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  • Articles  (880)
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  • 1
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    Crystal structure of the long-chain fatty acid transporter FadL (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-05
    Description: The mechanisms by which hydrophobic molecules, such as long-chain fatty acids, enter cells are poorly understood. In Gram-negative bacteria, the lipopolysaccharide layer in the outer membrane is an efficient barrier for fatty acids and aromatic hydrocarbons destined for biodegradation. We report crystal structures of the long-chain fatty acid transporter FadL from Escherichia coli at 2.6 and 2.8 angstrom resolution. FadL forms a 14-stranded beta barrel that is occluded by a central hatch domain. The structures suggest that hydrophobic compounds bind to multiple sites in FadL and use a transport mechanism that involves spontaneous conformational changes in the hatch.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van den Berg, Bert -- Black, Paul N -- Clemons, William M Jr -- Rapoport, Tom A -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1506-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. lvandenberg@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178802" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/metabolism ; Binding Sites ; Biological Transport ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/metabolism ; Fatty Acid Transport Proteins ; Fatty Acids/*metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
    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
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    Separate neural systems value immediate and delayed monetary rewards (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-16
    Description: When humans are offered the choice between rewards available at different points in time, the relative values of the options are discounted according to their expected delays until delivery. Using functional magnetic resonance imaging, we examined the neural correlates of time discounting while subjects made a series of choices between monetary reward options that varied by delay to delivery. We demonstrate that two separate systems are involved in such decisions. Parts of the limbic system associated with the midbrain dopamine system, including paralimbic cortex, are preferentially activated by decisions involving immediately available rewards. In contrast, regions of the lateral prefrontal cortex and posterior parietal cortex are engaged uniformly by intertemporal choices irrespective of delay. Furthermore, the relative engagement of the two systems is directly associated with subjects' choices, with greater relative fronto-parietal activity when subjects choose longer term options.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McClure, Samuel M -- Laibson, David I -- Loewenstein, George -- Cohen, Jonathan D -- AG05842/AG/NIA NIH HHS/ -- MH065214/MH/NIMH NIH HHS/ -- MH132804/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 15;306(5695):503-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology and Center for the Study of Brain, Mind, and Behavior, Princeton University, Princeton, NJ 08544, USA. smcclure@princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486304" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Basal Ganglia/physiology ; Brain Mapping ; *Decision Making ; Dopamine/physiology ; Female ; Frontal Lobe/physiology ; Humans ; Limbic System/*physiology ; Magnetic Resonance Imaging ; Male ; Parietal Lobe/*physiology ; Prefrontal Cortex/*physiology ; *Reward ; Time Factors
    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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    The structure and receptor binding properties of the 1918 influenza hemagglutinin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: The 1918 influenza pandemic resulted in about 20 million deaths. This enormous impact, coupled with renewed interest in emerging infections, makes characterization of the virus involved a priority. Receptor binding, the initial event in virus infection, is a major determinant of virus transmissibility that, for influenza viruses, is mediated by the hemagglutinin (HA) membrane glycoprotein. We have determined the crystal structures of the HA from the 1918 virus and two closely related HAs in complex with receptor analogs. They explain how the 1918 HA, while retaining receptor binding site amino acids characteristic of an avian precursor HA, is able to bind human receptors and how, as a consequence, the virus was able to spread in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamblin, S J -- Haire, L F -- Russell, R J -- Stevens, D J -- Xiao, B -- Ha, Y -- Vasisht, N -- Steinhauer, D A -- Daniels, R S -- Elliot, A -- Wiley, D C -- Skehel, J J -- AI-13654/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1838-42. Epub 2004 Feb 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764886" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Birds ; Crystallography, X-Ray ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/*metabolism ; History, 20th Century ; Humans ; Hydrogen Bonding ; Influenza A virus/*immunology/metabolism/pathogenicity ; Influenza, Human/epidemiology/history/*virology ; Membrane Glycoproteins/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*metabolism ; Sequence Alignment ; Sialic Acids/metabolism ; Species Specificity ; Swine
    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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    Very low gene duplication rate in the yeast genome (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: The gene duplication rate in the yeast genome is estimated without assuming the molecular clock model to be approximately 0.01 to 0.06 per gene per billion years; this rate is two orders of magnitude lower than a previous estimate based on the molecular clock model. This difference is explained by extensive concerted evolution via gene conversion between duplicated genes, which violates the assumption of the molecular clock in the analyses of duplicated genes. The average length of the period of concerted evolution and the gene conversion rate are estimated to be approximately 25 million years and approximately 28 times the mutation rate, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Li-Zhi -- Innan, Hideki -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genetics Center, School of Public Health, University of Texas Health Science Center, 1200 Hermann Pressler, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550669" target="_blank"〉PubMed〈/a〉
    Keywords: Evolution, Molecular ; Gene Conversion ; *Gene Duplication ; *Genes, Duplicate ; *Genes, Fungal ; Models, Genetic ; Probability ; Saccharomyces/*genetics ; Saccharomyces cerevisiae/*genetics ; Time Factors
    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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  • 5
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    Mutations in a human ROBO gene disrupt hindbrain axon pathway crossing and morphogenesis (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-24
    Description: The mechanisms controlling axon guidance are of fundamental importance in understanding brain development. Growing corticospinal and somatosensory axons cross the midline in the medulla to reach their targets and thus form the basis of contralateral motor control and sensory input. The motor and sensory projections appeared uncrossed in patients with horizontal gaze palsy with progressive scoliosis (HGPPS). In patients affected with HGPPS, we identified mutations in the ROBO3 gene, which shares homology with roundabout genes important in axon guidance in developing Drosophila, zebrafish, and mouse. Like its murine homolog Rig1/Robo3, but unlike other Robo proteins, ROBO3 is required for hindbrain axon midline crossing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618874/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618874/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jen, Joanna C -- Chan, Wai-Man -- Bosley, Thomas M -- Wan, Jijun -- Carr, Janai R -- Rub, Udo -- Shattuck, David -- Salamon, Georges -- Kudo, Lili C -- Ou, Jing -- Lin, Doris D M -- Salih, Mustafa A M -- Kansu, Tulay -- Al Dhalaan, Hesham -- Al Zayed, Zayed -- MacDonald, David B -- Stigsby, Bent -- Plaitakis, Andreas -- Dretakis, Emmanuel K -- Gottlob, Irene -- Pieh, Christina -- Traboulsi, Elias I -- Wang, Qing -- Wang, Lejin -- Andrews, Caroline -- Yamada, Koki -- Demer, Joseph L -- Karim, Shaheen -- Alger, Jeffry R -- Geschwind, Daniel H -- Deller, Thomas -- Sicotte, Nancy L -- Nelson, Stanley F -- Baloh, Robert W -- Engle, Elizabeth C -- DC00162/DC/NIDCD NIH HHS/ -- DC05524/DC/NIDCD NIH HHS/ -- EY12498/EY/NEI NIH HHS/ -- EY13583/EY/NEI NIH HHS/ -- EY15298/EY/NEI NIH HHS/ -- EY15311/EY/NEI NIH HHS/ -- MH60233/MH/NIMH NIH HHS/ -- P30 HD 18655/HD/NICHD NIH HHS/ -- R01 EY008313/EY/NEI NIH HHS/ -- R01 EY008313-14/EY/NEI NIH HHS/ -- R01 HL066251/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1509-13. Epub 2004 Apr 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of California, Los Angeles, CA 90095, USA. jjen@ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15105459" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Alternative Splicing ; Amino Acid Motifs ; Amino Acid Sequence ; Axons/*physiology ; Evoked Potentials, Motor ; Evoked Potentials, Somatosensory ; Female ; Functional Laterality ; Genetic Linkage ; Humans ; In Situ Hybridization ; Magnetic Resonance Imaging ; Male ; Medulla Oblongata/growth & development/pathology ; Microsatellite Repeats ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Neural Pathways ; Ophthalmoplegia/*genetics/pathology/physiopathology ; Pedigree ; Protein Structure, Tertiary ; Receptors, Immunologic/chemistry/*genetics/*metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Rhombencephalon/*growth & development/pathology ; Scoliosis/*genetics/pathology/physiopathology ; Sequence Analysis, DNA ; Syndrome
    Print ISSN: 0036-8075
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  • 6
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    Biomedicine. An end to the prion debate? Don't count on it (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2004 Jul 30;305(5684):589.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15286333" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/chemistry/metabolism ; Animals ; Brain Chemistry ; Escherichia coli/genetics/metabolism ; Mice ; Mice, Transgenic ; Prion Diseases/*etiology ; Prions/administration & dosage/biosynthesis/chemistry/*pathogenicity ; Protein Folding ; Recombinant Proteins/administration & dosage/chemistry ; Time Factors
    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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  • 7
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    A link between mRNA turnover and RNA interference in Arabidopsis (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-06
    Description: In RNA interference (RNAi), double-stranded RNA (dsRNA) triggers degradation of homologous messenger RNA. In many organisms, RNA-dependent RNA polymerase (RdRp) is required to initiate or amplify RNAi, but the substrate for dsRNA synthesis in vivo is not known. Here, we show that RdRp-dependent transgene silencing in Arabidopsis was caused by mutation of XRN4, which is a ribonuclease (RNase) implicated in mRNA turnover by means of decapping and 5'-3' exonucleolysis. When both XRN4 and the RdRp were mutated, the plants accumulated decapped transgene mRNA. We propose that mRNAs lacking a cap structure become exposed to RdRp to initiate or maintain RNAi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gazzani, S -- Lawrenson, T -- Woodward, C -- Headon, D -- Sablowski, R -- BBS/E/J/00000594/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2004 Nov 5;306(5698):1046-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528448" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arabidopsis/*genetics ; Arabidopsis Proteins/genetics ; Exoribonucleases/genetics ; Gene Silencing ; Homeodomain Proteins/genetics ; Mutation ; Plant Proteins/genetics ; Plants, Genetically Modified ; RNA Caps ; *RNA Interference ; RNA Replicase/metabolism ; RNA, Messenger/*metabolism ; RNA, Plant/*metabolism ; Rats ; Recombinant Fusion Proteins/genetics
    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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  • 8
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    Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: The protein-remodeling factor Hsp104 governs inheritance of [PSI+], a yeast prion formed by self-perpetuating amyloid conformers of the translation termination factor Sup35. Perplexingly, either excess or insufficient Hsp104 eliminates [PSI+]. In vitro, at low concentrations, Hsp104 catalyzed the formation of oligomeric intermediates that proved critical for the nucleation of Sup 35 fibrillization de novo and displayed a conformation common among amyloidogenic polypeptides. At higher Hsp104 concentrations, amyloidogenic oligomerization and contingent fibrillization were abolished. Hsp104 also disassembled mature fibers in a manner that initially exposed new surfaces for conformational replication but eventually exterminated prion conformers. These Hsp104 activities differed in their reaction mechanism and can explain [PSI+] inheritance patterns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shorter, James -- Lindquist, Susan -- GM25874/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 18;304(5678):1793-7. Epub 2004 May 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155912" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Amyloid/chemistry ; Amyloid beta-Peptides/chemistry/immunology ; Antibodies/immunology ; Biopolymers ; Catalysis ; Heat-Shock Proteins/chemistry/genetics/*metabolism ; Hydrolysis ; Mutation ; Peptide Fragments/chemistry/immunology ; Peptide Termination Factors ; Prions/*chemistry/*metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Biochemistry. How active sites communicate in thiamine enzymes (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jordan, Frank -- GM-50380/GM/NIGMS NIH HHS/ -- GM-62330/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):818-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Rutgers University, Newark, NJ 07102, USA. frjordan@newark.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Binding Sites ; Dihydrolipoyllysine-Residue Acetyltransferase ; Dimerization ; Geobacillus stearothermophilus/*enzymology ; Glutamic Acid/chemistry ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Kinetics ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits ; Protons ; Pyruvate Dehydrogenase (Lipoamide)/*chemistry/*metabolism ; Pyruvate Dehydrogenase Complex/*chemistry/*metabolism ; Thiamine Pyrophosphate/chemistry/*metabolism
    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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  • 10
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    Protein kinase C overactivity impairs prefrontal cortical regulation of working memory (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: The prefrontal cortex is a higher brain region that regulates thought, behavior, and emotion using representational knowledge, operations often referred to as working memory. We tested the influence of protein kinase C (PKC) intracellular signaling on prefrontal cortical cognitive function and showed that high levels of PKC activity in prefrontal cortex, as seen for example during stress exposure, markedly impair behavioral and electrophysiological measures of working memory. These data suggest that excessive PKC activation can disrupt prefrontal cortical regulation of behavior and thought, possibly contributing to signs of prefrontal cortical dysfunction such as distractibility, impaired judgment, impulsivity, and thought disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birnbaum, S G -- Yuan, P X -- Wang, M -- Vijayraghavan, S -- Bloom, A K -- Davis, D J -- Gobeske, K T -- Sweatt, J D -- Manji, H K -- Arnsten, A F T -- AG06036/AG/NIA NIH HHS/ -- P50 MH068789/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):882-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Yale Medical School, 333 Cedar Street, New Haven, CT 06520-8001, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514161" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic alpha-Agonists/pharmacology ; Alkaloids ; Animals ; Benzophenanthridines ; Carbolines/pharmacology ; Electrophysiology ; Enzyme Activation ; Female ; Imidazoles/pharmacology ; Lithium Carbonate/pharmacology ; Macaca mulatta ; Male ; Memory/drug effects/*physiology ; Neurons/drug effects/physiology ; Phenanthridines/pharmacology ; Prefrontal Cortex/enzymology/*physiology ; Protein Kinase C/antagonists & inhibitors/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Adrenergic, alpha-1/physiology ; Signal Transduction ; Stress, Physiological/physiopathology ; Tetradecanoylphorbol Acetate/pharmacology ; Valproic Acid/pharmacology
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  • 11
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    Synaptic changes in layer 2/3 underlying map plasticity of developing barrel cortex (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-05-01
    Description: The functional and anatomical rearrangements of cortical sensory maps accompanying changes in experience are not well understood. We examined in vivo and in vitro how the sensory map and underlying synaptic connectivity of the developing rat barrel cortex are altered when the sensory input to the cortex is partially deprived. In the nondeprived cortex, both the sensory responses and synaptic connectivity between columns were strengthened through an increase in the synaptic connection probability between L2/3 pyramids in adjacent columns. This was accompanied by a selective growth of L2/3pyramid axonal arbors between spared columns. In contrast, deprived and nondeprived cortical columns became weakly connected in their L2/3 pyramid connections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petersen, Carl C H -- Brecht, Michael -- Hahn, Thomas T G -- Sakmann, Bert -- New York, N.Y. -- Science. 2004 Apr 30;304(5671):739-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Physiology, Max-Planck-Institute for Medical Research, Jahnstrasse 29, Heidelberg D-69120, Germany. carl.petersen@epfl.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15118164" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Electric Stimulation ; Excitatory Postsynaptic Potentials ; Image Processing, Computer-Assisted ; In Vitro Techniques ; Nerve Net/physiology ; *Neuronal Plasticity ; Patch-Clamp Techniques ; Pyramidal Cells/*physiology/ultrastructure ; Rats ; Rats, Wistar ; Somatosensory Cortex/cytology/growth & development/*physiology ; Synapses/*physiology ; Synaptic Transmission ; Vibrissae/*physiology
