Seasons ; *Seawater/chemistry ; Spheniscidae ; Temperature ; Wind
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    A contemporary microbially maintained subglacial ferrous "ocean" (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-18
    Description: An active microbial assemblage cycles sulfur in a sulfate-rich, ancient marine brine beneath Taylor Glacier, an outlet glacier of the East Antarctic Ice Sheet, with Fe(III) serving as the terminal electron acceptor. Isotopic measurements of sulfate, water, carbonate, and ferrous iron and functional gene analyses of adenosine 5'-phosphosulfate reductase imply that a microbial consortium facilitates a catalytic sulfur cycle. These metabolic pathways result from a limited organic carbon supply because of the absence of contemporary photosynthesis, yielding a subglacial ferrous brine that is anoxic but not sulfidic. Coupled biogeochemical processes below the glacier enable subglacial microbes to grow in extended isolation, demonstrating how analogous organic-starved systems, such as Neoproterozoic oceans, accumulated Fe(II) despite the presence of an active sulfur cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mikucki, Jill A -- Pearson, Ann -- Johnston, David T -- Turchyn, Alexandra V -- Farquhar, James -- Schrag, Daniel P -- Anbar, Ariel D -- Priscu, John C -- Lee, Peter A -- New York, N.Y. -- Science. 2009 Apr 17;324(5925):397-400. doi: 10.1126/science.1167350.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth and Planetary Sciences, Harvard University, Cambridge, MA 02138 USA. jill.a.mikucki@dartmouth.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19372431" target="_blank"〉PubMed〈/a〉
    Keywords: Anaerobiosis ; Antarctic Regions ; Autotrophic Processes ; Bacteria/growth & development/*metabolism ; *Ecosystem ; Ferric Compounds/*metabolism ; Ferrous Compounds/*metabolism ; Heterotrophic Processes ; *Ice Cover ; Metabolic Networks and Pathways ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases Acting on Sulfur Group Donors/genetics/metabolism ; Oxygen/metabolism ; Oxygen Isotopes/analysis ; Phylogeny ; Seawater/chemistry/*microbiology ; Sulfates/metabolism ; Sulfites/metabolism ; Sulfur/*metabolism
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    Oysters booming on new reefs, but can they survive disease? (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):525. doi: 10.1126/science.325_525.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644081" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Crassostrea/parasitology/physiology ; *Ecosystem ; Haplosporida/pathogenicity ; Population Growth ; *Rivers ; Virginia
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    Epicontinental seas versus open-ocean settings: the kinetics of mass extinction and origination (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-12-08
    Description: Environmental perturbations during mass extinctions were likely manifested differently in epicontinental seas than in open-ocean-facing habitats of comparable depth. Here, we present a dissection of origination and extinction in epicontinental seas versus open-ocean-facing coastal regions in the Permian through Cretaceous periods, an interval through which both settings are well represented in the fossil record. Results demonstrate that extinction rates were significantly higher in open-ocean settings than in epicontinental seas during major mass extinctions but not at other times and that origination rates were significantly higher in open-ocean settings for a protracted interval from the Late Jurassic through the Late Cretaceous. These patterns are manifested even when other paleogeographic and environmental variables are held fixed, indicating that epicontinental seas and open-ocean-facing coastlines carry distinct macroevolutionary signatures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Arnold I -- Foote, Michael -- New York, N.Y. -- Science. 2009 Nov 20;326(5956):1106-9. doi: 10.1126/science.1180061.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology, University of Cincinnati, Post Office Box 210013, Cincinnati, OH 45221, USA. arnold.miller@uc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965428" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bivalvia ; *Ecosystem ; Environment ; *Extinction, Biological ; Geologic Sediments ; Geological Phenomena ; Kinetics ; Oceans and Seas
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    Environmental restoration. Obama moves to revitalize Chesapeake Bay restoration (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-05-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2009 May 29;324(5931):1138-9. doi: 10.1126/science.324_1138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19478162" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture ; Animals ; *Ecosystem ; *Environmental Restoration and Remediation ; Oceans and Seas ; *Seawater ; United States ; United States Environmental Protection Agency/*legislation & jurisprudence ; Water Pollution/prevention & control
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    Mechanically activated integrin switch controls alpha5beta1 function (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-01-31
    Description: The cytoskeleton, integrin-mediated adhesion, and substrate stiffness control a common set of cell functions required for development and homeostasis that are often deranged in cancer. The connection between these mechanical elements and chemical signaling processes is not known. Here, we show that alpha(5)beta(1) integrin switches between relaxed and tensioned states in response to myosin II-generated cytoskeletal force. Force combines with extracellular matrix stiffness to generate tension that triggers the integrin switch. This switch directly controls the alpha(5)beta(1)-fibronectin bond strength through engaging the synergy site in fibronectin and is required to generate signals through phosphorylation of focal adhesion kinase. In the context of tissues, this integrin switch connects cytoskeleton and extracellular matrix mechanics to adhesion-dependent motility and signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Friedland, Julie C -- Lee, Mark H -- Boettiger, David -- GM57388/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Jan 30;323(5914):642-4. doi: 10.1126/science.1168441.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19179533" target="_blank"〉PubMed〈/a〉
    Keywords: Actins ; Biophysical Phenomena ; Cell Adhesion ; Cell Line, Tumor ; Cytoskeleton/*physiology ; Fibronectins/chemistry/*metabolism ; Focal Adhesion Protein-Tyrosine Kinases/metabolism ; Humans ; Integrin alpha5beta1/*chemistry/*metabolism ; Ligands ; Models, Molecular ; Myosin Type II/antagonists & inhibitors/metabolism ; Phosphorylation ; Protein Binding ; Protein Conformation ; Signal Transduction
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    Synthetic heterochromatin bypasses RNAi and centromeric repeats to establish functional centromeres (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-06-27
    Description: In the central domain of fission yeast centromeres, the kinetochore is assembled on CENP-A(Cnp1) nucleosomes. Normally, small interfering RNAs generated from flanking outer repeat transcripts direct histone H3 lysine 9 methyltransferase Clr4 to homologous loci to form heterochromatin. Outer repeats, RNA interference (RNAi), and centromeric heterochromatin are required to establish CENP-A(Cnp1) chromatin. We demonstrated that tethering Clr4 via DNA-binding sites at euchromatic loci induces heterochromatin assembly, with or without active RNAi. This synthetic heterochromatin completely substitutes for outer repeats on plasmid-based minichromosomes, promoting de novo CENP-A(Cnp1) and kinetochore assembly, to allow their mitotic segregation, even with RNAi inactive. Thus, the role of outer repeats in centromere establishment is simply the provision of RNAi substrates to direct heterochromatin formation; H3K9 methylation-dependent heterochromatin is alone sufficient to form functional centromeres.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2949999/" 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/PMC2949999/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kagansky, Alexander -- Folco, Hernan Diego -- Almeida, Ricardo -- Pidoux, Alison L -- Boukaba, Abdelhalim -- Simmer, Femke -- Urano, Takeshi -- Hamilton, Georgina L -- Allshire, Robin C -- 065061/Wellcome Trust/United Kingdom -- 065061/Z/Wellcome Trust/United Kingdom -- G0301153/Medical Research Council/United Kingdom -- G0301153(69173)/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2009 Jun 26;324(5935):1716-9. doi: 10.1126/science.1172026.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Cell Biology, School of Biological Sciences, The University of Edinburgh, 6.34 Swann Building, Edinburgh EH9 3JR, Scotland, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19556509" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cell Cycle Proteins/metabolism ; Centromere/chemistry/*metabolism/ultrastructure ; *Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation ; DNA-Binding Proteins/genetics/metabolism ; Heterochromatin/*metabolism ; Histones/metabolism ; Kinetochores/metabolism ; Methyltransferases/metabolism ; Mitosis ; *RNA Interference ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Schizosaccharomyces/genetics/*metabolism ; Schizosaccharomyces pombe Proteins/metabolism ; Transcription Factors/genetics/metabolism ; Transcription, Genetic
