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  • 11
    Publication Date: 2019
    Description: 〈p〉Control of emergent magnetic orders in correlated electron materials promises new opportunities for applications in spintronics. For their technological exploitation, it is important to understand the role of surfaces and interfaces to other materials and their impact on the emergent magnetic orders. Here, we demonstrate for iron telluride, the nonsuperconducting parent compound of the iron chalcogenide superconductors, determination and manipulation of the surface magnetic structure by low-temperature spin-polarized scanning tunneling microscopy. Iron telluride exhibits a complex structural and magnetic phase diagram as a function of interstitial iron concentration. Several theories have been put forward to explain the different magnetic orders observed in the phase diagram, which ascribe a dominant role either to interactions mediated by itinerant electrons or to local moment interactions. Through the controlled removal of surface excess iron, we can separate the influence of the excess iron from that of the change in the lattice structure.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
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  • 12
    Publication Date: 2019
    Description: 〈p〉Manley 〈i〉et al.〈/i〉 (〈i〉Science Advances〈/i〉, 16 September 2016, p. e1501814) report the splitting of a transverse acoustic phonon branch below 〈i〉T〈/i〉〈i〉〈sub〉C〈/sub〉〈/i〉 in the relaxor ferroelectric Pb[(Mg〈sub〉1/3〈/sub〉Nb〈sub〉2/3〈/sub〉)〈sub〉1–〈i〉x〈/i〉〈/sub〉Ti〈i〉〈sub〉x〈/sub〉〈/i〉]O〈sub〉3〈/sub〉 with 〈i〉x〈/i〉 = 0.30 using neutron scattering methods. Manley 〈i〉et al.〈/i〉 argue that this splitting occurs because these phonons hybridize with local, harmonic lattice vibrations associated with polar nanoregions. We show that splitting is absent when the measurement is made using a different neutron wavelength, and we suggest an alternative interpretation.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
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  • 13
    Publication Date: 1995-04-28
    Description: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, J -- Stock, D -- Jap, B -- Zwickl, P -- Baumeister, W -- Huber, R -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):533-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung fur Strukturforschung, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725097" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Chaperonin 60/chemistry ; Computer Graphics ; Crystallography, X-Ray ; Cysteine Endopeptidases/*chemistry/metabolism ; Endopeptidases/*chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Leupeptins/chemistry/metabolism ; *Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Protease Inhibitors/chemistry/metabolism ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/metabolism ; Thermoplasma/*enzymology
    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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  • 14
    Publication Date: 1995-04-28
    Description: The catalytic mechanism of the 20S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the beta subunit and by inhibitor studies. Deletion of the amino-terminal threonine or its mutation to alanine led to inactivation of the enzyme. Mutation of the residue to serine led to a fully active enzyme, which was over ten times more sensitive to the serine protease inhibitor 3,4-dichloroisocoumarin. In combination with the crystal structure of a proteasome-inhibitor complex, the data show that the nucleophilic attack is mediated by the amino-terminal threonine of processed beta subunits. The conservation pattern of this residue in eukaryotic sequences suggests that at least three of the seven eukaryotic beta-type subunit branches should be proteolytically inactive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seemuller, E -- Lupas, A -- Stock, D -- Lowe, J -- Huber, R -- Baumeister, W -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung fur Strukturbiologie Max-Planck Institut fur Biochemie, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Coumarins/pharmacology ; Endopeptidases/*chemistry/metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Mutagenesis ; Protein Folding ; Sequence Alignment ; Serine Proteinase Inhibitors/pharmacology ; Thermoplasma/*enzymology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, J -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):370-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. jstock@watson.