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  • 12
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    Lowland forest loss in protected areas of Indonesian Borneo (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-14
    Description: The ecology of Bornean rainforests is driven by El Nino-induced droughts that trigger synchronous fruiting among trees and bursts of faunal reproduction that sustain vertebrate populations. However, many of these species- and carbon-rich ecosystems have been destroyed by logging and conversion, which increasingly threaten protected areas. Our satellite, Geographic Information System, and field-based analyses show that from 1985 to 2001, Kalimantan's protected lowland forests declined by more than 56% (〉29,000 square kilometers). Even uninhabited frontier parks are logged to supply international markets. "Protected" forests have become increasingly isolated and deforested and their buffer zones degraded. Preserving the ecological integrity of Kalimantan's rainforests requires immediate transnational management.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Curran, L M -- Trigg, S N -- McDonald, A K -- Astiani, D -- Hardiono, Y M -- Siregar, P -- Caniago, I -- Kasischke, E -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):1000-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale School of Forestry and Environmental Studies, 205 Prospect Street, New Haven, CT 06511, USA. lisa.curran@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963327" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Borneo ; *Conservation of Natural Resources ; *Ecosystem ; Forestry ; Industry ; Population Density ; Time Factors ; *Trees/growth & development ; Tropical Climate ; Vertebrates ; Wood
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  • 13
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    Reflectins: the unusual proteins of squid reflective tissues (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-13
    Description: A family of unusual proteins is deposited in flat, structural platelets in reflective tissues of the squid Euprymna scolopes. These proteins, which we have named reflectins, are encoded by at least six genes in three subfamilies and have no reported homologs outside of squids. Reflectins possess five repeating domains, which are highly conserved among members of the family. The proteins have a very unusual composition, with four relatively rare residues (tyrosine, methionine, arginine, and tryptophan) comprising approximately 57% of a reflectin, and several common residues (alanine, isoleucine, leucine, and lysine) occurring in none of the family members. These protein-based reflectors in squids provide a marked example of nanofabrication in animal systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crookes, Wendy J -- Ding, Lin-Lin -- Huang, Qing Ling -- Kimbell, Jennifer R -- Horwitz, Joseph -- McFall-Ngai, Margaret J -- NEI R01 EY3897/EY/NEI NIH HHS/ -- R01 A150661/PHS HHS/ -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):235-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kewalo Marine Laboratory, Pacific Biomedical Research Center, University of Hawaii-Manoa, 41 Ahui Street, Honolulu, HI 96813, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716016" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; DNA, Complementary ; Decapodiformes/anatomy & histology/*chemistry/genetics ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Immunohistochemistry ; *Light ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Proteins/*analysis/*chemistry/genetics/isolation & purification ; Sequence Alignment ; Solubility
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Society for Neuroscience meeting. Brain cells may pay the price for a bad night's sleep (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2004 Nov 12;306(5699):1126.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539581" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Death ; *Cell Hypoxia ; Cyclic AMP Response Element-Binding Protein/metabolism ; *Diet ; Dietary Carbohydrates/administration & dosage ; Dietary Fats/administration & dosage ; Exercise ; Hippocampus/*cytology/physiology ; Humans ; *Learning ; Long-Term Potentiation ; Memory ; Neurons/*physiology ; Rats ; Sleep Apnea Syndromes/*physiopathology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    2004 Nobel Prizes. Axel, Buck share award for deciphering how the nose knows (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):207.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472044" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; History, 20th Century ; History, 21st Century ; Humans ; *Nobel Prize ; Olfactory Receptor Neurons/physiology ; Rats ; *Receptors, Odorant/genetics/physiology ; Smell/*physiology ; United States
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    Cellular distribution of nonionic micelles (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moghimi, S M -- Hunter, A C -- Murray, J C -- Szewczyk, A -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):626-8; author reply 626-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752144" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Azides/*chemistry ; Cations ; Drug Carriers/*metabolism ; Endocytosis ; Ethylene Oxide/chemistry/metabolism ; Hydrogen-Ion Concentration ; Lactones/chemistry/metabolism ; Lysosomes/metabolism ; *Micelles ; Nanotechnology ; Organelles/*metabolism ; PC12 Cells ; Polymers ; Rats ; Rhodamines/*chemistry ; Solubility ; Surface-Active Agents
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  • 17
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    Derivatives of erythropoietin that are tissue protective but not erythropoietic (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-13
    Description: Erythropoietin (EPO) is both hematopoietic and tissue protective, putatively through interaction with different receptors. We generated receptor subtype-selective ligands allowing the separation of EPO's bioactivities at the cellular level and in animals. Carbamylated EPO (CEPO) or certain EPO mutants did not bind to the classical EPO receptor (EPOR) and did not show any hematopoietic activity in human cell signaling assays or upon chronic dosing in different animal species. Nevertheless, CEPO and various nonhematopoietic mutants were cytoprotective in vitro and conferred neuroprotection against stroke, spinal cord compression, diabetic neuropathy, and experimental autoimmune encephalomyelitis at a potency and efficacy comparable to EPO.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leist, Marcel -- Ghezzi, Pietro -- Grasso, Giovanni -- Bianchi, Roberto -- Villa, Pia -- Fratelli, Maddalena -- Savino, Costanza -- Bianchi, Marina -- Nielsen, Jacob -- Gerwien, Jens -- Kallunki, Pekka -- Larsen, Anna Kirstine -- Helboe, Lone -- Christensen, Soren -- Pedersen, Lars O -- Nielsen, Mette -- Torup, Lars -- Sager, Thomas -- Sfacteria, Alessandra -- Erbayraktar, Serhat -- Erbayraktar, Zubeyde -- Gokmen, Necati -- Yilmaz, Osman -- Cerami-Hand, Carla -- Xie, Qiao-Wen -- Coleman, Thomas -- Cerami, Anthony -- Brines, Michael -- New York, N.Y. -- Science. 2004 Jul 9;305(5681):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉H. Lundbeck A/S, 2500 Valby, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15247477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Binding Sites ; Cells, Cultured ; Diabetic Neuropathies/drug therapy ; Drug Design ; Encephalomyelitis, Autoimmune, Experimental/drug therapy ; Erythropoiesis ; Erythropoietin/*analogs & ; derivatives/chemistry/genetics/metabolism/pharmacology/*therapeutic use ; Female ; Hematocrit ; Humans ; Ligands ; Mice ; Mice, Inbred C3H ; Mutagenesis ; Nervous System Diseases/*drug therapy ; Neurons/metabolism ; Neuroprotective Agents/chemistry/metabolism/pharmacology/*therapeutic use ; Rats ; Rats, Sprague-Dawley ; Receptors, Erythropoietin/metabolism ; Recombinant Proteins ; Signal Transduction ; Spinal Cord Compression/drug therapy ; Stroke/drug therapy ; Structure-Activity Relationship
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    Neuroscience. Sealing cortical cell fate (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levitt, Pat -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):48-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vanderbilt Kennedy Center for Research on Human Development and Department of Pharmacology, Vanderbilt University, Nashville, TN 37203, USA. pat.levitt@vanderbilt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704417" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Lineage ; Cerebral Cortex/*cytology/embryology ; DNA-Binding Proteins/*genetics/*metabolism ; Down-Regulation ; Forkhead Transcription Factors ; Gene Expression Regulation, Developmental ; Mice ; Nerve Tissue Proteins/*genetics/*metabolism ; Neurons/*cytology/*physiology ; Stem Cells/cytology/*physiology ; Time Factors ; Transcription Factors/genetics/*metabolism
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    Neuroscience. Epileptic neurons go wireless (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Staley, Kevin -- New York, N.Y. -- Science. 2004 Jul 23;305(5683):482-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Pediatrics, University of Colorado Health Sciences Center, Denver, CO 80262, USA. kevin.staley@uchsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15273382" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Axons/physiology ; Dendrites/*physiology ; Epilepsy, Temporal Lobe/*physiopathology ; Feedback, Physiological ; Hippocampus/cytology/*physiopathology ; Humans ; Nerve Net/physiology ; Neural Inhibition ; Neurons/*physiology ; Pilocarpine/administration & dosage ; Potassium/*metabolism ; Potassium Channels/*physiology ; Rats ; Synapses/physiology ; Synaptic Transmission
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    SUMO modification of Huntingtin and Huntington's disease pathology (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-06
    Description: Huntington's disease (HD) is characterized by the accumulation of a pathogenic protein, Huntingtin (Htt), that contains an abnormal polyglutamine expansion. Here, we report that a pathogenic fragment of Htt (Httex1p) can be modified either by small ubiquitin-like modifier (SUMO)-1 or by ubiquitin on identical lysine residues. In cultured cells, SUMOylation stabilizes Httex1p, reduces its ability to form aggregates, and promotes its capacity to repress transcription. In a Drosophila model of HD, SUMOylation of Httex1p exacerbates neurodegeneration, whereas ubiquitination of Httex1p abrogates neurodegeneration. Lysine mutations that prevent both SUMOylation and ubiquitination of Httex1p reduce HD pathology, indicating that the contribution of SUMOylation to HD pathology extends beyond preventing Htt ubiquitination and degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steffan, Joan S -- Agrawal, Namita -- Pallos, Judit -- Rockabrand, Erica -- Trotman, Lloyd C -- Slepko, Natalia -- Illes, Katalin -- Lukacsovich, Tamas -- Zhu, Ya-Zhen -- Cattaneo, Elena -- Pandolfi, Pier Paolo -- Thompson, Leslie Michels -- Marsh, J Lawrence -- CA-62203/CA/NCI NIH HHS/ -- HD36049/HD/NICHD NIH HHS/ -- HD36081/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 2;304(5667):100-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry and Human Behavior, Gillespie 2121, University of California, Irvine, CA 92697, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15064418" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Cell Line ; Cell Nucleus/metabolism ; Corpus Striatum/cytology ; Cytoplasm/metabolism ; Drosophila ; Genes, MDR ; HeLa Cells ; Humans ; Huntington Disease/metabolism/*pathology ; Lysine/genetics/metabolism ; Mutation ; Nerve Degeneration ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/metabolism ; Nuclear Proteins/chemistry/genetics/*metabolism ; Proline/genetics/metabolism ; Promoter Regions, Genetic ; Rats ; Recombinant Fusion Proteins/metabolism ; SUMO-1 Protein/genetics/*metabolism ; Transcription, Genetic ; Transfection ; Ubiquitin/metabolism
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    Living and nonliving matter (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stec, Boguslaw -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):41-4; author reply 41-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232089" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; *Cells ; *Life ; Physical Phenomena ; Physics ; Proteins/*chemistry ; Selection, Genetic ; Thermodynamics
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    Medicine. A wily recruiter in the battle against toxic beta amyloid aggregation (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, Ingrid -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):791-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514121" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid beta-Peptides/*chemistry/metabolism/toxicity ; Animals ; Cell Death/drug effects ; Cells, Cultured ; Congo Red/*analogs & derivatives/*chemical ; synthesis/chemistry/*metabolism/*pharmacology ; Ligands ; Neurons/cytology/*drug effects ; Piperidines/*chemical synthesis/chemistry/metabolism/*pharmacology ; Protein Conformation ; Rats ; Tacrolimus Binding Proteins/*metabolism/pharmacology
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    Coordinated activation of Hsp70 chaperones (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-06
    Description: Hsp70s are a ubiquitous family of molecular chaperones involved in many cellular processes. Two Hsp70s, Lhs1p and Kar2p, are required for protein biogenesis in the yeast endoplasmic reticulum. Here, we found that Lhs1p and Kar2p specifically interacted to couple, and coordinately regulate, their respective activities. Lhs1p stimulated Kar2p by providing a specific nucleotide exchange activity, whereas Kar2p reciprocally activated the Lhs1p adenosine triphosphatase (ATPase). The two ATPase activities are coupled, and their coordinated regulation is essential for normal function in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steel, Gregor J -- Fullerton, Donna M -- Tyson, John R -- Stirling, Colin J -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):98-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704430" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Carrier Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; *Guanine Nucleotide Exchange Factors ; HSP70 Heat-Shock Proteins/chemistry/genetics/*metabolism ; Heat-Shock Proteins/chemistry/metabolism ; Membrane Transport Proteins/chemistry/metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Mutation ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism
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    Distinct ensemble codes in hippocampal areas CA3 and CA1 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-24
    Description: The hippocampus has differentiated into an extensively connected recurrent stage (CA3) followed by a feed-forward stage (CA1). We examined the function of this structural differentiation by determining how cell ensembles in rat CA3 and CA1 generate representations of rooms with common spatial elements. In CA3, distinct subsets of pyramidal cells were activated in each room, regardless of the similarity of the testing enclosure. In CA1, the activated populations overlapped, and the overlap increased in similar enclosures. After exposure to a novel room, ensemble activity developed slower in CA3 than CA1, suggesting that the representations emerged independently.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leutgeb, Stefan -- Leutgeb, Jill K -- Treves, Alessandro -- Moser, May-Britt -- Moser, Edvard I -- New York, N.Y. -- Science. 2004 Aug 27;305(5688):1295-8. Epub 2004 Jul 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for the Biology of Memory, Medical-Technical Research Centre, Norwegian University of Science and Technology, 7489 Trondheim, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15272123" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Cues ; Electrodes, Implanted ; Entorhinal Cortex/physiology ; Hippocampus/cytology/*physiology ; Male ; *Memory ; Nerve Net/*physiology ; Neurons/*physiology ; Pyramidal Cells/*physiology ; Rats ; Rats, Long-Evans ; *Space Perception
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    Regulation of cell migration by the C2 domain of the tumor suppressor PTEN (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-21
    Description: PTEN is a tumor suppressor protein that dephosphorylates phosphatidylinositol 3,4,5 trisphosphate and antagonizes the phosphatidylinositol-3 kinase signaling pathway. We show here that PTEN can also inhibit cell migration through its C2 domain, independent of its lipid phosphatase activity. This activity depends on the protein phosphatase activity of PTEN and on dephosphorylation at a single residue, threonine(383). The ability of PTEN to control cell migration through its C2 domain is likely to be an important feature of its tumor suppressor activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raftopoulou, Myrto -- Etienne-Manneville, Sandrine -- Self, Annette -- Nicholls, Sarah -- Hall, Alan -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1179-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory for Molecular Cell Biology and Cell Biology Unit, Cancer Research UK Oncogene and Signal Transduction Group, University College London, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976311" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Catalysis ; Catalytic Domain ; Cell Line, Tumor ; Cell Movement/*physiology ; Cercopithecus aethiops ; Glioma ; Humans ; Mutation ; PTEN Phosphohydrolase ; Phosphoprotein Phosphatases/chemistry/metabolism ; Phosphoric Monoester Hydrolases/*chemistry/genetics/metabolism/*physiology ; Phosphorylation ; Phosphothreonine/metabolism ; Precipitin Tests ; Protein Structure, Tertiary ; Recombinant Proteins/pharmacology ; Sequence Deletion ; Transfection ; Tumor Suppressor Proteins/*chemistry/genetics/metabolism/*physiology
