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  • 2005-2009  (464)
  • 2000-2004  (402)
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  • 1
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    In:  Tectonophys., Kyoto, AGU, vol. 408, no. 1-4, pp. 63-77, pp. 2215, (ISSN: 1340-4202)
    Publication Date: 2005
    Keywords: Review article ; paleo ; Seismicity ; Geol. aspects ; Earthquake hazard ; Earthquake ; Chi-Chi ; China ; Earthquake ; fault ; Trenching ; study ; Coseismic ; coastal ; uplift
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  • 2
    Publication Date: 2006
    Keywords: Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Geodesy ; Earthquake ; China ; Inversion ; Fracture ; Source ; GRL ; 1734 ; History ; of ; Geophysics: ; Seismology ; 1744 ; Tectonophysics ; 8004 ; Structural ; Geology: ; Dynamics ; and ; mechanics ; of ; faulting ; (8118) ; 8123 ; Tectonophysics: ; Dynamics: ; seismotectonics ; 8175 ; Tectonics ; and ; landscape ; evolution
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  • 3
    Publication Date: 2003-11-01
    Description: Mutations in MeCP2, which encodes a protein that has been proposed to function as a global transcriptional repressor, are the cause of Rett syndrome (RT T), an X-linked progressive neurological disorder. Although the selective inactivation of MeCP2 in neurons is sufficient to confer a Rett-like phenotype in mice, the specific functions of MeCP2 in postmitotic neurons are not known. We find that MeCP2 binds selectively to BDNF promoter III and functions to repress expression of the BDNF gene. Membrane depolarization triggers the calcium-dependent phosphorylation and release of MeCP2 from BDNF promoter III, thereby facilitating transcription. These studies indicate that MeCP2 plays a key role in the control of neuronal activity-dependent gene regulation and suggest that the deregulation of this process may underlie the pathology of RT T.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wen G -- Chang, Qiang -- Lin, Yingxi -- Meissner, Alexander -- West, Anne E -- Griffith, Eric C -- Jaenisch, Rudolf -- Greenberg, Michael E -- HD 18655/HD/NICHD NIH HHS/ -- NS28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):885-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593183" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/*genetics ; Calcium/*metabolism ; Cell Membrane/physiology ; Cells, Cultured ; *Chromosomal Proteins, Non-Histone ; Cloning, Molecular ; CpG Islands ; DNA Methylation ; DNA-Binding Proteins/*metabolism ; Electrophoretic Mobility Shift Assay ; *Gene Expression Regulation ; Gene Silencing ; Histones/metabolism ; Methyl-CpG-Binding Protein 2 ; Methylation ; Mice ; Mice, Knockout ; Neurons/metabolism/physiology ; Phosphorylation ; Potassium Chloride/pharmacology ; Precipitin Tests ; Promoter Regions, Genetic ; Rats ; *Repressor Proteins ; Rett Syndrome/genetics ; *Transcription, Genetic
    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: 2001-09-22
    Description: We combined coherent nonlinear optical spectroscopy with nano-electron volt energy resolution and low-temperature near-field microscopy with subwavelength resolution (〈lambda/2) to provide direct and local access to the excitonic dipole in a semiconductor nanostructure quantum system. Our technique allows the ability to address, excite, and probe single eigenstates of solid-state quantum systems with spectral and spatial selectivity while simultaneously providing a measurement of all the various time scales of the excitation including state relaxation and decoherence rates. In analogy to scanning tunneling microscopy measurements, we can now map the optical local density of states of a disordered nanostructure. These measurements lay the groundwork for studying and exploiting spatial and temporal coherence in the nanoscopic regime of solid-state systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guest, J R -- Stievater, T H -- Chen, G -- Tabak, E A -- Orr, B G -- Steel, D G -- Gammon, D -- Katzer, D S -- New York, N.Y. -- Science. 2001 Sep 21;293(5538):2224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harrison M. Randall Laboratory of Physics, The University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11567131" 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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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-06-01
