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  • 1
    Call number: PIK N 454-01-0394
    Type of Medium: Monograph available for loan
    Pages: 488 p.
    ISBN: 3895183415
    Location: A 18 - must be ordered
    Branch Library: PIK Library
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  • 2
    Publication Date: 1999-07-03
    Description: Two main types of material survive from the Canyon Diablo impactor, which produced Meteor Crater in Arizona: iron meteorites, which did not melt during the impact; and spheroids, which did. Ultrasensitive measurements using accelerator mass spectrometry show that the meteorites contain about seven times as much nickel-59 as the spheroids. Lower average nickel-59 contents in the spheroids indicate that they typically came from 0.5 to 1 meter deeper in the impactor than did the meteorites. Numerical modeling for an impact velocity of 20 kilometers per second shows that a shell 1.5 to 2 meters thick, corresponding to 16 percent of the projectile volume, remained solid on the rear surface; that most of the projectile melted; and that little, if any, vaporized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schnabel -- Pierazzo -- Xue -- Herzog -- Masarik -- Cresswell -- di Tada ML -- Liu -- Fifield -- New York, N.Y. -- Science. 1999 Jul 2;285(5424):85-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Rutgers University, Piscataway, NJ 08854, USA. Lunar and Planetary Laboratory, University of Arizona, Tucson, AZ 87521, USA. Graduate School of Oceanography, Narragansett Bay Campus, University of Rhode Island, Narraganse.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10390367" 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
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  • 3
    Publication Date: 2006-12-16
    Description: The Stardust spacecraft collected thousands of particles from comet 81P/Wild 2 and returned them to Earth for laboratory study. The preliminary examination of these samples shows that the nonvolatile portion of the comet is an unequilibrated assortment of materials that have both presolar and solar system origin. The comet contains an abundance of silicate grains that are much larger than predictions of interstellar grain models, and many of these are high-temperature minerals that appear to have formed in the inner regions of the solar nebula. Their presence in a comet proves that the formation of the solar system included mixing on the grandest scales.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brownlee, Don -- Tsou, Peter -- Aleon, Jerome -- Alexander, Conel M O'd -- Araki, Tohru -- Bajt, Sasa -- Baratta, Giuseppe A -- Bastien, Ron -- Bland, Phil -- Bleuet, Pierre -- Borg, Janet -- Bradley, John P -- Brearley, Adrian -- Brenker, F -- Brennan, Sean -- Bridges, John C -- Browning, Nigel D -- Brucato, John R -- Bullock, E -- Burchell, Mark J -- Busemann, Henner -- Butterworth, Anna -- Chaussidon, Marc -- Cheuvront, Allan -- Chi, Miaofang -- Cintala, Mark J -- Clark, B C -- Clemett, Simon J -- Cody, George -- Colangeli, Luigi -- Cooper, George -- Cordier, Patrick -- Daghlian, C -- Dai, Zurong -- D'Hendecourt, Louis -- Djouadi, Zahia -- Dominguez, Gerardo -- Duxbury, Tom -- Dworkin, Jason P -- Ebel, Denton S -- Economou, Thanasis E -- Fakra, Sirine -- Fairey, Sam A J -- Fallon, Stewart -- Ferrini, Gianluca -- Ferroir, T -- Fleckenstein, Holger -- Floss, Christine -- Flynn, George -- Franchi, Ian A -- Fries, Marc -- Gainsforth, Z -- Gallien, J-P -- Genge, Matt -- Gilles, Mary K -- Gillet, Philipe -- Gilmour, Jamie -- Glavin, Daniel P -- Gounelle, Matthieu -- Grady, Monica M -- Graham, Giles A -- Grant, P G -- Green, Simon F -- Grossemy, Faustine -- Grossman, Lawrence -- Grossman, Jeffrey N -- Guan, Yunbin -- Hagiya, Kenji -- Harvey, Ralph -- Heck, Philipp -- Herzog, Gregory F -- Hoppe, Peter -- Horz, Friedrich -- Huth, Joachim -- Hutcheon, Ian D -- Ignatyev, Konstantin -- Ishii, Hope -- Ito, Motoo -- Jacob, Damien -- Jacobsen, Chris -- Jacobsen, Stein -- Jones, Steven -- Joswiak, David -- Jurewicz, Amy -- Kearsley, Anton T -- Keller, Lindsay P -- Khodja, H -- Kilcoyne, A L David -- Kissel, Jochen -- Krot, Alexander -- Langenhorst, Falko -- Lanzirotti, Antonio -- Le, Loan -- Leshin, Laurie A -- Leitner, J -- Lemelle, L -- Leroux, Hugues -- Liu, Ming-Chang -- Luening, K -- Lyon, Ian -- Macpherson, Glen -- Marcus, Matthew A -- Marhas, Kuljeet -- Marty, Bernard -- Matrajt, Graciela -- McKeegan, Kevin -- Meibom, Anders -- Mennella, Vito -- Messenger, Keiko -- Messenger, Scott -- Mikouchi, Takashi -- Mostefaoui, Smail -- Nakamura, Tomoki -- Nakano, T -- Newville, M -- Nittler, Larry R -- Ohnishi, Ichiro -- Ohsumi, Kazumasa -- Okudaira, Kyoko -- Papanastassiou, Dimitri A -- Palma, Russ -- Palumbo, Maria E -- Pepin, Robert O -- Perkins, David -- Perronnet, Murielle -- Pianetta, P -- Rao, William -- Rietmeijer, Frans J M -- Robert, Francois -- Rost, D -- Rotundi, Alessandra -- Ryan, Robert -- Sandford, Scott A -- Schwandt, Craig S -- See, Thomas H -- Schlutter, Dennis -- Sheffield-Parker, J -- Simionovici, Alexandre -- Simon, Steven -- Sitnitsky, I -- Snead, Christopher J -- Spencer, Maegan K -- Stadermann, Frank J -- Steele, Andrew -- Stephan, Thomas -- Stroud, Rhonda -- Susini, Jean -- Sutton, S R -- Suzuki, Y -- Taheri, Mitra -- Taylor, Susan -- Teslich, Nick -- Tomeoka, Kazu -- Tomioka, Naotaka -- Toppani, Alice -- Trigo-Rodriguez, Josep M -- Troadec, David -- Tsuchiyama, Akira -- Tuzzolino, Anthony J -- Tyliszczak, Tolek -- Uesugi, K -- Velbel, Michael -- Vellenga, Joe -- Vicenzi, E -- Vincze, L -- Warren, Jack -- Weber, Iris -- Weisberg, Mike -- Westphal, Andrew J -- Wirick, Sue -- Wooden, Diane -- Wopenka, Brigitte -- Wozniakiewicz, Penelope -- Wright, Ian -- Yabuta, Hikaru -- Yano, Hajime -- Young, Edward D -- Zare, Richard N -- Zega, Thomas -- Ziegler, Karen -- Zimmerman, Laurent -- Zinner, Ernst -- Zolensky, Michael -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1711-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy, University of Washington, Seattle, WA 98195, USA. brownlee@astro.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170289" 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
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  • 4
    Publication Date: 2006-12-16
    Description: We measured the elemental compositions of material from 23 particles in aerogel and from residue in seven craters in aluminum foil that was collected during passage of the Stardust spacecraft through the coma of comet 81P/Wild 2. These particles are chemically heterogeneous at the largest size scale analyzed ( approximately 180 ng). The mean elemental composition of this Wild 2 material is consistent with the CI meteorite composition, which is thought to represent the bulk composition of the solar system, for the elements Mg, Si, Mn, Fe, and Ni to 35%, and for Ca and Ti to 60%. The elements Cu, Zn, and Ga appear enriched in this Wild 2 material, which suggests that the CI meteorites may not represent the solar system composition for these moderately volatile minor elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flynn, George J -- Bleuet, Pierre -- Borg, Janet -- Bradley, John P -- Brenker, Frank E -- Brennan, Sean -- Bridges, John -- Brownlee, Don E -- Bullock, Emma S -- Burghammer, Manfred -- Clark, Benton C -- Dai, Zu Rong -- Daghlian, Charles P -- Djouadi, Zahia -- Fakra, Sirine -- Ferroir, Tristan -- Floss, Christine -- Franchi, Ian A -- Gainsforth, Zack -- Gallien, Jean-Paul -- Gillet, Philippe -- Grant, Patrick G -- Graham, Giles A -- Green, Simon F -- Grossemy, Faustine -- Heck, Philipp R -- Herzog, Gregory F -- Hoppe, Peter -- Horz, Friedrich -- Huth, Joachim -- Ignatyev, Konstantin -- Ishii, Hope A -- Janssens, Koen -- Joswiak, David -- Kearsley, Anton T -- Khodja, Hicham -- Lanzirotti, Antonio -- Leitner, Jan -- Lemelle, Laurence -- Leroux, Hugues -- Luening, Katharina -- Macpherson, Glenn J -- Marhas, Kuljeet K -- Marcus, Matthew A -- Matrajt, Graciela -- Nakamura, Tomoki -- Nakamura-Messenger, Keiko -- Nakano, Tsukasa -- Newville, Matthew -- Papanastassiou, Dimitri A -- Pianetta, Piero -- Rao, William -- Riekel, Christian -- Rietmeijer, Frans J M -- Rost, Detlef -- Schwandt, Craig S -- See, Thomas H -- Sheffield-Parker, Julie -- Simionovici, Alexandre -- Sitnitsky, Ilona -- Snead, Christopher J -- Stadermann, Frank J -- Stephan, Thomas -- Stroud, Rhonda M -- Susini, Jean -- Suzuki, Yoshio -- Sutton, Stephen R -- Taylor, Susan -- Teslich, Nick -- Troadec, D -- Tsou, Peter -- Tsuchiyama, Akira -- Uesugi, Kentaro -- Vekemans, Bart -- Vicenzi, Edward P -- Vincze, Laszlo -- Westphal, Andrew J -- Wozniakiewicz, Penelope -- Zinner, Ernst -- Zolensky, Michael E -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1731-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, State University of New York at Plattsburgh, 101 Broad Street, Plattsburgh, NY 12901, USA. george.flynn@plattsburgh.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170294" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 5
    Publication Date: 2009-03-17
    Description: Once all chromosomes are connected to the mitotic spindle (bioriented), anaphase is initiated by the protein ubiquitylation activity of the anaphase-promoting complex/cyclosome (APC/C) and its coactivator Cdc20 (APC/C(Cdc20)). Before chromosome biorientation, anaphase is delayed by a mitotic checkpoint complex (MCC) that inhibits APC/C(Cdc20). We used single-particle electron microscopy to obtain three-dimensional models of human APC/C in various functional states: bound to MCC, to Cdc20, or to neither (apo-APC/C). These experiments revealed that MCC associates with the Cdc20 binding site on APC/C, locks the otherwise flexible APC/C in a "closed" state, and prevents binding and ubiquitylation of a wide range of different APC/C substrates. These observations clarify the structural basis for the inhibition of APC/C by spindle checkpoint proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2989460/" 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/PMC2989460/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzog, Franz -- Primorac, Ivana -- Dube, Prakash -- Lenart, Peter -- Sander, Bjorn -- Mechtler, Karl -- Stark, Holger -- Peters, Jan-Michael -- F 3407/Austrian Science Fund FWF/Austria -- New York, N.Y. -- Science. 2009 Mar 13;323(5920):1477-81. doi: 10.1126/science.1163300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19286556" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cdc20 Proteins ; Cell Cycle Proteins/chemistry/metabolism ; HeLa Cells ; Humans ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Microscopy, Electron ; *Mitosis ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Spindle Apparatus/*metabolism ; Ubiquitin-Conjugating Enzymes/chemistry/metabolism ; Ubiquitin-Protein Ligase Complexes/*chemistry/*metabolism ; Ubiquitination
    Print ISSN: 0036-8075
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  • 6
    Publication Date: 2012-09-18
    Description: The identification of proximate amino acids by chemical cross-linking and mass spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes. We gained distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying an adapted XL-MS protocol. Systematic analysis of human protein phosphatase 2A (PP2A) complexes identified 176 interprotein and 570 intraprotein cross-links that link specific trimeric PP2A complexes to a multitude of adaptor proteins that control their cellular functions. Spatial restraints guided molecular modeling of the binding interface between immunoglobulin binding protein 1 (IGBP1) and PP2A and revealed the topology of TCP1 ring complex (TRiC) chaperonin interacting with the PP2A regulatory subunit 2ABG. This study establishes XL-MS as an integral part of hybrid structural biology approaches for the analysis of endogenous protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzog, Franz -- Kahraman, Abdullah -- Boehringer, Daniel -- Mak, Raymond -- Bracher, Andreas -- Walzthoeni, Thomas -- Leitner, Alexander -- Beck, Martin -- Hartl, Franz-Ulrich -- Ban, Nenad -- Malmstrom, Lars -- Aebersold, Ruedi -- New York, N.Y. -- Science. 2012 Sep 14;337(6100):1348-52. doi: 10.1126/science.1221483.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Institute of Molecular Systems Biology, Eidgenossische Technische Hochschule Zurich, Wolfgang-Pauli Strasse 16, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22984071" target="_blank"〉PubMed〈/a〉