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    Functional stoichiometry and local enrichment of calmodulin interacting with Ca2+ channels (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: Calmodulin (CaM) interactions with Ca2+ channels mediate both Ca2+ regulation of channels and local Ca2+ triggering of transcription factors implicated in neuronal memory. Crucial to these functions are the number of CaM molecules (CaMs) regulating each channel, and the number of CaMs privy to the local Ca2+ signal from each channel. To resolve these parameters, we fused L-type Ca2+ channels to single CaM molecules. These chimeric molecules revealed that a single CaM directs L-type channel regulation. Similar fusion molecules were used to estimate the local CaM concentration near Ca2+ channels. This estimate indicates marked enrichment of local CaM, as if a "school" of nearby CaMs were poised to enhance the transduction of local Ca2+ entry into diverse signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mori, Masayuki X -- Erickson, Michael G -- Yue, David T -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):432-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ca2+ Signals Laboratory, Department of Biomedical Engineering , Johns Hopkins University School of Medicine, 720 Rutland Avenue, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087548" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium/*metabolism ; Calcium Channels, L-Type/chemistry/*metabolism ; Calcium Signaling ; Calmodulin/chemistry/genetics/*metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Fluorescence Resonance Energy Transfer ; Humans ; Mathematics ; Mutation ; Patch-Clamp Techniques ; Peptides/chemistry/genetics ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection
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  • 27
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    Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: The 1918 "Spanish" influenza pandemic represents the largest recorded outbreak of any infectious disease. The crystal structure of the uncleaved precursor of the major surface antigen of the extinct 1918 virus was determined at 3.0 angstrom resolution after reassembly of the hemagglutinin gene from viral RNA fragments preserved in 1918 formalin-fixed lung tissues. A narrow avian-like receptor-binding site, two previously unobserved histidine patches, and a less exposed surface loop at the cleavage site that activates viral membrane fusion reveal structural features primarily found in avian viruses, which may have contributed to the extraordinarily high infectivity and mortality rates observed during 1918.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, James -- Corper, Adam L -- Basler, Christopher F -- Taubenberger, Jeffery K -- Palese, Peter -- Wilson, Ian A -- AI058113/AI/NIAID NIH HHS/ -- AI42266/AI/NIAID NIH HHS/ -- AI50619/AI/NIAID NIH HHS/ -- CA55896/CA/NCI NIH HHS/ -- P50-GM 62411/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1866-70. Epub 2004 Feb 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764887" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Carbohydrate Conformation ; Cloning, Molecular ; Crystallography, X-Ray ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/metabolism ; Histidine/chemistry/metabolism ; History, 20th Century ; Humans ; Hydrogen Bonding ; Influenza A virus/classification/*immunology/pathogenicity ; Influenza, Human/epidemiology/history/virology ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Virus/metabolism ; Sialic Acids/metabolism
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    Ecology. How 'virgin' is virgin rainforest? (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willis, K J -- Gillson, L -- Brncic, T M -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):402-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oxford Long-term Ecology Laboratory, Biodiversity Research Group, School of Geography and the Environment, University of Oxford, Oxford OX1 3TB, UK. kathy.willis@geog.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087539" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Agriculture ; Animals ; Archaeology ; Asia, Southeastern ; *Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; Forestry ; Human Activities ; Humans ; Population Dynamics ; South America ; Time Factors ; *Trees ; *Tropical Climate
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    Obesity research. New data on appetite-suppressing peptide challenge critics (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gura, Trisha -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1453-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567820" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Appetite/*drug effects ; Appetite Depressants/administration & dosage/*pharmacology ; Body Weight/drug effects ; Dose-Response Relationship, Drug ; Gastric Emptying/drug effects ; Humans ; Macaca mulatta ; Peptide Fragments ; Peptide YY/administration & dosage/metabolism/*pharmacology ; Rats
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    Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-13
    Description: Numerous degenerative disorders are associated with elevated levels of prooxidants and declines in mitochondrial aconitase activity. Deficiency in the mitochondrial iron-binding protein frataxin results in diminished activity of various mitochondrial iron-sulfur proteins including aconitase. We found that aconitase can undergo reversible citrate-dependent modulation in activity in response to pro-oxidants. Frataxin interacted with aconitase in a citrate-dependent fashion, reduced the level of oxidant-induced inactivation, and converted inactive [3Fe-4S]1+ enzyme to the active [4Fe-4S]2+ form of the protein. Thus, frataxin is an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bulteau, Anne-Laure -- O'Neill, Heather A -- Kennedy, Mary Claire -- Ikeda-Saito, Masao -- Isaya, Grazia -- Szweda, Luke I -- AG-15709/AG/NIA NIH HHS/ -- AG-16339/AG/NIA NIH HHS/ -- NRSA 44748/NR/NINR NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 9;305(5681):242-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15247478" target="_blank"〉PubMed〈/a〉
    Keywords: Aconitate Hydratase/antagonists & inhibitors/*metabolism ; Animals ; Citric Acid/metabolism/pharmacology ; Dithiothreitol/metabolism ; Electron Spin Resonance Spectroscopy ; Enzyme Activation ; Ferrous Compounds/metabolism ; Hydrogen Peroxide/pharmacology ; Iron/*metabolism ; Iron-Binding Proteins/*metabolism ; Male ; Mitochondria/*metabolism ; Mitochondria, Heart/*metabolism ; Molecular Chaperones/*metabolism ; Oxidation-Reduction ; Oxidative Stress ; Oxygen Consumption ; Rats ; Rats, Sprague-Dawley ; Saccharomyces cerevisiae/*metabolism ; Saccharomyces cerevisiae Proteins/metabolism
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    RAD51C is required for Holliday junction processing in mammalian cells (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-13
    Description: During genetic recombination and the recombinational repair of chromosome breaks, DNA molecules become linked at points of strand exchange. Branch migration and resolution of these crossovers, or Holliday junctions (HJs), complete the recombination process. Here, we show that extracts from cells carrying mutations in the recombination/repair genes RAD51C or XRCC3 have reduced levels of HJ resolvase activity. Moreover, depletion of RAD51C from fractionated human extracts caused a loss of branch migration and resolution activity, but these functions were restored by complementation with a variety of RAD51 paralog complexes containing RAD51C. We conclude that the RAD51 paralogs are involved in HJ processing in human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Yilun -- Masson, Jean-Yves -- Shah, Rajvee -- O'Regan, Paul -- West, Stephen C -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK, London Research Institute, Clare Hall Laboratories, South Mimms, Hertfordshire EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716019" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; CHO Cells ; Cell Line ; Cricetinae ; DNA Repair ; DNA, Cruciform/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; Electrophoresis, Polyacrylamide Gel ; Female ; HeLa Cells ; Holliday Junction Resolvases/*metabolism ; Humans ; Mutation ; Protein Structure, Tertiary ; Recombinant Proteins/metabolism ; Recombination, Genetic
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    The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-24
    Description: Jun N-terminal kinases (JNKs) are essential for neuronal microtubule assembly and apoptosis. Phosphorylation of the activating protein 1 (AP1) transcription factor c-Jun, at multiple sites within its transactivation domain, is required for JNK-induced neurotoxicity. We report that in neurons the stability of c-Jun is regulated by the E3 ligase SCF(Fbw7), which ubiquitinates phosphorylated c-Jun and facilitates c-Jun degradation. Fbw7 depletion resulted in accumulation of phosphorylated c-Jun, stimulation of AP1 activity, and neuronal apoptosis. SCF(Fbw7) therefore antagonizes the apoptotic c-Jun-dependent effector arm of JNK signaling, allowing neurons to tolerate potentially neurotoxic JNK activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nateri, Abdolrahman S -- Riera-Sans, Lluis -- Da Costa, Clive -- Behrens, Axel -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1374-8. Epub 2004 Jan 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mammalian Genetics Laboratory, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739463" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; Base Sequence ; Cell Cycle Proteins/genetics/*metabolism ; Cell Line ; F-Box Proteins/genetics/*metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Signaling System ; Mice ; Mitogen-Activated Protein Kinases/*metabolism ; Molecular Sequence Data ; Neurons/*physiology ; PC12 Cells ; Phosphorylation ; Proto-Oncogene Proteins c-jun/*metabolism ; RNA, Small Interfering/metabolism ; Rats ; Transcription Factor AP-1/metabolism ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/genetics/*metabolism
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    Extracellular replication of Listeria monocytogenes in the murine gall bladder (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: The bacterium Listeria monocytogenes can cause a life-threatening systemic illness in humans. Despite decades of progress in animal models of listeriosis, much remains unknown about the processes of infection and colonization. Here, we report that L. monocytogenes can replicate in the murine gall bladder and provide evidence that its replication there is extracellular and intraluminal. In vivo bioluminescence imaging was employed to determine the location of the infection over time in live animals, revealing strong signals from the gall bladder over a period of several days, in diseased as well as asymptomatic animals. The data suggest that L. monocytogenes may be carried in the human gall bladder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardy, Jonathan -- Francis, Kevin P -- DeBoer, Monica -- Chu, Pauline -- Gibbs, Karine -- Contag, Christopher H -- R01HD37543/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):851-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764883" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Colony Count, Microbial ; Female ; Gallbladder/*microbiology ; Gallbladder Diseases/*microbiology ; Listeria monocytogenes/genetics/*growth & development/isolation & ; purification/pathogenicity ; Listeriosis/*microbiology ; Liver/microbiology ; Luminescence ; Mice ; Mice, Inbred BALB C ; Mutation ; Spleen/microbiology ; Time Factors ; Virulence
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    Femtomolar sensitivity of a NO sensor from Clostridium botulinum (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-09
    Description: Nitric oxide (NO) is extremely toxic to Clostridium botulinum, but its molecular targets are unknown. Here, we identify a heme protein sensor (SONO) that displays femtomolar affinity for NO. The crystal structure of the SONO heme domain reveals a previously undescribed fold and a strategically placed tyrosine residue that modulates heme-nitrosyl coordination. Furthermore, the domain architecture of a SONO ortholog cloned from Chlamydomonas reinhardtii indicates that NO signaling through cyclic guanosine monophosphate arose before the origin of multicellular eukaryotes. Our findings have broad implications for understanding bacterial responses to NO, as well as for the activation of mammalian NO-sensitive guanylyl cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nioche, Pierre -- Berka, Vladimir -- Vipond, Julia -- Minton, Nigel -- Tsai, Ah-Lim -- Raman, C S -- AY343540/PHS HHS/ -- R01 AI054444/AI/NIAID NIH HHS/ -- R01 AI054444-05/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1550-3. Epub 2004 Oct 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Research Center and Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472039" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Bacterial Proteins/chemistry/metabolism ; Biological Evolution ; Carrier Proteins/*chemistry/genetics/*metabolism ; Chemotaxis ; Chlamydomonas reinhardtii/chemistry/genetics/metabolism ; Cloning, Molecular ; Clostridium botulinum/*chemistry/genetics/*metabolism ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Escherichia coli/genetics/growth & development ; Guanylate Cyclase ; Heme/chemistry/metabolism ; Hemeproteins/*chemistry/genetics/*metabolism ; Humans ; Hydrogen Bonding ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Nitric Oxide/*metabolism ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protoporphyrins/analysis/metabolism ; Receptors, Cytoplasmic and Nuclear/chemistry/metabolism ; Sequence Alignment ; Signal Transduction ; Static Electricity ; Thermoanaerobacter/chemistry
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    Periodical cicadas as resource pulses in North American forests (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-11-30
    Description: Resource pulses are occasional events of ephemeral resource superabundance that occur in many ecosystems. Aboveground consumers in diverse communities often respond strongly to resource pulses, but few studies have investigated the belowground consequences of resource pulses in natural ecosystems. This study shows that resource pulses of 17-year periodical cicadas (Magicicada spp.) directly increase microbial biomass and nitrogen availability in forest soils, with indirect effects on growth and reproduction in forest plants. These findings suggest that pulses of periodical cicadas create "bottom-up cascades," resulting in strong and reciprocal links between the aboveground and belowground components of a North American forest ecosystem.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Louie H -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1565-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Population Biology, Section of Evolution and Ecology, University of California, One Shields Avenue, Davis, CA 95616, USA. lhyang@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567865" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/growth & development ; Biomass ; Campanulaceae/chemistry/*growth & development ; *Ecosystem ; Fatty Acids/analysis ; Fungi/growth & development ; Hemiptera/growth & development/*physiology ; Life Cycle Stages ; Nitrates/analysis ; Nitrogen Isotopes/analysis ; Quaternary Ammonium Compounds/analysis ; Seeds/growth & development ; Soil/analysis ; Soil Microbiology ; Time Factors ; *Trees/growth & development ; United States
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    Comment on "Metapopulation persistence with age-dependent disturbance or succession" (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dushoff, Jonathan -- New York, N.Y. -- Science. 2004 Apr 30;304(5671):684; author reply 684.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and, Evolutionary Biology, Princeton University, Princeton, NJ 08540, USA. dushoff@eno.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15118146" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Ecosystem ; *Environment ; Population Dynamics ; Probability ; Time Factors
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    Neuroscience. The where and when of intention (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eagleman, David M -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1144-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Perception and Action, Department of Neurobiology and Anatomy, University of Texas, Houston Medical School, Houston, TX 77030, USA. david.eagleman@uth.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976300" target="_blank"〉PubMed〈/a〉
    Keywords: *Attention ; Brain/*physiology ; Brain Mapping ; Humans ; *Intention ; Magnetic Resonance Imaging ; *Motor Activity ; Motor Cortex/blood supply/*physiology ; Parietal Lobe/blood supply/physiology ; Prefrontal Cortex/blood supply/physiology ; Regional Blood Flow ; Time Factors
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    Structure-based assembly of protein complexes in yeast (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-03-27
    Description: 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〉
    Keywords: 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
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    Tracking SNARE complex formation in live endocrine cells (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-11-06
    Description: Syntaxin, synaptosome-associated protein of 25 kD (SNAP25), and vesicle-associated membrane protein/synaptobrevin are collectively called SNAP receptor (SNARE) proteins, and they catalyze neuronal exocytosis by forming a "core complex." The steps in core complex formation are unknown. Here, we monitored SNARE complex formation in vivo with the use of a fluorescent version of SNAP25. In PC12 cells, we found evidence for a syntaxin-SNAP25 complex that formed with high affinity, required only the amino-terminal SNARE motif of SNAP25, tolerated a mutation that blocks formation of other syntaxin-SNAP25 complexes, and assembled reversibly when Ca2+ entered cells during depolarization. The complex may represent a precursor to the core complex formed during a Ca2+-dependent priming step of exocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉An, Seong J -- Almers, Wolfhard -- MH60600/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 5;306(5698):1042-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute L-474, Oregon Health Sciences University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528447" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Medulla/cytology ; Animals ; Bacterial Proteins ; Cell Line ; Fluorescence Resonance Energy Transfer ; Green Fluorescent Proteins ; Humans ; Luminescent Proteins ; Membrane Proteins/genetics/physiology ; Nerve Tissue Proteins/genetics/physiology ; PC12 Cells ; Qa-SNARE Proteins ; Rats ; Recombinant Fusion Proteins ; SNARE Proteins ; Synaptosomal-Associated Protein 25 ; Vesicular Transport Proteins/*physiology
