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  • 1
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    Evapotranspiration along an elevation gradient in California's Sierra Nevada (2013)
    Wiley
    Details
    Publication Date: 2013-01-03
    Description: [1]  We combined observations from four eddy covariance towers with remote sensing to better understand the altitudinal patterns of climate, plant phenology, Gross Ecosystem CO 2 Uptake, and Evapotranspiration (ET) around the Upper Kings River basin in the southern Sierra Nevada Mountains. Precipitation (P) increased with elevation to ∼500 m, and more gradually at higher elevations, while vegetation graded from savanna at 405 m to evergreen oak and pine forest to mid-montane forest to subalpine forest at 2700 m. CO 2 uptake and transpiration at 405 m peaked in spring (March to May) and declined in summer; gas exchange at 1160 and 2015 m continued year-round; gas exchange at 2700 m peaked in summer and ceased in winter. A phenological threshold occurred between 2015 and 2700 m, associated with the development of winter dormancy. Annual ET and Gross Primary Production were greatest at 1160 and 2015 m and reduced at 405 m coincident with less P, and at 2700 m coincident with colder temperatures. The large decline in ET above 2015 m raises the possibility that an upslope redistribution of vegetation with climate change could cause a large increase in upper elevation ET. We extrapolated ET to the entire basin using remote sensing. The 2003–11 P for the entire Upper Kings River basin was 984 mm y −1 and the ET was 429 mm y −1 , yielding a P-ET of 554 mm y −1 , which agrees well with the observed Kings River flow of 563 mm y −1 . ET averaged across the entire basin was nearly constant from year to year.
    Print ISSN: 0148-0227
    Topics: Biology , Geosciences
    Published by Wiley on behalf of American Geophysical Union (AGU).
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  • 2
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    Evapotranspiration along an elevation gradient in California's Sierra Nevada (2012)
    Wiley
    Details
    Publication Date: 2012-09-06
    Description: We combined observations from four eddy covariance towers with remote sensing to better understand the altitudinal patterns of climate, plant phenology, Gross Ecosystem CO2 Uptake, and Evapotranspiration (ET) around the Upper Kings River basin in the southern Sierra Nevada Mountains. Precipitation (P) increased with elevation to ∼500 m, and more gradually at higher elevations, while vegetation graded from savanna at 405 m to evergreen oak and pine forest to mid-montane forest to subalpine forest at 2700 m. CO2 uptake and transpiration at 405 m peaked in spring (March to May) and declined in summer; gas exchange at 1160 and 2015 m continued year-round; gas exchange at 2700 m peaked in summer and ceased in winter. A phenological threshold occurred between 2015 and 2700 m, associated with the development of winter dormancy. Annual ET and Gross Primary Production were greatest at 1160 and 2015 m and reduced at 405 m coincident with less P, and at 2700 m coincident with colder temperatures. The large decline in ET above 2015 m raises the possibility that an upslope redistribution of vegetation with climate change could cause a large increase in upper elevation ET. We extrapolated ET to the entire basin using remote sensing. The 2003–11 P for the entire Upper Kings River basin was 984 mm y−1 and the ET was 429 mm y−1, yielding a P-ET of 554 mm y−1, which agrees well with the observed Kings River flow of 563 mm y−1. ET averaged across the entire basin was nearly constant from year to year.
    Print ISSN: 0148-0227
    Topics: Biology , Geosciences
    Published by Wiley on behalf of American Geophysical Union (AGU).
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  • 3
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    Analytical steady state solutions for water-limited cropping systems using saline irrigation water (2014)
    Wiley
    Details
    Publication Date: 2014-11-25
    Description: Due to the diminishing availability of good quality water for irrigation, it is increasingly important that irrigation and salinity management tools be able to target submaximal crop yields and support the use of marginal quality waters. In this work, we present a steady-state irrigated systems modeling framework that accounts for reduced plant water uptake due to root zone salinity. Two explicit, closed-form analytical solutions for the root zone solute concentration profile are obtained, corresponding to two alternative functional forms of the uptake reduction function. The solutions express a general relationship between irrigation water salinity, irrigation rate, crop salt tolerance, crop transpiration, and (using standard approximations) crop yield. Example applications are illustrated, including the calculation of irrigation requirements for obtaining targeted submaximal yields, and the generation of crop-water production functions for varying irrigation waters, irrigation rates, and crops. Model predictions are shown to be mostly consistent with existing models and available experimental data. Yet the new solutions possess advantages over available alternatives, including: (i) the solutions were derived from a complete physical-mathematical description of the system, rather than based on an ad hoc formulation; (ii) the analytical solutions are explicit and can be evaluated without iterative techniques; (iii) the solutions permit consideration of two common functional forms of salinity induced reductions in crop water uptake, rather than being tied to one particular representation; and (iv) the utilized modeling framework is compatible with leading transient-state numerical models. This article is protected by copyright. All rights reserved.