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    Three-dimensional structural view of the central metabolic network of Thermotoga maritima (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-09-19
    Description: Metabolic pathways have traditionally been described in terms of biochemical reactions and metabolites. With the use of structural genomics and systems biology, we generated a three-dimensional reconstruction of the central metabolic network of the bacterium Thermotoga maritima. The network encompassed 478 proteins, of which 120 were determined by experiment and 358 were modeled. Structural analysis revealed that proteins forming the network are dominated by a small number (only 182) of basic shapes (folds) performing diverse but mostly related functions. Most of these folds are already present in the essential core (approximately 30%) of the network, and its expansion by nonessential proteins is achieved with relatively few additional folds. Thus, integration of structural data with networks analysis generates insight into the function, mechanism, and evolution of biological networks.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2833182/" 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/PMC2833182/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Ying -- Thiele, Ines -- Weekes, Dana -- Li, Zhanwen -- Jaroszewski, Lukasz -- Ginalski, Krzysztof -- Deacon, Ashley M -- Wooley, John -- Lesley, Scott A -- Wilson, Ian A -- Palsson, Bernhard -- Osterman, Andrei -- Godzik, Adam -- P20 GM076221/GM/NIGMS NIH HHS/ -- P20 GM076221-03/GM/NIGMS NIH HHS/ -- U54 GM074898/GM/NIGMS NIH HHS/ -- U54 GM074898-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Sep 18;325(5947):1544-9. doi: 10.1126/science.1174671.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joint Center for Molecular Modeling (JCMM), Burnham Institute for Medical Research, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19762644" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/*metabolism ; Computational Biology ; Computer Simulation ; Enzymes/*chemistry/*metabolism ; Evolution, Molecular ; Genes, Bacterial ; Genome, Bacterial ; *Metabolic Networks and Pathways ; Models, Biological ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Systems Biology ; Thermotoga maritima/chemistry/genetics/*metabolism
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    Anthropology. Coastal exploitation (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-08-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rick, Torben C -- Erlandson, Jon M -- New York, N.Y. -- Science. 2009 Aug 21;325(5943):952-3. doi: 10.1126/science.1178539.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Archaeobiology Program, Department of Anthropology, National Museum of Natural History, Smithsonian Institution, Washington, DC 20013, USA. rickt@si.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19696338" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthropology ; Archaeology ; *Ecosystem ; *Environment ; Fisheries ; Fishes ; Humans ; Marine Biology ; Otters ; Population Dynamics ; Sea Urchins ; Shellfish
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    The rise of restoration ecology (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, Leslie -- Stone, Richard -- Sugden, Andrew -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):555. doi: 10.1126/science.325_555.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644102" target="_blank"〉PubMed〈/a〉
    Keywords: *Conservation of Natural Resources ; *Ecology ; *Ecosystem
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    Biochemistry. Nascent proteins caught in the act (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kampmann, Martin -- Blobel, Gunter -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Dec 4;326(5958):1352-3. doi: 10.1126/science.1183690.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and The Rockefeller University, New York, NY 10065, USA. martin.kampmann@rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965743" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cryoelectron Microscopy ; Endoplasmic Reticulum/metabolism/ultrastructure ; Escherichia coli Proteins/chemistry/genetics/*metabolism/ultrastructure ; Gene Expression Regulation, Bacterial ; Membrane Proteins/chemistry/*metabolism/ultrastructure ; Operon ; Protein Biosynthesis ; Protein Multimerization ; Protein Sorting Signals ; Protein Transport ; Proteins/chemistry/*metabolism/ultrastructure ; RNA, Transfer/metabolism ; Ribosomes/*metabolism/ultrastructure ; Signal Recognition Particle/chemistry/metabolism/ultrastructure ; Transcription, Genetic ; Tryptophanase/chemistry/*genetics/metabolism
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    The structure of rat liver vault at 3.5 angstrom resolution (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-01-20
    Description: Vaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Roles in multidrug resistance and innate immunity have been suggested, but the cellular function remains unclear. We have determined the x-ray structure of rat liver vault at 3.5 angstrom resolution and show that the cage structure consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains. Each MVP monomer folds into 12 domains: nine structural repeat domains, a shoulder domain, a cap-helix domain, and a cap-ring domain. Interactions between the 42-turn-long cap-helix domains are key to stabilizing the particle. The shoulder domain is structurally similar to a core domain of stomatin, a lipid-raft component in erythrocytes and epithelial cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, Hideaki -- Kato, Koji -- Yamashita, Eiki -- Sumizawa, Tomoyuki -- Zhou, Yong -- Yao, Min -- Iwasaki, Kenji -- Yoshimura, Masato -- Tsukihara, Tomitake -- New York, N.Y. -- Science. 2009 Jan 16;323(5912):384-8. doi: 10.1126/science.1164975.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19150846" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Liver/*chemistry ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Vault Ribonucleoprotein Particles/*chemistry
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    Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-19
    Description: Inward-rectifier potassium (K+) channels conduct K+ ions most efficiently in one direction, into the cell. Kir2 channels control the resting membrane voltage in many electrically excitable cells, and heritable mutations cause periodic paralysis and cardiac arrhythmia. We present the crystal structure of Kir2.2 from chicken, which, excluding the unstructured amino and carboxyl termini, is 90% identical to human Kir2.2. Crystals containing rubidium (Rb+), strontium (Sr2+), and europium (Eu3+) reveal binding sites along the ion conduction pathway that are both conductive and inhibitory. The sites correlate with extensive electrophysiological data and provide a structural basis for understanding rectification. The channel's extracellular surface, with large structured turrets and an unusual selectivity filter entryway, might explain the relative insensitivity of eukaryotic inward rectifiers to toxins. These same surface features also suggest a possible approach to the development of inhibitory agents specific to each member of the inward-rectifier K+ channel family.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2819303/" 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/PMC2819303/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tao, Xiao -- Avalos, Jose L -- Chen, Jiayun -- MacKinnon, Roderick -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 GM043949/GM/NIGMS NIH HHS/ -- R01 GM043949-10/GM/NIGMS NIH HHS/ -- R01 GM043949-11/GM/NIGMS NIH HHS/ -- R01 GM043949-12/GM/NIGMS NIH HHS/ -- R01 GM043949-13/GM/NIGMS NIH HHS/ -- R01 GM043949-14/GM/NIGMS NIH HHS/ -- R01 GM043949-15/GM/NIGMS NIH HHS/ -- R01 GM043949-16/GM/NIGMS NIH HHS/ -- R01 GM043949-17/GM/NIGMS NIH HHS/ -- R01 GM043949-18/GM/NIGMS NIH HHS/ -- R01 GM043949-19/GM/NIGMS NIH HHS/ -- R01 GM043949-20/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Dec 18;326(5960):1668-74. doi: 10.1126/science.1180310.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20019282" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Chickens ; Cloning, Molecular ; Crystallography, X-Ray ; Europium/metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Oocytes ; Patch-Clamp Techniques ; Potassium/metabolism ; Potassium Channel Blockers/pharmacology ; Potassium Channels, Inwardly Rectifying/antagonists & ; inhibitors/*chemistry/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Rubidium/metabolism ; Sequence Alignment ; Strontium/metabolism ; Xenopus laevis