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    That's my hand! Activity in premotor cortex reflects feeling of ownership of a limb (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-07-03
    Description: When we look at our hands, we immediately know that they are part of our own body. This feeling of ownership of our limbs is a fundamental aspect of self-consciousness. We have studied the neuronal counterparts of this experience. A perceptual illusion was used to manipulate feelings of ownership of a rubber hand presented in front of healthy subjects while brain activity was measured by functional magnetic resonance imaging. The neural activity in the premotor cortex reflected the feeling of ownership of the hand. This suggests that multisensory integration in the premotor cortex provides a mechanism for bodily self-attribution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrsson, H Henrik -- Spence, Charles -- Passingham, Richard E -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):875-7. Epub 2004 Jul 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Department of Imaging Neuroscience, Institute of Neurology, 12 Queen Square, London WC1N 3BG, UK. h.ehrsson@fil.ion.ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232072" target="_blank"〉PubMed〈/a〉
    Keywords: *Body Image ; Brain/physiology ; Brain Mapping ; Cerebellum/physiology ; Female ; Hand ; Humans ; Magnetic Resonance Imaging ; Male ; Motor Cortex/*physiology ; Neurons/*physiology ; Parietal Lobe/physiology ; Proprioception ; Time Factors ; Touch ; Vision, Ocular
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    Nanotubular highways for intercellular organelle transport (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-14
    Description: Cell-to-cell communication is a crucial prerequisite for the development and maintenance of multicellular organisms. To date, diverse mechanisms of intercellular exchange of information have been documented, including chemical synapses, gap junctions, and plasmodesmata. Here, we describe highly sensitive nanotubular structures formed de novo between cells that create complex networks. These structures facilitate the selective transfer of membrane vesicles and organelles but seem to impede the flow of small molecules. Accordingly, we propose a novel biological principle of cell-to-cell interaction based on membrane continuity and intercellular transfer of organelles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rustom, Amin -- Saffrich, Rainer -- Markovic, Ivanka -- Walther, Paul -- Gerdes, Hans-Hermann -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):1007-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Interdisciplinary Center of Neuroscience (IZN), Institute of Neurobiology, University of Heidelberg, INF 364, Heidelberg 69120, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963329" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; Biological Transport ; Carbocyanines/metabolism ; *Cell Communication ; Cell Line ; Cell Membrane/metabolism ; Cell Surface Extensions/*metabolism/*ultrastructure ; Endocytosis ; Endosomes/metabolism ; Fluorescent Dyes/metabolism ; Green Fluorescent Proteins ; Luminescent Proteins/metabolism ; Membrane Proteins/metabolism ; Microscopy, Electron, Scanning ; Microscopy, Fluorescence ; Microscopy, Video ; Organelles/*metabolism ; PC12 Cells ; Protein Prenylation ; Protein Transport ; Pseudopodia/metabolism/ultrastructure ; Rats ; Recombinant Fusion Proteins/metabolism ; Synaptophysin/metabolism
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    Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-02
    Description: We show that activated collagenase (MMP-1) moves processively on the collagen fibril. The mechanism of movement is a biased diffusion with the bias component dependent on the proteolysis of its substrate, not adenosine triphosphate (ATP) hydrolysis. Inactivation of the enzyme by a single amino acid residue substitution in the active center eliminates the bias without noticeable effect on rate of diffusion. Monte Carlo simulations using a model similar to a "burnt bridge" Brownian ratchet accurately describe our experimental results and previous observations on kinetics of collagen digestion. The biological implications of MMP-1 acting as a molecular ratchet tethered to the cell surface suggest new mechanisms for its role in tissue remodeling and cell-matrix interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saffarian, Saveez -- Collier, Ivan E -- Marmer, Barry L -- Elson, Elliot L -- Goldberg, Gregory -- AR39472/AR/NIAMS NIH HHS/ -- AR40618/AR/NIAMS NIH HHS/ -- GM-38838/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459390" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Substitution ; Animals ; Collagen/*metabolism ; Computer Simulation ; Diffusion ; Fluorescence ; Humans ; Hydrolysis ; Mathematics ; Matrix Metalloproteinase 1/chemistry/genetics/*metabolism ; Microscopy, Fluorescence ; Models, Chemical ; Molecular Motor Proteins/chemistry/metabolism ; Monte Carlo Method ; Point Mutation ; Protein Transport ; Rats ; Recombinant Proteins/chemistry/metabolism
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    Realistic species losses disproportionately reduce grassland resistance to biological invaders (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-13
    Description: Consequences of progressive biodiversity declines depend on the functional roles of individual species and the order in which species are lost. Most studies of the biodiversity-ecosystem functioning relation tackle only the first of these factors. We used observed variation in grassland diversity to design an experimental test of how realistic species losses affect invasion resistance. Because entire plant functional groups disappeared faster than expected by chance, resistance declined dramatically with progressive species losses. Realistic biodiversity losses, even of rare species, can thus affect ecosystem processes far more than indicated by randomized-loss experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zavaleta, Erika S -- Hulvey, Kristin B -- New York, N.Y. -- Science. 2004 Nov 12;306(5699):1175-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Environmental Studies Department, University of California, Santa Cruz, CA 95064, USA. zavaleta@ucsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539600" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/*growth & development ; *Biodiversity ; Biomass ; California ; Centaurea/*growth & development ; *Ecosystem ; Environment ; Poaceae/*growth & development ; Seasons ; Time Factors
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    Ecology. A head start for some redstarts (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, Geoffrey E -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2201-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Science, Auburn University, Auburn, AL 36849, USA. ghill@acesag.auburn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15619587" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Migration ; Animals ; Carotenoids/*analysis ; Feathers/*chemistry/growth & development ; Female ; Hydrogen/*analysis ; Isotopes ; Life Cycle Stages ; Male ; *Molting ; Pigmentation ; *Reproduction ; Seasons ; Songbirds/growth & development/*physiology ; Time Factors
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    A host-targeting signal in virulence proteins reveals a secretome in malarial infection (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-14
    Description: Malaria parasites secrete proteins across the vacuolar membrane into the erythrocyte, inducing modifications linked to disease and parasite survival. We identified an 11-amino acid signal required for the secretion of proteins from the Plasmodium falciparum vacuole to the human erythrocyte. Bioinformatics predicted a secretome of 〉320 proteins and conservation of the signal across parasite species. Functional studies indicated the predictive value of the signal and its role in targeting virulence proteins to the erythrocyte and implicated its recognition by a receptor/transporter. Erythrocyte modification by the parasite may involve plasmodial heat shock proteins and be vastly more complex than hitherto realized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hiller, N Luisa -- Bhattacharjee, Souvik -- van Ooij, Christiaan -- Liolios, Konstantinos -- Harrison, Travis -- Lopez-Estrano, Carlos -- Haldar, Kasturi -- AI39071/AI/NIAID NIH HHS/ -- HL69630/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1934-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Pathology and Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15591203" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Computational Biology ; Cytosol/metabolism ; Erythrocytes/*metabolism/parasitology ; Genes, Protozoan ; Humans ; Malaria, Falciparum/parasitology ; Membrane Proteins/chemistry/metabolism ; Molecular Sequence Data ; Plasmodium falciparum/genetics/growth & development/*metabolism/*pathogenicity ; *Protein Sorting Signals ; Protein Structure, Tertiary ; Protein Transport ; Protozoan Proteins/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transgenes ; Vacuoles/metabolism/parasitology ; Virulence Factors/chemistry/genetics/*metabolism
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    bHLH transcription factor Olig1 is required to repair demyelinated lesions in the CNS (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: Olig1 and Olig2 are closely related basic helix-loop-helix (bHLH) transcription factors that are expressed in myelinating oligodendrocytes and their progenitor cells in the developing central nervous system (CNS). Olig2 is necessary for the specification of oligodendrocytes, but the biological functions of Olig1 during oligodendrocyte lineage development are poorly understood. We show here that Olig1 function in mice is required not to develop the brain but to repair it. Specifically, we demonstrate a genetic requirement for Olig1 in repairing the types of lesions that occur in patients with multiple sclerosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnett, Heather A -- Fancy, Stephen P J -- Alberta, John A -- Zhao, Chao -- Plant, Sheila R -- Kaing, Sovann -- Raine, Cedric S -- Rowitch, David H -- Franklin, Robin J M -- Stiles, Charles D -- 689/Multiple Sclerosis Society/United Kingdom -- NS08952/NS/NINDS NIH HHS/ -- NS11920/NS/NINDS NIH HHS/ -- NS4051/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2111-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604411" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Basic Helix-Loop-Helix Transcription Factors ; Brain/growth & development/*physiology ; Cell Nucleus/metabolism ; Cuprizone/pharmacology ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Demyelinating Diseases/*physiopathology ; Ethidium/pharmacology ; Humans ; Lysophosphatidylcholines/pharmacology ; Mice ; Mice, Inbred C57BL ; Multiple Sclerosis/physiopathology ; Myelin Sheath/*physiology ; Nerve Tissue Proteins/genetics/*metabolism/physiology ; Oligodendroglia/*physiology ; Rats ; Rats, Sprague-Dawley ; Spinal Cord/growth & development/*physiology ; Stem Cells/physiology ; Transcription Factors/genetics/*metabolism
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    The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-07
    Description: Plexins are cell surface receptors for semaphorin molecules, and their interaction governs cell adhesion and migration in a variety of tissues. We report that the Semaphorin 4D (Sema4D) receptor Plexin-B1 directly stimulates the intrinsic guanosine triphosphatase (GTPase) activity of R-Ras, a member of the Ras superfamily of small GTP-binding proteins that has been implicated in promoting cell adhesion and neurite outgrowth. This activity required the interaction of Plexin-B1 with Rnd1, a small GTP-binding protein of the Rho family. Down-regulation of R-Ras activity by the Plexin-B1-Rnd1 complex was essential for the Sema4D-induced growth cone collapse in hippocampal neurons. Thus, Plexin-B1 mediates Sema4D-induced repulsive axon guidance signaling by acting as a GTPase activating protein for R-Ras.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oinuma, Izumi -- Ishikawa, Yukio -- Katoh, Hironori -- Negishi, Manabu -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):862-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297673" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Axons/physiology ; COS Cells ; Cells, Cultured ; Down-Regulation ; GTP Phosphohydrolases/*metabolism ; GTPase-Activating Proteins/chemistry/genetics/*metabolism ; Guanosine Triphosphate/metabolism ; Hippocampus/cytology ; Humans ; Membrane Glycoproteins/*metabolism/pharmacology ; Neurites/physiology ; Neurons/*metabolism ; PC12 Cells ; Protein Structure, Tertiary ; RNA, Small Interfering ; Rats ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Semaphorins ; Signal Transduction ; Transfection ; ras Proteins/*metabolism ; rho GTP-Binding Proteins/genetics/metabolism ; rhoA GTP-Binding Protein/metabolism
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    Comment on "Transmembrane segments of syntaxin line the fusion pore of Ca2+-triggered exocytosis" (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szule, Joseph A -- Coorssen, Jens R -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):813; author reply 813.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Cellular and Molecular NeurobiologyResearch Group, Faculty of Medicine, University of Calgary, Calgary, Alberta, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514140" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cell Membrane Structures/*chemistry/metabolism ; *Exocytosis ; Membrane Fusion ; Membrane Microdomains/metabolism ; Membrane Proteins/chemistry/genetics/*metabolism ; Models, Biological ; Mutation ; Neurons/*physiology ; PC12 Cells ; Qa-SNARE Proteins ; Rats
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    Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: Mobilization of fatty acids from triglyceride stores in adipose tissue requires lipolytic enzymes. Dysfunctional lipolysis affects energy homeostasis and may contribute to the pathogenesis of obesity and insulin resistance. Until now, hormone-sensitive lipase (HSL) was the only enzyme known to hydrolyze triglycerides in mammalian adipose tissue. Here, we report that a second enzyme, adipose triglyceride lipase (ATGL), catalyzes the initial step in triglyceride hydrolysis. It is interesting that ATGL contains a "patatin domain" common to plant acyl-hydrolases. ATGL is highly expressed in adipose tissue of mice and humans. It exhibits high substrate specificity for triacylglycerol and is associated with lipid droplets. Inhibition of ATGL markedly decreases total adipose acyl-hydrolase activity. Thus, ATGL and HSL coordinately catabolize stored triglycerides in adipose tissue of mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmermann, Robert -- Strauss, Juliane G -- Haemmerle, Guenter -- Schoiswohl, Gabriele -- Birner-Gruenberger, Ruth -- Riederer, Monika -- Lass, Achim -- Neuberger, Georg -- Eisenhaber, Frank -- Hermetter, Albin -- Zechner, Rudolf -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1383-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biosciences, University of Graz, Graz, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550674" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3-L1 Cells ; Adipocytes/enzymology/*metabolism ; Adipose Tissue/enzymology/*metabolism ; Adipose Tissue, Brown/enzymology/metabolism ; Amino Acid Sequence ; Animals ; COS Cells ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cytoplasm/enzymology ; DNA, Complementary ; Diglycerides/metabolism ; Fatty Acids/metabolism ; Gene Silencing ; Glycerol/metabolism ; Humans ; Isoproterenol/pharmacology ; *Lipid Mobilization ; Lipolysis ; Lipoprotein Lipase/chemistry/genetics/immunology/*metabolism ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Structure, Tertiary ; RNA, Messenger/genetics/metabolism ; Sterol Esterase/genetics/*metabolism ; Substrate Specificity ; Transfection ; Triglycerides/metabolism
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    Reversible immunocontraception in male monkeys immunized with eppin (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-11-13
    Description: Various forms of birth control have been developed for women; however, there are currently few options for men. The development of male contraceptives that are effective, safe, and reversible is desired for family planning throughout the world. We now report contraception of male nonhuman primates (Macaca radiata) immunized with Eppin, a testis/epididymis-specific protein. Seven out of nine males (78%) developed high titers to Eppin, and all of these high-titer monkeys were infertile. Five out of seven (71%) high-anti-Eppin titer males recovered fertility when immunization was stopped. This study demonstrates that effective and reversible male immunocontraception is an attainable goal. This method of immunocontraception may be extended to humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'rand, M G -- Widgren, E E -- Sivashanmugam, P -- Richardson, R T -- Hall, S H -- French, F S -- VandeVoort, C A -- Ramachandra, S G -- Ramesh, V -- Jagannadha Rao, A -- New York, N.Y. -- Science. 2004 Nov 12;306(5699):1189-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories for Reproductive Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. morand@unc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539605" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/analysis/blood ; *Contraception, Immunologic ; Female ; Fertility ; Freund's Adjuvant ; Immunization, Secondary ; Macaca mulatta ; Macaca radiata ; Male ; Proteinase Inhibitory Proteins, Secretory ; Proteins/*immunology ; Recombinant Proteins/immunology ; Semen/immunology ; Time Factors ; Vaccination ; *Vaccines, Contraceptive
