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  • Articles  (69)
  • *Ecosystem  (39)
  • Rats  (30)
  • American Association for the Advancement of Science (AAAS)  (69)
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  • 1
    Publication Date: 2003-12-04
    Description: The net ecosystem exchange of carbon dioxide was measured by eddy covariance methods for 3 years in two old-growth forest sites near Santarem, Brazil. Carbon was lost in the wet season and gained in the dry season, which was opposite to the seasonal cycles of both tree growth and model predictions. The 3-year average carbon loss was 1.3 (confidence interval: 0.0 to 2.0) megagrams of carbon per hectare per year. Biometric observations confirmed the net loss but imply that it is a transient effect of recent disturbance superimposed on long-term balance. Given that episodic disturbances are characteristic of old-growth forests, it is likely that carbon sequestration is lower than has been inferred from recent eddy covariance studies at undisturbed sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saleska, Scott R -- Miller, Scott D -- Matross, Daniel M -- Goulden, Michael L -- Wofsy, Steven C -- da Rocha, Humberto R -- de Camargo, Plinio B -- Crill, Patrick -- Daube, Bruce C -- de Freitas, Helber C -- Hutyra, Lucy -- Keller, Michael -- Kirchhoff, Volker -- Menton, Mary -- Munger, J William -- Pyle, Elizabeth Hammond -- Rice, Amy H -- Silva, Hudson -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1554-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth and Planetary Sciences, Harvard University, Cambridge, MA 02138, USA. saleska@fas.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645845" target="_blank"〉PubMed〈/a〉
    Keywords: Brazil ; Carbon/*analysis/metabolism ; Carbon Dioxide/*analysis/metabolism ; Confidence Intervals ; *Ecosystem ; Oxygen Consumption ; Photosynthesis ; Rain ; *Seasons ; *Trees/growth & development/metabolism ; Wood
    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
    Publication Date: 2004-09-28
    Description: Unexpected sudden catastrophic shifts may occur in ecosystems, with concomitant losses or gains of ecological and economic resources. Such shifts have been theoretically attributed to positive feedback and bistability of ecosystem states. However, verifications and predictive power with respect to catastrophic responses to a changing environment are lacking for spatially extensive ecosystems. This situation impedes management and recovery strategies for such ecosystems. Here, we review recent studies on various ecosystems that link self-organized patchiness to catastrophic shifts between ecosystem states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rietkerk, Max -- Dekker, Stefan C -- de Ruiter, Peter C -- van de Koppel, Johan -- New York, N.Y. -- Science. 2004 Sep 24;305(5692):1926-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental Sciences, Copernicus Institute, Utrecht University, P.O. Box 80115, 3508 TC Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15448261" target="_blank"〉PubMed〈/a〉
    Keywords: *Ecosystem ; Feedback, Physiological ; Models, Biological ; Plant Physiological Phenomena ; Water
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2009-03-03
    Description: Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease that is familial in 10% of cases. We have identified a missense mutation in the gene encoding fused in sarcoma (FUS) in a British kindred, linked to ALS6. In a survey of 197 familial ALS index cases, we identified two further missense mutations in eight families. Postmortem analysis of three cases with FUS mutations showed FUS-immunoreactive cytoplasmic inclusions and predominantly lower motor neuron degeneration. Cellular expression studies revealed aberrant localization of mutant FUS protein. FUS is involved in the regulation of transcription and RNA splicing and transport, and it has functional homology to another ALS gene, TARDBP, which suggests that a common mechanism may underlie motor neuron degeneration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4516382/" 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/PMC4516382/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vance, Caroline -- Rogelj, Boris -- Hortobagyi, Tibor -- De Vos, Kurt J -- Nishimura, Agnes Lumi -- Sreedharan, Jemeen -- Hu, Xun -- Smith, Bradley -- Ruddy, Deborah -- Wright, Paul -- Ganesalingam, Jeban -- Williams, Kelly L -- Tripathi, Vineeta -- Al-Saraj, Safa -- Al-Chalabi, Ammar -- Leigh, P Nigel -- Blair, Ian P -- Nicholson, Garth -- de Belleroche, Jackie -- Gallo, Jean-Marc -- Miller, Christopher C -- Shaw, Christopher E -- 078662/Wellcome Trust/United Kingdom -- G0300329/Medical Research Council/United Kingdom -- G0500289/Medical Research Council/United Kingdom -- G0501573/Medical Research Council/United Kingdom -- G0600676/Medical Research Council/United Kingdom -- G0600974/Medical Research Council/United Kingdom -- G0900688/Medical Research Council/United Kingdom -- MC_G1000733/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Feb 27;323(5918):1208-11. doi: 10.1126/science.1165942.