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    Alternative zippering as an on-off switch for SNARE-mediated fusion (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-01-24
    Description: Membrane fusion between vesicles and target membranes involves the zippering of a four-helix bundle generated by constituent helices derived from target- and vesicle-soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). In neurons, the protein complexin clamps otherwise spontaneous fusion by SNARE proteins, allowing neurotransmitters and other mediators to be secreted when and where they are needed as this clamp is released. The membrane-proximal accessory helix of complexin is necessary for clamping, but its mechanism of action is unknown. Here, we present experiments using a reconstituted fusion system that suggest a simple model in which the complexin accessory helix forms an alternative four-helix bundle with the target-SNARE near the membrane, preventing the vesicle-SNARE from completing its zippering.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3736854/" 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/PMC3736854/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giraudo, Claudio G -- Garcia-Diaz, Alejandro -- Eng, William S -- Chen, Yuhang -- Hendrickson, Wayne A -- Melia, Thomas J -- Rothman, James E -- R01 GM071458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Jan 23;323(5913):512-6. doi: 10.1126/science.1166500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Cellular Biophysics, Columbia University, College of Physicians and Surgeons, 1150 Saint Nicholas Avenue, Russ Berrie Building, Room 520, New York, NY 10032, USA. claudio.giraudo@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19164750" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Vesicular Transport ; Amino Acid Motifs ; Amino Acid Sequence ; HeLa Cells ; Humans ; Hydrophobic and Hydrophilic Interactions ; *Membrane Fusion ; Models, Molecular ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Mutation ; Nerve Tissue Proteins/*chemistry/genetics/*metabolism ; Protein Binding ; Protein Structure, Secondary ; Recombinant Fusion Proteins/chemistry/metabolism ; SNARE Proteins/*chemistry/*metabolism ; Vesicle-Associated Membrane Protein 2/*chemistry/*metabolism
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    Cell biology. Evolving cell signals (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-09-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collins, Mark O -- New York, N.Y. -- Science. 2009 Sep 25;325(5948):1635-6. doi: 10.1126/science.1180331.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Proteomic Mass Spectrometry Group, Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1SA, UK. moc@sanger.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19779182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; *Biological Evolution ; CDC2 Protein Kinase/antagonists & inhibitors/metabolism ; *Evolution, Molecular ; Fungi/metabolism ; Phosphorylation ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/*chemistry/*metabolism ; Serine/metabolism ; *Signal Transduction ; Threonine/metabolism ; Tyrosine/metabolism
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    Ecology. Biodiversity under global change (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collins, Scott L -- New York, N.Y. -- Science. 2009 Dec 4;326(5958):1353-4. doi: 10.1126/science.1183271.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of New Mexico, Albuquerque, NM 87131, USA. scollins@sevilleta.unm.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965744" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Carbon Dioxide ; *Ecosystem ; Minnesota ; *Nitrogen/metabolism ; Plant Development ; *Plants/metabolism ; Soil/analysis
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    C3PO, an endoribonuclease that promotes RNAi by facilitating RISC activation (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-08
    Description: The catalytic engine of RNA interference (RNAi) is the RNA-induced silencing complex (RISC), wherein the endoribonuclease Argonaute and single-stranded small interfering RNA (siRNA) direct target mRNA cleavage. We reconstituted long double-stranded RNA- and duplex siRNA-initiated RISC activities with the use of recombinant Drosophila Dicer-2, R2D2, and Ago2 proteins. We used this core reconstitution system to purify an RNAi regulator that we term C3PO (component 3 promoter of RISC), a complex of Translin and Trax. C3PO is a Mg2+-dependent endoribonuclease that promotes RISC activation by removing siRNA passenger strand cleavage products. These studies establish an in vitro RNAi reconstitution system and identify C3PO as a key activator of the core RNAi machinery.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855623/" 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/PMC2855623/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Ying -- Ye, Xuecheng -- Jiang, Feng -- Liang, Chunyang -- Chen, Dongmei -- Peng, Junmin -- Kinch, Lisa N -- Grishin, Nick V -- Liu, Qinghua -- AG025688/AG/NIA NIH HHS/ -- GM078163/GM/NIGMS NIH HHS/ -- GM084010/GM/NIGMS NIH HHS/ -- R01 GM078163/GM/NIGMS NIH HHS/ -- R01 GM078163-03/GM/NIGMS NIH HHS/ -- R01 GM084010/GM/NIGMS NIH HHS/ -- R01 GM084010-02/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Aug 7;325(5941):750-3. doi: 10.1126/science.1176325.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19661431" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Argonaute Proteins ; Carrier Proteins/chemistry/genetics/isolation & purification/*metabolism ; Catalytic Domain ; Drosophila Proteins/chemistry/genetics/isolation & purification/*metabolism ; Drosophila melanogaster/chemistry/enzymology/*genetics ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; RNA Helicases/genetics/metabolism ; *RNA Interference ; RNA, Double-Stranded/chemistry/metabolism ; RNA, Small Interfering/chemistry/metabolism ; RNA-Binding Proteins/genetics/metabolism ; RNA-Induced Silencing Complex/genetics/*metabolism ; Recombinant Proteins/metabolism ; Ribonuclease III/genetics/metabolism
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    Ecology. Controlling eutrophication: nitrogen and phosphorus (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conley, Daniel J -- Paerl, Hans W -- Howarth, Robert W -- Boesch, Donald F -- Seitzinger, Sybil P -- Havens, Karl E -- Lancelot, Christiane -- Likens, Gene E -- New York, N.Y. -- Science. 2009 Feb 20;323(5917):1014-5. doi: 10.1126/science.1167755.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉GeoBiosphere Science Centre, Department of Geology, Lund University, Solvegatan 12, SE-223 62 Lund, Sweden. daniel.conley@geol.lu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19229022" target="_blank"〉PubMed〈/a〉
    Keywords: Cyanobacteria/growth & development/metabolism ; *Ecosystem ; Eukaryota/growth & development/metabolism ; *Eutrophication ; Fresh Water/*chemistry/microbiology ; Geologic Sediments/chemistry ; Nitrogen/*analysis/metabolism ; Nitrogen Fixation ; Phosphorus/*analysis/metabolism ; Salinity ; Seawater/*chemistry/microbiology ; Water Microbiology
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    Plant science. An invasive plant paradox (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rout, Marnie E -- Callaway, Ragan M -- New York, N.Y. -- Science. 2009 May 8;324(5928):734-5. doi: 10.1126/science.1173651.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences, University of Montana, Missoula, MT 59812, USA. marnie.rout@mso.umt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19423809" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Physiological Phenomena ; Biodiversity ; *Ecosystem ; Nitrogen/analysis/metabolism ; Photosynthesis ; *Plant Development ; Plant Leaves/anatomy & histology/chemistry ; Plants/anatomy & histology/metabolism ; *Soil/analysis ; *Soil Microbiology
