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  • Artikel  (251)
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  • 1
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    Parasitology. Close encounters: good, bad, and ugly (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-02-24
    Beschreibung: Microbiologists often focus on one organism and its relationship to its host at one point in time. But viewed in light of evolution, host-parasite relationships range from deadly to helpful, depending on the communication between them. At a meeting here last month of virologists, bacteriologists, parasitologists, and molecular biologists--each dealing with different microorganisms in distinct ways--researchers lamented that evolution is often considered outside the bailiwick of microbiologists, particularly those studying infectious diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1491-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11185502" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Bacteria/genetics/*pathogenicity ; Bacterial Infections/microbiology ; *Bacterial Physiological Phenomena ; *Biological Evolution ; Escherichia coli/genetics/pathogenicity/physiology ; *Host-Parasite Interactions ; Humans ; Leishmania/pathogenicity/*physiology ; Leishmaniasis/parasitology ; Mutation ; Rhizobium/physiology ; *Symbiosis ; Virulence
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    Development. Survival is impossible without an editor (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-02-24
    Beschreibung: RNA editing is a fascinating phenomenon that is found in both animal and plant cells. By converting an adenosine base to an inosine (which behaves like guanosine) in RNA that has already been transcribed, certain RNA sequences (and hence the amino acids they encode) are altered. In a Perspective, Keegan, Gallo and O'Connell explore new results showing that activity of the editing enzyme ADAR1 is crucial for normal development of red blood cells in mouse embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keegan, L P -- Gallo, A -- O'Connell, M A -- New York, N.Y. -- Science. 2000 Dec 1;290(5497):1707-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, UK. liam.keegan@hgu.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11186391" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine/metabolism ; Adenosine Deaminase/chemistry/*genetics/*metabolism ; Animals ; Base Pairing ; Central Nervous System/metabolism ; Chimera ; Drosophila/genetics/metabolism ; Embryo, Mammalian/cytology ; Embryo, Nonmammalian ; *Erythropoiesis ; Gene Dosage ; Hematopoietic Stem Cells/cytology/enzymology ; Inosine/metabolism ; Liver/metabolism ; Mice ; Mutation ; Phenotype ; Protein Structure, Tertiary ; *RNA Editing ; RNA Precursors/metabolism ; RNA, Double-Stranded/metabolism ; RNA-Binding Proteins ; Receptors, AMPA/genetics ; Stem Cells/cytology/enzymology ; Teratoma/genetics/pathology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
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    Signal transduction. Are there close encounters between signaling pathways? (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-02-24
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noselli, S -- Perrimon, N -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):68-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Recherches, UMR 65643-CNRS, Parc Valrose 06108, Nice cedex 2 France. noselli@unice.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11183153" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Drosophila/genetics/metabolism ; Gene Expression Profiling ; Humans ; Mutation ; Neoplasms/genetics/metabolism ; Phenotype ; *Receptor Cross-Talk ; *Signal Transduction
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 4
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    Translational roots for mental retardation? (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-02-24
    Beschreibung: A flurry of findings points to protein translation in the dendrites of neurons as a key feature leading to the changes at synapses that are vital to learning (see main text). And one recent discovery suggests that when this translation goes awry, it can lead to mental retardation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Oct 27;290(5492):737.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11184206" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Dendrites/*metabolism ; Fragile X Mental Retardation Protein ; Fragile X Syndrome/etiology/genetics/metabolism ; Humans ; Intellectual Disability/*etiology/genetics/metabolism ; Mice ; Mutation ; Nerve Tissue Proteins/*genetics/metabolism ; *Protein Biosynthesis ; *RNA-Binding Proteins ; Synapses/*physiology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 5
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    Unfolding pathways of individual bacteriorhodopsins (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-02-07
    Beschreibung: Atomic force microscopy and single-molecule force spectroscopy were combined to image and manipulate purple membrane patches from Halobacterium salinarum. Individual bacteriorhodopsin molecules were first localized and then extracted from the membrane; the remaining vacancies were imaged again. Anchoring forces between 100 and 200 piconewtons for the different helices were found. Upon extraction, the helices were found to unfold. The force spectra revealed the individuality of the unfolding pathways. Helices G and F as well as helices E and D always unfolded pairwise, whereas helices B and C occasionally unfolded one after the other. Experiments with cleaved loops revealed the origin of the individuality: stabilization of helix B by neighboring helices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oesterhelt, F -- Oesterhelt, D -- Pfeiffer, M -- Engel, A -- Gaub, H E -- Muller, D J -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):143-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CeNS and Lehrstuhl fur angewandte Physik, Ludwig Maximilians-Universitat Munchen, Amalienstrasse 54, 80799 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10753119" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Bacteriorhodopsins/*chemistry/genetics ; Cysteine/chemistry ; Halobacterium salinarum/*chemistry ; Membrane Proteins/*chemistry/genetics ; *Microscopy, Atomic Force ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Protein Structure, Secondary ; Purple Membrane/*chemistry ; Serine Endopeptidases/metabolism ; Spectrum Analysis
