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  • 1
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    Tracing groundwater Nitrate Sources in the Dakar suburban Area: an Isotopic Multi-tracer Approach (2011)
    Wiley
    Details
    Publication Date: 2011-06-01
    Description: The Dakar region is a mega city with multiple contaminant sources from urban expansion as well as industrial and agricultural activities. The major part of the region is underlain by unconfined sandy aquifer, which is vulnerable to contaminants derived from human land use. At present, the contaminated groundwater which extends over a large area in the suburban zone of Thiaroye poses a threat in the future of this valuable resource and more specifically a health threat. This study focuses on nitrate pollution occurrences and associated processes using nitrate isotope data ( 15 N NO3 , 18 O NO3 ) combined with environmental isotopic tracers ( 18 O, 2 H and 3 H). Samples from 36 wells were collected to determine the level, distribution and sources of contamination in relation to land use. Results indicate that shallow groundwater in the urbanized area of Thiaroye shows distinct evidence of surface contamination with nitrate as much as 300 mg/l NO 3 - . In rural area not serviced by water supply distribution network, much higher NO 3 - contents were found in few wells due to household and livestock feedlots. In most groundwater samples δ 15 N values ranged from + 10 to + 22‰, indicative of predominantly human and animal wastes. This was confirmed by environmental isotope data which suggest a mixture of polluted recharge waters. By using the dual δ 15 N vs. δ 18 O as well as δ 15 N vs. NO 3 - approach, denitrification may occur to some extent but it is blurred by mixing with new infiltrated nitrates and cycling derived from continuous leaky septic system. Results suggest that nitrate contamination of the aquifer is a consequence of unregulated urbanization (home-made latrines), continuing contaminant transfer in shallow water depth where aerobic conditions prevail. Copyright © 2011 John Wiley & Sons, Ltd.
    Print ISSN: 0885-6087
    Electronic ISSN: 1099-1085
    Topics: Architecture, Civil Engineering, Surveying , Geography
    Published by Wiley
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  • 2
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    Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-26
    Description: Outer hair cells (OHCs) of the mammalian cochlea actively change their cell length in response to changes in membrane potential. This electromotility, thought to be the basis of cochlear amplification, is mediated by a voltage-sensitive motor molecule recently identified as the membrane protein prestin. Here, we show that voltage sensitivity is conferred to prestin by the intracellular anions chloride and bicarbonate. Removal of these anions abolished fast voltage-dependent motility, as well as the characteristic nonlinear charge movement ("gating currents") driving the underlying structural rearrangements of the protein. The results support a model in which anions act as extrinsic voltage sensors, which bind to the prestin molecule and thus trigger the conformational changes required for motility of OHCs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oliver, D -- He, D Z -- Klocker, N -- Ludwig, J -- Schulte, U -- Waldegger, S -- Ruppersberg, J P -- Dallos, P -- Fakler, B -- DC00089/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 22;292(5525):2340-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology II, University of Tubingen, 72074 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423665" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Anion Transport Proteins ; Anions/pharmacology ; Bicarbonates/*metabolism/pharmacology ; CHO Cells ; Cations/pharmacology ; Cell Membrane/metabolism ; Chlorides/*metabolism/pharmacology ; Cricetinae ; Electric Conductivity ; Electrophysiology ; Hair Cells, Auditory, Outer/*physiology ; Models, Biological ; Mutation ; Patch-Clamp Techniques ; Protein Conformation ; Proteins/chemistry/genetics/*metabolism ; Rats
    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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  • 3
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    BKCa-Cav channel complexes mediate rapid and localized Ca2+-activated K+ signaling (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-28