    Keywords: Chaperonins/chemistry ; Cross-Linking Reagents/chemistry ; Crystallography, X-Ray ; Humans ; Mass Spectrometry/*methods ; *Metabolic Networks and Pathways ; Protein Conformation ; Protein Interaction Mapping/*methods ; Protein Phosphatase 2/*chemistry
    Print ISSN: 0036-8075
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  • 7
    Publication Date: 2014-11-22
    Description: Chromosome segregation depends on sister chromatid cohesion mediated by cohesin. The cohesin subunits Smc1, Smc3, and Scc1 form tripartite rings that are thought to open at distinct sites to allow entry and exit of DNA. However, direct evidence for the existence of open forms of cohesin is lacking. We found that cohesin's proposed DNA exit gate is formed by interactions between Scc1 and the coiled-coil region of Smc3. Mutation of this interface abolished cohesin's ability to stably associate with chromatin and to mediate cohesion. Electron microscopy revealed that weakening of the Smc3-Scc1 interface resulted in opening of cohesin rings, as did proteolytic cleavage of Scc1. These open forms may resemble intermediate states of cohesin normally generated by the release factor Wapl and the protease separase, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huis in 't Veld, Pim J -- Herzog, Franz -- Ladurner, Rene -- Davidson, Iain F -- Piric, Sabina -- Kreidl, Emanuel -- Bhaskara, Venugopal -- Aebersold, Ruedi -- Peters, Jan-Michael -- New York, N.Y. -- Science. 2014 Nov 21;346(6212):968-72. doi: 10.1126/science.1256904.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology (IMP), Vienna Biocenter (VBC), 1030 Vienna, Austria. ; Department of Biology, Institute of Molecular Systems Biology, Eidgenossische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland. Department of Biochemistry, Gene Center, Ludwig-Maximilian University, 81377 Munich, Germany. ; Department of Biology, Institute of Molecular Systems Biology, Eidgenossische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland. ; Research Institute of Molecular Pathology (IMP), Vienna Biocenter (VBC), 1030 Vienna, Austria. peters@imp.ac.at.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25414306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/genetics/metabolism ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Chondroitin Sulfate Proteoglycans/chemistry/genetics/*metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/chemistry/genetics/*metabolism ; *Chromosome Segregation ; DNA/*metabolism ; DNA Replication ; Humans ; Mass Spectrometry ; Microscopy, Electron ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*metabolism ; Phosphoproteins/chemistry/genetics/*metabolism ; Protein Multimerization ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/genetics/metabolism ; Separase/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
    Publication Date: 2017-10-14
    Description: The spin splitting of conduction band electrons in inversion-asymmetric InGaAs/InP quantum wells (QWs) is studied by Shubnikov-de Haas measurements combining the analysis of beating patterns and coincidence measurements in doubly tilted magnetic fields. The method allows us to determine the absolute values of the Rashba and linear Dresselhaus spin–orbit interaction (SOI) coefficients, their relative sign and the full Landé g-tensor. This is achieved by analyzing the anisotropy of the beat node positions with respect to both polar and azimuthal angles between the magnetic field direction and the QW normal. We show that the SOI is dominated by a large Rashba coefficient together with a linear Dresselhaus coefficient that is 10% of the Rashba coefficient. Their relative sign is found to be positive. The g-tensor is found to have a marked out-of-plane anisotropy and a smaller but distinct in-plane anisotropy due to SOI.