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Clinical Neuroscience, King's College London, Medical Research Council (MRC) Centre for Neurodegeneration Research, Institute of Psychiatry, London SE5 8AF, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19251628" target="_blank"〉PubMed〈/a〉
    Keywords: Age of Onset ; Amino Acid Sequence ; Amyotrophic Lateral Sclerosis/*genetics/metabolism/pathology ; Animals ; Brain/pathology ; Cell Line ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; DNA-Binding Proteins/analysis/genetics/metabolism ; Female ; Humans ; Inclusion Bodies/chemistry/ultrastructure ; Male ; Molecular Sequence Data ; Motor Neurons/metabolism ; *Mutation, Missense ; Pedigree ; RNA-Binding Protein FUS/analysis/*genetics/*metabolism ; Rats ; Spinal Cord/pathology ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2010-05-15
    Description: It is predicted that climate change will cause species extinctions and distributional shifts in coming decades, but data to validate these predictions are relatively scarce. Here, we compare recent and historical surveys for 48 Mexican lizard species at 200 sites. Since 1975, 12% of local populations have gone extinct. We verified physiological models of extinction risk with observed local extinctions and extended projections worldwide. Since 1975, we estimate that 4% of local populations have gone extinct worldwide, but by 2080 local extinctions are projected to reach 39% worldwide, and species extinctions may reach 20%. Global extinction projections were validated with local extinctions observed from 1975 to 2009 for regional biotas on four other continents, suggesting that lizards have already crossed a threshold for extinctions caused by climate change.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sinervo, Barry -- Mendez-de-la-Cruz, Fausto -- Miles, Donald B -- Heulin, Benoit -- Bastiaans, Elizabeth -- Villagran-Santa Cruz, Maricela -- Lara-Resendiz, Rafael -- Martinez-Mendez, Norberto -- Calderon-Espinosa, Martha Lucia -- Meza-Lazaro, Rubi Nelsi -- Gadsden, Hector -- Avila, Luciano Javier -- Morando, Mariana -- De la Riva, Ignacio J -- Victoriano Sepulveda, Pedro -- Rocha, Carlos Frederico Duarte -- Ibarguengoytia, Nora -- Aguilar Puntriano, Cesar -- Massot, Manuel -- Lepetz, Virginie -- Oksanen, Tuula A -- Chapple, David G -- Bauer, Aaron M -- Branch, William R -- Clobert, Jean -- Sites, Jack W Jr -- New York, N.Y. -- Science. 2010 May 14;328(5980):894-9. doi: 10.1126/science.1184695.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, University of California, Santa Cruz, CA 95064, USA. lizardrps@gmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20466932" target="_blank"〉PubMed〈/a〉
    Keywords: Acclimatization ; Animals ; *Biodiversity ; Biological Evolution ; Body Temperature ; *Climate Change ; *Ecosystem ; *Extinction, Biological ; Female ; Forecasting ; Geography ; Global Warming ; *Lizards/genetics/physiology ; Male ; Mexico ; Models, Biological ; Phylogeny ; Population Dynamics ; Reproduction ; Seasons ; Selection, Genetic ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2011-06-28
    Description: Ecological theory predicts that animal movement is shaped by its efficiency of resource acquisition. Focusing solely on efficiency, however, ignores the fact that animal activity can affect resource availability and distribution. Here, we show that feedback between individual behavior and environmental complexity can explain movement strategies in mussels. Specifically, experiments show that mussels use a Levy walk during the formation of spatially patterned beds, and models reveal that this Levy movement accelerates pattern formation. The emergent patterning in mussel beds, in turn, improves individual fitness. These results suggest that Levy walks evolved as a result of the selective advantage conferred by autonomously generated, emergent spatial patterns in mussel beds. Our results emphasize that an interaction between individual selection and habitat complexity shapes animal movement in natural systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Jager, Monique -- Weissing, Franz J -- Herman, Peter M J -- Nolet, Bart A -- van de Koppel, Johan -- New York, N.Y. -- Science. 2011 Jun 24;332(6037):1551-3. doi: 10.1126/science.1201187.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Spatial Ecology Department, Netherlands Institute of Ecology (NIOO-KNAW), Yerseke, Netherlands. m.dejager@nioo.knaw.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21700872" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Computer Simulation ; Cyanobacteria ; *Ecosystem ; Environment ; Feeding Behavior ; Genetic Fitness ; Locomotion ; Models, Biological ; Mytilus edulis/*physiology ; Population Density ; Probability ; Selection, Genetic
