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  • 1
    Publication Date: 2015-05-06
    Description: Author(s): Zahra Yamani, W. J. L. Buyers, F. Wang, Y.-J. Kim, J.-H. Chung, S. Chang, P. M. Gehring, G. Gasparovic, C. Stock, C. L. Broholm, J. C. Baglo, Ruixing Liang, D. A. Bonn, and W. N. Hardy Neutron scattering from high-quality YBa 2 Cu 3 O 6.33 ( YBCO6.33 ) single crystals with a T c of 8.4 K shows no evidence of a coexistence of superconductivity with long-range antiferromagnetic order at this very low, near-critical doping of p ∼ 0.055 . However, we find short-range three-dimensional spin correl... [Phys. Rev. B 91, 134427] Published Wed Apr 29, 2015
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 2
    Publication Date: 2011-06-23
    Description: Author(s): M. Charilaou, J. F. Löffler, and A. U. Gehring In this study, the spin-glass-like properties of ( x )FeTiO 3 – (1- x )Fe 2 O 3 , with x =0.8 and 0.9, as prominent mixed-valence state solid solution, were investigated by means of ac susceptibility and dc magnetization measurements. Dynamic ac susceptibility indicates freezing at finite temperature T f , obeyi... [Phys. Rev. B 83, 224414] Published Wed Jun 22, 2011
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
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  • 3
    Publication Date: 2012-07-31
    Description: Author(s): M. Charilaou, D. Sheptyakov, J. F. Löffler, and A. U. Gehring We present neutron diffraction data and magnetic susceptibility measurements of FeTiO 3 ilmenite and Fe(III)-doped ilmenites (with 10 and 20 mol. % Fe 2 O 3 ) at temperatures of 1.9 K 〈 T 〈 300 K. The magnetic moments of the Fe cations in FeTiO 3 lie predominantly along the c axis, with a weak compone... [Phys. Rev. B 86, 024439] Published Mon Jul 30, 2012
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
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  • 4
    Publication Date: 2012-09-13
    Description: Author(s): M. Charilaou, K. K. Sahu, A. U. Gehring, and J. F. Löffler We present a mean-field model with competing interlayer interactions which give rise to organized frustration. The frustration arises due to the difference in modulation length of the interlayer exchange coupling in the mixed-spin state. We calculate the energy landscapes and the equations of state ... [Phys. Rev. B 86, 104415] Published Wed Sep 12, 2012
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
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  • 5
    Publication Date: 2011-12-29
    Description: Author(s): M. Charilaou, K. K. Sahu, A. U. Gehring, and J. F. Löffler [Phys. Rev. B 84, 224434] Published Wed Dec 28, 2011
    Keywords: Magnetism
    Print ISSN: 1098-0121
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  • 6
    Publication Date: 2014-10-29
    Description: Author(s): Marzook S. Alshammari, Mohammed S. Alqahtani, Hasan B. Albargi, Salman A. Alfihed, Yaser A. Alshetwi, Abdulrahman A. Alghihab, Abdullah M. Alsamrah, Nawaf M. Alshammari, Mohammed A. Aldosari, Ahmed Alyamani, Ali M. H. R. Hakimi, Steve M. Heald, Harry J. Blythe, Mark G. Blamire, A. Mark Fox, and Gillian A. Gehring Films of Fe-doped In2O3 that were deliberately fabricated so they contained Fe3O4 nanoparticles were deposited on sapphire substrates by pulsed laser deposition at low oxygen pressure. The concentration of Fe was varied between 1% and 5%, and the effect of including 5% of Sn and vacuum annealing wer... [Phys. Rev. B 90, 144433] Published Tue Oct 28, 2014
    Keywords: Magnetism
    Print ISSN: 1098-0121
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  • 7
    Publication Date: 2001-07-28
