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  • *Climate Change  (50)
  • *Ecosystem  (32)
  • Protein Structure, Tertiary  (32)
  • American Association for the Advancement of Science (AAAS)  (106)
  • Copernicus
  • Hindawi
  • 2010-2014  (106)
  • 1980-1984
  • 2013  (106)
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Keywords
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  • 2010-2014  (106)
  • 1980-1984
Year
  • 101
    Publication Date: 2013-08-03
    Description: Biotic interactions drive key ecological and evolutionary processes and mediate ecosystem responses to climate change. The direction, frequency, and intensity of biotic interactions can in turn be altered by climate change. Understanding the complex interplay between climate and biotic interactions is thus essential for fully anticipating how ecosystems will respond to the fast rates of current warming, which are unprecedented since the end of the last glacial period. We highlight episodes of climate change that have disrupted ecosystems and trophic interactions over time scales ranging from years to millennia by changing species' relative abundances and geographic ranges, causing extinctions, and creating transient and novel communities dominated by generalist species and interactions. These patterns emerge repeatedly across disparate temporal and spatial scales, suggesting the possibility of similar underlying processes. Based on these findings, we identify knowledge gaps and fruitful areas for research that will further our understanding of the effects of climate change on ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blois, Jessica L -- Zarnetske, Phoebe L -- Fitzpatrick, Matthew C -- Finnegan, Seth -- New York, N.Y. -- Science. 2013 Aug 2;341(6145):499-504. doi: 10.1126/science.1237184.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Natural Sciences, University of California, Merced, Merced, CA 95343, USA. jblois@ucmerced.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23908227" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Climate Change ; *Ecosystem ; *Extinction, Biological ; Forecasting ; Fossils ; Invertebrates ; Plants
    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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  • 102
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2013-08-03
    Description: As climates change across already stressed ecosystems, there is no doubt that species will be affected, but to what extent and which will be most vulnerable remain uncertain. The fossil record suggests that most species persisted through past climate change, whereas forecasts of future impacts predict large-scale range reduction and extinction. Many species have altered range limits and phenotypes through 20th-century climate change, but responses are highly variable. The proximate causes of species decline relative to resilience remain largely obscure; however, recent examples of climate-associated species decline can help guide current management in parallel with ongoing research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moritz, Craig -- Agudo, Rosa -- New York, N.Y. -- Science. 2013 Aug 2;341(6145):504-8. doi: 10.1126/science.1237190.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research School of Biology and Centre for Biodiversity Analysis, The Australian National University, Canberra, ACT 0200, Australia. gekkojessie@gmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23908228" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birds ; *Climate Change ; *Ecosystem ; *Extinction, Biological ; Forecasting ; Mammals ; Temperature
    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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  • 103
    Publication Date: 2013-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moss, R H -- Meehl, G A -- Lemos, M C -- Smith, J B -- Arnold, J R -- Arnott, J C -- Behar, D -- Brasseur, G P -- Broomell, S B -- Busalacchi, A J -- Dessai, S -- Ebi, K L -- Edmonds, J A -- Furlow, J -- Goddard, L -- Hartmann, H C -- Hurrell, J W -- Katzenberger, J W -- Liverman, D M -- Mote, P W -- Moser, S C -- Kumar, A -- Pulwarty, R S -- Seyller, E A -- Turner, B L 2nd -- Washington, W M -- Wilbanks, T J -- New York, N.Y. -- Science. 2013 Nov 8;342(6159):696-8. doi: 10.1126/science.1239569.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24202163" target="_blank"〉PubMed〈/a〉
    Keywords: *Climate Change ; *Disaster Planning ; *Floods ; Research/*organization & administration ; United States
    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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  • 104
    Publication Date: 2013-01-19
    Description: The retinoic acid-inducible gene I (RIG-I)-like receptor (RLR) melanoma differentiation-associated protein 5 (MDA5) senses cytoplasmic viral RNA and activates antiviral innate immunity. To reveal how paramyxoviruses counteract this response, we determined the crystal structure of the MDA5 adenosine 5'-triphosphate (ATP)-hydrolysis domain in complex with the viral inhibitor V protein. The V protein unfolded the ATP-hydrolysis domain of MDA5 via a beta-hairpin motif and recognized a structural motif of MDA5 that is normally buried in the conserved helicase fold. This leads to disruption of the MDA5 ATP-hydrolysis site and prevention of RNA-bound MDA5 filament formation. The structure explains why V proteins inactivate MDA5, but not RIG-I, and mutating only two amino acids in RIG-I induces robust V protein binding. Our results suggest an inhibition mechanism of RLR signalosome formation by unfolding of receptor and inhibitor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Motz, Carina -- Schuhmann, Kerstin Monika -- Kirchhofer, Axel -- Moldt, Manuela -- Witte, Gregor -- Conzelmann, Karl-Klaus -- Hopfner, Karl-Peter -- U19AI083025/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2013 Feb 8;339(6120):690-3. doi: 10.1126/science.1230949. Epub 2013 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Gene Center, Ludwig-Maximilians-University, Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23328395" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; DEAD-box RNA Helicases/*chemistry/genetics/*metabolism ; HEK293 Cells ; Humans ; Hydrolysis ; Immunity, Innate ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Parainfluenza Virus 5/immunology ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; RNA, Double-Stranded/*metabolism ; Signal Transduction ; Sus scrofa ; Viral Proteins/*chemistry/genetics/*metabolism
    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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  • 105
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2013-05-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fadeel, Bengt -- Karlsson, Hanna L -- Bhattacharya, Kunal -- New York, N.Y. -- Science. 2013 May 3;340(6132):548-9. doi: 10.1126/science.340.6132.548-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23641092" target="_blank"〉PubMed〈/a〉
    Keywords: *Climate Change ; Earth Sciences/*standards ; *Government Regulation ; Research/*standards ; *Social Control, Informal
    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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  • 106
    Publication Date: 2013-05-25
    Description: The Ski2-like RNA helicase Brr2 is a core component of the spliceosome that must be tightly regulated to ensure correct timing of spliceosome activation. Little is known about mechanisms of regulation of Ski2-like helicases by protein cofactors. Here we show by crystal structure and biochemical analyses that the Prp8 protein, a major regulator of the spliceosome, can insert its C-terminal tail into Brr2's RNA-binding tunnel, thereby intermittently blocking Brr2's RNA-binding, adenosine triphosphatase, and U4/U6 unwinding activities. Inefficient Brr2 repression is the only recognizable phenotype associated with certain retinitis pigmentosa-linked Prp8 mutations that map to its C-terminal tail. Our data show how a Ski2-like RNA helicase can be reversibly inhibited by a protein cofactor that directly competes with RNA substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mozaffari-Jovin, Sina -- Wandersleben, Traudy -- Santos, Karine F -- Will, Cindy L -- Luhrmann, Reinhard -- Wahl, Markus C -- New York, N.Y. -- Science. 2013 Jul 5;341(6141):80-4. doi: 10.1126/science.1237515. Epub 2013 May 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23704370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; *Binding, Competitive ; Carrier Proteins/genetics/*metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Protein Structure, Tertiary ; RNA/*metabolism ; RNA Helicases/metabolism ; RNA-Binding Proteins ; Ribonucleoprotein, U4-U6 Small Nuclear/metabolism ; Ribonucleoprotein, U5 Small Nuclear/metabolism ; Ribonucleoproteins, Small Nuclear/*antagonists & inhibitors/chemistry/*metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Spliceosomes/*metabolism ; Substrate Specificity
    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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