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  • American Association for the Advancement of Science (AAAS)  (16)
  • American Geophysical Union (AGU)
  • 2000-2004
  • 1995-1999  (16)
  • 1999  (16)
  • 1
    Publication Date: 1999-04-02
    Description: Observations of core-diffracted P (Pdiff) and SH (SHdiff) waves recorded by the Missouri-to-Massachusetts (MOMA) seismic array show that the ratio of compressional (P) seismic velocities to horizontal shear (SH) velocities at the base of the mantle changes abruptly from beneath the mid-Pacific (VP/VS = 1.88, also the value predicted by reference Earth models) to beneath Alaska (VP/VS = 1.83). This change signifies a sudden lateral variation in material properties that may have a mineralogical or textural origin. A textural change could be a result of shear stresses induced during the arrival at the core of ancient lithosphere from the northern Pacific paleotrench.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wysession -- Langenhorst -- Fouch -- Fischer -- Al-Eqabi -- Shore -- Clarke -- New York, N.Y. -- Science. 1999 Apr 2;284(5411):120-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth and Planetary Sciences, Washington University, St. Louis, MO 63130, USA. Department of Geological Sciences, Northwestern University, Evanston, IL 60208, USA. Department of Geological Sciences, Brown University, Provide.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10102807" 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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  • 2
    Publication Date: 1999-09-18
    Description: Induction of long-term synaptic changes at one synapse can facilitate the induction of long-term plasticity at another synapse. Evidence is presented here that if Aplysia sensory neuron somata and their remote motor neuron synapses are simultaneously exposed to serotonin pulses insufficient to induce long-term facilitation (LTF) at either site alone, processes activated at these sites interact to induce LTF. This coincident induction of LTF requires that (i) the synaptic pulse occur within a brief temporal window of the somatic pulse, and (ii) local protein synthesis occur immediately at the synapse, followed by delayed protein synthesis at the soma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherff, C M -- Carew, T J -- F32-MH12004/MH/NIMH NIH HHS/ -- R01MH-14-1083/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 17;285(5435):1911-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology and Department of Cellular, Molecular and Developmental Biology, Yale University, New Haven, CT 06520-8205 USA. carolyn.sherff@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10489370" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia ; Emetine/pharmacology ; Interneurons/*physiology ; Membrane Potentials ; Neuronal Plasticity/*physiology ; Neurons, Afferent/*physiology ; Protein Biosynthesis ; Protein Synthesis Inhibitors/pharmacology ; Serotonin/physiology ; Synapses/*physiology ; Synaptic Transmission/physiology ; Time Factors
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  • 3
    Publication Date: 1999-07-20
    Description: A vertebrate securin (vSecurin) was identified on the basis of its biochemical analogy to the Pds1p protein of budding yeast and the Cut2p protein of fission yeast. The vSecurin protein bound to a vertebrate homolog of yeast separins Esp1p and Cut1p and was degraded by proteolysis mediated by an anaphase-promoting complex in a manner dependent on a destruction motif. Furthermore, expression of a stable Xenopus securin mutant protein blocked sister-chromatid separation but did not block the embryonic cell cycle. The vSecurin proteins share extensive sequence similarity with each other but show no sequence similarity to either of their yeast counterparts. Human securin is identical to the product of the gene called pituitary tumor-transforming gene (PTTG), which is overexpressed in some tumors and exhibits transforming activity in NIH 3T3 cells. The oncogenic nature of increased expression of vSecurin may result from chromosome gain or loss, produced by errors in chromatid separation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, H -- McGarry, T J -- Bernal, T -- Kirschner, M W -- GM26875/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 16;285(5426):418-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10411507" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; *Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Animals ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/chemistry/metabolism ; *Cell Transformation, Neoplastic ; Chromatids/*physiology ; Conserved Sequence ; Cyclin B/metabolism ; Cyclin B1 ; *Endopeptidases ; Fungal Proteins/chemistry/metabolism ; HeLa Cells ; Humans ; Ligases/metabolism ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Neoplasm Proteins/chemistry/genetics/*metabolism ; Neoplasms/etiology ; Nuclear Proteins/chemistry/metabolism ; Oncogene Proteins/chemistry/genetics/*metabolism ; Oncogenes ; *Saccharomyces cerevisiae Proteins ; *Schizosaccharomyces pombe Proteins ; Securin ; Separase ; Spindle Apparatus/metabolism ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Xenopus