    Description: Large-conductance calcium- and voltage-activated potassium channels (BKCa) are dually activated by membrane depolarization and elevation of cytosolic calcium ions (Ca2+). Under normal cellular conditions, BKCa channel activation requires Ca2+ concentrations that typically occur in close proximity to Ca2+ sources. We show that BKCa channels affinity-purified from rat brain are assembled into macromolecular complexes with the voltage-gated calcium channels Cav1.2 (L-type), Cav2.1 (P/Q-type), and Cav2.2 (N-type). Heterologously expressed BKCa-Cav complexes reconstitute a functional "Ca2+ nanodomain" where Ca2+ influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics. Complex formation with distinct Cav channels enables BKCa-mediated membrane hyperpolarization that controls neuronal firing pattern and release of hormones and transmitters in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berkefeld, Henrike -- Sailer, Claudia A -- Bildl, Wolfgang -- Rohde, Volker -- Thumfart, Jorg-Oliver -- Eble, Silke -- Klugbauer, Norbert -- Reisinger, Ellen -- Bischofberger, Josef -- Oliver, Dominik -- Knaus, Hans-Gunther -- Schulte, Uwe -- Fakler, Bernd -- New York, N.Y. -- Science. 2006 Oct 27;314(5799):615-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology, University of Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068255" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain Chemistry ; CHO Cells ; Calcium/*metabolism ; Calcium Channels, L-Type/drug effects/isolation & purification/*metabolism ; Calcium Channels, N-Type/drug effects/isolation & purification/*metabolism ; Calcium Signaling ; Chromaffin Cells/drug effects/metabolism ; Cricetinae ; Cricetulus ; Egtazic Acid/analogs & derivatives/pharmacology ; Large-Conductance Calcium-Activated Potassium Channels/drug effects/isolation & ; purification/*metabolism ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Patch-Clamp Techniques ; Potassium/*metabolism ; Rats ; *Signal Transduction ; Transfection ; Xenopus
    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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  • 4
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    PIP2 and PIP as determinants for ATP inhibition of KATP channels (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-06
    Description: Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple electrical activity to cellular metabolism through their inhibition by intracellular ATP. ATP inhibition of KATP channels varies among tissues and is affected by the metabolic and regulatory state of individual cells, suggesting involvement of endogenous factors. It is reported here that phosphatidylinositol-4, 5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1). These phospholipids acted on the Kir6.2 subunit and shifted ATP sensitivity by several orders of magnitude. Receptor-mediated activation of phospholipase C resulted in inhibition of KATP-mediated currents. These results represent a mechanism for control of excitability through phospholipids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baukrowitz, T -- Schulte, U -- Oliver, D -- Herlitze, S -- Krauter, T -- Tucker, S J -- Ruppersberg, J P -- Fakler, B -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1141-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology II, University of Tubingen, Gmelinstrasse 5, 72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9804555" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/metabolism/*pharmacology ; Animals ; Cloning, Molecular ; Diazoxide/pharmacology ; Dose-Response Relationship, Drug ; Mutation ; Oocytes ; Patch-Clamp Techniques ; Phosphatidylinositol 4,5-Diphosphate/metabolism/*pharmacology ; Phosphatidylinositol Phosphates/metabolism/*pharmacology ; Phosphatidylinositols/pharmacology ; *Potassium Channel Blockers ; Potassium Channels/genetics/metabolism ; *Potassium Channels, Inwardly Rectifying ; Receptors, Drug/metabolism ; Receptors, Purinergic P2/metabolism ; Receptors, Purinergic P2Y2 ; Recombinant Fusion Proteins/metabolism ; Sulfonylurea Receptors ; Type C Phospholipases/metabolism ; Xenopus laevis
    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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    Native GABA(B) receptors are heteromultimers with a family of auxiliary subunits (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-04-20