    Electronic ISSN: 1367-2630
    Topics: Physics
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  • 9
    Publication Date: 2016-01-21
    Description: RNA polymerase (Pol) II produces messenger RNA during transcription of protein-coding genes in all eukaryotic cells. The Pol II structure is known at high resolution from X-ray crystallography for two yeast species. Structural studies of mammalian Pol II, however, remain limited to low-resolution electron microscopy analysis of human Pol II and its complexes with various proteins. Here we report the 3.4 A resolution cryo-electron microscopy structure of mammalian Pol II in the form of a transcribing complex comprising DNA template and RNA transcript. We use bovine Pol II, which is identical to the human enzyme except for seven amino-acid residues. The obtained atomic model closely resembles its yeast counterpart, but also reveals unknown features. Binding of nucleic acids to the polymerase involves 'induced fit' of the mobile Pol II clamp and active centre region. DNA downstream of the transcription bubble contacts a conserved 'TPSA motif' in the jaw domain of the Pol II subunit RPB5, an interaction that is apparently already established during transcription initiation. Upstream DNA emanates from the active centre cleft at an angle of approximately 105 degrees with respect to downstream DNA. This position of upstream DNA allows for binding of the general transcription elongation factor DSIF (SPT4-SPT5) that we localize over the active centre cleft in a conserved position on the clamp domain of Pol II. Our results define the structure of mammalian Pol II in its functional state, indicate that previous crystallographic analysis of yeast Pol II is relevant for understanding gene transcription in all eukaryotes, and provide a starting point for a mechanistic analysis of human transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernecky, Carrie -- Herzog, Franz -- Baumeister, Wolfgang -- Plitzko, Jurgen M -- Cramer, Patrick -- England -- Nature. 2016 Jan 28;529(7587):551-4. doi: 10.1038/nature16482. Epub 2016 Jan 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Gottingen, Germany. ; Gene Center Munich, Ludwig-Maximilians-Universitat Munchen, Feodor-Lynen-Strasse 25, 81377 Munich, Germany. ; Max Planck Institute for Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18, 82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26789250" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Motifs ; Animals ; Catalytic Domain ; Cattle ; *Cryoelectron Microscopy ; DNA/genetics/metabolism/ultrastructure ; Humans ; Models, Molecular ; Nucleic Acids/chemistry/metabolism ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; RNA Polymerase II/chemistry/*metabolism/*ultrastructure ; RNA, Messenger/biosynthesis/genetics/ultrastructure ; Saccharomyces cerevisiae/enzymology ; Templates, Genetic ; *Transcription Elongation, Genetic
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 1982-11-19
    Description: Each of seven Australasian tektites contains about 1 x l0(8) atoms of beryllium-10 (half-life, 1.53 x 10(6) years) per gram. Cosmic-ray bombardment of the australites cannot have produced the measured amounts of beryllium-10 either at the earth's surface or in space. The beryllium-10 contents of these australites are consistent with a sedimentary precursor that adsorbed from precipitation beryllium-10 produced in the atmosphere. The sediments must have spent several thousand years at the earth's surface within a few million years of the tektite-producing event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pal, D K -- Tuniz, C -- Moniot, R K -- Kruse, T H -- Herzog, G F -- New York, N.Y. -- Science. 1982 Nov 19;218(4574):787-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17771035" target="_blank"〉PubMed〈/a〉
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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