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  • 4
    Publication Date: 1999-12-11
    Description: Tubby-like proteins (TULPs) are found in a broad range of multicellular organisms. In mammals, genetic mutation of tubby or other TULPs can result in one or more of three disease phenotypes: obesity (from which the name "tubby" is derived), retinal degeneration, and hearing loss. These disease phenotypes indicate a vital role for tubby proteins; however, no biochemical function has yet been ascribed to any member of this protein family. A structure-directed approach was employed to investigate the biological function of these proteins. The crystal structure of the core domain from mouse tubby was determined at a resolution of 1.9 angstroms. From primarily structural clues, experiments were devised, the results of which suggest that TULPs are a unique family of bipartite transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boggon, T J -- Shan, W S -- Santagata, S -- Myers, S C -- Shapiro, L -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2119-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Program, Department of Physiology and Biophysics, Ruttenberg Cancer Center, Mount Sinai School of Medicine of New York University, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10591637" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Nucleus/chemistry ; Crystallography, X-Ray ; DNA/metabolism ; Eye Proteins/*chemistry/genetics/*metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry/genetics/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Sequence Alignment ; Transcription Factors/*chemistry/genetics/*metabolism ; Transcriptional Activation
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  • 5
    Publication Date: 1999-07-20
    Description: Low-temperature single-molecule spectroscopic techniques were applied to a light-harvesting pigment-protein complex (LH2) from purple photosynthetic bacteria. The properties of the electronically excited states of the two circular assemblies (B800 and B850) of bacteriochlorophyll a (BChl a) pigment molecules in the individual complexes were revealed, without ensemble averaging. The results show that the excited states of the B800 ring of pigments are mainly localized on individual BChl a molecules. In contrast, the absorption of a photon by the B850 ring can be consistently described in terms of an excitation that is completely delocalized over the ring. This property may contribute to the high efficiency of energy transfer in these photosynthetic complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Oijen AM -- Ketelaars -- Kohler -- Aartsma -- Schmidt -- New York, N.Y. -- Science. 1999 Jul 16;285(5426):400-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for the Study of Excited States of Molecules, Department of Biophysics, Huygens Laboratory, Leiden University, Post Office Box 9504, 2300 RA Leiden, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10411501" target="_blank"〉PubMed〈/a〉
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  • 6
    Publication Date: 1999-11-05
    Description: Small molecules that perturb specific protein functions are valuable tools for dissecting complex processes in mammalian cells. A combination of two phenotype-based screens, one based on a specific posttranslational modification, the other visualizing microtubules and chromatin, was used to identify compounds that affect mitosis. One compound, here named monastrol, arrested mammalian cells in mitosis with monopolar spindles. In vitro, monastrol specifically inhibited the motility of the mitotic kinesin Eg5, a motor protein required for spindle bipolarity. All previously known small molecules that specifically affect the mitotic machinery target tubulin. Monastrol will therefore be a particularly useful tool for studying mitotic mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayer, T U -- Kapoor, T M -- Haggarty, S J -- King, R W -- Schreiber, S L -- Mitchison, T J -- CA78048/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Oct 29;286(5441):971-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, and Institute of Chemistry and Cell Biology, Harvard Medical School, Boston, MA 02115, USA. Thomas_Mayer@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10542155" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/drug effects ; Animals ; Cattle ; Cell Line ; Cytoskeleton/drug effects ; Golgi Apparatus/drug effects ; Kinesin/*drug effects ; Microtubules/drug effects ; Mitosis/*drug effects ; Molecular Motor Proteins/drug effects ; Phenotype ; Phosphoproteins/metabolism ; Protein Processing, Post-Translational ; Pyrimidines/*pharmacology ; RNA-Binding Proteins/metabolism ; Spindle Apparatus/*drug effects ; Thiones/*pharmacology ; Tumor Cells, Cultured ; Xenopus ; *Xenopus Proteins
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  • 7
    Publication Date: 1999-11-24
