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  • American Association for the Advancement of Science (AAAS)
  • 2010-2014
  • 2000-2004  (3)
  • 1995-1999  (1)
  • 1960-1964
  • 2002  (3)
  • 1998  (1)
  • 1
    Publication Date: 2002-05-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baird, Andrew H -- Bellwood, David R -- Connell, Joseph H -- Cornell, Howard V -- Hughes, Terry P -- Karlson, Ronald H -- Rosen, Brian R -- New York, N.Y. -- Science. 2002 May 10;296(5570):1026-8; author reply 1026-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004903" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Climate ; *Cnidaria ; *Conservation of Natural Resources ; *Ecosystem ; Nephropidae ; Seawater ; Snails
    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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  • 2
    Publication Date: 1998-03-04
    Description: The heterogeneous replacement of chloride by nitrate in individual sea-salt particles was monitored continuously over time in the troposphere with the use of aerosol time-of-flight mass spectrometry. Modeling calculations show that the observed chloride displacement process is consistent with a heterogeneous chemical reaction between sea-salt particles and gas-phase nitric acid, leading to sodium nitrate production in the particle phase accompanied by liberation of gaseous HCl from the particles. Such single-particle measurements, combined with a single-particle model, make it possible to monitor and explain heterogeneous gas/particle chemistry as it occurs in the atmosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gard -- Kleeman -- Gross -- Hughes -- Allen -- Morrical -- Fergenson -- Dienes -- E Galli M -- Johnson -- Cass -- Prather -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1184-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. E. Gard, D. S. Gross, B. D. Morrical, D. P. Fergenson, T. Dienes, M. E. Galli, K. A. Prather, Department of Chemistry, University of California, Riverside, CA 92521, USA. M. J. Kleeman, L. S. Hughes, J. O. Allen, R. J. Johnson, G. R. Cass, Departme.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469803" 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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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-05-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, Malcolm K -- New York, N.Y. -- Science. 2002 May 3;296(5569):848-9 author reply 848-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11989486" target="_blank"〉PubMed〈/a〉
    Keywords: *Climate ; Temperature ; Time Factors ; Trees/growth & development/*physiology
    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: 2002-04-06
    Description: The essential Cdc13 protein in the yeast Saccharomyces cerevisiae is a single-stranded telomeric DNA binding protein required for chromosome end protection and telomere replication. Here we report the solution structure of the Cdc13 DNA binding domain in complex with telomeric DNA. The structure reveals the use of a single OB (oligonucleotide/oligosaccharide binding) fold augmented by an unusually large loop for DNA recognition. This OB fold is structurally similar to OB folds found in the ciliated protozoan telomere end-binding protein, although no sequence similarity is apparent between them. The common usage of an OB fold for telomeric DNA interaction demonstrates conservation of end-protection mechanisms among eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitton-Fry, Rachel M -- Anderson, Emily M -- Hughes, Timothy R -- Lundblad, Victoria -- Wuttke, Deborah S -- GM55867/GM/NIGMS NIH HHS/ -- GM59414/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):145-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11935027" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; DNA, Fungal/chemistry/*metabolism ; DNA, Single-Stranded/chemistry/*metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Ligands ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/*chemistry/metabolism ; Telomere/*metabolism ; *Telomere-Binding Proteins
    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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