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    Oceans. Legal bedrock for rebuilding America's ocean ecosystems (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-11
    Description: The public trust doctrine would provide a powerful framework for restructuring the way we manage U.S. oceans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turnipseed, Mary -- Crowder, Larry B -- Sagarin, Raphael D -- Roady, Stephen E -- New York, N.Y. -- Science. 2009 Apr 10;324(5924):183-4. doi: 10.1126/science.1170889.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nicholas School of the Environment, Duke University, Durham, NC 27708, USA. mary.turnipseed@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19359567" target="_blank"〉PubMed〈/a〉
    Keywords: *Ecosystem ; *Federal Government ; Jurisprudence ; Legislation as Topic ; Oceans and Seas ; *Public Policy ; United States ; United States Government Agencies
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    Biofuels: forests and carbon (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kauppi, Pekka E -- Saikku, Laura -- New York, N.Y. -- Science. 2009 Dec 4;326(5958):1345; author reply 1346. doi: 10.1126/science.326.5958.1345-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965738" target="_blank"〉PubMed〈/a〉
    Keywords: *Biofuels ; Carbon ; *Ecosystem ; *Trees ; Wood
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    Deep-sea archaea fix and share nitrogen in methane-consuming microbial consortia (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-17
    Description: Nitrogen-fixing (diazotrophic) microorganisms regulate productivity in diverse ecosystems; however, the identities of diazotrophs are unknown in many oceanic environments. Using single-cell-resolution nanometer secondary ion mass spectrometry images of 15N incorporation, we showed that deep-sea anaerobic methane-oxidizing archaea fix N2, as well as structurally similar CN-, and share the products with sulfate-reducing bacterial symbionts. These archaeal/bacterial consortia are already recognized as the major sink of methane in benthic ecosystems, and we now identify them as a source of bioavailable nitrogen as well. The archaea maintain their methane oxidation rates while fixing N2 but reduce their growth, probably in compensation for the energetic burden of diazotrophy. This finding extends the demonstrated lower limits of respiratory energy capable of fueling N2 fixation and reveals a link between the global carbon, nitrogen, and sulfur cycles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dekas, Anne E -- Poretsky, Rachel S -- Orphan, Victoria J -- New York, N.Y. -- Science. 2009 Oct 16;326(5951):422-6. doi: 10.1126/science.1178223.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 91125, USA. dekas@gps.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19833965" target="_blank"〉PubMed〈/a〉
    Keywords: Anaerobiosis ; Archaea/genetics/growth & development/*metabolism ; Bacteria, Anaerobic/genetics/growth & development/metabolism ; Deltaproteobacteria/genetics/growth & development/*metabolism ; *Ecosystem ; Genes, Archaeal ; Genes, Bacterial ; Geologic Sediments/*microbiology ; Mass Spectrometry/methods ; Methane/*metabolism ; *Nitrogen Fixation/genetics ; Nitrogen Isotopes/metabolism ; Operon ; Oxidation-Reduction ; Oxidoreductases/genetics ; Seawater/microbiology ; Sulfates/metabolism ; *Symbiosis
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    Fire in the Earth system (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-25
    Description: Fire is a worldwide phenomenon that appears in the geological record soon after the appearance of terrestrial plants. Fire influences global ecosystem patterns and processes, including vegetation distribution and structure, the carbon cycle, and climate. Although humans and fire have always coexisted, our capacity to manage fire remains imperfect and may become more difficult in the future as climate change alters fire regimes. This risk is difficult to assess, however, because fires are still poorly represented in global models. Here, we discuss some of the most important issues involved in developing a better understanding of the role of fire in the Earth system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowman, David M J S -- Balch, Jennifer K -- Artaxo, Paulo -- Bond, William J -- Carlson, Jean M -- Cochrane, Mark A -- D'Antonio, Carla M -- Defries, Ruth S -- Doyle, John C -- Harrison, Sandy P -- Johnston, Fay H -- Keeley, Jon E -- Krawchuk, Meg A -- Kull, Christian A -- Marston, J Brad -- Moritz, Max A -- Prentice, I Colin -- Roos, Christopher I -- Scott, Andrew C -- Swetnam, Thomas W -- van der Werf, Guido R -- Pyne, Stephen J -- New York, N.Y. -- Science. 2009 Apr 24;324(5926):481-4. doi: 10.1126/science.1163886.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Tasmania, Hobart, TAS 7001, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19390038" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Carbon ; Climate ; Earth (Planet) ; *Ecosystem ; *Fires ; Humans ; Plants
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    Self-assembling sequence-adaptive peptide nucleic acids (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-13
    Description: Several classes of nucleic acid analogs have been reported, but no synthetic informational polymer has yet proven responsive to selection pressures under enzyme-free conditions. Here, we introduce an oligomer family that efficiently self-assembles by means of reversible covalent anchoring of nucleobase recognition units onto simple oligo-dipeptide backbones [thioester peptide nucleic acids (tPNAs)] and undergoes dynamic sequence modification in response to changing templates in solution. The oligomers specifically self-pair with complementary tPNA strands and cross-pair with RNA and DNA in Watson-Crick fashion. Thus, tPNA combines base-pairing interactions with the side-chain functionalities of typical peptides and proteins. These characteristics might prove advantageous for the design or selection of catalytic constructs or biomaterials that are capable of dynamic sequence repair and adaptation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ura, Yasuyuki -- Beierle, John M -- Leman, Luke J -- Orgel, Leslie E -- Ghadiri, M Reza -- New York, N.Y. -- Science. 2009 Jul 3;325(5936):73-7. doi: 10.1126/science.1174577. Epub 2009 Jun 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19520909" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/chemistry ; Amino Acids/chemistry ; Base Pairing ; Base Sequence ; Biotinylation ; DNA/*chemistry ; Dipeptides/chemistry ; Models, Molecular ; Molecular Structure ; Nucleic Acid Conformation ; Oligonucleotides/chemistry ; Peptide Nucleic Acids/*chemistry ; Peptides/chemistry ; RNA/chemistry
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    Stretching single talin rod molecules activates vinculin binding (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-01-31
    Description: The molecular mechanism by which a mechanical stimulus is translated into a chemical response in biological systems is still unclear. We show that mechanical stretching of single cytoplasmic proteins can activate binding of other molecules. We used magnetic tweezers, total internal reflection fluorescence, and atomic force microscopy to investigate the effect of force on the interaction between talin, a protein that links liganded membrane integrins to the cytoskeleton, and vinculin, a focal adhesion protein that is activated by talin binding, leading to reorganization of the cytoskeleton. Application of physiologically relevant forces caused stretching of single talin rods that exposed cryptic binding sites for vinculin. Thus in the talin-vinculin system, molecular mechanotransduction can occur by protein binding after exposure of buried binding sites in the talin-vinculin system. Such protein stretching may be a more general mechanism for force transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉del Rio, Armando -- Perez-Jimenez, Raul -- Liu, Ruchuan -- Roca-Cusachs, Pere -- Fernandez, Julio M -- Sheetz, Michael P -- New York, N.Y. -- Science. 2009 Jan 30;323(5914):638-41. doi: 10.1126/science.1162912.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19179532" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biophysical Phenomena ; Chickens ; Mechanotransduction, Cellular ; Microscopy, Fluorescence ; Models, Molecular ; Photobleaching ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Talin/*chemistry/*metabolism ; Vinculin/*chemistry/*metabolism