    Description: The human adenovirus serotype 5 (Ad5) is used widely for applications in human gene therapy. Cellular attachment of Ad5 is mediated by binding of the carboxyl-terminal knob of its fiber coat protein to the Coxsackie adenovirus receptor (CAR) protein. However, Ad5 binding to CAR hampers the development of adenovirus vectors capable of specifically targeting (diseased) tissues or organs. Through sequence analysis and mutagenesis, a conserved receptor-binding region was identified on the side of three divergent CAR-binding knobs. The feasibility of simultaneous CAR ablation and redirection of an adenovirus to a new receptor is demonstrated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roelvink, P W -- Mi Lee, G -- Einfeld, D A -- Kovesdi, I -- Wickham, T J -- New York, N.Y. -- Science. 1999 Nov 19;286(5444):1568-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research and Development, GenVec Inc., 65 West Watkins Mill Road, Gaithersburg, MD 20879, USA. genecloner@genvec.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10567265" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*chemistry/metabolism ; Amino Acid Sequence ; Binding Sites ; Capsid/*chemistry/genetics/*metabolism ; *Capsid Proteins ; Cell Line ; Conserved Sequence ; Coxsackie and Adenovirus Receptor-Like Membrane Protein ; Genetic Vectors ; Humans ; Models, Molecular ; Mutagenesis, Site-Directed ; Point Mutation ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Virus/*metabolism ; Sequence Deletion ; Transfection ; Tumor Cells, Cultured
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-03-12
    Description: A central question in immunology is the origin of long-lived T cell memory that confers protection against recurrent infection. The differentiation of naive T cell receptor transgenic CD8+ cells into effector cytotoxic T lymphocytes (CTLs) and memory CD8+ cells was studied. Memory CD8+ cells that were generated after strong antigenic stimulation were the progeny of cytotoxic effectors and retained antigen-specific cytolytic activity 10 weeks after adoptive transfer to antigen-free recipient mice. Thus, potential vaccines based on CTL memory will require the differentiation of naive cells into post-effector memory T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Opferman, J T -- Ober, B T -- Ashton-Rickardt, P G -- 5T32 AI07090/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1999 Mar 12;283(5408):1745-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Committee on Immunology, Department of Pathology, Committee on Developmental Biology, The University of Chicago, Gwen Knapp Center for Lupus and Immunology Research, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10073942" target="_blank"〉PubMed〈/a〉
    Keywords: Adoptive Transfer ; Animals ; Apoptosis ; CD8-Positive T-Lymphocytes/*cytology/*immunology ; Cell Differentiation ; Cell Division ; Cell Lineage ; Cells, Cultured ; Cytotoxicity, Immunologic ; Dose-Response Relationship, Immunologic ; H-Y Antigen/immunology ; *Immunologic Memory ; Lymphocyte Activation ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Transgenic ; Perforin ; Pore Forming Cytotoxic Proteins ; T-Lymphocyte Subsets/cytology/*immunology ; T-Lymphocytes, Cytotoxic/cytology/*immunology
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horwitz, A R -- Parsons, J T -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1102-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Microbiology, Health Sciences Center, University of Virginia, Charlottesville, VA 22908, USA. horwitz@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610524" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; *Cell Adhesion ; Cell Adhesion Molecules/metabolism ; *Cell Movement ; Cytoskeleton/physiology ; Fibroblasts/*cytology/physiology ; Integrins/metabolism ; Microtubules/physiology ; Models, Biological ; Myosin Light Chains/metabolism ; Myosins/metabolism ; cdc42 GTP-Binding Protein/metabolism ; rac GTP-Binding Proteins/metabolism ; rho GTP-Binding Proteins/metabolism
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  • 10
    Publication Date: 1999-11-27
    Description: Climate in the tropical North Atlantic is controlled largely by variations in the strength of the trade winds, the position of the Intertropical Convergence Zone, and sea surface temperatures. A high-resolution study of Caribbean sediments provides a subdecadally resolved record of tropical upwelling and trade wind variability spanning the past 825 years. These results confirm the importance of a decadal (12- to 13-year) mode of Atlantic variability believed to be driven by coupled tropical ocean-atmosphere dynamics. Although a well-defined interdecadal mode of variability does not appear to be characteristic of the tropical Atlantic, there is evidence that century-scale variability is substantial. The tropical Atlantic may also have been involved in a major shift in Northern Hemisphere climate variability that took place about 700 years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Black -- Peterson -- Overpeck -- Kaplan -- Evans -- Kashgarian -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1709-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel School of Marine and Atmospheric Science, University of Miami, Miami, FL 33149, USA. National Oceanic and Atmospheric Administration Paleoclimatology Program and the Institute for Arctic and Alpine Research, University of Colorado, B.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576732" target="_blank"〉PubMed〈/a〉
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