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927993" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Catalysis ; Chemoreceptor Cells ; Dimerization ; *Escherichia coli Proteins ; Humans ; Ligands ; Membrane Proteins/chemistry/genetics/*metabolism ; Protein Kinases/metabolism ; Receptors, Cell Surface/chemistry/*metabolism ; Receptors, Somatotropin/chemistry/metabolism ; Signal Transduction/*physiology
    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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  • 16
    Publication Date: 1993-04-09
    Description: The Landers earthquake, which had a moment magnitude (M(w)) of 7.3, was the largest earthquake to strike the contiguous United States in 40 years. This earthquake resulted from the rupture of five major and many minor right-lateral faults near the southern end of the eastern California shear zone, just north of the San Andreas fault. Its M(w) 6.1 preshock and M(w) 6.2 aftershock had their own aftershocks and foreshocks. Surficial geological observations are consistent with local and far-field seismologic observations of the earthquake. Large surficial offsets (as great as 6 meters) and a relatively short rupture length (85 kilometers) are consistent with seismological calculations of a high stress drop (200 bars), which is in turn consistent with an apparently long recurrence interval for these faults.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sieh, K -- Jones, L -- Hauksson, E -- Hudnut, K -- Eberhart-Phillips, D -- Heaton, T -- Hough, S -- Hutton, K -- Kanamori, H -- Lilje, A -- Lindvall, S -- McGill, S F -- Mori, J -- Rubin, C -- Spotila, J A -- Stock, J -- Thio, H K -- Treiman, J -- Wernicke, B -- Zachariasen, J -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):171-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17807175" target="_blank"〉PubMed〈/a〉
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  • 17
    Publication Date: 1993-05-07
    Description: The fabrication of improved ceramic-matrix composites will require a better understanding of processing variables and how they control the development of the composite microstructure. Noninvasive, high-resolution methods of x-ray tomography have been used to measure the growth of silicon carbide in a woven Nicalon-fiber composite during chemical vapor infiltration. The high spatial resolution allows one to measure the densification within individual fiber tows and to follow the closure of macroscopic pores in situ. The experiments provide a direct test of a recently proposed model that describes how the surface area available for matrix deposition changes during infiltration. The measurements indicate that this surface area is independent of the fiber architecture and location within the preform and is dominated by large-scale macroporosity during the final stages of composite consolidation. The measured surface areas are in good agreement with the theoretical model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kinney, J H -- Breunig, T M -- Starr, T L -- Haupt, D -- Nichols, M C -- Stock, S R -- Butts, M D -- Saroyan, R A -- New York, N.Y. -- Science. 1993 May 7;260(5109):789-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17746112" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
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  • 18
    Publication Date: 1993-02-12