    Description: Tumor necrosis factor (TNF) is a major mediator of apoptosis as well as inflammation and immunity, and it has been implicated in the pathogenesis of a wide spectrum of human diseases, including sepsis, diabetes, cancer, osteoporosis, multiple sclerosis, rheumatoid arthritis, and inflammatory bowel diseases. The interaction of TNF with TNF receptor-1 (TNF-R1) activates several signal transduction pathways. A common feature of each pathway is the TNF-induced formation of a multiprotein signaling complex at the cell membrane. Over the past decade, many of the components and mechanisms of these signaling pathways have been elucidated. We provide an overview of current knowledge of TNF signaling and introduce an STKE Connections Map that depicts a canonical view of this process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Guoqing -- Goeddel, David V -- New York, N.Y. -- Science. 2002 May 31;296(5573):1634-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik Inc., Two Corporate Drive, South San Francisco, CA 94080, USA. goeddel@tularik.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040173" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*metabolism ; Apoptosis ; Cell Membrane/metabolism ; Humans ; I-kappa B Kinase ; I-kappa B Proteins/metabolism ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/metabolism ; Models, Biological ; Multiprotein Complexes ; NF-kappa B/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Tumor Necrosis Factor/*metabolism ; Receptors, Tumor Necrosis Factor, Type I ; *Signal Transduction ; Tumor Necrosis Factor-alpha/chemistry/*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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  • 6
    Publication Date: 2000-08-19
    Description: TR3, an immediate-early response gene and an orphan member of the steroid-thyroid hormone-retinoid receptor superfamily of transcription factors, regulates apoptosis through an unknown mechanism. In response to apoptotic stimuli, TR3 translocates from the nucleus to mitochondria to induce cytochrome c release and apoptosis. Mitochondrial targeting of TR3, but not its DNA binding and transactivation, is essential for its proapoptotic effect. Our results reveal a mechanism by which a nuclear transcription factor translocates to mitochondria to initiate apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, H -- Kolluri, S K -- Gu, J -- Dawson, M I -- Cao, X -- Hobbs, P D -- Lin, B -- Chen, G -- Lu, J -- Lin, F -- Xie, Z -- Fontana, J A -- Reed, J C -- Zhang, X -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1159-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947977" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Cell Fractionation ; Cell Nucleus/metabolism ; Cytochrome c Group/*metabolism ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Fatty Acids, Unsaturated/pharmacology ; Genes, Reporter ; Humans ; Intracellular Membranes/metabolism/physiology ; Mitochondria/*metabolism ; Mutation ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
    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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  • 7
    Publication Date: 2001-06-16
    Description: The alpha subunit of a prototypical heterotrimeric GTP-binding protein (G protein), which is encoded by a single gene (GPA1) in Arabidopsis, is a modulator of plant cell proliferation. gpa1 null mutants have reduced cell division in aerial tissues throughout development. Inducible overexpression of GPA1 in Arabidopsis confers inducible ectopic cell division. GPA1 overexpression in synchronized BY-2 cells causes premature advance of the nuclear cycle and the premature appearance of a division wall. Results from loss of function and ectopic expression and activation of GPA1 indicate that this subunit is a positive modulator of cell division in plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullah, H -- Chen, J G -- Young, J C -- Im, K H -- Sussman, M R -- Jones, A M -- New York, N.Y. -- Science. 2001 Jun 15;292(5524):2066-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11408654" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4-Dichlorophenoxyacetic Acid/pharmacology ; Alleles ; Arabidopsis/*cytology/genetics/growth & development/*metabolism ; *Arabidopsis Proteins ; Cell Size ; *GTP-Binding Protein alpha Subunits ; Genes, Plant ; Genes, Reporter ; Glucuronidase/analysis/genetics ; Guanosine Triphosphate/metabolism ; Heterotrimeric GTP-Binding Proteins/chemistry/genetics/*metabolism ; Indoleacetic Acids/pharmacology ; Light ; MAP Kinase Signaling System ; Morphogenesis ; Mutation ; Peptides/pharmacology ; Phenotype ; Plant Leaves/cytology/growth & development ; Plants, Toxic ; Protein Subunits ; Recombinant Proteins/metabolism ; Signal Transduction ; Tobacco
    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: 2000-09-16