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    Ecology. Oh the locusts sang, then they dropped dead (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ostfeld, Richard S -- Keesing, Felicia -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1488-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Ecosystem Studies, Millbrook, NY 12545, USA. rostfeld@ecostudies.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567844" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/growth & development ; Biomass ; Campanulaceae/*growth & development ; *Ecosystem ; Fertilizers ; Fungi/growth & development ; Hemiptera/growth & development/*physiology ; Life Cycle Stages ; Nitrogen/analysis ; Plant Roots ; Soil/analysis ; Soil Microbiology ; Time Factors ; Trees/growth & development
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    Regulation of bone mass in mice by the lipoxygenase gene Alox15 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-13
    Description: The development of osteoporosis involves the interaction of multiple environmental and genetic factors. Through combined genetic and genomic approaches, we identified the lipoxygenase gene Alox15 as a negative regulator of peak bone mineral density in mice. Crossbreeding experiments with Alox15 knockout mice confirmed that 12/15-lipoxygenase plays a role in skeletal development. Pharmacologic inhibitors of this enzyme improved bone density and strength in two rodent models of osteoporosis. These results suggest that drugs targeting the 12/15-lipoxygenase pathway merit investigation as a therapy for osteoporosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, Robert F -- Allard, John -- Avnur, Zafrira -- Nikolcheva, Tania -- Rotstein, David -- Carlos, Amy S -- Shea, Marie -- Waters, Ruth V -- Belknap, John K -- Peltz, Gary -- Orwoll, Eric S -- AR44659/AR/NIAMS NIH HHS/ -- HG02322/HG/NHGRI NIH HHS/ -- R01 AR044659/AR/NIAMS NIH HHS/ -- R01 AR044659-08/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):229-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bone and Mineral Research Unit, Department of Medicine, School of Medicine, Oregon Health and Science University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97239, USA. kleinro@ohsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716014" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachidonate 12-Lipoxygenase/*genetics/*metabolism ; Arachidonate 15-Lipoxygenase/*genetics/*metabolism ; Bone Density/drug effects/*genetics ; Bone Marrow Cells/metabolism ; Cell Differentiation ; Cells, Cultured ; Crosses, Genetic ; Enzyme Inhibitors/pharmacology ; Female ; Fluorenes/pharmacology ; Gene Expression Profiling ; Genetic Linkage ; Kidney/metabolism ; Lipoxygenase Inhibitors ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Mice, Knockout ; Mice, Transgenic ; Oligonucleotide Array Sequence Analysis ; Osteoblasts/cytology/metabolism/physiology ; Osteogenesis ; Osteoporosis/enzymology ; Polymorphism, Genetic ; Quantitative Trait Loci ; Rats ; Receptors, Cytoplasmic and Nuclear/metabolism ; Stromal Cells/metabolism ; Transcription Factors/metabolism
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    Force-clamp spectroscopy monitors the folding trajectory of a single protein (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-16
    Description: We used force-clamp atomic force microscopy to measure the end-to-end length of the small protein ubiquitin during its folding reaction at the single-molecule level. Ubiquitin was first unfolded and extended at a high force, then the stretching force was quenched and protein folding was observed. The folding trajectories were continuous and marked by several distinct stages. The time taken to fold was dependent on the contour length of the unfolded protein and the stretching force applied during folding. The folding collapse was marked by large fluctuations in the end-to-end length of the protein, but these fluctuations vanished upon the final folding contraction. These direct observations of the complete folding trajectory of a protein provide a benchmark to determine the physical basis of the folding reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, Julio M -- Li, Hongbin -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1674-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA. jfernandez@columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15017000" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; *Microscopy, Atomic Force ; Physicochemical Phenomena ; Polyubiquitin/*chemistry ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Protein Structure, Secondary ; Time Factors ; Ubiquitin/*chemistry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Inflammatory exposure and historical changes in human life-spans (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-18
    Description: Most explanations of the increase in life expectancy at older ages over history emphasize the importance of medical and public health factors of a particular historical period. We propose that the reduction in lifetime exposure to infectious diseases and other sources of inflammation--a cohort mechanism--has also made an important contribution to the historical decline in old-age mortality. Analysis of birth cohorts across the life-span since 1751 in Sweden reveals strong associations between early-age mortality and subsequent mortality in the same cohorts. We propose that a "cohort morbidity phenotype" represents inflammatory processes that persist from early age into adult life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finch, Caleb E -- Crimmins, Eileen M -- AG05142/AG/NIA NIH HHS/ -- AG13499/AG/NIA NIH HHS/ -- AG14751/AG/NIA NIH HHS/ -- AG17265/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 17;305(5691):1736-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Andrus Gerontology Center and Departments of Biological Sciencesand of Sociology, University of Southern California, Los Angeles, CA 90089, USA. cefinch@usc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15375259" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Child ; Cohort Studies ; Humans ; Infant ; *Infection/epidemiology ; *Inflammation/epidemiology ; *Life Expectancy ; Longevity ; Morbidity ; *Mortality ; Nutritional Physiological Phenomena ; Time Factors
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Cdh1-APC controls axonal growth and patterning in the mammalian brain (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-13
    Description: The anaphase-promoting complex (APC) is highly expressed in postmitotic neurons, but its function in the nervous system was previously unknown. We report that the inhibition of Cdh1-APC in primary neurons specifically enhanced axonal growth. Cdh1 knockdown in cerebellar slice overlay assays and in the developing rat cerebellum in vivo revealed cell-autonomous abnormalities in layer-specific growth of granule neuron axons and parallel fiber patterning. Cdh1 RNA interference in neurons was also found to override the inhibitory influence of myelin on axonal growth. Thus, Cdh1-APC appears to play a role in regulating axonal growth and patterning in the developing brain that may also limit the growth of injured axons in the adult brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Konishi, Yoshiyuki -- Stegmuller, Judith -- Matsuda, Takahiko -- Bonni, Shirin -- Bonni, Azad -- R01NS41021/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):1026-30. Epub 2004 Jan 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716021" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase-Promoting Complex-Cyclosome ; Animals ; Axons/*physiology/ultrastructure ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Nucleus/metabolism ; Cells, Cultured ; Cerebellar Cortex/*cytology/growth & development ; Dendrites/physiology/ultrastructure ; Electroporation ; Morphogenesis ; Mutation ; Myelin Sheath/metabolism ; Neurons/*physiology ; Organ Culture Techniques ; RNA Interference ; Rats ; Rats, Long-Evans ; Transfection ; Ubiquitin-Protein Ligase Complexes/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    CO2 elicits long-term decline in nitrogen fixation (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hungate, Bruce A -- Stiling, Peter D -- Dijkstra, Paul -- Johnson, Dale W -- Ketterer, Michael E -- Hymus, Graham J -- Hinkle, C Ross -- Drake, Bert G -- New York, N.Y. -- Science. 2004 May 28;304(5675):1291.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences and Merriam-Powell Center for Environmental Research, Northern Arizona University, Flagstaff, AZ 86011, USA. bruce.hungate@nau.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166370" target="_blank"〉PubMed〈/a〉
    Keywords: *Atmosphere ; Biomass ; *Carbon Dioxide ; Ecosystem ; Fabaceae/*metabolism ; Florida ; Light ; Molybdenum/metabolism ; *Nitrogen Fixation ; Plant Leaves/anatomy & histology/metabolism ; Quercus/metabolism ; Time Factors
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    Hereditary early-onset Parkinson's disease caused by mutations in PINK1 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: Parkinson's disease (PD) is a neurodegenerative disorder characterized by degeneration of dopaminergic neurons in the substantia nigra. We previously mapped a locus for a rare familial form of PD to chromosome 1p36 (PARK6). Here we show that mutations in PINK1 (PTEN-induced kinase 1) are associated with PARK6. We have identified two homozygous mutations affecting the PINK1 kinase domain in three consanguineous PARK6 families: a truncating nonsense mutation and a missense mutation at a highly conserved amino acid. Cell culture studies suggest that PINK1 is mitochondrially located and may exert a protective effect on the cell that is abrogated by the mutations, resulting in increased susceptibility to cellular stress. These data provide a direct molecular link between mitochondria and the pathogenesis of PD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valente, Enza Maria -- Abou-Sleiman, Patrick M -- Caputo, Viviana -- Muqit, Miratul M K -- Harvey, Kirsten -- Gispert, Suzana -- Ali, Zeeshan -- Del Turco, Domenico -- Bentivoglio, Anna Rita -- Healy, Daniel G -- Albanese, Alberto -- Nussbaum, Robert -- Gonzalez-Maldonado, Rafael -- Deller, Thomas -- Salvi, Sergio -- Cortelli, Pietro -- Gilks, William P -- Latchman, David S -- Harvey, Robert J -- Dallapiccola, Bruno -- Auburger, Georg -- Wood, Nicholas W -- G-4029/Parkinson's UK/United Kingdom -- GGP02089/Telethon/Italy -- New York, N.Y. -- Science. 2004 May 21;304(5674):1158-60. Epub 2004 Apr 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSS IRCCS, Mendel Institute, viale Regina Margherita 261, 00198 Rome, Italy. e.valente@css-mendel.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087508" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apoptosis ; COS Cells ; Cell Line, Tumor ; Codon, Nonsense ; Exons ; Humans ; Leupeptins/pharmacology ; Membrane Potentials ; Mitochondria/enzymology/*metabolism ; Molecular Sequence Data ; *Mutation ; Mutation, Missense ; Neurons/metabolism/physiology ; Oxidative Stress ; Parkinson Disease/enzymology/*genetics/metabolism ; Protein Kinases/chemistry/*genetics/*metabolism ; Protein Structure, Tertiary ; Transfection
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    Synfire chains and cortical songs: temporal modules of cortical activity (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-24
    Description: How can neural activity propagate through cortical networks built with weak, stochastic synapses? We find precise repetitions of spontaneous patterns of synaptic inputs in neocortical neurons in vivo and in vitro. These patterns repeat after minutes, maintaining millisecond accuracy. Calcium imaging of slices reveals reactivation of sequences of cells during the occurrence of repeated intracellular synaptic patterns. The spontaneous activity drifts with time, engaging different cells. Sequences of active neurons have distinct spatial structures and are repeated in the same order over tens of seconds, revealing modular temporal dynamics. Higher order sequences are replayed with compressed timing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ikegaya, Yuji -- Aaron, Gloster -- Cossart, Rosa -- Aronov, Dmitriy -- Lampl, Ilan -- Ferster, David -- Yuste, Rafael -- New York, N.Y. -- Science. 2004 Apr 23;304(5670):559-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15105494" target="_blank"〉PubMed〈/a〉
    Keywords: 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine/pharmacology ; 2-Amino-5-phosphonovalerate/pharmacology ; Action Potentials ; Animals ; Benzazepines/pharmacology ; Calcium/metabolism ; Cats ; Excitatory Postsynaptic Potentials ; In Vitro Techniques ; Mice ; Mice, Inbred C57BL ; Microscopy, Confocal ; Nerve Net/physiology ; Neurons/*physiology ; Patch-Clamp Techniques ; Prefrontal Cortex/cytology/*physiology ; Pyramidal Cells/physiology ; Receptors, Dopamine D1/physiology ; Receptors, N-Methyl-D-Aspartate/physiology ; Synapses/physiology ; *Synaptic Transmission ; Time Factors ; Visual Cortex/cytology/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structural basis of mitochondrial tethering by mitofusin complexes (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-07
    Description: Vesicle fusion involves vesicle tethering, docking, and membrane merger. We show that mitofusin, an integral mitochondrial membrane protein, is required on adjacent mitochondria to mediate fusion, which indicates that mitofusin complexes act in trans (that is, between adjacent mitochondria). A heptad repeat region (HR2) mediates mitofusin oligomerization by assembling a dimeric, antiparallel coiled coil. The transmembrane segments are located at opposite ends of the 95 angstrom coiled coil and provide a mechanism for organelle tethering. Consistent with this proposal, truncated mitofusin, in an HR2-dependent manner, causes mitochondria to become apposed with a uniform gap. Our results suggest that HR2 functions as a mitochondrial tether before fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshiba, Takumi -- Detmer, Scott A -- Kaiser, Jens T -- Chen, Hsiuchen -- McCaffery, J Michael -- Chan, David C -- R01 GM62967/GM/NIGMS NIH HHS/ -- S10 RR019409-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):858-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, 1200 East California Boulevard, MC114-96, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297672" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cell Line ; Crystallography, X-Ray ; Dimerization ; GTP Phosphohydrolases/*chemistry/*metabolism ; Humans ; Hybrid Cells ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes/physiology/ultrastructure ; Membrane Fusion ; Mice ; Mitochondria/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Intracellular acidosis enhances the excitability of working muscle (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-25
    Description: Intracellular acidification of skeletal muscles is commonly thought to contribute to muscle fatigue. However, intracellular acidosis also acts to preserve muscle excitability when muscles become depolarized, which occurs with working muscles. Here, we show that this process may be mediated by decreased chloride permeability, which enables action potentials to still be propagated along the internal network of tubules in a muscle fiber (the T system) despite muscle depolarization. These results implicate chloride ion channels in muscle function and emphasize that intracellular acidosis of muscle has protective effects during muscle fatigue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pedersen, Thomas H -- Nielsen, Ole B -- Lamb, Graham D -- Stephenson, D George -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1144-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Aarhus, DK-8000, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15326352" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/metabolism ; Chloride Channels/*metabolism ; Chlorides/metabolism ; Electric Stimulation ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Lactic Acid/metabolism ; Membrane Potentials ; Muscle Contraction ; *Muscle Fatigue ; Muscle Fibers, Skeletal/metabolism/*physiology ; Muscle, Skeletal/metabolism/*physiology ; Permeability ; Potassium/metabolism ; Rats ; Sarcoplasmic Reticulum/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Neuroscience. Let there be (NADH) light (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellerin, Luc -- Magistretti, Pierre J -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):50-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Physiologie, 1005 Lausanne, Switzerland. luc.pellerin@iphysiol.unil.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232095" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/*metabolism ; Citric Acid Cycle ; Cytoplasm/metabolism ; Dendrites/metabolism ; Fluorescence ; *Glycolysis ; Hippocampus/cytology/*metabolism ; In Vitro Techniques ; Lactic Acid/metabolism ; Microscopy, Confocal ; Mitochondria/metabolism ; Models, Neurological ; NAD/*metabolism ; Neurons/*metabolism ; Oxidation-Reduction ; Oxidative Phosphorylation ; Rats
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    Acquired dendritic channelopathy in temporal lobe epilepsy (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-07-27
    Description: Inherited channelopathies are at the origin of many neurological disorders. Here we report a form of channelopathy that is acquired in experimental temporal lobe epilepsy (TLE), the most common form of epilepsy in adults. The excitability of CA1 pyramidal neuron dendrites was increased in TLE because of decreased availability of A-type potassium ion channels due to transcriptional (loss of channels) and posttranslational (increased channel phosphorylation by extracellular signal-regulated kinase) mechanisms. Kinase inhibition partly reversed dendritic excitability to control levels. Such acquired channelopathy is likely to amplify neuronal activity and may contribute to the initiation and/or propagation of seizures in TLE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernard, Christophe -- Anderson, Anne -- Becker, Albert -- Poolos, Nicholas P -- Beck, Heinz -- Johnston, Daniel -- MH44754/MH/NIMH NIH HHS/ -- MH48432/MH/NIMH NIH HHS/ -- NS37444/NS/NINDS NIH HHS/ -- NS39943/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 23;305(5683):532-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Baylor College of Medicine, Houston, TX 77030, USA. cbernard@inmed.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15273397" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/pharmacology ; 4-Aminopyridine/pharmacology ; Action Potentials/drug effects ; Animals ; Butadienes/pharmacology ; Dendrites/*physiology ; Enzyme Inhibitors/pharmacology ; Epilepsy, Temporal Lobe/*physiopathology ; Hippocampus/cytology/*physiopathology ; Male ; Membrane Potentials ; Mitogen-Activated Protein Kinases/antagonists & inhibitors/metabolism ; Nitriles/pharmacology ; Phosphorylation ; Pilocarpine/administration & dosage ; Potassium Channel Blockers/pharmacology ; Potassium Channels/drug effects/metabolism/*physiology ; *Potassium Channels, Voltage-Gated ; Protein Kinase C/antagonists & inhibitors/metabolism ; Pyramidal Cells/*physiology ; Rats ; Rats, Sprague-Dawley ; Shal Potassium Channels