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  • 6
    Publication Date: 2012-06-16
    Description: Seagrasses evolved from terrestrial plants into marine foundation species around 100 million years ago. Their ecological success, however, remains a mystery because natural organic matter accumulation within the beds should result in toxic sediment sulfide levels. Using a meta-analysis, a field study, and a laboratory experiment, we reveal how an ancient three-stage symbiosis between seagrass, lucinid bivalves, and their sulfide-oxidizing gill bacteria reduces sulfide stress for seagrasses. We found that the bivalve-sulfide-oxidizer symbiosis reduced sulfide levels and enhanced seagrass production as measured in biomass. In turn, the bivalves and their endosymbionts profit from organic matter accumulation and radial oxygen release from the seagrass roots. These findings elucidate the long-term success of seagrasses in warm waters and offer new prospects for seagrass ecosystem conservation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van der Heide, Tjisse -- Govers, Laura L -- de Fouw, Jimmy -- Olff, Han -- van der Geest, Matthijs -- van Katwijk, Marieke M -- Piersma, Theunis -- van de Koppel, Johan -- Silliman, Brian R -- Smolders, Alfons J P -- van Gils, Jan A -- New York, N.Y. -- Science. 2012 Jun 15;336(6087):1432-4. doi: 10.1126/science.1219973.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Community and Conservation Ecology Group, Centre for Ecological and Evolutionary Studies, University of Groningen, Post Office Box 11103, 9700 CC Groningen, Netherlands. t.van.der.heide@rug.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22700927" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/growth & development/*physiology ; Animals ; Bacteria/growth & development/*metabolism ; Biomass ; Bivalvia/metabolism/microbiology/*physiology ; Chemoautotrophic Growth ; *Ecosystem ; Geologic Sediments/chemistry ; Gills/microbiology ; Oxidation-Reduction ; Oxygen/metabolism ; Plant Roots/metabolism ; *Seawater/chemistry ; Sulfides/analysis/metabolism ; *Symbiosis ; Zosteraceae/growth & development/*physiology
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  • 7
    Publication Date: 1985-04-19
    Description: Mammalian atria contain peptides that promote the excretion of salt and water from the kidney. When rat atrial tissue is extracted under conditions known to inhibit proteolysis, four natriuretic peptides, cardionatrins I to IV, are consistently isolated. These peptides derive from a common precursor, preprocardionatrin, of 152 amino acids, whose sequence was determined by DNA sequencing of a complementary DNA clone. Amino acid sequencing located the start points of cardionatrins I, III, and IV in the overall sequence. Cardionatrin IV most closely resembles procardionatrin because it begins immediately after the signal sequence at residue 25. Cardionatrin III begins at residue 73, and cardionatrin I, sequenced previously, begins at residue 123. Compositional analysis indicated that each of these cardionatrins extends up to tyrosine at position 150 but lacks the terminal two arginine residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flynn, T G -- Davies, P L -- Kennedy, B P -- de Bold, M L -- de Bold, A J -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):323-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3157217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Atrial Function ; Atrial Natriuretic Factor ; Base Sequence ; Chromatography, High Pressure Liquid ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Muscle Proteins/*genetics/isolation & purification ; *Peptide Fragments ; Protein Precursors/*genetics/isolation & purification ; Rats
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  • 8
    Publication Date: 1998-08-07