    Description: In human neutrophils, as in other cell types, Ras-related guanosine triphosphate-binding proteins are directed toward their regulatory targets in membranes by a series of posttranslational modifications that include methyl esterification of a carboxyl-terminal prenylcysteine residue. In intact cells and in a reconstituted in vitro system, the amount of carboxyl methylation of Ras-related proteins increased in response to the chemoattractant N-formyl-methionyl-leucyl-phenylalanine (FMLP). Activation of Ras-related proteins by guanosine-5'-O-(3-thiotriphosphate) had a similar effect and induced translocation of p22rac2 from cytosol to plasma membrane. Inhibitors of prenylcysteine carboxyl methylation effectively blocked neutrophil responses to FMLP. These findings suggest a direct link between receptor-mediated signal transduction and the carboxyl methylation of Ras-related proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philips, M R -- Pillinger, M H -- Staud, R -- Volker, C -- Rosenfeld, M G -- Weissmann, G -- Stock, J B -- AR-07176-18/AR/NIAMS NIH HHS/ -- GM 20277/GM/NIGMS NIH HHS/ -- GM-8309/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):977-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438158" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Cytosol/metabolism ; GTP-Binding Proteins/*metabolism ; *Guanine Nucleotide Dissociation Inhibitors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/pharmacology ; Humans ; Methionine/analogs & derivatives/metabolism ; Methylation ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/*physiology ; Protein Methyltransferases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins p21(ras)/metabolism ; S-Adenosylmethionine/metabolism ; Signal Transduction/*physiology ; Tritium ; rap GTP-Binding Proteins ; rho-Specific Guanine Nucleotide Dissociation Inhibitors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, Joann M -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1250-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 91125, USA. jstock@gps.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946060" target="_blank"〉PubMed〈/a〉
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  • 20
    Publication Date: 2010-03-06
    Description: Nuclear collisions recreate conditions in the universe microseconds after the Big Bang. Only a very small fraction of the emitted fragments are light nuclei, but these states are of fundamental interest. We report the observation of antihypertritons--comprising an antiproton, an antineutron, and an antilambda hyperon--produced by colliding gold nuclei at high energy. Our analysis yields 70 +/- 17 antihypertritons ((Lambda)(3)-H) and 157 +/- 30 hypertritons (Lambda3H). The measured yields of Lambda3H ((Lambda)(3)-H) and 3He (3He) are similar, suggesting an equilibrium in coordinate and momentum space populations of up, down, and strange quarks and antiquarks, unlike the pattern observed at lower collision energies. The production and properties of antinuclei, and of nuclei containing strange quarks, have implications spanning nuclear and particle physics, astrophysics, and cosmology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉STAR Collaboration -- Abelev, B I -- Aggarwal, M M -- Ahammed, Z -- Alakhverdyants, A V -- Alekseev, I -- Anderson, B D -- Arkhipkin, D -- Averichev, G S -- Balewski, J -- Barnby, L S -- Baumgart, S -- Beavis, D R -- Bellwied, R -- Betancourt, M J -- Betts, R R -- Bhasin, A -- Bhati, A K -- Bichsel, H -- Bielcik, J -- Bielcikova, J -- Biritz, B -- Bland, L C -- Bonner, B E -- Bouchet, J -- Braidot, E -- Brandin, A V -- Bridgeman, A -- Bruna, E -- Bueltmann, S -- Bunzarov, I -- Burton, T P -- Cai, X Z -- Caines, H -- Calderon, M -- Catu, O -- Cebra, D -- Cendejas, R -- Cervantes, M C -- Chajecki, Z -- Chaloupka, P -- Chattopadhyay, S -- Chen, H F -- Chen, J H -- Chen, J Y -- Cheng, J -- Cherney, M -- Chikanian, A -- Choi, K E -- Christie, W -- Chung, P -- Clarke, R F -- Codrington, M J M -- Corliss, R -- Cramer, J G -- Crawford, H J -- Das, D -- Dash, S -- Davila Leyva, A -- De Silva, L C -- Debbe, R R -- Dedovich, T G -- DePhillips, M -- Derevschikov, A A -- Derradi de Souza, R -- Didenko, L -- Djawotho, P -- Dogra, S M -- Dong, X -- Drachenberg, J L -- Draper, J E -- Dunlop, J C -- Dutta Mazumdar, M R -- Efimov, L G -- Elhalhuli, E -- Elnimr, M -- Engelage, J -- Eppley, G -- Erazmus, B -- Estienne, M -- Eun, L -- Evdokimov, O -- Fachini, P -- Fatemi, R -- Fedorisin, J -- Fersch, R G -- Filip, P -- Finch, E -- Fine, V -- Fisyak, Y -- Gagliardi, C A -- Gangadharan, D R -- Ganti, M S -- Garcia-Solis, E J -- Geromitsos, A -- Geurts, F -- Ghazikhanian, V -- Ghosh, P -- Gorbunov, Y N -- Gordon, A -- Grebenyuk, O -- Grosnick, D -- Grube, B -- Guertin, S