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  • Animals  (3)
  • *Protein Interaction Mapping  (1)
  • American Association for the Advancement of Science (AAAS)  (4)
  • 2000-2004  (3)
  • 1995-1999  (1)
  • 2004  (3)
  • 1995  (1)
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  • American Association for the Advancement of Science (AAAS)  (4)
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  • 2000-2004  (3)
  • 1995-1999  (1)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2004-06-12
    Beschreibung: During speech acquisition, children form quick and rough hypotheses about the meaning of a new word after only a single exposure-a process dubbed "fast mapping." Here we provide evidence that a border collie, Rico, is able to fast map. Rico knew the labels of over 200 different items. He inferred the names of novel items by exclusion learning and correctly retrieved those items right away as well as 4 weeks after the initial exposure. Fast mapping thus appears to be mediated by general learning and memory mechanisms also found in other animals and not by a language acquisition device that is special to humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaminski, Juliane -- Call, Josep -- Fischer, Julia -- New York, N.Y. -- Science. 2004 Jun 11;304(5677):1682-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental and Comparative Psychology, Max-Planck Institute for Evolutionary Anthropology, Deutscher Platz 6, 04103 Leipzig, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15192233" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Dogs ; *Learning ; Male ; *Memory ; Random Allocation ; *Vocabulary
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Publikationsdatum: 2004-03-27
    Beschreibung: Images of entire cells are preceding atomic structures of the separate molecular machines that they contain. The resulting gap in knowledge can be partly bridged by protein-protein interactions, bioinformatics, and electron microscopy. Here we use interactions of known three-dimensional structure to model a large set of yeast complexes, which we also screen by electron microscopy. For 54 of 102 complexes, we obtain at least partial models of interacting subunits. For 29, including the exosome, the chaperonin containing TCP-1, a 3'-messenger RNA degradation complex, and RNA polymerase II, the process suggests atomic details not easily seen by homology, involving the combination of two or more known structures. We also consider interactions between complexes (cross-talk) and use these to construct a structure-based network of molecular machines in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aloy, Patrick -- Bottcher, Bettina -- Ceulemans, Hugo -- Leutwein, Christina -- Mellwig, Christian -- Fischer, Susanne -- Gavin, Anne-Claude -- Bork, Peer -- Superti-Furga, Giulio -- Serrano, Luis -- Russell, Robert B -- New York, N.Y. -- Science. 2004 Mar 26;303(5666):2026-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Structural and Computational Biology Programme, 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15044803" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Chaperonins/chemistry/metabolism ; Computational Biology ; Image Processing, Computer-Assisted ; Microscopy, Electron ; Models, Biological ; Models, Molecular ; Nuclear Proteins/chemistry/metabolism ; Protein Binding ; Protein Conformation ; *Protein Interaction Mapping ; Protein Structure, Tertiary ; RNA Polymerase II/chemistry/metabolism ; Ribonuclease P/chemistry/metabolism ; Saccharomyces cerevisiae/chemistry/*metabolism/ultrastructure ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Transcription Factors/chemistry/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Publikationsdatum: 2004-03-27
    Beschreibung: In the nervous system of vertebrates, myelination is essential for rapid and accurate impulse conduction. Myelin thickness depends on axon fiber size. We use mutant and transgenic mouse lines to show that axonal Neuregulin-1 (Nrg1) signals information about axon size to Schwann cells. Reduced Nrg1 expression causes hypomyelination and reduced nerve conduction velocity. Neuronal overexpression of Nrg1 induces hypermyelination and demonstrates that Nrg1 type III is the responsible isoform. We suggest a model by which myelin-forming Schwann cells integrate axonal Nrg1 signals as a biochemical measure of axon size.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Michailov, Galin V -- Sereda, Michael W -- Brinkmann, Bastian G -- Fischer, Tobias M -- Haug, Bernhard -- Birchmeier, Carmen -- Role, Lorna -- Lai, Cary -- Schwab, Markus H -- Nave, Klaus-Armin -- New York, N.Y. -- Science. 2004 Apr 30;304(5671):700-3. Epub 2004 Mar 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurogenetics, Max Planck Institute of Experimental Medicine, 37075 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15044753" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Axons/*physiology/*ultrastructure ; Ganglia, Spinal/chemistry ; Gene Targeting ; Genes, erbB ; Genes, erbB-2 ; Heterozygote ; Mice ; Mice, Knockout ; Mice, Transgenic ; Models, Neurological ; Myelin Sheath/*physiology/*ultrastructure ; Neural Conduction ; Neuregulin-1/genetics/*physiology ; Protein Isoforms/physiology ; Receptor, Epidermal Growth Factor/analysis/physiology ; Receptor, ErbB-2/analysis/physiology ; Receptor, ErbB-3/analysis/physiology ; Schwann Cells/physiology ; Sciatic Nerve/chemistry ; Signal Transduction
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
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    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1995-12-15
    Beschreibung: Ubiquitin is a highly conserved polypeptide found in all eukaryotes. The major function of ubiquitin is to target proteins for complete or partial degradation by a multisubunit protein complex called the proteasome. Here, the Drosophila fat facets gene, which is required for the appropriate determination of particular cells in the fly eye, was shown to encode a ubiquitin-specific protease (Ubp), an enzyme that cleaves ubiquitin from ubiquitin-protein conjugates. The Fat facets protein (FAF) acts as a regulatory Ubp that prevents degradation of its substrate by the proteasome. Flies bearing fat facets gene mutations were used to show that a Ubp is cell type--and substrate-specific and a regulator of cell fate decisions in a multicellular organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Y -- Baker, R T -- Fischer-Vize, J A -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1828-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525378" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; *Cell Differentiation/genetics ; Cysteine/metabolism ; Drosophila/embryology/enzymology/genetics ; Endopeptidases/genetics/*metabolism ; Escherichia coli ; Eye/embryology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Recombinant Fusion Proteins/genetics/metabolism ; Ubiquitins/*metabolism ; beta-Galactosidase/genetics
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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