    Print ISSN: 0043-1397
    Electronic ISSN: 1944-7973
    Topics: Architecture, Civil Engineering, Surveying , Geography
    Published by Wiley on behalf of American Geophysical Union (AGU).
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  • 4
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    Potocytosis: sequestration and transport of small molecules by caveolae (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, R G -- Kamen, B A -- Rothberg, K G -- Lacey, S W -- New York, N.Y. -- Science. 1992 Jan 24;255(5043):410-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1310359" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/physiology ; Cell Membrane/*physiology/ultrastructure ; Cells, Cultured ; *Endocytosis ; Folate Receptors, GPI-Anchored ; Folic Acid/metabolism ; Glycolipids/physiology ; Glycosylphosphatidylinositols ; In Vitro Techniques ; Membrane Glycoproteins/physiology ; Phosphatidylinositols/physiology ; Receptors, Cell Surface/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    LRP: role in vascular wall integrity and protection from atherosclerosis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-12
    Description: Vascular smooth muscle cell (SMC) proliferation and migration are important events in the development of atherosclerosis. The low-density lipoprotein receptor-related protein (LRP1) mediates suppression of SMC migration induced by platelet-derived growth factor (PDGF). Here we show that LRP1 forms a complex with the PDGF receptor (PDGFR). Inactivation of LRP1 in vascular SMCs of mice causes PDGFR overexpression and abnormal activation of PDGFR signaling, resulting in disruption of the elastic layer, SMC proliferation, aneurysm formation, and marked susceptibility to cholesterol-induced atherosclerosis. The development of these abnormalities was reduced by treatment with Gleevec, an inhibitor of PDGF signaling. Thus, LRP1 has a pivotal role in protecting vascular wall integrity and preventing atherosclerosis by controlling PDGFR activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boucher, Philippe -- Gotthardt, Michael -- Li, Wei-Ping -- Anderson, Richard G W -- Herz, Joachim -- GM 52016/GM/NIGMS NIH HHS/ -- HL20948/HL/NHLBI NIH HHS/ -- HL63762/HL/NHLBI NIH HHS/ -- NS43408/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):329-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9046, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690199" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/cytology/metabolism/*pathology ; Arteriosclerosis/*pathology/physiopathology/*prevention & control ; Benzamides ; Cattle ; Cell Division ; Cell Line ; Cholesterol, Dietary/administration & dosage ; Diet, Atherogenic ; Elastin/analysis ; Enzyme Inhibitors/pharmacology ; Imatinib Mesylate ; Ligands ; Low Density Lipoprotein Receptor-Related ; Protein-1/genetics/metabolism/*physiology ; Mesenteric Arteries/cytology/pathology ; Mice ; Mice, Knockout ; Mice, Transgenic ; Muscle, Smooth, Vascular/cytology/*metabolism/pathology ; Myocytes, Smooth Muscle/*metabolism/physiology ; Phosphorylation ; Piperazines/pharmacology ; Platelet-Derived Growth Factor/metabolism/pharmacology ; Proto-Oncogene Proteins c-sis ; Pyrimidines/pharmacology ; Receptor, Platelet-Derived Growth Factor beta/metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-05
    Description: Oxysterol-binding protein (OSBP) is the founding member of a family of sterol-binding proteins implicated in vesicle transport, lipid metabolism, and signal transduction. Here, OSBP was found to function as a cholesterol-binding scaffolding protein coordinating the activity of two phosphatases to control the extracellular signal-regulated kinase (ERK) signaling pathway. Cytosolic OSBP formed a approximately 440-kilodalton oligomer with a member of the PTPPBS family of tyrosine phosphatases, the serine/threonine phosphatase PP2A, and cholesterol. This oligomer had dual specific phosphatase activity for phosphorylated ERK (pERK). When cell cholesterol was lowered, the oligomer disassembled and the level of pERK rose. The oligomer also disassembled when exposed to oxysterols. Increasing the amount of OSBP oligomer rendered cells resistant to the effects of cholesterol depletion and decreased the basal level of pERK. Thus, cholesterol functions through its interaction with OSBP outside of membranes to regulate the assembly of an oligomeric phosphatase that controls a key signaling pathway in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Ping-Yuan -- Weng, Jian -- Anderson, Richard G W -- GM 52016/GM/NIGMS NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1472-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746430" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cholesterol/*metabolism ; Cytosol/metabolism ; Enzyme Activation ; HeLa Cells ; Humans ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase 1/*metabolism ; Mitogen-Activated Protein Kinase 3/*metabolism ; Multiprotein Complexes/metabolism ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Conformation ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/metabolism ; RNA Interference ; Receptors, Steroid/chemistry/genetics/*metabolism ; Transfection ; beta-Cyclodextrins/pharmacology