    Description: Optically induced entanglement is identified by the spectrum of the phase-sensitive homodyne-detected coherent nonlinear optical response in a single gallium arsenide quantum dot. The electron-hole entanglement involves two magneto-excitonic states differing in transition energy and polarization. The strong coupling needed for entanglement is provided through the Coulomb interaction involving the electrons and holes. The result presents a first step toward the optical realization of quantum logic operations using two or more quantum dots.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen -- Bonadeo -- Steel -- Gammon -- Katzer -- Park -- Sham -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1906-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harrison M. Randall Laboratory of Physics, University of Michigan, Ann Arbor, MI 48109-1120, USA. The Naval Research Laboratory, Washington, DC 20375, USA. Department of Physics, University of California San Diego, La Jolla, CA 92093-0319〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10988065" 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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  • 9
    Publication Date: 2001-08-11
    Description: Dynamic control of interferon-beta (IFN-beta) gene expression requires the regulated assembly and disassembly of the enhanceosome, a higher-order nucleoprotein complex formed in response to virus infection. The enhanceosome activates transcription by recruiting the histone acetyltransferase proteins CREB binding protein (CBP) and p300/CBP-associated factors (PCAF)/GCN5, which, in addition to modifying histones, acetylate HMGI(Y), the architectural component required for enhanceosome assembly. We show that the accurate execution of the IFN-beta transcriptional switch depends on the ordered acetylation of the high-mobility group I protein HMGI(Y) by PCAF/GCN5 and CBP, which acetylate HMGI(Y) at distinct lysine residues on endogenous promoters. Whereas acetylation of HMGI(Y) by CBP at lysine-65 destabilizes the enhanceosome, acetylation of HMGI(Y) by PCAF/GCN5 at lysine-71 potentiates transcription by stabilizing the enhanceosome and preventing acetylation by CBP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munshi, N -- Agalioti, T -- Lomvardas, S -- Merika, M -- Chen, G -- Thanos, D -- 1RO1GM54605/GM/NIGMS NIH HHS/ -- 5-T32-GM07367/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1133-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11498590" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/metabolism ; Amino Acid Sequence ; CREB-Binding Protein ; Cell Cycle Proteins ; *Enhancer Elements, Genetic ; *Gene Expression Regulation ; HMGA1a Protein ; HeLa Cells ; High Mobility Group Proteins/chemistry/*metabolism ; Histone Acetyltransferases ; Histones/metabolism ; Humans ; Interferon-beta/*genetics ; Lysine/metabolism ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/metabolism ; Promoter Regions, Genetic ; Protein Binding ; Recombinant Proteins/metabolism ; Respirovirus/physiology ; *Saccharomyces cerevisiae Proteins ; Trans-Activators/metabolism ; Transcription Factors/chemistry/*metabolism ; *Transcriptional Activation ; Transfection ; p300-CBP Transcription Factors
    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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  • 10
    Publication Date: 2006-03-25
    Description: Traditionally the dispersion of particles in polymeric materials has proven difficult and frequently results in phase separation and agglomeration. We show that thermodynamically stable dispersion of nanoparticles into a polymeric liquid is enhanced for systems where the radius of gyration of the linear polymer is greater than the radius of the nanoparticle. Dispersed nanoparticles swell the linear polymer chains, resulting in a polymer radius of gyration that grows with the nanoparticle volume fraction. It is proposed that this entropically unfavorable process is offset by an enthalpy gain due to an increase in molecular contacts at dispersed nanoparticle surfaces as compared with the surfaces of phase-separated nanoparticles. Even when the dispersed state is thermodynamically stable, it may be inaccessible unless the correct processing strategy is adopted, which is particularly important for the case of fullerene dispersion into linear polymers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackay, Michael E -- Tuteja, Anish -- Duxbury, Phillip M -- Hawker, Craig J -- Van Horn, Brooke -- Guan, Zhibin -- Chen, Guanghui -- Krishnan, R S -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1740-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering and Materials Science, Michigan State University, East Lansing, MI 48824, USA. mackay@msu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556836" 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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