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    Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-01-06
    Description: The crystal structure of biotin synthase from Escherichia coli in complex with S-adenosyl-L-methionine and dethiobiotin has been determined to 3.4 angstrom resolution. This structure addresses how "AdoMet radical" or "radical SAM" enzymes use Fe4S4 clusters and S-adenosyl-L-methionine to generate organic radicals. Biotin synthase catalyzes the radical-mediated insertion of sulfur into dethiobiotin to form biotin. The structure places the substrates between the Fe4S4 cluster, essential for radical generation, and the Fe2S2 cluster, postulated to be the source of sulfur, with both clusters in unprecedented coordination environments.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1456065/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1456065/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berkovitch, Frederick -- Nicolet, Yvain -- Wan, Jason T -- Jarrett, Joseph T -- Drennan, Catherine L -- NSLS X25/NS/NINDS NIH HHS/ -- R01 GM059175/GM/NIGMS NIH HHS/ -- R01-GM59175/GM/NIGMS NIH HHS/ -- R01-GM65337/GM/NIGMS NIH HHS/ -- T32-GM07229/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):76-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704425" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Biotin/*analogs & derivatives/*chemistry/metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Escherichia coli/*enzymology ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrogen/chemistry ; Hydrogen Bonding ; Iron/chemistry ; Ligands ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; S-Adenosylmethionine/*chemistry/metabolism ; Sulfur/chemistry ; Sulfurtransferases/*chemistry/*metabolism
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    Sites of neocortical reorganization critical for remote spatial memory (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-03
    Description: The hippocampus is crucial for spatial memory formation, yet it does not store long-lasting memories. By combining functional brain imaging and region-specific neuronal inactivation in mice, we identified prefrontal and anterior cingulate cortices as critical for storage and retrieval of remote spatial memories [correction]. Imaging of activity-dependent genes also revealed an involvement of parietal and retrosplenial cortices during consolidation of remote memory. Long-term memory storage within some of these neocortical regions was accompanied by structural changes including synaptogenesis and laminar reorganization, concomitant with a functional disengagement of the hippocampus and posterior cingulate cortex [correction]. Thus, consolidation of spatial memory requires a time-dependent hippocampal-cortical dialogue, ultimately enabling widespread cortical networks to mediate effortful recall and use of cortically stored remote memories independently.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maviel, Thibault -- Durkin, Thomas P -- Menzaghi, Frederique -- Bontempi, Bruno -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):96-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Neurosciences Cognitives, CNRS UMR 5106, Universite de Bordeaux 1, Avenue des Facultes, 33405 Talence, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232109" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Mapping ; GAP-43 Protein/metabolism ; Gene Expression Regulation ; Genes, Immediate-Early ; Gyrus Cinguli/*physiology ; Immediate-Early Proteins/metabolism ; Lidocaine/pharmacology ; Male ; Memory/drug effects/*physiology ; Mental Recall ; Mice ; Mice, Inbred C57BL ; Neocortex/*physiology ; Nerve Net/physiology ; Neuronal Plasticity ; Neurons/physiology ; Parietal Lobe/physiology ; Prefrontal Cortex/*physiology ; Synapses/physiology ; Time Factors
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    The scaling of animal space use (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-09
    Description: Space used by animals increases with increasing body size. Energy requirements alone can explain how population density decreases, but not the steep rate at which home range area increases. We present a general mechanistic model that predicts the frequency of interaction, spatial overlap, and loss of resources to neighbors. Extensive empirical evidence supports the model, demonstrating that spatial constraints on defense cause exclusivity of home range use to decrease with increasing body size. In large mammals, over 90% of available resources may be lost to neighbors. Our model offers a general framework to understand animal space use and sociality.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jetz, Walter -- Carbone, Chris -- Fulford, Jenny -- Brown, James H -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):266-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08544-1003, USA. wjetz@princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472074" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Constitution ; Body Weight ; Conservation of Natural Resources ; *Ecosystem ; Energy Metabolism ; Environment ; *Homing Behavior ; *Mammals/anatomy & histology/metabolism ; Mathematics ; *Models, Biological ; Physical Phenomena ; Physics ; Population Density
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    Robust temporal coding in the trigeminal system (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-26
    Description: The ability of rats to use their whiskers for fine tactile discrimination rivals that of humans using their fingertips. Rats perform discriminations rapidly and accurately while palpating the environment with their whiskers. This suggests that whisker deflections produce a robust and reliable neural code. Whisker primary afferents respond with highly reproducible temporal spike patterns to transient stimuli. Here we show that, with the use of a linear kernel, any of these reproducible response trains recorded from an individual neuron can reliably predict complex whisker deflections. These predictions are significantly improved by integrating responses from neurons with opposite angular preferences.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1557422/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1557422/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Lauren M -- Depireux, Didier A -- Simons, Daniel J -- Keller, Asaf -- F31 NS046100/NS/NINDS NIH HHS/ -- F31 NS46100-01/NS/NINDS NIH HHS/ -- NS19950/NS/NINDS NIH HHS/ -- R01 DC-05937-01/DC/NIDCD NIH HHS/ -- R01 DC005937/DC/NIDCD NIH HHS/ -- R01 NS019950/NS/NINDS NIH HHS/ -- R01 NS031078/NS/NINDS NIH HHS/ -- R01 NS31078/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 25;304(5679):1986-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Neuroscience and Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15218153" target="_blank"〉PubMed〈/a〉
    Keywords: Acoustic Stimulation ; Action Potentials ; Afferent Pathways ; Analysis of Variance ; Animals ; Female ; Neurons/*physiology ; Rats ; Touch ; Trigeminal Ganglion/cytology/*physiology ; Vibrissae/*innervation/*physiology
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    Neuroscience. In the place space (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bilkey, David K -- New York, N.Y. -- Science. 2004 Aug 27;305(5688):1245-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, University of Otago, Dunedin, New Zealand. dbilkey@psy.otago.ac.nz〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15333826" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Mapping ; Cues ; Entorhinal Cortex/cytology/*physiology ; Hippocampus/cytology/*physiology ; Humans ; *Memory ; Nerve Net/*physiology ; Neurons/physiology ; Pyramidal Cells/physiology ; Rats ; *Space Perception
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    Biochemistry. Completing the view of transcriptional regulation (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Hippel, Peter H -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 16;305(5682):350-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, OR 97403, USA. petevh@molbio.uoregon.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15256661" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/*metabolism ; Binding Sites ; DNA, Bacterial/*chemistry/*metabolism ; Diffusion ; Dimerization ; Escherichia coli/chemistry/genetics/metabolism ; Escherichia coli Proteins/chemistry/metabolism ; *Gene Expression Regulation, Bacterial ; Hydrogen Bonding ; Kinetics ; Lac Operon ; Lac Repressors ; Models, Genetic ; Models, Molecular ; Nucleic Acid Conformation ; Operator Regions, Genetic ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Repressor Proteins/*chemistry/*metabolism ; Static Electricity ; Thermodynamics ; *Transcription, Genetic
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    Placebo-induced changes in FMRI in the anticipation and experience of pain (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-21
    Description: The experience of pain arises from both physiological and psychological factors, including one's beliefs and expectations. Thus, placebo treatments that have no intrinsic pharmacological effects may produce analgesia by altering expectations. However, controversy exists regarding whether placebos alter sensory pain transmission, pain affect, or simply produce compliance with the suggestions of investigators. In two functional magnetic resonance imaging (fMRI) experiments, we found that placebo analgesia was related to decreased brain activity in pain-sensitive brain regions, including the thalamus, insula, and anterior cingulate cortex, and was associated with increased activity during anticipation of pain in the prefrontal cortex, providing evidence that placebos alter the experience of pain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wager, Tor D -- Rilling, James K -- Smith, Edward E -- Sokolik, Alex -- Casey, Kenneth L -- Davidson, Richard J -- Kosslyn, Stephen M -- Rose, Robert M -- Cohen, Jonathan D -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1162-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, University of Michigan, 525 East University, Ann Arbor, MI 48109-1109, USA. torw@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976306" target="_blank"〉PubMed〈/a〉
    Keywords: *Analgesia ; Brain/*physiology ; Brain Mapping ; Cerebral Cortex/physiology ; Electroshock ; Frontal Lobe/physiology ; Gyrus Cinguli/physiology ; Hot Temperature ; Humans ; Magnetic Resonance Imaging ; Mesencephalon/physiology ; *Pain ; *Placebo Effect ; Placebos/*pharmacology ; Prefrontal Cortex/physiology ; Thalamus/physiology ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Selective differentiation of neural progenitor cells by high-epitope density nanofibers (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-24
    Description: Neural progenitor cells were encapsulated in vitro within a three-dimensional network of nanofibers formed by self-assembly of peptide amphiphile molecules. The self-assembly is triggered by mixing cell suspensions in media with dilute aqueous solutions of the molecules, and cells survive the growth of the nanofibers around them. These nanofibers were designed to present to cells the neurite-promoting laminin epitope IKVAV at nearly van der Waals density. Relative to laminin or soluble peptide, the artificial nanofiber scaffold induced very rapid differentiation of cells into neurons, while discouraging the development of astrocytes. This rapid selective differentiation is linked to the amplification of bioactive epitope presentation to cells by the nanofibers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silva, Gabriel A -- Czeisler, Catherine -- Niece, Krista L -- Beniash, Elia -- Harrington, Daniel A -- Kessler, John A -- Stupp, Samuel I -- NS20013/NS/NINDS NIH HHS/ -- NS20778/NS/NINDS NIH HHS/ -- NS34758/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1352-5. Epub 2004 Jan 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Bioengineering and Nanoscience in Advanced Medicine, Northwestern University, Chicago, IL 60611, USA. gsilva@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739465" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/cytology ; *Cell Differentiation ; Cell Movement ; Cell Survival ; Cells, Cultured ; Diffusion ; Epitopes ; Glial Fibrillary Acidic Protein/analysis ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Laminin/administration & dosage/chemistry/immunology/*metabolism ; Mice ; *Nanotechnology ; Neurites/physiology/ultrastructure ; Neurons/*cytology/physiology ; Peptide Fragments/administration & dosage/chemistry/*metabolism ; Rats ; Spinal Cord ; Stem Cells/*cytology/physiology ; Tubulin/analysis
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    Molecular biology. Argonaute journeys into the heart of RISC (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sontheimer, Erik J -- Carthew, Richard W -- R01 GM068743/GM/NIGMS NIH HHS/ -- R01 GM077581/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 3;305(5689):1409-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA. erik@northwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15353786" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Archaeal Proteins/*chemistry ; Argonaute Proteins ; Catalytic Domain ; Crystallography, X-Ray ; Embryonic and Fetal Development ; Eukaryotic Initiation Factor-2 ; Humans ; Mice ; MicroRNAs/metabolism ; Peptide Initiation Factors/chemistry/genetics/*metabolism ; Point Mutation ; Protein Structure, Tertiary ; Pyrococcus furiosus/chemistry ; *RNA Interference ; RNA, Double-Stranded/metabolism ; RNA, Messenger/metabolism ; RNA, Small Interfering/metabolism ; RNA-Induced Silencing Complex/*metabolism
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    Phosphoryl transfer and calcium ion occlusion in the calcium pump (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-12
    Description: A tight coupling between adenosine triphosphate (ATP) hydrolysis and vectorial ion transport has to be maintained by ATP-consuming ion pumps. We report two crystal structures of Ca2+-bound sarco(endo)plasmic reticulum Ca2+-adenosine triphosphatase (SERCA) at 2.6 and 2.9 angstrom resolution in complex with (i) a nonhydrolyzable ATP analog [adenosine (beta-gamma methylene)-triphosphate] and (ii) adenosine diphosphate plus aluminum fluoride. SERCA reacts with ATP by an associative mechanism mediated by two Mg2+ ions to form an aspartyl-phosphorylated intermediate state (Ca2-E1 approximately P). The conformational changes that accompany the reaction with ATP pull the transmembrane helices 1 and 2 and close a cytosolic entrance for Ca2+, thereby preventing backflow before Ca2+ is released on the other side of the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sorensen, Thomas Lykke-Moller -- Moller, Jesper Vuust -- Nissen, Poul -- New York, N.Y. -- Science. 2004 Jun 11;304(5677):1672-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15192230" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/*analogs & derivatives/*metabolism ; Aluminum Compounds/metabolism ; Animals ; Binding Sites ; Calcium/*metabolism ; Calcium-Transporting ATPases/*chemistry/*metabolism ; Crystallization ; Crystallography, X-Ray ; Cytosol/metabolism ; Fluorides/metabolism ; Models, Molecular ; Muscle Fibers, Fast-Twitch/*enzymology ; Phosphorylation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rabbits ; Sarcoplasmic Reticulum Calcium-Transporting ATPases
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    Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-08
    Description: Copper active sites play a major role in enzymatic activation of dioxygen. We trapped the copper-dioxygen complex in the enzyme peptidylglycine-alphahydroxylating monooxygenase (PHM) by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen. The x-ray crystal structure of this precatalytic complex, determined to 1.85-angstrom resolution, shows that oxygen binds to one of the coppers in the enzyme with an end-on geometry. Given this structure, it is likely that dioxygen is directly involved in the electron transfer and hydrogen abstraction steps of the PHM reaction. These insights may apply to other copper oxygen-activating enzymes, such as dopamine beta-monooxygenase, and to the design of biomimetic complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prigge, Sean T -- Eipper, Betty A -- Mains, Richard E -- Amzel, L Mario -- DK32949/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2004 May 7;304(5672):864-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Immunology, The Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131304" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Catalysis ; Catalytic Domain ; Copper/*metabolism ; Crystallization ; Crystallography, X-Ray ; Dipeptides/chemistry/metabolism ; Electron Transport ; Glycine/chemistry/metabolism ; Hydrogen/metabolism ; Hydrogen Bonding ; Ligands ; Mixed Function Oxygenases/*chemistry/*metabolism ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Oxidation-Reduction ; Oxygen/*metabolism ; Peptides/metabolism ; Protein Conformation ; Rats ; Water/metabolism
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    Synthetic mammalian prions (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-08-03
    Description: Recombinant mouse prion protein (recMoPrP) produced in Escherichia coli was polymerized into amyloid fibrils that represent a subset of beta sheet-rich structures. Fibrils consisting of recMoPrP(89-230) were inoculated intracerebrally into transgenic (Tg) mice expressing MoPrP(89-231). The mice developed neurologic dysfunction between 380 and 660 days after inoculation. Brain extracts showed protease-resistant PrP by Western blotting; these extracts transmitted disease to wild-type FVB mice and Tg mice overexpressing PrP, with incubation times of 150 and 90 days, respectively. Neuropathological findings suggest that a novel prion strain was created. Our results provide compelling evidence that prions are infectious proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Legname, Giuseppe -- Baskakov, Ilia V -- Nguyen, Hoang-Oanh B -- Riesner, Detlev -- Cohen, Fred E -- DeArmond, Stephen J -- Prusiner, Stanley B -- AG02132/AG/NIA NIH HHS/ -- AG021601/AG/NIA NIH HHS/ -- AG10770/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 30;305(5684):673-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Neurodegenerative Diseases, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15286374" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/chemistry/metabolism ; Animals ; Biopolymers ; Brain/metabolism/pathology ; Brain Chemistry ; Escherichia coli/genetics ; Female ; Glycosylation ; Male ; Mice ; Mice, Transgenic ; Plaque, Amyloid/pathology ; PrPSc Proteins/analysis/metabolism ; Prion Diseases/*etiology/pathology/transmission ; Prions/administration & dosage/biosynthesis/chemistry/*pathogenicity ; Protein Conformation ; Protein Folding ; Recombinant Proteins/administration & dosage/biosynthesis/chemistry ; Time Factors ; Tissue Extracts/administration & dosage ; Vacuoles/pathology