    Description: GABA(B) receptors are the G-protein-coupled receptors for gamma-aminobutyric acid (GABA), the main inhibitory neurotransmitter in the brain. They are expressed in almost all neurons of the brain, where they regulate synaptic transmission and signal propagation by controlling the activity of voltage-gated calcium (Ca(v)) and inward-rectifier potassium (K(ir)) channels. Molecular cloning revealed that functional GABA(B) receptors are formed by the heteromeric assembly of GABA(B1) with GABA(B2) subunits. However, cloned GABA(B(1,2)) receptors failed to reproduce the functional diversity observed with native GABA(B) receptors. Here we show by functional proteomics that GABA(B) receptors in the brain are high-molecular-mass complexes of GABA(B1), GABA(B2) and members of a subfamily of the KCTD (potassium channel tetramerization domain-containing) proteins. KCTD proteins 8, 12, 12b and 16 show distinct expression profiles in the brain and associate tightly with the carboxy terminus of GABA(B2) as tetramers. This co-assembly changes the properties of the GABA(B(1,2)) core receptor: the KCTD proteins increase agonist potency and markedly alter the G-protein signalling of the receptors by accelerating onset and promoting desensitization in a KCTD-subtype-specific manner. Taken together, our results establish the KCTD proteins as auxiliary subunits of GABA(B) receptors that determine the pharmacology and kinetics of the receptor response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwenk, Jochen -- Metz, Michaela -- Zolles, Gerd -- Turecek, Rostislav -- Fritzius, Thorsten -- Bildl, Wolfgang -- Tarusawa, Etsuko -- Kulik, Akos -- Unger, Andreas -- Ivankova, Klara -- Seddik, Riad -- Tiao, Jim Y -- Rajalu, Mathieu -- Trojanova, Johana -- Rohde, Volker -- Gassmann, Martin -- Schulte, Uwe -- Fakler, Bernd -- Bettler, Bernhard -- Wellcome Trust/United Kingdom -- England -- Nature. 2010 May 13;465(7295):231-5. doi: 10.1038/nature08964. Epub 2010 Apr 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology II, University of Freiburg, Engesserstrasse 4, 79108 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20400944" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Cricetinae ; Cricetulus ; Electric Conductivity ; GABA-B Receptor Agonists ; Heterotrimeric GTP-Binding Proteins/metabolism ; Kinetics ; Mice ; Multiprotein Complexes/*chemistry/*metabolism ; Neurons/metabolism ; Oocytes/metabolism ; Potassium/metabolism ; Potassium Channels/metabolism ; *Protein Multimerization ; Protein Structure, Tertiary ; Protein Subunits/*chemistry/*metabolism ; Rats ; Rats, Wistar ; Receptors, GABA-B/*chemistry/*metabolism ; Signal Transduction ; Xenopus
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-07
    Description: Glutamate receptors of the AMPA-subtype (AMPARs), together with the transmembrane AMPAR regulatory proteins (TARPs), mediate fast excitatory synaptic transmission in the mammalian brain. Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. Coassembly with cornichon homologs 2 and 3 affects AMPARs in two ways: Cornichons increase surface expression of AMPARs, and they alter channel gating by markedly slowing deactivation and desensitization kinetics. These results demonstrate that cornichons are intrinsic auxiliary subunits of native AMPARs and provide previously unknown molecular determinants for glutamatergic neurotransmission in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwenk, Jochen -- Harmel, Nadine -- Zolles, Gerd -- Bildl, Wolfgang -- Kulik, Akos -- Heimrich, Bernd -- Chisaka, Osamu -- Jonas, Peter -- Schulte, Uwe -- Fakler, Bernd -- Klocker, Nikolaj -- New York, N.Y. -- Science. 2009 Mar 6;323(5919):1313-9. doi: 10.1126/science.1167852.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology II, University of Freiburg, Engesserstrasse 4, 79108 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19265014" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/*metabolism ; Cell Membrane/metabolism ; Glutamic Acid/metabolism ; Immunohistochemistry ; *Ion Channel Gating ; Kinetics ; Membrane Proteins/chemistry/metabolism ; Mice ; Neurons/*metabolism ; Patch-Clamp Techniques ; Protein Subunits/chemistry/metabolism ; Proteomics ; Rats ; Receptors, AMPA/chemistry/*metabolism ; Signal Transduction ; Synapses/metabolism ; *Synaptic Transmission ; Xenopus
    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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  • 7