    Description: Studies that combine experimental manipulations with long-term data collection reveal elaborate interactions among species that affect the structure and dynamics of ecosystems. Research programs in U.S. desert shrubland and pinyon-juniper woodland have shown that (i) complex dynamics of species populations reflect interactions with other organisms and fluctuating climate; (ii) genotype x environment interactions affect responses of species to environmental change; (iii) herbivore-resistance traits of dominant plant species and impacts of "keystone" animal species cascade through the system to affect many organisms and ecosystem processes; and (iv) some environmental perturbations can cause wholesale reorganization of ecosystems because they exceed the ecological tolerances of dominant or keystone species, whereas other changes may be buffered because of the compensatory dynamics of complementary species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, J H -- Whitham, T G -- Morgan Ernest, S K -- Gehring, C A -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):643-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of New Mexico, Albuquerque, NM 87131, USA. jhbrown@unm.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474100" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arizona ; Desert Climate ; *Ecosystem ; Environment ; Genotype ; *Gymnosperms ; Moths/physiology ; Plants ; Population Dynamics ; *Rodentia/physiology ; Time Factors ; *Trees ; Weather
    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: 2008-11-21
    Description: The Ca(2+)-dependent cysteine proteases, calpains, regulate cell migration, cell death, insulin secretion, synaptic function and muscle homeostasis. Their endogenous inhibitor, calpastatin, consists of four inhibitory repeats, each of which neutralizes an activated calpain with exquisite specificity and potency. Despite the physiological importance of this interaction, the structural basis of calpain inhibition by calpastatin is unknown. Here we report the 3.0 A structure of Ca(2+)-bound m-calpain in complex with the first calpastatin repeat, both from rat, revealing the mechanism of exclusive specificity. The structure highlights the complexity of calpain activation by Ca(2+), illustrating key residues in a peripheral domain that serve to stabilize the protease core on Ca(2+) binding. Fully activated calpain binds ten Ca(2+) atoms, resulting in several conformational changes allowing recognition by calpastatin. Calpain inhibition is mediated by the intimate contact with three critical regions of calpastatin. Two regions target the penta-EF-hand domains of calpain and the third occupies the substrate-binding cleft, projecting a loop around the active site thiol to evade proteolysis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2847431/" 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/PMC2847431/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moldoveanu, Tudor -- Gehring, Kalle -- Green, Douglas R -- P01 CA069381/CA/NCI NIH HHS/ -- P01 CA069381-140010/CA/NCI NIH HHS/ -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 AI040646/AI/NIAID NIH HHS/ -- R01 AI040646-14/AI/NIAID NIH HHS/ -- R01 AI044828/AI/NIAID NIH HHS/ -- R01 AI044828-12/AI/NIAID NIH HHS/ -- R01 AI047891/AI/NIAID NIH HHS/ -- R01 AI047891-12/AI/NIAID NIH HHS/ -- R37 GM052735/GM/NIGMS NIH HHS/ -- R37 GM052735-19/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 Nov 20;456(7220):404-8. doi: 10.1038/nature07353.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, St Jude Children's Research Hospital, 332 N Lauderdale, Memphis, Tennessee 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19020622" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biocatalysis ; Calcium/metabolism ; Calcium-Binding Proteins/*chemistry/genetics/*metabolism ; Calpain/antagonists & inhibitors/*chemistry/*metabolism ; *Catalytic Domain ; Crystallography, X-Ray ; EF Hand Motifs ; Enzyme Activation ; Protein Binding ; Protein Multimerization ; Protein Processing, Post-Translational ; Rats ; Structure-Activity Relationship ; Substrate Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2013-04-19
