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  • American Association for the Advancement of Science (AAAS)  (3)
  • Blackwell Publishing Ltd  (3)
  • 2010-2014
  • 2000-2004  (6)
  • 1995-1999
  • 1960-1964
  • 2002  (6)
Collection
Keywords
Publisher
Years
  • 2010-2014
  • 2000-2004  (6)
  • 1995-1999
  • 1960-1964
Year
  • 1
    Electronic Resource
    Electronic Resource
    Adaptive search in juvenile plaice foraging for aggregated and dispersed prey (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 61 (2002), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Juvenile plaice Pleuronectes platessa in a laboratory arena used intensive search behaviour, characterized by short movements and frequent turning, in the five movements before and after attacking a prey in an aggregated distribution. They used extensive search behaviour with, on average, longer movements and less turning at all other times. Intensive search was, apparently, triggered by a high local density of prey but not by isolated prey. This response to local prey density resulted in area-restricted search when prey were aggregated and win-shift behaviour when prey were dispersed. There was no evidence that the use of intensive search increased with experience of aggregated prey. It therefore appears that the fish were able to exploit encountered prey distribution patterns using their immediate perceptions rather than prior experience.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.2002.tb02469.x
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Artificial dietary regime may impair subsequent foraging behaviour of hatchery-reared turbot released into the natural environment (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 61 (2002), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: When offered a size range of shrimp Crangon crangon, fewer naïve reared turbot Scophthalmus maximus fed than did wild fish, and those that fed took smaller prey. Analysis of feeding behaviour indicated differences between wild and naïve reared fish in the motivation to feed on novel prey and in prey recognition and capture efficiency. Feeding efficiency and motivation increased with experience and reared fish achieved the feeding rate of wild fish within the 9 days of the experiment. The ‘creep’ style of approach to shrimp was innate to naïve reared turbot. A comparative feeding experiment confirmed that experienced reared fish ate more prey than naïve reared fish. Naïve reared turbot selected pellets and attacked stones preferentially to shrimp, in contrast to wild and experienced reared fish, which selected shrimp. Stones were attacked due to the memory of pellet-like visual characteristics and this behaviour persisted in some reared fish for at least 6 weeks, illustrating a cost of memory in which changing environmental conditions cause previously learnt information to become misleading. The experimental data also demonstrated that differences may arise in the prey and feeding behaviour of wild and naïve reared fish, but that such differences diminish with experience.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.2002.tb01750.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Nitric oxide releases intracellular zinc from prokaryotic metallothionein in Escherichia coli (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 213 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Nitric oxide (NO) has a broad spectrum of signalling and regulatory functions and multiple molecular targets. Recently, the intrabacterial toxicity of NO and mechanisms for NO resistance have been intensively investigated. Here we report for the first time that NO elicits release of zinc from a bacterial protein. Using the zinc-responsive expression of zntA (encoding a Zn-exporting P-type ATPase) fused to lacZ, i.e. Φ(zntA-lacZ), to monitor intracellular zinc, and SmtA (the Synechococcus metallothionein) as zinc store, we have shown that the NO donors NOC-5 and NOC-7 elicit zinc ejection. No increase in Φ(zntA-lacZ) activity was observed in a zntR mutant, indicating the specificity of the zntA promoter response to zinc ions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11295.x
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  • 4
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    Coral reef biodiversity and conservation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Tree-ring chronologies and climate variability (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Conserved structure for single-stranded telomeric DNA recognition (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Published by American Association for the Advancement of Science (AAAS)
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