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  • 1
    Publication Date: 2011-01-26
    Description: A general understanding of rifted margins, which form by thinning of the continental lithosphere, exists. Nevertheless, the exact form of thinning is unclear. This debate has been stimulated by acquisition of dense seismic wide-angle and deep reflection surveys from Atlantic Ocean margins. A central issue concerns the way in which thinning changes with depth. We have tackled this issue by developing a generalized inverse model. This model attempts to fit subsidence and crustal thinning observations by varying strain rate as a function of time and space. Depth-dependent thinning is permitted but we do not prescribe its existence or form. Here, the algorithm is applied to six margins, including two of the most contentious conjugate margins: Newfoundland-Iberia and Brazil-Angola. Calculated strain rate histories predict thinning estimates which broadly match estimates inferred from normal faulting. The Eastern Indian and Beaufort Sea margins formed by largely uniform lithospheric thinning. In contrast, the Newfoundland-Iberian conjugate margins formed by a pattern of strongly depth-dependent strain rate. To account for the paucity of syn-rift decompression melting of the underlying asthenosphere, the lithospheric mantle close to oceanic-continent transition must thin more slowly than the overlying crust. This form of depth dependency is not common. For example, the Brazil-Angolan conjugate margin could have formed by uniform lithospheric thinning provided thick layers of salt were deposited in a preexisting 400 m deep topographic depression. Depth-dependent thinning is not required to account for rapid subsidence of presalt strata.
    Print ISSN: 0278-7407
    Electronic ISSN: 1944-9194
    Topics: Geosciences
    Published by Wiley on behalf of American Geophysical Union (AGU).
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  • 2
    Publication Date: 2000-08-11
    Description: Previous work has identified two families of proteins that transport classical neurotransmitters into synaptic vesicles, but the protein responsible for vesicular transport of the principal excitatory transmitter glutamate has remained unknown. We demonstrate that a protein that is unrelated to any known neurotransmitter transporters and that was previously suggested to mediate the Na(+)-dependent uptake of inorganic phosphate across the plasma membrane transports glutamate into synaptic vesicles. In addition, we show that this vesicular glutamate transporter, VGLUT1, exhibits a conductance for chloride that is blocked by glutamate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bellocchio, E E -- Reimer, R J -- Fremeau, R T Jr -- Edwards, R H -- New York, N.Y. -- Science. 2000 Aug 11;289(5481):957-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of California at San Francisco School of Medicine, 513 Parnassus Avenue, San Francisco, CA 94143-0435, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10938000" target="_blank"〉PubMed〈/a〉
    Keywords: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid/pharmacology ; Adenosine Triphosphate/metabolism ; Animals ; Biological Transport, Active/drug effects ; Carrier Proteins/genetics/*metabolism ; Cell Membrane/metabolism ; Chlorides/metabolism ; Glutamic Acid/*metabolism ; Hydrogen-Ion Concentration ; PC12 Cells ; Phosphates/metabolism ; Potassium Chloride/metabolism ; Rats ; Sodium-Phosphate Cotransporter Proteins ; *Symporters ; Synaptic Vesicles/*metabolism ; Transfection
    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
    Publication Date: 2009-11-17
    Description: Mechanical pain contributes to the morbidity associated with inflammation and trauma, but primary sensory neurons that convey the sensation of acute and persistent mechanical pain have not been identified. Dorsal root ganglion (DRG) neurons transmit sensory information to the spinal cord using the excitatory transmitter glutamate, a process that depends on glutamate transport into synaptic vesicles for regulated exocytotic release. Here we report that a small subset of cells in the DRG expresses the low abundance vesicular glutamate transporter VGLUT3 (also known as SLC17A8). In the dorsal horn of the spinal cord, these afferents project to lamina I and the innermost layer of lamina II, which has previously been implicated in persistent pain caused by injury. Because the different VGLUT isoforms generally have a non-redundant pattern of expression, we used Vglut3 knockout mice to assess the role of VGLUT3(+) primary afferents in the behavioural response to somatosensory input. The loss of VGLUT3 specifically impairs mechanical pain sensation, and in particular the mechanical hypersensitivity to normally innocuous stimuli that accompanies inflammation, nerve injury and trauma. Direct recording from VGLUT3(+) neurons in the DRG further identifies them as a poorly understood population of unmyelinated, low threshold mechanoreceptors (C-LTMRs). The analysis of Vglut3(-/-) mice now indicates a critical role for C-LTMRs in the mechanical hypersensitivity caused by injury.