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    Ecology. Thriving in salt (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boetius, Antje -- Joye, Samantha -- New York, N.Y. -- Science. 2009 Jun 19;324(5934):1523-5. doi: 10.1126/science.1172979.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉HGF-MPG Joint Research Group for Deep Sea Ecology and Technology, Alfred Wegener Institute for Polar and Marine Research, 27515 Bremerhaven, Germany. aboetius@mpi-bremen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19541984" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Artemia/physiology ; Chlorophyta/physiology ; *Ecosystem ; Halobacteriaceae/physiology ; *Salinity ; Salts ; Sodium Chloride ; *Water Microbiology
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    Wood energy: protect local ecosystems (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Titus, Brian D -- Maynard, Douglas G -- Dymond, Caren C -- Stinson, Graham -- Kurz, Werner A -- New York, N.Y. -- Science. 2009 Jun 12;324(5933):1389-90; author reply 1390-1. doi: 10.1126/science.324_1389c.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Natural Resources Canada, Pacific Forestry Centre, Victoria, BC V8Z 1M5, Canada. Brian.Titus@NRCan-RNCan.gc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19520938" target="_blank"〉PubMed〈/a〉
    Keywords: Biomass ; *Ecosystem ; *Energy-Generating Resources ; European Union ; *Trees ; United States ; *Wood
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    Conservation biology. Exxon Valdez turns 20 (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guterman, Lila -- New York, N.Y. -- Science. 2009 Mar 20;323(5921):1558-9. doi: 10.1126/science.323.5921.1558.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19299600" target="_blank"〉PubMed〈/a〉
    Keywords: Accidents ; Alaska ; Animals ; *Animals, Wild ; Birds ; Conservation of Natural Resources ; *Ecosystem ; *Environmental Pollution ; Fishes ; Otters ; *Petroleum ; Population Dynamics ; Research ; Ships ; Whales
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    Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-06-27
    Description: Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2764269/" 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/PMC2764269/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Horn, Wade D -- Kim, Hak-Jun -- Ellis, Charles D -- Hadziselimovic, Arina -- Sulistijo, Endah S -- Karra, Murthy D -- Tian, Changlin -- Sonnichsen, Frank D -- Sanders, Charles R -- R01 GM047485/GM/NIGMS NIH HHS/ -- R01 GM047485-17/GM/NIGMS NIH HHS/ -- R01 GM47485/GM/NIGMS NIH HHS/ -- T32 NS007491/NS/NINDS NIH HHS/ -- T32 NS007491-09/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2009 Jun 26;324(5935):1726-9. doi: 10.1126/science.1171716.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19556511" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Biocatalysis ; Catalytic Domain ; Cell Membrane/enzymology ; Diacylglycerol Kinase/*chemistry/metabolism ; Escherichia coli/*enzymology ; Escherichia coli Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Protein Folding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Protein dynamism and evolvability (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-11
    Description: The traditional view that proteins possess absolute functional specificity and a single, fixed structure conflicts with their marked ability to adapt and evolve new functions and structures. We consider an alternative, "avant-garde view" in which proteins are conformationally dynamic and exhibit functional promiscuity. We surmise that these properties are the foundation stones of protein evolvability; they facilitate the divergence of new functions within existing folds and the evolution of entirely new folds. Packing modes of proteins also affect their evolvability, and poorly packed, disordered, and conformationally diverse proteins may exhibit high evolvability. This dynamic view of protein structure, function, and evolvability is extrapolated to describe hypothetical scenarios for the evolution of the early proteins and future research directions in the area of protein dynamism and evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tokuriki, Nobuhiko -- Tawfik, Dan S -- New York, N.Y. -- Science. 2009 Apr 10;324(5924):203-7. doi: 10.1126/science.1169375.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19359577" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; *Evolution, Molecular ; Ligands ; Models, Molecular ; Mutation ; Protein Conformation ; Protein Folding ; Proteins/*chemistry/genetics/*physiology
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    Cell biology. The force is with us (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwartz, Martin A -- New York, N.Y. -- Science. 2009 Jan 30;323(5914):588-9. doi: 10.1126/science.1169414.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Cardiovascular Research Center and Mellon Urological Cancer Research Institute, University of Virginia, Charlottesville, VA 22908, USA. maschwartz@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19179515" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Adhesion ; Fibronectins/chemistry/*metabolism ; Focal Adhesion Protein-Tyrosine Kinases/metabolism ; Humans ; Integrin alpha5beta1/chemistry/*metabolism ; *Mechanotransduction, Cellular ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Talin/chemistry/*metabolism ; Vinculin/*metabolism
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    Widespread increase of tree mortality rates in the western United States (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-01-24
    Description: Persistent changes in tree mortality rates can alter forest structure, composition, and ecosystem services such as carbon sequestration. Our analyses of longitudinal data from unmanaged old forests in the western United States showed that background (noncatastrophic) mortality rates have increased rapidly in recent decades, with doubling periods ranging from 17 to 29 years among regions. Increases were also pervasive across elevations, tree sizes, dominant genera, and past fire histories. Forest density and basal area declined slightly, which suggests that increasing mortality was not caused by endogenous increases in competition. Because mortality increased in small trees, the overall increase in mortality rates cannot be attributed solely to aging of large trees. Regional warming and consequent increases in water deficits are likely contributors to the increases in tree mortality rates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Mantgem, Phillip J -- Stephenson, Nathan L -- Byrne, John C -- Daniels, Lori D -- Franklin, Jerry F -- Fule, Peter Z -- Harmon, Mark E -- Larson, Andrew J -- Smith, Jeremy M -- Taylor, Alan H -- Veblen, Thomas T -- New York, N.Y. -- Science. 2009 Jan 23;323(5913):521-4. doi: 10.1126/science.1165000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Geological Survey, Western Ecological Research Center, Three Rivers, CA 93271, USA. pvanmantgem@usgs.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19164752" target="_blank"〉PubMed〈/a〉
    Keywords: Abies/anatomy & histology/growth & development ; *Climate ; *Coniferophyta/anatomy & histology/growth & development ; *Ecosystem ; Fires ; Models, Statistical ; Nonlinear Dynamics ; Northwestern United States ; Pinus/anatomy & histology/growth & development ; Temperature ; *Trees/growth & development ; Tsuga/anatomy & histology/growth & development ; United States
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    Science and regulation. New science for chemicals policy (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarzman, Megan R -- Wilson, Michael P -- 5U19EH000097-04/EH/NCEH CDC HHS/ -- New York, N.Y. -- Science. 2009 Nov 20;326(5956):1065-6. doi: 10.1126/science.1177537.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Occupational and Environmental Health, School of Public Health, University of California at Berkeley, Berkeley, CA 94720, USA. mschwarzman@berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965413" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Industry/*legislation & jurisprudence ; *Ecosystem ; *Endocrine Disruptors/toxicity ; *Environmental Pollutants/toxicity ; European Union ; *Hazardous Substances/toxicity ; *Public Policy ; Risk Assessment ; United States ; United States Environmental Protection Agency