    Description: Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin into complexes that also included clathrin and AP-2. Phosphorylation of dynamin 1 and synaptojanin 1 inhibited their binding to amphiphysin, whereas phosphorylation of amphiphysin inhibited its binding to AP-2 and clathrin. Thus, phosphorylation regulates the association and dissociation cycle of the clathrin-based endocytic machinery, and calcium-dependent dephosphorylation of endocytic proteins could prepare nerve terminals for a burst of endocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slepnev, V I -- Ochoa, G C -- Butler, M H -- Grabs, D -- De Camilli, P -- CA46128/CA/NCI NIH HHS/ -- NS36251/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):821-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cell Biology, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694653" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Protein Complex alpha Subunits ; Adaptor Protein Complex beta Subunits ; Adaptor Proteins, Vesicular Transport ; Adenosine Triphosphate/metabolism ; Animals ; Binding Sites ; Carbazoles/pharmacology ; Chromatography, Affinity ; Clathrin/*metabolism ; Cyclosporine/pharmacology ; Dimerization ; Dynamin I ; Dynamins ; *Endocytosis ; Enzyme Inhibitors/pharmacology ; GTP Phosphohydrolases/*metabolism ; Indole Alkaloids ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Phosphoric Monoester Hydrolases/*metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; src Homology Domains
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-08-24
    Description: Clathrin-mediated endocytosis is initiated by the recruitment of the clathrin adaptor protein AP-2 to the plasma membrane where the membrane protein synaptotagmin is thought to act as a docking site. AP-2 also interacts with endocytic motifs present in other cargo proteins. Peptides with a tyrosine-based endocytic motif stimulated binding of AP-2 to synaptotagmin and enhanced AP-2 recruitment to the plasma membrane of neuronal and non-neuronal cells. This suggests a mechanism by which nucleation of clathrin-coated pits is stimulated by the loading of cargo proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haucke, V -- De Camilli, P -- CA46128/CA/NCI NIH HHS/ -- NS36252/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 20;285(5431):1268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10455054" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Protein Complex alpha Subunits ; Adaptor Proteins, Vesicular Transport ; Animals ; Binding Sites ; CHO Cells ; *Calcium-Binding Proteins ; Cattle ; Cell Membrane/metabolism ; Clathrin/*metabolism ; Coated Pits, Cell-Membrane/*metabolism ; Cricetinae ; *Endocytosis ; Membrane Glycoproteins/chemistry/*metabolism ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/chemistry/*metabolism ; Neurons/metabolism ; Oligopeptides/chemistry/metabolism/*pharmacology ; Phospholipase D/metabolism ; Protein Binding ; Rats ; Recombinant Fusion Proteins/metabolism ; Synaptic Membranes/*metabolism ; Synaptotagmins ; Tyrosine/chemistry
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  • 10
    Publication Date: 2001-09-29
    Description: Late Pleistocene changes in oceanic primary productivity along the equator in the Indian and Pacific oceans are revealed by quantitative changes in nanoplankton communities preserved in nine deep-sea cores. We show that variations in equatorial productivity are primarily caused by glacial-interglacial variability and by precession-controlled changes in the east-west thermocline slope of the Indo-Pacific. The precession-controlled variations in productivity are linked to processes similar to the Southern Oscillation phenomenon, and they precede changes in the oxygen isotopic ratio, which indicates that they are not the result of ice sheet fluctuations. The 30,000-year spectral peak in the tropical Indo-Pacific Ocean productivity records is also present in the Antarctica atmospheric CO2 record, suggesting an important role for equatorial biological productivity in modifying atmospheric CO2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beaufort, L -- de Garidel-Thoron, T -- Mix, A C -- Pisias, N G -- New York, N.Y. -- Science. 2001 Sep 28;293(5539):2440-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS-CEREGE, BP 80, 13545 Aix-en-Provence Cedex 04, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11577233" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atmosphere ; Carbon Dioxide ; *Climate ; *Ecosystem ; *Eukaryota ; *Fossils ; Indian Ocean ; Light ; Marine Biology ; Oxygen Isotopes ; Pacific Ocean ; *Plankton ; Seawater ; Time
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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