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2810205/" 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/PMC2810205/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seal, Rebecca P -- Wang, Xidao -- Guan, Yun -- Raja, Srinivasa N -- Woodbury, C Jeffery -- Basbaum, Allan I -- Edwards, Robert H -- F32 MH068085/MH/NIMH NIH HHS/ -- F32 MH068085-02/MH/NIMH NIH HHS/ -- R01 MH050712/MH/NIMH NIH HHS/ -- R01 MH050712-17/MH/NIMH NIH HHS/ -- R01 NS044094/NS/NINDS NIH HHS/ -- R01 NS044094-06/NS/NINDS NIH HHS/ -- England -- Nature. 2009 Dec 3;462(7273):651-5. doi: 10.1038/nature08505. Epub 2009 Nov 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco School of Medicine, California 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19915548" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Transport Systems, Acidic/genetics/*metabolism ; Animals ; Behavior, Animal/physiology ; Female ; Ganglia, Spinal/*metabolism ; Gene Expression Regulation ; Hypersensitivity/*genetics/*physiopathology ; Mechanoreceptors/*physiology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Pain/*genetics ; Wounds and Injuries/*physiopathology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1992-12-28
    Description: Opiate drugs have potent analgesic and addictive properties. These drugs interact with receptors that also mediate the response to endogenous opioid peptide ligands. However, the receptors for opioids have eluded definitive molecular characterization. By transient expression in COS cells and screening with an iodinated analog of the opioid peptide enkephalin, a complementary DNA clone encoding a functional delta opioid receptor has been identified. The sequence shows homology to G protein-coupled receptors, in particular the receptors for somatostatin, angiotensin, and interleukin-8.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, C J -- Keith, D E Jr -- Morrison, H -- Magendzo, K -- Edwards, R H -- DA05010/DA/NIDA NIH HHS/ -- P50 DA005010/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of California, School of Medicine, Los Angeles 90024-1759.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1335167" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Blotting, Northern ; Blotting, Southern ; Cell Line ; Cyclic AMP/metabolism ; Diprenorphine/metabolism ; Enkephalin, D-Penicillamine (2,5)- ; Enkephalins/pharmacology ; Etorphine/pharmacology ; Gene Expression ; Humans ; Kinetics ; Models, Structural ; Molecular Sequence Data ; Naloxone/pharmacology ; Narcotics/pharmacology ; Protein Structure, Secondary ; Receptors, Opioid, delta/chemistry/*genetics/*metabolism ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
    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
    Publication Date: 2004-05-01
    Description: Vesicular glutamate transporters (VGLUTs) 1 and 2 show a mutually exclusive distribution in the adult brain that suggests specialization for synapses with different properties of release. Consistent with this distribution, inactivation of the VGLUT1 gene silenced a subset of excitatory neurons in the adult. However, the same cell populations exhibited VGLUT1-independent transmission early in life. Developing hippocampal neurons transiently coexpressed VGLUT2 and VGLUT1 at distinct synaptic sites with different short-term plasticity. The loss of VGLUT1 also reduced the reserve pool of synaptic vesicles. Thus, VGLUT1 plays an unanticipated role in membrane trafficking at the nerve terminal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fremeau, Robert T Jr -- Kam, Kaiwen -- Qureshi, Tayyaba -- Johnson, Juliette -- Copenhagen, David R -- Storm-Mathisen, Jon -- Chaudhry, Farrukh A -- Nicoll, Roger A -- Edwards, Robert H -- R01 EY001869/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 18;304(5678):1815-9. Epub 2004 Apr 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Graduate Programs in Neuroscience and Cell Biology, University of California San Francisco School of Medicine, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15118123" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Brain/cytology/*metabolism ; Carrier Proteins/genetics/*metabolism ; Cell Membrane/physiology ; Cells, Cultured ; Cerebellum/metabolism/ultrastructure ; Excitatory Postsynaptic Potentials ; Glutamic Acid/metabolism ; Hippocampus/cytology/metabolism/ultrastructure ; In Situ Hybridization ; *Membrane Transport Proteins ; Mice ; Mice, Knockout ; Nerve Tissue Proteins/metabolism ; Neurons/*metabolism/physiology ; Patch-Clamp Techniques ; Purkinje Cells/physiology ; Pyramidal Cells/metabolism ; Synapses/*metabolism/ultrastructure ; *Synaptic Transmission ; Synaptic Vesicles/*metabolism/physiology ; Vesicular Glutamate Transport Protein 1 ; Vesicular Glutamate Transport Protein 2 ; *Vesicular Transport Proteins
    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
    Publication Date: 2009-05-09