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    Bringing coral reefs back from the living dead (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):559-61. doi: 10.1126/science.325_559.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644105" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa/genetics/growth & development/physiology ; Biodiversity ; *Conservation of Natural Resources/economics/methods ; *Ecosystem ; Genetic Variation ; Larva/physiology ; Reproduction
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    Restoring a 'biological desert' on Borneo (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):557. doi: 10.1126/science.325_557.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644104" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Borneo ; *Conservation of Natural Resources ; *Ecosystem ; *Pongo pygmaeus ; *Trees/growth & development
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  • 84
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    Good genes and good luck: ammonoid diversity and the end-Permian mass extinction (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-29
    Description: The end-Permian mass extinction removed more than 80% of marine genera. Ammonoid cephalopods were among the organisms most affected by this crisis. The analysis of a global diversity data set of ammonoid genera covering about 106 million years centered on the Permian-Triassic boundary (PTB) shows that Triassic ammonoids actually reached levels of diversity higher than in the Permian less than 2 million years after the PTB. The data favor a hierarchical rather than logistic model of diversification coupled with a niche incumbency hypothesis. This explosive and nondelayed diversification contrasts with the slow and delayed character of the Triassic biotic recovery as currently illustrated for other, mainly benthic groups such as bivalves and gastropods.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brayard, Arnaud -- Escarguel, Gilles -- Bucher, Hugo -- Monnet, Claude -- Bruhwiler, Thomas -- Goudemand, Nicolas -- Galfetti, Thomas -- Guex, Jean -- New York, N.Y. -- Science. 2009 Aug 28;325(5944):1118-21. doi: 10.1126/science.1174638.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UMR-CNRS 5561 Biogeosciences, Universite de Bourgogne, 6 Boulevard Gabriel, F-21000, Dijon, France. arnaud.brayard@u-bourgogne.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19713525" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Biological Evolution ; *Cephalopoda/classification/genetics ; Climate ; Databases, Factual ; *Ecosystem ; *Extinction, Biological ; Oceans and Seas ; Paleontology ; Population Dynamics ; Seawater
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    A sulfilimine bond identified in collagen IV (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-09-05
    Description: Collagen IV networks are ancient proteins of basement membranes that underlie epithelia in metazoa from sponge to human. The networks provide structural integrity to tissues and serve as ligands for integrin cell-surface receptors. They are assembled by oligomerization of triple-helical protomers and are covalently crosslinked, a key reinforcement that stabilizes networks. We used Fourier-transform ion cyclotron resonance mass spectrometry and nuclear magnetic resonance spectroscopy to show that a sulfilimine bond (-S=N-) crosslinks hydroxylysine-211 and methionine-93 of adjoining protomers, a bond not previously found in biomolecules. This bond, the nitrogen analog of a sulfoxide, appears to have arisen at the divergence of sponge and cnidaria, an adaptation of the extracellular matrix in response to mechanical stress in metazoan evolution.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2876822/" 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/PMC2876822/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vanacore, Roberto -- Ham, Amy-Joan L -- Voehler, Markus -- Sanders, Charles R -- Conrads, Thomas P -- Veenstra, Timothy D -- Sharpless, K Barry -- Dawson, Philip E -- Hudson, Billy G -- DC007416/DC/NIDCD NIH HHS/ -- DK065123/DK/NIDDK NIH HHS/ -- DK18381/DK/NIDDK NIH HHS/ -- GM059380/GM/NIGMS NIH HHS/ -- P01 DK065123/DK/NIDDK NIH HHS/ -- P01 DK065123-07/DK/NIDDK NIH HHS/ -- R01 DC007416/DC/NIDCD NIH HHS/ -- R01 DC007416-05/DC/NIDCD NIH HHS/ -- R01 GM059380/GM/NIGMS NIH HHS/ -- R01 GM059380-09/GM/NIGMS NIH HHS/ -- R37 DK018381/DK/NIDDK NIH HHS/ -- R37 DK018381-37/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2009 Sep 4;325(5945):1230-4. doi: 10.1126/science.1176811.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Nephrology, Department of Medicine and Center for Matrix Biology, Vanderbilt University, Nashville, TN 37232, USA. roberto.vanacore@vanderbilt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19729652" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Collagen Type IV/*chemistry ; Humans ; Hydroxylysine/chemistry ; Mass Spectrometry ; Methionine/chemistry ; Models, Molecular ; Molecular Sequence Data ; Nitrogen/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Physicochemical Processes ; Protein Conformation ; Protein Multimerization ; Protein Subunits/chemistry ; Sequence Alignment ; Stress, Mechanical ; Sulfur/chemistry
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    Regulators of PP2C phosphatase activity function as abscisic acid sensors (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-02
    Description: The plant hormone abscisic acid (ABA) acts as a developmental signal and as an integrator of environmental cues such as drought and cold. Key players in ABA signal transduction include the type 2C protein phosphatases (PP2Cs) ABI1 and ABI2, which act by negatively regulating ABA responses. In this study, we identify interactors of ABI1 and ABI2 which we have named regulatory components of ABA receptor (RCARs). In Arabidopsis, RCARs belong to a family with 14 members that share structural similarity with class 10 pathogen-related proteins. RCAR1 was shown to bind ABA, to mediate ABA-dependent inactivation of ABI1 or ABI2 in vitro, and to antagonize PP2C action in planta. Other RCARs also mediated ABA-dependent regulation of ABI1 and ABI2, consistent with a combinatorial assembly of receptor complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ma, Yue -- Szostkiewicz, Izabela -- Korte, Arthur -- Moes, Daniele -- Yang, Yi -- Christmann, Alexander -- Grill, Erwin -- New York, N.Y. -- Science. 2009 May 22;324(5930):1064-8. doi: 10.1126/science.1172408. Epub 2009 Apr 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl fur Botanik, Technische Universitat Munchen, Am Hochanger 4, D-85354 Freising, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19407143" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*metabolism/pharmacology ; Amino Acid Sequence ; Arabidopsis/genetics/*metabolism/physiology ; Arabidopsis Proteins/antagonists & inhibitors/chemistry/genetics/*metabolism ; Binding Sites ; Carrier Proteins/chemistry/genetics/*metabolism ; Gene Expression Regulation, Plant ; Germination ; Molecular Sequence Data ; Phosphoprotein Phosphatases/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; Plant Roots/growth & development ; Plant Stomata/physiology ; Plants, Genetically Modified ; Point Mutation ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Stereoisomerism ; Up-Regulation
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    Paleontology. Flourishing after the end-Permian mass extinction (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, Charles R -- Jacobs, David K -- New York, N.Y. -- Science. 2009 Aug 28;325(5944):1079-80. doi: 10.1126/science.1178325.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Invertebrate Paleontology, Museum of Comparative Zoology, Harvard University, Cambridge, MA 02138, USA. cmarshall@oeb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19713513" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Cephalopoda ; *Ecosystem ; *Extinction, Biological ; *Fossils ; Greenhouse Effect ; Oceans and Seas ; Oxygen ; Paleontology ; Population Dynamics ; Seawater
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    Ecology. Peter principle packs a peck of phytoplankton (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grunbaum, Daniel -- New York, N.Y. -- Science. 2009 Feb 20;323(5917):1022-3. doi: 10.1126/science.1170662.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Oceanography, University of Washington, Seattle, WA 98195-7940, USA. grunbaum@ocean.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19229028" target="_blank"〉PubMed〈/a〉
    Keywords: Biodiversity ; Biomechanical Phenomena ; Cell Shape ; *Ecosystem ; Eukaryota/cytology/*physiology ; Flagella/physiology ; Movement ; Phytoplankton/cytology/*physiology ; *Water ; *Water Movements