M -- Gupta, A -- Gupta, N -- Guryn, W -- Haag, B -- Hamed, A -- Han, L-X -- Harris, J W -- Hays-Wehle, J P -- Heinz, M -- Heppelmann, S -- Hirsch, A -- Hjort, E -- Hoffman, A M -- Hoffmann, G W -- Hofman, D J -- Hollis, R S -- Huang, B -- Huang, H Z -- Humanic, T J -- Huo, L -- Igo, G -- Iordanova, A -- Jacobs, P -- Jacobs, W W -- Jakl, P -- Jena, C -- Jin, F -- Jones, C L -- Jones, P G -- Joseph, J -- Judd, E G -- Kabana, S -- Kajimoto, K -- Kang, K -- Kapitan, J -- Kauder, K -- Keane, D -- Kechechyan, A -- Kettler, D -- Kikola, D P -- Kiryluk, J -- Kisiel, A -- Klein, S R -- Knospe, A G -- Kocoloski, A -- Koetke, D D -- Kollegger, T -- Konzer, J -- Kopytine, M -- Koralt, I -- Koroleva, L -- Korsch, W -- Kotchenda, L -- Kouchpil, V -- Kravtsov, P -- Krueger, K -- Krus, M -- Kumar, L -- Kurnadi, P -- Lamont, M A C -- Landgraf, J M -- LaPointe, S -- Lauret, J -- Lebedev, A -- Lednicky, R -- Lee, C-H -- Lee, J H -- Leight, W -- Levine, M J -- Li, C -- Li, L -- Li, N -- Li, W -- Li, X -- Li, Y -- Li, Z -- Lin, G -- Lindenbaum, S J -- Lisa, M A -- Liu, F -- Liu, H -- Liu, J -- Ljubicic, T -- Llope, W J -- Longacre, R S -- Love, W A -- Lu, Y -- Luo, X -- Ma, G L -- Ma, Y G -- Mahapatra, D P -- Majka, R -- Mal, O I -- Mangotra, L K -- Manweiler, R -- Margetis, S -- Markert, C -- Masui, H -- Matis, H S -- Matulenko, Yu A -- McDonald, D -- McShane, T S -- Meschanin, A -- Milner, R -- Minaev, N G -- Mioduszewski, S -- Mischke, A -- Mitrovski, M K -- Mohanty, B -- Mondal, M M -- Morozov, B -- Morozov, D A -- Munhoz, M G -- Nandi, B K -- Nattrass, C -- Nayak, T K -- Nelson, J M -- Netrakanti, P K -- Ng, M J -- Nogach, L V -- Nurushev, S B -- Odyniec, G -- Ogawa, A -- Okada, H -- Okorokov, V -- Olson, D -- Pachr, M -- Page, B S -- Pal, S K -- Pandit, Y -- Panebratsev, Y -- Pawlak, T -- Peitzmann, T -- Perevoztchikov, V -- Perkins, C -- Peryt, W -- Phatak, S C -- Pile, P -- Planinic, M -- Ploskon, M A -- Pluta, J -- Plyku, D -- Poljak, N -- Poskanzer, A M -- Potukuchi, B V K S -- Powell, C B -- Prindle, D -- Pruneau, C -- Pruthi, N K -- Pujahari, P R -- Putschke, J -- Qiu, H -- Raniwala, R -- Raniwala, S -- Ray, R L -- Redwine, R -- Reed, R -- Ritter, H G -- Roberts, J B -- Rogachevskiy, O V -- Romero, J L -- Rose, A -- Roy, C -- Ruan, L -- Sahoo, R -- Sakai, S -- Sakrejda, I -- Sakuma, T -- Salur, S -- Sandweiss, J -- Sangaline, E -- Schambach, J -- Scharenberg, R P -- Schmitz, N -- Schuster, T R -- Seele, J -- Seger, J -- Selyuzhenkov, I -- Seyboth, P -- Shahaliev, E -- Shao, M -- Sharma, M -- Shi, S S -- Sichtermann, E P -- Simon, F -- Singaraju, R N -- Skoby, M J -- Smirnov, N -- Sorensen, P -- Sowinski, J -- Spinka, H M -- Srivastava, B -- Stanislaus, T D S -- Staszak, D -- Stevens, J R -- Stock, R -- Strikhanov, M -- Stringfellow, B -- Suaide, A A P -- Suarez, M C -- Subba, N L -- Sumbera, M -- Sun, X M -- Sun, Y -- Sun, Z -- Surrow, B -- Svirida, D N -- Symons, T J M -- Szanto de Toledo, A -- Takahashi, J -- Tang, A H -- Tang, Z -- Tarini, L H -- Tarnowsky, T -- Thein, D -- Thomas, J H -- Tian, J -- Timmins, A R -- Timoshenko, S -- Tlusty, D -- Tokarev, M -- Trainor, T A -- Tram, V N -- Trentalange, S -- Tribble, R E -- Tsai, O D -- Ulery, J -- Ullrich, T -- Underwood, D G -- Van Buren, G -- van Leeuwen, M -- van Nieuwenhuizen, G -- Vanfossen, J A Jr -- Varma, R -- Vasconcelos, G M S -- Vasiliev, A N -- Videbaek, F -- Viyogi, Y P -- Vokal, S -- Voloshin, S A -- Wada, M -- Walker, M -- Wang, F -- Wang, G -- Wang, H -- Wang, J S -- Wang, Q -- Wang, X L -- Wang, Y -- Webb, G -- Webb, J C -- Westfall, G D -- Whitten, C Jr -- Wieman, H -- Wingfield, E -- Wissink, S W -- Witt, R -- Wu, Y -- Xie, W -- Xu, H -- Xu, N -- Xu, Q H -- Xu, W -- Xu, Y -- Xu, Z -- Xue, L -- Yang, Y -- Yepes, P -- Yip, K -- Yoo, I-K -- Yue, Q -- Zawisza, M -- Zbroszczyk, H -- Zhan, W -- Zhang, J -- Zhang, S -- Zhang, W M -- Zhang, X P -- Zhang, Y -- Zhang, Z P -- Zhao, J -- Zhong, C -- Zhou, J -- Zhou, W -- Zhu, X -- Zhu, Y H -- Zoulkarneev, R -- Zoulkarneeva, Y -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):58-62. doi: 10.1126/science.1183980. Epub 2010 Mar 4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20203011" target="_blank"〉PubMed〈/a〉
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