    Description: Zebrafish have become a popular organism for the study of vertebrate gene function. The virtually transparent embryos of this species, and the ability to accelerate genetic studies by gene knockdown or overexpression, have led to the widespread use of zebrafish in the detailed investigation of vertebrate gene function and increasingly, the study of human genetic disease. However, for effective modelling of human genetic disease it is important to understand the extent to which zebrafish genes and gene structures are related to orthologous human genes. To examine this, we generated a high-quality sequence assembly of the zebrafish genome, made up of an overlapping set of completely sequenced large-insert clones that were ordered and oriented using a high-resolution high-density meiotic map. Detailed automatic and manual annotation provides evidence of more than 26,000 protein-coding genes, the largest gene set of any vertebrate so far sequenced. Comparison to the human reference genome shows that approximately 70% of human genes have at least one obvious zebrafish orthologue. In addition, the high quality of this genome assembly provides a clearer understanding of key genomic features such as a unique repeat content, a scarcity of pseudogenes, an enrichment of zebrafish-specific genes on chromosome 4 and chromosomal regions that influence sex determination.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3703927/" 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/PMC3703927/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Howe, Kerstin -- Clark, Matthew D -- Torroja, Carlos F -- Torrance, James -- Berthelot, Camille -- Muffato, Matthieu -- Collins, John E -- Humphray, Sean -- McLaren, Karen -- Matthews, Lucy -- McLaren, Stuart -- Sealy, Ian -- Caccamo, Mario -- Churcher, Carol -- Scott, Carol -- Barrett, Jeffrey C -- Koch, Romke -- Rauch, Gerd-Jorg -- White, Simon -- Chow, William -- Kilian, Britt -- Quintais, Leonor T -- Guerra-Assuncao, Jose A -- Zhou, Yi -- Gu, Yong -- Yen, Jennifer -- Vogel, Jan-Hinnerk -- Eyre, Tina -- Redmond, Seth -- Banerjee, Ruby -- Chi, Jianxiang -- Fu, Beiyuan -- Langley, Elizabeth -- Maguire, Sean F -- Laird, Gavin K -- Lloyd, David -- Kenyon, Emma -- Donaldson, Sarah -- Sehra, Harminder -- Almeida-King, Jeff -- Loveland, Jane -- Trevanion, Stephen -- Jones, Matt -- Quail, Mike -- Willey, Dave -- Hunt, Adrienne -- Burton, John -- Sims, Sarah -- McLay, Kirsten -- Plumb, Bob -- Davis, Joy -- Clee, Chris -- Oliver, Karen -- Clark, Richard -- Riddle, Clare -- Elliot, David -- Threadgold, Glen -- Harden, Glenn -- Ware, Darren -- Begum, Sharmin -- Mortimore, Beverley -- Kerry, Giselle -- Heath, Paul -- Phillimore, Benjamin -- Tracey, Alan -- Corby, Nicole -- Dunn, Matthew -- Johnson, Christopher -- Wood, Jonathan -- Clark, Susan -- Pelan, Sarah -- Griffiths, Guy -- Smith, Michelle -- Glithero, Rebecca -- Howden, Philip -- Barker, Nicholas -- Lloyd, Christine -- Stevens, Christopher -- Harley, Joanna -- Holt, Karen -- Panagiotidis, Georgios -- Lovell, Jamieson -- Beasley, Helen -- Henderson, Carl -- Gordon, Daria -- Auger, Katherine -- Wright, Deborah -- Collins, Joanna -- Raisen, Claire -- Dyer, Lauren -- Leung, Kenric -- Robertson, Lauren -- Ambridge, Kirsty -- Leongamornlert, Daniel -- McGuire, Sarah -- Gilderthorp, Ruth -- Griffiths, Coline -- Manthravadi, Deepa -- Nichol, Sarah -- Barker, Gary -- Whitehead, Siobhan -- Kay, Michael -- Brown, Jacqueline -- Murnane, Clare -- Gray, Emma -- Humphries, Matthew -- Sycamore, Neil -- Barker, Darren -- Saunders, David -- Wallis, Justene -- Babbage, Anne -- Hammond, Sian -- Mashreghi-Mohammadi, Maryam -- Barr, Lucy -- Martin, Sancha -- Wray, Paul -- Ellington, Andrew -- Matthews, Nicholas -- Ellwood, Matthew -- Woodmansey, Rebecca -- Clark, Graham -- Cooper, James D -- Tromans, Anthony -- Grafham, Darren -- Skuce, Carl -- Pandian, Richard -- Andrews, Robert -- Harrison, Elliot -- Kimberley, Andrew -- Garnett, Jane -- Fosker, Nigel -- Hall, Rebekah -- Garner, Patrick -- Kelly, Daniel -- Bird, Christine -- Palmer, Sophie -- Gehring, Ines -- Berger, Andrea -- Dooley, Christopher M -- Ersan-Urun, Zubeyde -- Eser, Cigdem -- Geiger, Horst -- Geisler, Maria -- Karotki, Lena -- Kirn, Anette -- Konantz, Judith -- Konantz, Martina -- Oberlander, Martina -- Rudolph-Geiger, Silke -- Teucke, Mathias -- Lanz, Christa -- Raddatz, Gunter -- Osoegawa, Kazutoyo -- Zhu, Baoli -- Rapp, Amanda -- Widaa, Sara -- Langford, Cordelia -- Yang, Fengtang -- Schuster, Stephan C -- Carter, Nigel P -- Harrow, Jennifer -- Ning, Zemin -- Herrero, Javier -- Searle, Steve M J -- Enright, Anton -- Geisler, Robert -- Plasterk, Ronald H A -- Lee, Charles -- Westerfield, Monte -- de Jong, Pieter J -- Zon, Leonard I -- Postlethwait, John H -- Nusslein-Volhard, Christiane -- Hubbard, Tim J P -- Roest Crollius, Hugues -- Rogers, Jane -- Stemple, Derek L -- 095908/Wellcome Trust/United Kingdom -- 098051/Wellcome Trust/United Kingdom -- 1 R01 DK55377-01A1/DK/NIDDK NIH HHS/ -- P01 HD022486/HD/NICHD NIH HHS/ -- P01 HD22486/HD/NICHD NIH HHS/ -- R01 GM085318/GM/NIGMS NIH HHS/ -- R01 OD011116/OD/NIH HHS/ -- R01 RR010715/RR/NCRR NIH HHS/ -- R01 RR020833/RR/NCRR NIH HHS/ -- England -- Nature. 2013 Apr 25;496(7446):498-503. doi: 10.1038/nature12111. Epub 2013 Apr 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23594743" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes/genetics ; Conserved Sequence/*genetics ; Evolution, Molecular ; Female ; Genes/genetics ; Genome/*genetics ; Genome, Human/genetics ; Genomics ; Humans ; Male ; Meiosis/genetics ; Molecular Sequence Annotation ; Pseudogenes/genetics ; Reference Standards ; Sex Determination Processes/genetics ; Zebrafish/*genetics ; Zebrafish Proteins/genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 10
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-24
    Description: The Drosophila gene eyeless (ey) encodes a transcription factor with both a paired domain and a homeodomain. It is homologous to the mouse Small eye (Pax-6) gene and to the Aniridia gene in humans. These genes share extensive sequence identity, the position of three intron splice sites is conserved, and these genes are expressed similarly in the developing nervous system and in the eye during morphogenesis. Loss-of-function mutations in both the insect and in the mammalian genes have been shown to lead to a reduction or absence of eye structures, which suggests that ey functions in eye morphogenesis. By targeted expression of the ey complementary DNA in various imaginal disc primordia of Drosophila, ectopic eye structures were induced on the wings, the legs, and on the antennae. The ectopic eyes appeared morphologically normal and consisted of groups of fully differentiated ommatidia with a complete set of photoreceptor cells. These results support the proposition that ey is the master control gene for eye morphogenesis. Because homologous genes are present in vertebrates, ascidians, insects, cephalopods, and nemerteans, ey may function as a master control gene throughout the metazoa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halder, G -- Callaerts, P -- Gehring, W J -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1788-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila/*embryology/*genetics ; Eye/embryology ; Gene Expression Regulation/physiology ; Genes, Homeobox/physiology ; Genes, Insect/*physiology ; Genes, Reporter ; Microscopy, Electron, Scanning ; Mutation ; Photoreceptor Cells, Invertebrate/embryology ; beta-Galactosidase/genetics
    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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