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  • 1
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    Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-26
    Description: Mature erythrocytes in mammals have no nuclei, although they differentiate from nucleated precursor cells. The mechanism by which enucleation occurs is not well understood. Here we show that deoxyribonuclease II (DNase II) is indispensable for definitive erythropoiesis in mouse fetal liver. No live DNase II-null mice were born, owing to severe anemia. When mutant fetal liver cells were transferred into lethally irradiated wild-type mice, mature red blood cells were generated from the mutant cells, suggesting that DNase II functions in a non-cell-autonomous manner. Histochemical analyses indicated that the critical cellular sources of DNase II are macrophages present at the site of definitive erythropoiesis in the fetal liver. Thus, DNase II in macrophages appears to be responsible for destroying the nuclear DNA expelled from erythroid precursor cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawane, K -- Fukuyama, H -- Kondoh, G -- Takeda, J -- Ohsawa, Y -- Uchiyama, Y -- Nagata, S -- New York, N.Y. -- Science. 2001 May 25;292(5521):1546-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Osaka University Medical School, and Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Suita, Osaka 565-0871, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11375492" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Cell Differentiation ; Cell Transplantation ; DNA/analysis/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Endodeoxyribonucleases/genetics/*metabolism ; Erythroblasts/cytology/metabolism ; Erythroid Precursor Cells/cytology/metabolism ; *Erythropoiesis ; Fetus/enzymology ; Gene Targeting ; Globins/genetics/metabolism ; *Hematopoiesis, Extramedullary ; Kruppel-Like Transcription Factors ; Liver/cytology/*embryology/enzymology/*physiology ; Lysosomes/enzymology ; Macrophages/chemistry/*enzymology/ultrastructure ; Mice ; Mice, Knockout ; Mutation ; RNA, Messenger/genetics/metabolism ; Transcription Factors/genetics/metabolism
    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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  • 2
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    Language control in the bilingual brain (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-06-10
    Description: How does the bilingual brain distinguish and control which language is in use? Previous functional imaging experiments have not been able to answer this question because proficient bilinguals activate the same brain regions irrespective of the language being tested. Here, we reveal that neuronal responses within the left caudate are sensitive to changes in the language or the meaning of words. By demonstrating this effect in populations of German-English and Japanese-English bilinguals, we suggest that the left caudate plays a universal role in monitoring and controlling the language in use.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crinion, J -- Turner, R -- Grogan, A -- Hanakawa, T -- Noppeney, U -- Devlin, J T -- Aso, T -- Urayama, S -- Fukuyama, H -- Stockton, K -- Usui, K -- Green, D W -- Price, C J -- 051067/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Jun 9;312(5779):1537-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Department of Imaging Neuroscience, University College London, London WC1N 3BG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16763154" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Brain Mapping ; Caudate Nucleus/*physiology ; Female ; Humans ; Magnetic Resonance Imaging ; Male ; Middle Aged ; *Multilingualism ; Neurons/physiology ; Positron-Emission Tomography ; Semantics
    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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    Solvent tuning of electrochemical potentials in the active sites of HiPIP versus ferredoxin (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-12-01
    Description: A persistent puzzle in the field of biological electron transfer is the conserved iron-sulfur cluster motif in both high potential iron-sulfur protein (HiPIP) and ferredoxin (Fd) active sites. Despite this structural similarity, HiPIPs react oxidatively at physiological potentials, whereas Fds are reduced. Sulfur K-edge x-ray absorption spectroscopy uncovers the substantial influence of hydration on this variation in reactivity. Fe-S covalency is much lower in natively hydrated Fd active sites than in HiPIPs but increases upon water removal; similarly, HiPIP covalency decreases when unfolding exposes an otherwise hydrophobically shielded active site to water. Studies on model compounds and accompanying density functional theory calculations support a correlation of Fe-S covalency with ease of oxidation and therefore suggest that hydration accounts for most of the difference between Fd and HiPIP reduction potentials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dey, Abhishek -- Jenney, Francis E Jr -- Adams, Michael W W -- Babini, Elena -- Takahashi, Yasuhiro -- Fukuyama, Keiichi -- Hodgson, Keith O -- Hedman, Britt -- Solomon, Edward I -- GM 60329/GM/NIGMS NIH HHS/ -- P41 RR-001209/RR/NCRR NIH HHS/ -- RR-01209/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1464-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048692" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry ; Binding Sites ; Electrochemistry ; Ferredoxins/*chemistry ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Iron/chemistry ; Iron-Sulfur Proteins/*chemistry ; Ligands ; Oxidation-Reduction ; Photosynthetic Reaction Center Complex Proteins/*chemistry ; Protein Folding ; Solvents ; Spectrum Analysis ; Static Electricity ; Sulfur/chemistry ; Water/chemistry
    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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    Estimation of fault strength: reconstruction of stress before the 1995 Kobe earthquake (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-09
    Description: We have estimated the stress field before the 1995 Kobe, Japan, earthquake (moment magnitude 6.9) using in situ post-shock stress measurements obtained from hydraulic fracturing experiments near the fault. We reconstructed the pre-shock stress field using a kinematic source model inverted from seismic waveforms and geodetic deformations. We found that at the center of the fault, two sides of the fault surface coupled completely before the earthquake, with a coefficient of friction of 0.6, which is equivalent to strong crust. At the edge of the fault, a possible aseismic slip is expected to occur from the pre-shock stress orientation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamashita, Futoshi -- Fukuyama, Eiichi -- Omura, Kentaro -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):261-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Research Institute for Earth Science and Disaster Prevention, 3 -1, Tennodai, Tsukuba, Ibaraki, 305-0006, Japan. yamafuto@bosai.go.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472072" 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
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    SCIENCE GOVERNANCE. A more systematic approach to biological risk (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-12-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palmer, Megan J -- Fukuyama, Francis -- Relman, David A -- New York, N.Y. -- Science. 2015 Dec 18;350(6267):1471-3. doi: 10.1126/science.aad8849.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for International Security and Cooperation, Stanford University, Stanford, CA, USA. ; Center on Democracy, Development, and the Rule of Law, and Freeman Spogli Institute for International Studies, Stanford University, Stanford, CA, USA. Department of Microbiology and Immunology, Stanford University, Stanford, CA, USA. ; Center for International Security and Cooperation, Stanford University, Stanford, CA, USA. Department of Microbiology and Immunology, Stanford University, Stanford, CA, USA. Department of Medicine, Stanford University, Stanford, CA, USA. relman@stanford.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26680180" target="_blank"〉PubMed〈/a〉
    Keywords: Biohazard Release/*prevention & control ; Biological Science Disciplines/*trends ; Biomedical Technology/*trends ; Humans ; Risk ; Safety ; Safety Management/*methods ; Security Measures ; United States
    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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