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    Hydrochemical and microbiological properties of groundwater from pristine aquifer sampled at the Lower Rhine Embayment
    PANGAEA
    In:  Supplement to: Detmers, Jan; Strauss, H; Schulte, U; Bergmann, A; Knittel, Katrin; Kuever, Jan (2003): FISH shows that Desulfotomaculum spp. are the dominating Sulfate-Reducing Bacteria in a Pristine Aquifer. Microbial Ecology, 47(3), https://doi.org/10.1007/s00248-004-9952-6
    Details
    Publication Date: 2023-05-12
    Description: The hydrochemistry and the microbial diversity of a pristine aquifer system near Garzweiler, Germany next to the open-pit lignite mine Garzweiler 1, were characterized. Hydrogeochemical and isotopic data indicate a recent activity of sulfate-reducing bacteria in the Tertiary marine sands. The community structure in the aquifer was studied by fluorescence in situ hybridization (FISH). Up to 7.3 x 10**5 cells/ml were detected by DAPIstaining. Bacteria (identified by the probe EUB338) were dominant, representing 51.9% of the total cell number (DAPI). Another 25.7% of total cell were affiliated with the domain Archaea as identified by the probe ARCH915. Within the domain Bacteria, the beta-Proteobacteria were most abundant (21.0% of total cell counts). Using genusspecific probes for sulfate-reducing bacteria (SRB), 2.5% of the total cells were identified as members of the genus Desulfotomaculum. This reflects the predominant role these microorganisms have been found to play in sulfatereducing zones of aquifers at other sites. Previously, all SRB cultured from this site were from the spore-forming genera Desulfotomaculum and Desulfosporosinus. Samples were taken after pumping for 〉= 40 min and after parameters such as temperature, pH, redox potential, oxygen and conductivity of the groundwater had remained stable for 〉= 15 min due to recharge of aquifer water. Hybridization and microscopy counts of hybridized and 4',6'-diamidino-2-phenylindole (DAPI)- stained cells were performed as described in Snaidr et al., (1997, http://aem.asm.org/content/63/7/2884.full.pdf). Means were calculated from 10 to 20 randomly chosen fields on each filter section, corresponding to 800-1000 DAPI stained cells. Counting results were always corrected by subtracting signals observed with the probe NON338. Formamide concentrations and oligonucleotide probes used please see further details.
    Keywords: Archaea, targed with ARCH915 oligonucleotide FISH-probe; Bacteria, targeted with EUB338 l oligonucleotides FISH-probe; Carbon, organic, dissolved; DEPTH, water; Epifluorescence microscopy after DAPI staining; Event label; Fluorescence in situ hybridization (FISH); Latitude of event; Longitude of event; LRG; Nitrate; Oxygen; pH; Prokaryotes, abundance as single cells; Rhine, Germany, Europe; Sample ID; Sampling Well; Sulfate; Temperature, water; WELL; δ13C, dissolved inorganic carbon; δ34S, sulfate
    Type: Dataset
    Format: text/tab-separated-values, 48 data points
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  • 8
    Electronic Resource
    Electronic Resource
    Molecular genetic studies of complex I in Neurospora crassa, Aspergillus niger and Escherichia coli
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1101 (1992), S. 177-180 
    Details
    ISSN: 0005-2728
    Keywords: (A. niger) ; (E. coli) ; (N. crassa) ; Assembly ; Chaperone ; Complex I ; NADH: ubiquinone oxidoreductase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0005-2728(05)80013-1
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  • 9
    Electronic Resource
    Electronic Resource
    In vivo dissection of the mitochondrial respiratory NADH:ubiquinone oxidoreductase (complex I)
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1187 (1994), S. 121-124 
    Details
    ISSN: 0005-2728
    Keywords: (N. crassa) ; Assembly ; Complex I ; Gene disruption ; NADH:ubiquinone oxidoreductase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(94)90096-5
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular genetic studies of complex I in Neurospora crassa, Aspergillus niger and Escherichia coli
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1101 (1992), S. 177-180 
    Details
    ISSN: 0005-2728
    Keywords: (A. niger) ; (E. coli) ; (N. crassa) ; Assembly ; Chaperone ; Complex I ; NADH: ubiquinone oxidoreductase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0005-2728(92)90218-Q
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