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Bushmeat hunting as climate threat (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brodie, Jedediah F -- Gibbs, Holly K -- New York, N.Y. -- Science. 2009 Oct 16;326(5951):364-5. doi: 10.1126/science.326_364b.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wildlife Biology Program, University of Montana, Missoula, MT 59802, USA. jedediah.brodie@gmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19833939" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; *Climatic Processes ; *Conservation of Natural Resources ; *Ecosystem ; Extinction, Biological ; Meat ; Population Dynamics ; *Tropical Climate ; *Vertebrates
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    Deep-sea, swimming worms with luminescent "bombs" (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-22
    Description: By using remotely operated vehicles, we found seven previously unknown species of swimming annelid worms below 1800 meters. Specimens were large and bore a variety of elaborate head appendages. In addition, five species have pairs of ellipsoidal organs homologous to branchiae that produce brilliant green bioluminescence when autotomized. Five genes were used to determine the evolutionary relationships of these worms within Cirratuliformia. These species form a clade within Acrocirridae and were not closely related to either of the two known pelagic cirratuliforms. Thus, this clade represents a third invasion of the pelagic realm from Cirratuliformia. This finding emphasizes the wealth of discoveries to be made in pelagic and deep demersal habitats.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Osborn, Karen J -- Haddock, Steven H D -- Pleijel, Fredrik -- Madin, Laurence P -- Rouse, Greg W -- New York, N.Y. -- Science. 2009 Aug 21;325(5943):964. doi: 10.1126/science.1172488.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Institution of Oceanography, La Jolla, CA 92093, USA. kjosborn@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19696343" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Ecosystem ; Luminescence ; Molecular Sequence Data ; Polychaeta/*anatomy & histology/classification/genetics/*physiology ; *Seawater ; Swimming
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  • 91
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    Structural insight into nascent polypeptide chain-mediated translational stalling (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-11-26
    Description: Expression of the Escherichia coli tryptophanase operon depends on ribosome stalling during translation of the upstream TnaC leader peptide, a process for which interactions between the TnaC nascent chain and the ribosomal exit tunnel are critical. We determined a 5.8 angstrom-resolution cryo-electron microscopy and single-particle reconstruction of a ribosome stalled during translation of the tnaC leader gene. The nascent chain was extended within the exit tunnel, making contacts with ribosomal components at distinct sites. Upon stalling, two conserved residues within the peptidyltransferase center adopted conformations that preclude binding of release factors. We propose a model whereby interactions within the tunnel are relayed to the peptidyltransferase center to inhibit translation. Moreover, we show that nascent chains adopt distinct conformations within the ribosomal exit tunnel.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2920484/" 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/PMC2920484/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seidelt, Birgit -- Innis, C Axel -- Wilson, Daniel N -- Gartmann, Marco -- Armache, Jean-Paul -- Villa, Elizabeth -- Trabuco, Leonardo G -- Becker, Thomas -- Mielke, Thorsten -- Schulten, Klaus -- Steitz, Thomas A -- Beckmann, Roland -- GM022778/GM/NIGMS NIH HHS/ -- P41 RR005969/RR/NCRR NIH HHS/ -- P41 RR005969-19/RR/NCRR NIH HHS/ -- P41-RR05969/RR/NCRR NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Dec 4;326(5958):1412-5. doi: 10.1126/science.1177662. Epub 2009 Oct 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Center and Center for Integrated Protein Science Munich (CIPSM), Department for Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19933110" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cryoelectron Microscopy ; Escherichia coli/*genetics/metabolism ; Escherichia coli Proteins/*chemistry/genetics/*metabolism/ultrastructure ; Gene Expression Regulation, Bacterial ; Image Processing, Computer-Assisted ; Models, Biological ; Models, Molecular ; Operon ; Peptidyl Transferases/metabolism ; *Protein Biosynthesis ; Protein Conformation ; RNA-Binding Proteins/chemistry/metabolism/ultrastructure ; Ribosomal Proteins/chemistry/metabolism/ultrastructure ; Ribosomes/*metabolism/ultrastructure ; Tryptophanase/biosynthesis/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Species invasions and the limits to restoration: learning from the New Zealand experience (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: Species invasions impose key biotic thresholds limiting the success of ecological restoration projects. These thresholds may be difficult to reverse and will have long-term consequences for restoration because of invasion legacies such as extinctions; because most invasive species cannot be eliminated given current technology and resources; and because even when controlled to low levels, invasive species continue to exert substantial pressure on native biodiversity. Restoration outcomes in the face of biological invasions are likely to be novel and will require long-term resource commitment, as any letup in invasive species management will result in the loss of the conservation gains achieved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norton, David A -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):569-71. doi: 10.1126/science.1172978.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rural Ecology Research Group, School of Forestry, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand. david.norton@canterbury.ac.nz〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644109" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Conservation of Natural Resources/trends ; *Ecosystem ; *Environment ; Forecasting ; New Zealand ; Pest Control ; Plant Development ; *Plants ; Population Dynamics ; Trees
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-17
    Description: The ribosome selects a correct transfer RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA. Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. The signaling pathway that leads to GTP hydrolysis upon codon recognition is critical to accurate decoding. Here we present the crystal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolution. The structure reveals details of the tRNA distortion that allows aminoacyl-tRNA to interact simultaneously with the decoding center of the 30S subunit and EF-Tu at the factor binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the guanosine triphosphatase center of EF-Tu.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3763470/" 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/PMC3763470/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmeing, T Martin -- Voorhees, Rebecca M -- Kelley, Ann C -- Gao, Yong-Gui -- Murphy, Frank V 4th -- Weir, John R -- Ramakrishnan, V -- 082086/Wellcome Trust/United Kingdom -- MC_U105184332/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Oct 30;326(5953):688-94. doi: 10.1126/science.1179700. Epub 2009 Oct 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19833920" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Enzyme Activation ; GTP Phosphohydrolases/metabolism ; Genetic Code ; Models, Molecular ; Nucleic Acid Conformation ; Peptide Elongation Factor Tu/*chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Bacterial/*chemistry ; RNA, Transfer, Amino Acyl/*chemistry ; RNA, Transfer, Phe/chemistry ; RNA, Transfer, Thr/chemistry ; Ribosomes/*chemistry ; Thermus thermophilus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Ecology. The forgotten megafauna (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hansen, Dennis M -- Galetti, Mauro -- New York, N.Y. -- Science. 2009 Apr 3;324(5923):42-3. doi: 10.1126/science.1172393.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, 371 Serra Mall, Stanford University, Stanford, CA 94305, USA. dmhansen@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19342573" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Body Size ; *Ecosystem ; *Extinction, Biological ; Feeding Behavior ; Geography ; Seeds ; *Vertebrates/anatomy & histology/physiology
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  • 95