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    Cancer. A bull's eye for targeted lung cancer therapy (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Minna, John D -- Gazdar, Adi F -- Sprang, Stephen R -- Herz, Joachim -- P50CA70907/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1458-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. john.minna@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178790" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/drug therapy/genetics/metabolism ; Amino Acid Substitution ; Antineoplastic Agents/therapeutic use ; Carcinoma, Non-Small-Cell Lung/drug therapy/*genetics/metabolism ; Controlled Clinical Trials as Topic ; Enzyme Inhibitors/therapeutic use ; Epidermal Growth Factor/metabolism ; *Genes, erbB-1 ; Humans ; Japan ; Ligands ; Lung Neoplasms/*drug therapy/*genetics/metabolism ; *Mutation ; Phosphorylation ; Protein Structure, Tertiary ; Quinazolines/*therapeutic use ; Receptor, Epidermal Growth Factor/*antagonists & ; inhibitors/chemistry/genetics/metabolism ; Sequence Deletion ; Smoking ; Treatment Outcome ; United States
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    Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-10-09
    Description: Very rare cases of human T cell acute lymphoblastic leukemia (T-ALL) harbor chromosomal translocations that involve NOTCH1, a gene encoding a transmembrane receptor that regulates normal T cell development. Here, we report that more than 50% of human T-ALLs, including tumors from all major molecular oncogenic subtypes, have activating mutations that involve the extracellular heterodimerization domain and/or the C-terminal PEST domain of NOTCH1. These findings greatly expand the role of activated NOTCH1 in the molecular pathogenesis of human T-ALL and provide a strong rationale for targeted therapies that interfere with NOTCH signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weng, Andrew P -- Ferrando, Adolfo A -- Lee, Woojoong -- Morris, John P 4th -- Silverman, Lewis B -- Sanchez-Irizarry, Cheryll -- Blacklow, Stephen C -- Look, A Thomas -- Aster, Jon C -- CA109901/CA/NCI NIH HHS/ -- CA21765/CA/NCI NIH HHS/ -- CA68484/CA/NCI NIH HHS/ -- CA82308/CA/NCI NIH HHS/ -- CA94233/CA/NCI NIH HHS/ -- CA98093/CA/NCI NIH HHS/ -- P01 CA109901/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):269-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472075" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Alleles ; Amino Acid Sequence ; Amyloid Precursor Protein Secretases ; Aspartic Acid Endopeptidases ; Cell Cycle ; Cell Line, Tumor ; Child ; Dimerization ; Endopeptidases/metabolism ; Frameshift Mutation ; Humans ; Leukemia-Lymphoma, Adult T-Cell/*genetics/metabolism ; Molecular Sequence Data ; *Mutation ; Mutation, Missense ; Point Mutation ; Protease Inhibitors/pharmacology ; Protein Structure, Tertiary ; Receptor, Notch1 ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; Sequence Deletion ; Signal Transduction ; Transcription Factors/chemistry/*genetics/metabolism
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    A kinesin-like motor inhibits microtubule dynamic instability (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-03-06
    Description: The motility of molecular motors and the dynamic instability of microtubules are key dynamic processes for mitotic spindle assembly and function. We report here that one of the mitotic kinesins that localizes to chromosomes, Xklp1 from Xenopus laevis, could inhibit microtubule growth and shrinkage. This effect appeared to be mediated by a structural change in the microtubule lattice. We also found that Xklp1 could act as a fast, nonprocessive, plus end-directed molecular motor. The integration of the two properties, motility and inhibition of microtubule dynamics, in one molecule emphasizes the versatile properties of kinesin family members.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bringmann, Henrik -- Skiniotis, Georgios -- Spilker, Annina -- Kandels-Lewis, Stefanie -- Vernos, Isabelle -- Surrey, Thomas -- New York, N.Y. -- Science. 2004 Mar 5;303(5663):1519-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Biophysics Programme, European Molecular Biology Laboratory, Meyerhofstrabetae 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001780" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/metabolism/pharmacology ; Animals ; Centrosome/metabolism ; Chromosomes/metabolism ; Cryoelectron Microscopy ; Dimerization ; Kinetics ; Microtubule-Associated Proteins/chemistry/genetics/*metabolism ; Microtubules/drug effects/metabolism/*physiology/ultrastructure ; Molecular Motor Proteins/*metabolism ; Paclitaxel/pharmacology ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Tubulin/metabolism ; Xenopus Proteins/chemistry/genetics/*metabolism ; Xenopus laevis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Unifying the epidemiological and evolutionary dynamics of pathogens (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-17
    Description: A key priority for infectious disease research is to clarify how pathogen genetic variation, modulated by host immunity, transmission bottlenecks, and epidemic dynamics, determines the wide variety of pathogen phylogenies observed at scales that range from individual host to population. We call the melding of immunodynamics, epidemiology, and evolutionary biology required to achieve this synthesis pathogen "phylodynamics." We introduce a phylodynamic framework for the dissection of dynamic forces that determine the diversity of epidemiological and phylogenetic patterns observed in RNA viruses of vertebrates. A central pillar of this model is the Evolutionary Infectivity Profile, which captures the relationship between immune selection and pathogen transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grenfell, Bryan T -- Pybus, Oliver G -- Gog, Julia R -- Wood, James L N -- Daly, Janet M -- Mumford, Jenny A -- Holmes, Edward C -- BB/B524092/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2004 Jan 16;303(5656):327-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Downing Street, Cambridge, CB2 3EJ, UK. btg11@cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14726583" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Antigenic Variation/genetics ; Biological Evolution ; *Disease Outbreaks/veterinary ; Genetics, Population ; Humans ; Immunity ; Mutation ; *Phylogeny ; Population Dynamics ; RNA Virus Infections/*epidemiology/immunology/veterinary/*virology ; RNA Viruses/*genetics/immunology/*pathogenicity/physiology ; Selection, Genetic ; Time Factors ; Vaccination
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    Integrins regulate Rac targeting by internalization of membrane domains (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: Translocation of the small GTP-binding protein Rac1 to the cell plasma membrane is essential for activating downstream effectors and requires integrin-mediated adhesion of cells to extracellular matrix. We report that active Rac1 binds preferentially to low-density, cholesterol-rich membranes, and specificity is determined at least in part by membrane lipids. Cell detachment triggered internalization of plasma membrane cholesterol and lipid raft markers. Preventing internalization maintained Rac1 membrane targeting and effector activation in nonadherent cells. Regulation of lipid rafts by integrin signals may regulate the location of membrane domains such as lipid rafts and thereby control domain-specific signaling events in anchorage-dependent cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉del Pozo, Miguel A -- Alderson, Nazilla B -- Kiosses, William B -- Chiang, Hui-Hsien -- Anderson, Richard G W -- Schwartz, Martin A -- GM52016/GM/NIGMS NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- R01 GM47214/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. mdelpozo@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764880" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD29/metabolism ; Binding Sites ; Cell Adhesion ; Cell Line ; Cell Membrane/*metabolism ; Cells, Cultured ; Cholera Toxin/metabolism ; Cholesterol/metabolism ; G(M1) Ganglioside/metabolism ; Glycosylphosphatidylinositols/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Integrins/*metabolism ; Liposomes/metabolism ; Membrane Microdomains/*metabolism ; Mice ; NIH 3T3 Cells ; Rats ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; rac1 GTP-Binding Protein/genetics/*metabolism
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    Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-23
    Description: In mammalian cells, repair of DNA double-strand breaks (DSBs) by nonhomologous end-joining (NHEJ) is critical for genome stability. Although the end-bridging and ligation steps of NHEJ have been reconstituted in vitro, little is known about the end-processing reactions that occur before ligation. Recently, functionally homologous end-bridging and ligation activities have been identified in prokarya. Consistent with its homology to polymerases and nucleases, we demonstrate that DNA ligase D from Mycobacterium tuberculosis (Mt-Lig) possesses a unique variety of nucleotidyl transferase activities, including gap-filling polymerase, terminal transferase, and primase, and is also a 3' to 5' exonuclease. These enzyme activities allow the Mt-Ku and Mt-Lig proteins to join incompatible DSB ends in vitro, as well as to reconstitute NHEJ in vivo in yeast. These results demonstrate that prokaryotic Ku and ligase form a bona fide NHEJ system that encodes all the recognition, processing, and ligation activities required for DSB repair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Della, Marina -- Palmbos, Phillip L -- Tseng, Hui-Min -- Tonkin, Louise M -- Daley, James M -- Topper, Leana M -- Pitcher, Robert S -- Tomkinson, Alan E -- Wilson, Thomas E -- Doherty, Aidan J -- R01 CA102563/CA/NCI NIH HHS/ -- R01 CA102563-01A1/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 22;306(5696):683-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge Institute for Medical Research, University of Cambridge, Department of Haematology, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15499016" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/genetics/*metabolism ; DNA/*metabolism ; DNA Damage ; DNA Ligases/chemistry/genetics/*metabolism ; DNA Nucleotidyltransferases/chemistry/metabolism ; DNA Primase/chemistry/metabolism ; *DNA Repair ; DNA-Directed DNA Polymerase/chemistry/metabolism ; Exonucleases/chemistry/metabolism ; Mutation ; Mycobacterium tuberculosis/genetics/*metabolism ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Recombination, Genetic ; Saccharomyces cerevisiae/genetics
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  • 81
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    A putative Ca2+ and calmodulin-dependent protein kinase required for bacterial and fungal symbioses (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-14
    Description: Legumes can enter into symbiotic relationships with both nitrogen-fixing bacteria (rhizobia) and mycorrhizal fungi. Nodulation by rhizobia results from a signal transduction pathway induced in legume roots by rhizobial Nod factors. DMI3, a Medicago truncatula gene that acts immediately downstream of calcium spiking in this signaling pathway and is required for both nodulation and mycorrhizal infection, has high sequence similarity to genes encoding calcium and calmodulin-dependent protein kinases (CCaMKs). This indicates that calcium spiking is likely an essential component of the signaling cascade leading to nodule development and mycorrhizal infection, and sheds light on the biological role of plant CCaMKs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, Julien -- Bres, Cecile -- Geurts, Rene -- Chalhoub, Boulos -- Kulikova, Olga -- Duc, Gerard -- Journet, Etienne-Pascal -- Ane, Jean-Michel -- Lauber, Emmanuelle -- Bisseling, Ton -- Denarie, Jean -- Rosenberg, Charles -- Debelle, Frederic -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1361-4. Epub 2004 Feb 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire des Interactions Plantes-Microorganismes INRA-CNRS, BP27, 31326 Castanet-Tolosan Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963335" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium/metabolism ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinases/chemistry/genetics/*metabolism ; Calmodulin/metabolism ; Chromosomes, Artificial, Bacterial ; Cloning, Molecular ; EF Hand Motifs ; Expressed Sequence Tags ; Gene Expression Regulation, Plant ; Genes, Plant ; Lipopolysaccharides/metabolism ; Medicago/*enzymology/genetics/microbiology ; Molecular Sequence Data ; Mutation ; Mycorrhizae/*physiology ; Peas/*enzymology/genetics/microbiology ; Plant Roots/enzymology/microbiology ; Protein Structure, Tertiary ; Rhizobium/genetics ; Sinorhizobium meliloti/*physiology ; *Symbiosis ; Transformation, Genetic
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    Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-07-03
    Description: We have found that two-photon fluorescence imaging of nicotinamide adenine dinucleotide (NADH) provides the sensitivity and spatial three-dimensional resolution to resolve metabolic signatures in processes of astrocytes and neurons deep in highly scattering brain tissue slices. This functional imaging reveals spatiotemporal partitioning of glycolytic and oxidative metabolism between astrocytes and neurons during focal neural activity that establishes a unifying hypothesis for neurometabolic coupling in which early oxidative metabolism in neurons is eventually sustained by late activation of the astrocyte-neuron lactate shuttle. Our model integrates existing views of brain energy metabolism and is in accord with known macroscopic physiological changes in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasischke, Karl A -- Vishwasrao, Harshad D -- Fisher, Patricia J -- Zipfel, Warren R -- Webb, Watt W -- P41-EB001976-16/EB/NIBIB NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):99-103.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232110" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/*metabolism ; Citric Acid Cycle ; Cytoplasm ; Dendrites/metabolism ; Electron Transport ; Fluorescence ; *Glycolysis ; Hippocampus/*cytology/*metabolism ; In Vitro Techniques ; Lactic Acid/metabolism ; Mitochondria/metabolism ; NAD/metabolism ; Neurons/metabolism ; Oxidation-Reduction ; Oxygen Consumption ; Pyramidal Cells/*metabolism ; Rats ; Rats, Sprague-Dawley ; Spectrometry, Fluorescence
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    Breakthrough of the year. Scorecard 2003 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 2004 Dec 17;306(5704):2012.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604367" target="_blank"〉PubMed〈/a〉
    Keywords: Access to Information ; Animals ; Biological Warfare ; Ecosystem ; Genome ; Information Dissemination ; Mars ; Physical Phenomena ; Physics ; Publishing ; *Science ; Security Measures
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    Breakthrough of the year. The runners-up (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 2004 Dec 17;306(5704):2013-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604368" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Biological Evolution ; Cloning, Organism ; DNA, Intergenic ; Genome ; Hominidae/anatomy & histology ; Humans ; Physical Phenomena ; Physics ; Public Health ; *Science ; Water/chemistry
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    Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-02-14
    Description: The structure of the general transcription factor IIB (TFIIB) in a complex with RNA polymerase II reveals three features crucial for transcription initiation: an N-terminal zinc ribbon domain of TFIIB that contacts the "dock" domain of the polymerase, near the path of RNA exit from a transcribing enzyme; a "finger" domain of TFIIB that is inserted into the polymerase active center; and a C-terminal domain, whose interaction with both the polymerase and with a TATA box-binding protein (TBP)-promoter DNA complex orients the DNA for unwinding and transcription. TFIIB stabilizes an early initiation complex, containing an incomplete RNA-DNA hybrid region. It may interact with the template strand, which sets the location of the transcription start site, and may interfere with RNA exit, which leads to abortive initiation or promoter escape. The trajectory of promoter DNA determined by the C-terminal domain of TFIIB traverses sites of interaction with TFIIE, TFIIF, and TFIIH, serving to define their roles in the transcription initiation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bushnell, David A -- Westover, Kenneth D -- Davis, Ralph E -- Kornberg, Roger D -- AI21144/AI/NIAID NIH HHS/ -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):983-8.〈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/14963322" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Nucleic Acid Hybridization ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/chemistry/metabolism ; RNA Polymerase II/*chemistry/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; TATA Box ; TATA-Box Binding Protein/chemistry/metabolism ; Templates, Genetic ; Transcription Factor TFIIB/*chemistry/metabolism ; Transcription Factors, TFII/chemistry/metabolism ; *Transcription, Genetic ; Zinc/chemistry
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    Role of NMDA receptor subtypes in governing the direction of hippocampal synaptic plasticity (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-05-15