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 6
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    Circadian rhythms. A time to rest: clock signal identified (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-12-26
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2453.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752547" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Biological Clocks/physiology ; Circadian Rhythm/drug effects/*physiology ; Cricetinae ; Darkness ; Hypothalamus/*metabolism ; Light ; Mice ; *Motor Activity/drug effects ; Mutation ; Neurons/*metabolism ; Receptor, Epidermal Growth Factor/genetics/*metabolism ; Retinal Ganglion Cells/metabolism ; Signal Transduction ; Suprachiasmatic Nucleus/*metabolism ; Transforming Growth Factor alpha/*metabolism/pharmacology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 7
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    Active disruption of an RNA-protein interaction by a DExH/D RNA helicase (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-01-06
    Beschreibung: All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate-dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jankowsky, E -- Gross, C H -- Shuman, S -- Pyle, A M -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11141562" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 3' Untranslated Regions/metabolism ; Acid Anhydride Hydrolases/chemistry/*metabolism ; Adenosine Triphosphate/metabolism ; Base Sequence ; Binding Sites ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleoside-Triphosphatase ; Protein Binding ; Protein Conformation ; RNA/chemistry/*metabolism ; RNA Helicases/chemistry/*metabolism ; *RNA-Binding Proteins ; Ribonucleoprotein, U1 Small Nuclear/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 8
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    Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-04-21
    Beschreibung: Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cramer, P -- Bushnell, D A -- Kornberg, R D -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 8;292(5523):1863-76. Epub 2001 Apr 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11313498" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; DNA, Fungal/chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Magnesium/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; RNA Polymerase II/*chemistry/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Fungal/biosynthesis/chemistry/metabolism ; RNA, Messenger/biosynthesis/chemistry/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; Transcription Factors/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 9
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    SNARE function analyzed in synaptobrevin/VAMP knockout mice (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-11-03
    Beschreibung: SNAREs (soluble NSF-attachment protein receptors) are generally acknowledged as central components of membrane fusion reactions, but their precise function has remained enigmatic. Competing hypotheses suggest roles for SNAREs in mediating the specificity of fusion, catalyzing fusion, or actually executing fusion. We generated knockout mice lacking synaptobrevin/VAMP 2, the vesicular SNARE protein responsible for synaptic vesicle fusion in forebrain synapses, to make use of the exquisite temporal resolution of electrophysiology in measuring fusion. In the absence of synaptobrevin 2, spontaneous synaptic vesicle fusion and fusion induced by hypertonic sucrose were decreased approximately 10-fold, but fast Ca2+-triggered fusion was decreased more than 100-fold. Thus, synaptobrevin 2 may function in catalyzing fusion reactions and stabilizing fusion intermediates but is not absolutely required for synaptic fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schoch, S -- Deak, F -- Konigstorfer, A -- Mozhayeva, M -- Sara, Y -- Sudhof, T C -- Kavalali, E T -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1117-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Basic Neuroscience, Department of Molecular Genetics, Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, TX 75390-9111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691998" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Action Potentials ; Animals ; Calcium/metabolism/pharmacology ; Cells, Cultured ; Hypertonic Solutions ; *Membrane Fusion ; Membrane Proteins/genetics/*physiology ; Mice ; Mice, Knockout ; Mutation ; Patch-Clamp Techniques ; Potassium/pharmacology ; Presynaptic Terminals/physiology ; Prosencephalon/physiology ; R-SNARE Proteins ; SNARE Proteins ; Sucrose/pharmacology ; Synapses/*physiology ; Synaptic Transmission ; Synaptic Vesicles/*physiology ; *Vesicular Transport Proteins
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 10
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    Translating the histone code (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2001-08-11
    Beschreibung: Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or antagonistic interaction affinities for chromatin-associated proteins, which in turn dictate dynamic transitions between transcriptionally active or transcriptionally silent chromatin states. The combinatorial nature of histone amino-terminal modifications thus reveals a "histone code" that considerably extends the information potential of the genetic code. We propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenuwein, T -- Allis, C D -- GM53512/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1074-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology (IMP) at the Vienna Biocenter, Dr. Bohrgasse 7, A-1030 Vienna, Austria. jenuwein@nt.imp.univie.ac.at〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11498575" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acetylation ; Amino Acid Sequence ; Animals ; Chromatin/chemistry/metabolism/ultrastructure ; *Gene Expression Regulation ; *Gene Silencing ; Genomic Imprinting ; Histones/chemistry/genetics/*metabolism ; Methylation ; Molecular Sequence Data ; Phosphorylation ; Protein Structure, Tertiary ; Transcription, Genetic ; Transcriptional Activation
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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