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    Harnessing carbon payments to protect biodiversity (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: Initiatives to reduce carbon emissions from deforestation and degradation (REDD) are providing increasing incentives for forest protection. The collateral benefits for biodiversity depend on the extent to which emissions reductions and biodiversity conservation can be achieved in the same places. Globally, we demonstrate spatial trade-offs in allocating funds to protect forests for carbon and biodiversity and show that cost-effective spending for REDD would protect relatively few species of forest vertebrates. Because trade-offs are nonlinear, we discover that minor adjustments to the allocation of funds could double the biodiversity protected by REDD, while reducing carbon outcomes by only 4 to 8%.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venter, Oscar -- Laurance, William F -- Iwamura, Takuya -- Wilson, Kerrie A -- Fuller, Richard A -- Possingham, Hugh P -- New York, N.Y. -- Science. 2009 Dec 4;326(5958):1368. doi: 10.1126/science.1180289.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Ecology Centre, University of Queensland, Brisbane, Queensland 4072, Australia. oventer@uq.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965752" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atmosphere ; *Biodiversity ; *Carbon ; Conservation of Natural Resources/*economics ; Cost-Benefit Analysis ; Developing Countries ; *Ecosystem ; Models, Statistical ; *Trees
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Medicine. A reinnervating microRNA (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, Robert H -- New York, N.Y. -- Science. 2009 Dec 11;326(5959):1494-5. doi: 10.1126/science.1183842.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurology, Biochemistry and Molecular Pharmacology and Program in Neuroscience, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA. robert.brown@umassmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20007892" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/pathology/*physiopathology ; Animals ; Binding Sites ; Carrier Proteins/metabolism ; Disease Models, Animal ; Histone Deacetylases/metabolism ; Mice ; Mice, Transgenic ; MicroRNAs/genetics/*metabolism ; Muscle Cells/enzymology ; Muscle Denervation ; Muscle, Skeletal/innervation/metabolism ; Myostatin/genetics ; Neuromuscular Junction/*pathology/*physiology ; RNA Interference ; Sequence Analysis, RNA ; Signal Transduction
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  • 97
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    Climate-driven basin-scale decadal oscillations of oceanic phytoplankton (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: Phytoplankton--the microalgae that populate the upper lit layers of the ocean--fuel the oceanic food web and affect oceanic and atmospheric carbon dioxide levels through photosynthetic carbon fixation. Here, we show that multidecadal changes in global phytoplankton abundances are related to basin-scale oscillations of the physical ocean, specifically the Pacific Decadal Oscillation and the Atlantic Multidecadal Oscillation. This relationship is revealed in approximately 20 years of satellite observations of chlorophyll and sea surface temperature. Interaction between the main pycnocline and the upper ocean seasonal mixed layer is one mechanism behind this correlation. Our findings provide a context for the interpretation of contemporary changes in global phytoplankton and should improve predictions of their future evolution with climate change.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez, Elodie -- Antoine, David -- D'Ortenzio, Fabrizio -- Gentili, Bernard -- New York, N.Y. -- Science. 2009 Nov 27;326(5957):1253-6. doi: 10.1126/science.1177012.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UPMC University of Paris 06, UMR 7093, Laboratoire d'Oceanographie de Villefranche (LOV), 06230 Villefranche-sur-Mer, France. martinez@obs-vlfr.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965473" target="_blank"〉PubMed〈/a〉
    Keywords: Atlantic Ocean ; Biomass ; Chlorophyll/*analysis ; *Climate ; *Ecosystem ; Global Warming ; Indian Ocean ; Oceans and Seas ; Pacific Ocean ; Phytoplankton/*physiology ; Population Dynamics ; Seasons ; *Seawater/chemistry ; Temperature ; Time Factors
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  • 98
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    Rapid resurgence of marine productivity after the Cretaceous-Paleogene mass extinction (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-03
    Description: The course of the biotic recovery after the impact-related disruption of photosynthesis and mass extinction event at the Cretaceous-Paleogene boundary has been intensely debated. The resurgence of marine primary production in the aftermath remains poorly constrained because of the paucity of fossil records tracing primary producers that lack skeletons. Here we present a high-resolution record of geochemical variation in the remarkably thick Fiskeler (also known as the Fish Clay) boundary layer at Kulstirenden, Denmark. Converging evidence from the stable isotopes of carbon and nitrogen and abundances of algal steranes and bacterial hopanes indicates that algal primary productivity was strongly reduced for only a brief period of possibly less than a century after the impact, followed by a rapid resurgence of carbon fixation and ecological reorganization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sepulveda, Julio -- Wendler, Jens E -- Summons, Roger E -- Hinrichs, Kai-Uwe -- New York, N.Y. -- Science. 2009 Oct 2;326(5949):129-32. doi: 10.1126/science.1176233.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Organic Geochemistry Group, Department of Geosciences, and Center for Marine Environmental Sciences (MARUM), University of Bremen, 28334 Bremen, Germany. juliosep@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19797658" target="_blank"〉PubMed〈/a〉
    Keywords: Biomarkers/analysis ; Carbon Isotopes ; Cyanobacteria/physiology ; Denmark ; *Ecosystem ; Eukaryota/*physiology ; *Extinction, Biological ; Geologic Sediments ; Nitrogen Isotopes ; Photosynthesis ; Phytoplankton/physiology ; Polycyclic Compounds/analysis ; Seawater/chemistry/*microbiology ; Time ; Triterpenes/analysis
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    Environmental science. Peatland response to global change (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-11-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dise, Nancy B -- New York, N.Y. -- Science. 2009 Nov 6;326(5954):810-1. doi: 10.1126/science.1174268.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental and Geographical Sciences, Manchester Metropolitan University, John Dalton Building, Chester Street, Manchester M1 5GD, UK. n.dise@mmu.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19892972" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Agriculture ; Biomass ; *Carbon ; *Climate Change ; *Ecosystem ; Global Warming ; Methane ; Mining ; *Soil ; Sphagnopsida/growth & development/*physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Pollination and restoration (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-01
    Description: Pollination services underpin sustainability of restored ecosystems. Yet, outside of agri-environments, effective restoration of pollinator services in ecological restoration has received little attention. This deficiency in the knowledge needed to restore pollinator capability represents a major liability in restoration programs, particularly in regions where specialist invertebrate and vertebrate pollinators exist, such as global biodiversity hotspots. When compounded with the likely negative impacts of climate change on pollination services, the need to understand and manage pollinator services in restoration becomes paramount.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dixon, Kingsley W -- New York, N.Y. -- Science. 2009 Jul 31;325(5940):571-3. doi: 10.1126/science.1176295.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Plant Biology, The University of Western Australia, Nedlands, 6009 Kings Park and Botanic Garden, West Perth 6005, Western Australia, Australia. kingsley.dixon@bgpa.wa.gov.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19644110" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Climatic Processes ; *Conservation of Natural Resources ; *Ecosystem ; Extinction, Biological ; Geography ; Greenhouse Effect ; Plant Physiological Phenomena ; *Plants ; *Pollination
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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