    Description: Activation of N-methyl-d-aspartate subtype glutamate receptors (NMDARs) is required for long-term potentiation (LTP) and long-term depression (LTD) of excitatory synaptic transmission at hippocampal CA1 synapses, the proposed cellular substrates of learning and memory. However, little is known about how activation of NMDARs leads to these two opposing forms of synaptic plasticity. Using hippocampal slice preparations, we showed that selectively blocking NMDARs that contain the NR2B subunit abolishes the induction of LTD but not LTP. In contrast, preferential inhibition of NR2A-containing NMDARs prevents the induction of LTP without affecting LTD production. These results demonstrate that distinct NMDAR subunits are critical factors that determine the polarity of synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Lidong -- Wong, Tak Pan -- Pozza, Mario F -- Lingenhoehl, Kurt -- Wang, Yushan -- Sheng, Morgan -- Auberson, Yves P -- Wang, Yu Tian -- New York, N.Y. -- Science. 2004 May 14;304(5673):1021-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brain Research Centre, University of British Columbia, 2211 Wesbrook Mall, Vancouver, BC V6T 2B5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15143284" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Electric Stimulation ; Excitatory Amino Acid Antagonists/pharmacology ; Excitatory Postsynaptic Potentials/drug effects ; Hippocampus/cytology/drug effects/*physiology ; In Vitro Techniques ; *Long-Term Potentiation/drug effects ; *Long-Term Synaptic Depression/drug effects ; Patch-Clamp Techniques ; Phenols/pharmacology ; Piperidines/pharmacology ; Pyramidal Cells/drug effects/*physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/*metabolism ; Synapses/*physiology ; Synaptic Transmission/drug effects
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    Neuroscience. Time is precious (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abeles, Moshe -- New York, N.Y. -- Science. 2004 Apr 23;304(5670):523-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gonda Brain Research Center, Bar Ilan University, Ramat-Gan, Israel, and Center for Neural Computation, the Hebrew University, Jerusalem, Israel. moshe.abeles@mail.biu.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15105481" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Cats ; Cerebral Cortex/cytology/*physiology ; Mice ; Nerve Net/physiology ; Neurons/*physiology ; Synapses/physiology ; *Synaptic Transmission ; Time Factors ; Visual Cortex/cytology/*physiology
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  • 88
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    Transmembrane segments of syntaxin line the fusion pore of Ca2+-triggered exocytosis (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-16
    Description: The fusion pore of regulated exocytosis is a channel that connects and spans the vesicle and plasma membranes. The molecular composition of this important intermediate structure of exocytosis is unknown. Here, we found that mutations of some residues within the transmembrane segment of syntaxin (Syx), a plasma membrane protein essential for exocytosis, altered neurotransmitter flux through fusion pores and altered pore conductance. The residues that influenced fusion-pore flux lay along one face of an alpha-helical model. Thus, the fusion pore is formed at least in part by a circular arrangement of 5 to 8 Syx transmembrane segments in the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, Xue -- Wang, Chih-Tien -- Bai, Jihong -- Chapman, Edwin R -- Jackson, Meyer B -- GM56827/GM/NIGMS NIH HHS/ -- MH61876/MH/NIMH NIH HHS/ -- NS30016/NS/NINDS NIH HHS/ -- NS44057/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):289-92. Epub 2004 Mar 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15016962" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cell Membrane Structures/*chemistry/metabolism ; Electric Capacitance ; Electric Conductivity ; Electrophysiology ; *Exocytosis ; Membrane Fusion ; Membrane Proteins/*chemistry/genetics/*metabolism ; Models, Biological ; Mutation ; Neurons/*physiology ; Norepinephrine/metabolism ; PC12 Cells ; Patch-Clamp Techniques ; Protein Structure, Secondary ; Qa-SNARE Proteins ; Rats ; Transfection
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    Neuroscience. Crossing the midline (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woods, C Geoffrey -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1455-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Medicine Unit, School of Medicine, University of Leeds, LS9 7TF, UK. msjcgw@leeds.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178787" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/metabolism/*physiology ; Cell Adhesion Molecules/metabolism ; Down-Regulation ; Gene Expression Profiling ; Gene Expression Regulation ; Glycoproteins/metabolism ; Humans ; Mice ; Morphogenesis ; Mutation ; Nerve Growth Factors/metabolism ; Nerve Tissue Proteins/metabolism ; Neural Pathways ; Ophthalmoplegia/*genetics/pathology/physiopathology ; Protein Structure, Tertiary ; Receptors, Cell Surface/metabolism ; Receptors, Immunologic/chemistry/*genetics/*metabolism ; Rhombencephalon/growth & development/metabolism/*pathology ; Scoliosis/*genetics/pathology/physiopathology ; Syndrome ; Tumor Suppressor Proteins/metabolism
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    Nutrient availability regulates SIRT1 through a forkhead-dependent pathway (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-12-18
    Description: Nutrient availability regulates life-span in a wide range of organisms. We demonstrate that in mammalian cells, acute nutrient withdrawal simultaneously augments expression of the SIRT1 deacetylase and activates the Forkhead transcription factor Foxo3a. Knockdown of Foxo3a expression inhibited the starvation-induced increase in SIRT1 expression. Stimulation of SIRT1 transcription by Foxo3a was mediated through two p53 binding sites present in the SIRT1 promoter, and a nutrient-sensitive physical interaction was observed between Foxo3a and p53. SIRT1 expression was not induced in starved p53-deficient mice. Thus, in mammalian cells, p53, Foxo3a, and SIRT1, three proteins separately implicated in aging, constitute a nutrient-sensing pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nemoto, Shino -- Fergusson, Maria M -- Finkel, Toren -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2105-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Branch, National Heart, Lung, and Blood Institute (NHLBI), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604409" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Binding Sites ; Culture Media ; Culture Media, Serum-Free ; DNA-Binding Proteins/*metabolism ; Forkhead Transcription Factors ; Gene Deletion ; Genes, p53 ; Glucose ; HeLa Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Mutation ; PC12 Cells ; Promoter Regions, Genetic ; RNA, Small Interfering/pharmacology ; Rats ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Serum ; Sirtuin 1 ; Sirtuins/genetics/*metabolism ; *Starvation ; Transcription Factors/*metabolism ; Transcription, Genetic ; Tumor Suppressor Protein p53/metabolism
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    Behavior. A marketplace in the brain? (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ainslie, George -- Monterosso, John -- New York, N.Y. -- Science. 2004 Oct 15;306(5695):421-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Coatesville Veterans Affairs Medical Center, Coatesville, PA 19320, USA. george.ainslie@med.va.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486281" target="_blank"〉PubMed〈/a〉
    Keywords: Basal Ganglia/physiology ; Brain/*physiology ; Brain Mapping ; Conditioning (Psychology) ; Cues ; *Decision Making ; Frontal Lobe/physiology ; Humans ; Limbic System/physiology ; Magnetic Resonance Imaging ; Parietal Lobe/physiology ; Prefrontal Cortex/physiology ; *Reward ; Time Factors
    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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    KIF1A alternately uses two loops to bind microtubules (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-03
    Description: The motor protein kinesin moves along microtubules, driven by adenosine triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin converts the chemical energy into mechanical movement. We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with known structures of the ADP-bound state and the adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show that kinesin uses two microtubule-binding loops in an alternating manner to change its interaction with microtubules during the ATP hydrolysis cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is extended in the ADP structure. ADP-vanadate displays an intermediate structure in which a conformational change in two switch regions causes both loops to be raised from the microtubule, thus actively detaching kinesin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nitta, Ryo -- Kikkawa, Masahide -- Okada, Yasushi -- Hirokawa, Nobutaka -- New York, N.Y. -- Science. 2004 Jul 30;305(5684):678-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, University of Tokyo, Graduate School of Medicine, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15286375" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/metabolism ; Aluminum/metabolism ; Animals ; Binding Sites ; Crystallography, X-Ray ; Fluorides/metabolism ; Hydrogen Bonding ; Kinesin/*chemistry/*metabolism ; Mice ; Microtubules/*metabolism ; Models, Molecular ; Nerve Tissue Proteins/*chemistry/*metabolism ; Phosphates/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Vanadates/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The wheat VRN2 gene is a flowering repressor down-regulated by vernalization (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-16
    Description: Plants with a winter growth habit flower earlier when exposed for several weeks to cold temperatures, a process called vernalization. We report here the positional cloning of the wheat vernalization gene VRN2, a dominant repressor of flowering that is down-regulated by vernalization. Loss of function of VRN2, whether by natural mutations or deletions, resulted in spring lines, which do not require vernalization to flower. Reduction of the RNA level of VRN2 by RNA interference accelerated the flowering time of transgenic winter-wheat plants by more than a month.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4737501/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4737501/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, Liuling -- Loukoianov, Artem -- Blechl, Ann -- Tranquilli, Gabriela -- Ramakrishna, Wusirika -- SanMiguel, Phillip -- Bennetzen, Jeffrey L -- Echenique, Viviana -- Dubcovsky, Jorge -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2004 Mar 12;303(5664):1640-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Agronomy and Range Science, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15016992" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/genetics/growth & development ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; *Cold Temperature ; Down-Regulation ; Epistasis, Genetic ; Evolution, Molecular ; Flowers/*growth & development ; Gene Deletion ; *Gene Expression Regulation, Plant ; Genes, Plant ; Genetic Variation ; Hordeum/genetics ; Molecular Sequence Data ; Mutation ; Plant Proteins/chemistry/genetics/physiology ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; RNA Interference ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Seasons ; Transcription, Genetic ; Triticum/*genetics/*growth & development
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Genomics. Beyond nature and nurture (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robinson, Gene E -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):397-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology and Neuroscience Program, University of Illinois, Urbana, IL 61801, USA. generobi@life.uiuc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arvicolinae/genetics/physiology ; *Behavior, Animal ; Brain/*metabolism ; Cyclic GMP-Dependent Protein Kinases/genetics/metabolism ; Drosophila melanogaster/genetics/physiology ; *Environment ; Epigenesis, Genetic ; Feeding Behavior ; Gene Expression ; *Genetics, Behavioral ; Maternal Behavior ; Polymorphism, Genetic ; Rats ; Receptors, Glucocorticoid/genetics/metabolism ; Receptors, Vasopressin/genetics/metabolism ; Sexual Behavior, Animal ; Stress, Physiological/genetics/physiopathology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    Structural biology. Voltage sensor meets lipid membrane (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackinnon, Roderick -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1304-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, New York, NY 10021, USA. mackinn@rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550651" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry ; Crystallography, X-Ray ; *Ion Channel Gating ; *Lipid Bilayers ; Membrane Lipids/*chemistry ; Models, Molecular ; Potassium Channels, Voltage-Gated/*chemistry/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Minimal machinery of RNA polymerase holoenzyme sufficient for promoter melting (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-28
    Description: We determined the minimal portion of Escherichia coli RNA polymerase (RNAP) holoenzyme able to accomplish promoter melting, the crucial step in transcription initiation that provides RNAP access to the template strand. Upon duplex DNA binding, the N terminus of the beta' subunit (amino acids 1 to 314) and amino acids 94 to 507 of the sigma subunit, together comprising less than one-fifth of RNAP holoenzyme, were able to melt an extended -10 promoter in a reaction remarkably similar to that of authentic holoenzyme. Our results support the model that capture of nontemplate bases extruded from the DNA helix underlies the melting process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, Brian A -- Gruber, Tanja M -- Gross, Carol A -- GM 57755/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1382-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Stomatology and Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14988563" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Bacterial/chemistry/genetics/*metabolism ; DNA, Superhelical/chemistry/genetics/metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Escherichia coli/*enzymology/*genetics ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Tertiary ; Sigma Factor/chemistry/*metabolism ; Templates, Genetic ; Transcription, Genetic ; Zinc Fingers
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    TAF1 activates transcription by phosphorylation of serine 33 in histone H2B (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-15
    Description: Dynamic changes in chromatin structure, induced by posttranslational modification of histones, play a fundamental role in regulating eukaryotic transcription. Here we report that histone H2B is phosphorylated at evolutionarily conserved Ser33 (H2B-S33) by the carboxyl-terminal kinase domain (CTK) of the Drosophila TFIID subunit TAF1. Phosphorylation of H2B-S33 at the promoter of the cell cycle regulatory gene string and the segmentation gene giant coincides with transcriptional activation. Elimination of TAF1 CTK activity in Drosophila cells and embryos reduces transcriptional activation and phosphorylation of H2B-S33. These data reveal that H2B-S33 is a physiological substrate for the TAF1 CTK and that H2B-S33 phosphorylation is essential for transcriptional activation events that promote cell cycle progression and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maile, Tobias -- Kwoczynski, Simona -- Katzenberger, Rebeccah J -- Wassarman, David A -- Sauer, Frank -- GM066204-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 May 14;304(5673):1010-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California-Riverside, Riverside, CA 95121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15143281" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cell Cycle ; Cell Cycle Proteins ; DNA-Binding Proteins/genetics ; Drosophila/embryology/*genetics/metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Embryo, Nonmammalian/physiology ; Genes, Insect ; Histone Acetyltransferases ; Histones/chemistry/*metabolism ; Homeodomain Proteins/genetics ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Phosphoserine/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/genetics ; RNA Interference ; Recombinant Proteins/chemistry/metabolism ; Repressor Proteins/genetics ; TATA-Binding Protein Associated Factors ; Transcription Factor TFIID/chemistry/genetics/*metabolism ; Transcription Factors ; *Transcription, Genetic ; *Transcriptional Activation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Biochemistry. Oily barbarians breach ion channel gates (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hilgemann, Donald W -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):223-4. Epub 2004 Mar 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Texas Southwestern, Dallas, TX 75235, USA. donald.hilgemann@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15031439" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Eicosanoic Acids/*metabolism/pharmacology ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers ; Membrane Lipids/*metabolism ; Micelles ; Models, Biological ; Phosphatidylinositol 4,5-Diphosphate/*metabolism/pharmacology ; Potassium Channels, Voltage-Gated/*chemistry/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Signal Transduction ; Sodium-Calcium Exchanger/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Engineering peak performance (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Adrian -- New York, N.Y. -- Science. 2004 Jul 30;305(5684):643-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15286364" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomechanical Phenomena ; *Engineering ; History, 20th Century ; History, 21st Century ; Humans ; Mathematics ; Mechanics ; Physics ; Research Support as Topic ; *Sports ; *Sports Equipment ; United States
    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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    Profile: Rajan Gupta (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malakoff, David -- New York, N.Y. -- Science. 2004 May 28;304(5675):1281.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166361" target="_blank"〉PubMed〈/a〉
    Keywords: Career Choice ; Emigration and Immigration ; History, 20th Century ; History, 21st Century ; India ; Physics ; Public Health ; United States
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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