    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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    Integrins regulate Rac targeting by internalization of membrane domains (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: Translocation of the small GTP-binding protein Rac1 to the cell plasma membrane is essential for activating downstream effectors and requires integrin-mediated adhesion of cells to extracellular matrix. We report that active Rac1 binds preferentially to low-density, cholesterol-rich membranes, and specificity is determined at least in part by membrane lipids. Cell detachment triggered internalization of plasma membrane cholesterol and lipid raft markers. Preventing internalization maintained Rac1 membrane targeting and effector activation in nonadherent cells. Regulation of lipid rafts by integrin signals may regulate the location of membrane domains such as lipid rafts and thereby control domain-specific signaling events in anchorage-dependent cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉del Pozo, Miguel A -- Alderson, Nazilla B -- Kiosses, William B -- Chiang, Hui-Hsien -- Anderson, Richard G W -- Schwartz, Martin A -- GM52016/GM/NIGMS NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- R01 GM47214/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. mdelpozo@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764880" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD29/metabolism ; Binding Sites ; Cell Adhesion ; Cell Line ; Cell Membrane/*metabolism ; Cells, Cultured ; Cholera Toxin/metabolism ; Cholesterol/metabolism ; G(M1) Ganglioside/metabolism ; Glycosylphosphatidylinositols/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Integrins/*metabolism ; Liposomes/metabolism ; Membrane Microdomains/*metabolism ; Mice ; NIH 3T3 Cells ; Rats ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; rac1 GTP-Binding Protein/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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  • 8
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    A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: The surface membrane of cells is studded with morphologically distinct regions, or domains, like microvilli, cell-cell junctions, and coated pits. Each of these domains is specialized for a particular function, such as nutrient absorption, cell-cell communication, and endocytosis. Lipid domains, which include caveolae and rafts, are one of the least understood membrane domains. These domains are high in cholesterol and sphingolipids, have a light buoyant density, and function in both endocytosis and cell signaling. A major mystery, however, is how resident molecules are targeted to lipid domains. Here, we propose that the molecular address for proteins targeted to lipid domains is a lipid shell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, Richard G W -- Jacobson, Ken -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1821-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA. richard.anderson@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052946" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caveolae/chemistry/*metabolism/ultrastructure ; Cholesterol/chemistry/*metabolism ; Glycosylphosphatidylinositols/chemistry/metabolism ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers ; Membrane Microdomains/chemistry/*metabolism/ultrastructure ; Membrane Proteins/chemistry/*metabolism ; Protein Binding ; *Protein Transport ; Sphingolipids/chemistry/*metabolism ; Static Electricity ; Thermodynamics
    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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    Urban outdoor water use and response to drought assessed through mobile energy balance and vegetation greenness measurements (2017)
    Institute of Physics (IOP)
    Details
    Publication Date: 2017-07-29
    Description: Urban vegetation provides many highly valued ecosystem services but also requires extensive urban water resources. Increasingly, cities are experiencing water limitations and managing outdoor urban water use is an important concern. Quantifying the water lost via evapotranspiration (ET) is critical for urban water management and conservation, especially in arid or semi-arid regions. In this study, we deployed a mobile energy balance platform to measure evaporative fraction throughout Riverside, California, a warm, semi-arid, city. We observed the relationship between evaporative fraction and satellite derived vegetation index across 29 sites, which was then used to map whole-city ET for a representative mid-summer period. Resulting ET distributions were strongly associated with both neighborhood population density and income. By comparing 2014 and 2015 summer-period water uses, our results show 7.8% reductions in evapotranspiration, which were also correlated with neighborhood d...
    Print ISSN: 1748-9318
    Electronic ISSN: 1748-9326
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering
    Published by Institute of Physics (IOP)
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  • 10
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    A once-scarce commodity (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-08-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, R G -- New York, N.Y. -- Science. 1979 Aug 24;205(4408):778.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17814852" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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