    Description: The nervous system transmits signals between neurons via neurotransmitter release during synaptic vesicle fusion. In order to observe neurotransmitter uptake and release from individual presynaptic terminals directly, we designed fluorescent false neurotransmitters as substrates for the synaptic vesicle monoamine transporter. Using these probes to image dopamine release in the striatum, we made several observations pertinent to synaptic plasticity. We found that the fraction of synaptic vesicles releasing neurotransmitter per stimulus was dependent on the stimulus frequency. A kinetically distinct "reserve" synaptic vesicle population was not observed under these experimental conditions. A frequency-dependent heterogeneity of presynaptic terminals was revealed that was dependent in part on D2 dopamine receptors, indicating a mechanism for frequency-dependent coding of presynaptic selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gubernator, Niko G -- Zhang, Hui -- Staal, Roland G W -- Mosharov, Eugene V -- Pereira, Daniela B -- Yue, Minerva -- Balsanek, Vojtech -- Vadola, Paul A -- Mukherjee, Bipasha -- Edwards, Robert H -- Sulzer, David -- Sames, Dalibor -- R01 DA007418/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2009 Jun 12;324(5933):1441-4. doi: 10.1126/science.1172278. Epub 2009 May 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19423778" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benz(a)Anthracenes/*metabolism ; Cells, Cultured ; Chromaffin Cells/*metabolism ; Corpus Striatum/cytology/*metabolism ; Dopamine/*metabolism ; Dopamine Antagonists/pharmacology ; Dopamine D2 Receptor Antagonists ; Electric Stimulation ; Exocytosis ; Fluorescent Dyes ; Mice ; Mice, Transgenic ; Neuronal Plasticity ; Neurotransmitter Agents/*metabolism ; Presynaptic Terminals/*metabolism ; Receptors, Dopamine D2/metabolism ; Sulpiride/pharmacology ; Synaptic Vesicles/*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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  • 7
    Publication Date: 1981-12-04
    Description: Leucine catabolism is regulated by either of the first two degradative steps: (reversible) transamination to the keto acid or subsequent decarboxylation. A method is described to measure rates of leucine transamination, reamination, and keto acid oxidation. The method is applied directly to humans by infusing the nonradioactive tracer, L-[15N,1-13C]leucine. Leucine transamination was found to be operating several times faster than the keto acid decarboxylation and to be of equal magnitude in adult human males under two different dietary conditions, postabsorptive and fed. These results indicate that decarboxylation, not transamination, is the rate-limiting step in normal human leucine metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matthews, D E -- Bier, D M -- Rennie, M J -- Edwards, R H -- Halliday, D -- Millward, D J -- Clugston, G A -- AM-25994/AM/NIADDK NIH HHS/ -- HD-10667/HD/NICHD NIH HHS/ -- RR-00954/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 Dec 4;214(4525):1129-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7302583" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Carbon Isotopes ; Humans ; Kinetics ; Leucine/*metabolism ; Male ; Models, Biological ; Nitrogen Isotopes ; Oxidation-Reduction
    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
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Alfalfa juice, a highly proteinaceous liquid, was heated in steamfilled shell and tube and rotating coil heat exchangers to effect protein coagulation. The juice could be preheated prior to entering the heat exchanger by use of a recycle system. Lower fouling rates were obtained when the protein was denatured prior to contacting the exchanger surfaces and when the rotating coil exchanger was used. Chemical cleaning treatments could restore the heat transfer coefficient of a fouled exchanger to the original value.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 296 (1982), S. 165-167 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We studied seven normal fed adult men aged 22-65 yr and five boys with Duchenne muscular dystrophy, aged 12-1 Syr. Three of the patients were wheelchair bound and the two youngest were on the verge of becoming so. Investigations of these subjects using radioactive isotopes would not have been ...
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 45 (1980), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A pilot-scale process for preparing high-protein, low fiber (〈l%) products from 150-lb batches of wheat millrun and shorts using a wet alkaline method is described. The protein concentrates contained 60–70% protein when starch was removed prior to protein precipitation and 25–26% protein with the starch present. Yields of the protein concentrates ranged from 4.1 to 33.6% of the raw material starting weight (dry basis), depending on the processing conditions employed. Yield could be increased by re-extracting the pressed residue. Water requirements for extraction were lowered from 750 to 263 lb by extracting the raw material with the deproteinized mother liquor from the previous lot.
    Type of Medium: Electronic Resource
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