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  • International Union of Crystallography  (232)
  • American Association for the Advancement of Science (AAAS)  (211)
  • American Geophysical Union (AGU)
  • Copernicus
  • 1995-1999  (245)
  • 1990-1994  (207)
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  • 1
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    Overview of the Mars Pathfinder mission and assessment of landing site predictions (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Chemical analyses returned by Mars Pathfinder indicate that some rocks may be high in silica, implying differentiated parent materials. Rounded pebbles and cobbles and a possible conglomerate suggest fluvial processes that imply liquid water in equilibrium with the atmosphere and thus a warmer and wetter past. The moment of inertia indicates a central metallic core of 1300 to 2000 kilometers in radius. Composite airborne dust particles appear magnetized by freeze-dried maghemite stain or cement that may have been leached from crustal materials by an active hydrologic cycle. Remote-sensing data at a scale of generally greater than approximately 1 kilometer and an Earth analog correctly predicted a rocky plain safe for landing and roving with a variety of rocks deposited by catastrophic floods that are relatively dust-free.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golombek, M P -- Cook, R A -- Economou, T -- Folkner, W M -- Haldemann, A F -- Kallemeyn, P H -- Knudsen, J M -- Manning, R M -- Moore, H J -- Parker, T J -- Rieder, R -- Schofield, J T -- Smith, P H -- Vaughan, R M -- New York, N.Y. -- Science. 1997 Dec 5;278(5344):1743-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jet Propulsion Laboratory, California Institute of Technology, Pasadena, CA 91109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9388167" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Extraterrestrial Environment ; Geologic Sediments ; Magnetics ; *Mars ; Water
    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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    An STS-based map of the human genome (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: A physical map has been constructed of the human genome containing 15,086 sequence-tagged sites (STSs), with an average spacing of 199 kilobases. The project involved assembly of a radiation hybrid map of the human genome containing 6193 loci and incorporated a genetic linkage map of the human genome containing 5264 loci. This information was combined with the results of STS-content screening of 10,850 loci against a yeast artificial chromosome library to produce an integrated map, anchored by the radiation hybrid and genetic maps. The map provides radiation hybrid coverage of 99 percent and physical coverage of 94 percent of the human genome. The map also represents an early step in an international project to generate a transcript map of the human genome, with more than 3235 expressed sequences localized. The STSs in the map provide a scaffold for initiating large-scale sequencing of the human genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hudson, T J -- Stein, L D -- Gerety, S S -- Ma, J -- Castle, A B -- Silva, J -- Slonim, D K -- Baptista, R -- Kruglyak, L -- Xu, S H -- Hu, X -- Colbert, A M -- Rosenberg, C -- Reeve-Daly, M P -- Rozen, S -- Hui, L -- Wu, X -- Vestergaard, C -- Wilson, K M -- Bae, J S -- Maitra, S -- Ganiatsas, S -- Evans, C A -- DeAngelis, M M -- Ingalls, K A -- Nahf, R W -- Horton, L T Jr -- Anderson, M O -- Collymore, A J -- Ye, W -- Kouyoumjian, V -- Zemsteva, I S -- Tam, J -- Devine, R -- Courtney, D F -- Renaud, M T -- Nguyen, H -- O'Connor, T J -- Fizames, C -- Faure, S -- Gyapay, G -- Dib, C -- Morissette, J -- Orlin, J B -- Birren, B W -- Goodman, N -- Weissenbach, J -- Hawkins, T L -- Foote, S -- Page, D C -- Lander, E S -- HG00017/HG/NHGRI NIH HHS/ -- HG00098/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1945-54.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead-MIT Center for Genome Research, Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533086" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; *Chromosome Mapping ; Chromosomes, Artificial, Yeast ; Databases, Factual ; Gene Expression ; Genetic Markers ; *Genome, Human ; *Human Genome Project ; Humans ; Hybrid Cells ; Polymerase Chain Reaction ; *Sequence Analysis, DNA ; *Sequence Tagged Sites
    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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  • 3
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    A receptor for the malarial parasite Plasmodium vivax: the erythrocyte chemokine receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-27
    Description: Plasmodium vivax and P. falciparum are the major causes of human malaria, except in sub-Saharan Africa where people lack the Duffy blood group antigen, the erythrocyte receptor for P. vivax. Duffy negative human erythrocytes are resistant to invasion by P. vivax and the related monkey malaria, P. knowlesi. Several lines of evidence in the present study indicate that the Duffy blood group antigen is the erythrocyte receptor for the chemokines interleukin-8 (IL-8) and melanoma growth stimulatory activity (MGSA). First, IL-8 binds minimally to Duffy negative erythrocytes. Second, a monoclonal antibody to the Duffy blood group antigen blocked binding of IL-8 and other chemokines to Duffy positive erythrocytes. Third, both MGSA and IL-8 blocked the binding of the parasite ligand and the invasion of human erythrocytes by P. knowlesi, suggesting the possibility of receptor blockade for anti-malarial therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horuk, R -- Chitnis, C E -- Darbonne, W C -- Colby, T J -- Rybicki, A -- Hadley, T J -- Miller, L H -- HL 41382/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1182-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7689250" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Protozoan ; Chemokine CCL5 ; Chemokine CXCL1 ; *Chemokines, CXC ; Chemotactic Factors/metabolism ; Cytokines/metabolism ; *Duffy Blood-Group System ; Erythrocytes/*parasitology ; Growth Substances/metabolism ; Humans ; *Intercellular Signaling Peptides and Proteins ; Interleukin-8/*metabolism ; Lymphokines/metabolism ; Monocyte Chemoattractant Proteins ; Plasmodium knowlesi/*metabolism/physiology ; Plasmodium vivax/*metabolism/physiology ; *Protozoan Proteins ; Receptors, Cell Surface/*metabolism ; Receptors, Immunologic/*metabolism ; Receptors, Interleukin-8A
    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
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    Lateral variations in Compressional/Shear velocities at the base of the mantle (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 5
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    Electrical conductivity of olivine, wadsleyite, and ringwoodite under upper-mantle conditions (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-05
    Description: Geophysical models show that electrical conductivity in Earth's mantle rises about two orders of magnitude through the transition zone in the depth range 410 to 660 kilometers. Impedance measurements obtained on Mg1.8Fe0.2SiO4 olivine, wadsleyite, and ringwoodite at up to 20 gigapascals and 1400 degreesC show that the electrical conductivities of wadsleyite and ringwoodite are similar and are almost two orders of magnitude higher than that of olivine. A conductivity-depth profile to 660 kilometers, based on these laboratory data, shows a conductivity increase of almost two orders of magnitude across the 410-kilometer discontinuity; such a profile favors a two-layer model for the upper mantle. Activation enthalpies of 1.2 to 1.7 electron volts permit appreciable lateral variations of conductivity with lateral temperature variations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu -- Poe -- Shankland -- Rubie -- New York, N.Y. -- Science. 1998 May 29;280(5368):1415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bayerisches Geoinstitut, Universitat Bayreuth, D-95440 Bayreuth, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9603726" target="_blank"〉PubMed〈/a〉
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  • 6
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    Coincident induction of long-term facilitation in Aplysia: cooperativity between cell bodies and remote synapses (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 7
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    Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 8
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    Implication of tubby proteins as transcription factors by structure-based functional analysis (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 9
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    Unraveling the electronic structure of individual photosynthetic pigment-protein complexes (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 10
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    Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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