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  • Articles  (1,606)
  • Rats  (982)
  • Time Factors  (357)
  • Protein Conformation  (332)
  • American Association for the Advancement of Science (AAAS)  (1,606)
  • Annual Reviews
  • 2000-2004  (786)
  • 1980-1984  (820)
  • 1965-1969
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  • Articles  (1,606)
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  • American Association for the Advancement of Science (AAAS)  (1,606)
  • Annual Reviews
  • Springer  (15)
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  • 1
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    Enzymology. A moving story (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907122/" 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/PMC3907122/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falke, Joseph J -- R01 GM040731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1480-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biophysics Program and the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA. falke@colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859184" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry ; Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Nitrogen/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermodynamics
    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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    Cancer. BRCA2 enters the fray (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, John H -- Elledge, Stephen J -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1822-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228708" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BRCA1 Protein/metabolism ; BRCA2 Protein/*chemistry/*metabolism ; Binding Sites ; Breast Neoplasms/genetics ; Crystallography, X-Ray ; DNA/*metabolism ; DNA Damage ; *DNA Repair ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/metabolism ; Female ; Genes, BRCA1 ; Genes, BRCA2 ; Genetic Predisposition to Disease ; Humans ; Mice ; Ovarian Neoplasms/genetics ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rad51 Recombinase ; Rats ; Recombination, Genetic ; Replication Protein A
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Control of synaptic strength by glial TNFalpha (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: Activity-dependent modulation of synaptic efficacy in the brain contributes to neural circuit development and experience-dependent plasticity. Although glia are affected by activity and ensheathe synapses, their influence on synaptic strength has largely been ignored. Here, we show that a protein produced by glia, tumor necrosis factor alpha (TNFalpha), enhances synaptic efficacy by increasing surface expression of AMPA receptors. Preventing the actions of endogenous TNFalpha has the opposite effects. Thus, the continual presence of TNFalpha is required for preservation of synaptic strength at excitatory synapses. Through its effects on AMPA receptor trafficking, TNFalpha may play roles in synaptic plasticity and modulating responses to neural injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beattie, Eric C -- Stellwagen, David -- Morishita, Wade -- Bresnahan, Jacqueline C -- Ha, Byeong Keun -- Von Zastrow, Mark -- Beattie, Michael S -- Malenka, Robert C -- DA00439/DA/NIDA NIH HHS/ -- MH063394/MH/NIMH NIH HHS/ -- NS 31193/NS/NINDS NIH HHS/ -- NS38079/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nancy Pritzker Laboratory, Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, Palo Alto, CA 94304, USA. beattie.2@osu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/pharmacology ; Astrocytes/*metabolism ; Cells, Cultured ; Culture Media, Conditioned/pharmacology ; Gene Expression Regulation/drug effects ; Hippocampus/cytology/metabolism ; Neuronal Plasticity/drug effects ; Neurons/drug effects/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/metabolism ; Receptors, Tumor Necrosis Factor ; Receptors, Tumor Necrosis Factor, Type I ; Synapses/drug effects/*metabolism ; Synaptic Transmission/drug effects ; Tumor Necrosis Factor-alpha/antagonists & inhibitors/*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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  • 4
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    Visualization and functional analysis of RNA-dependent RNA polymerase lattices (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Positive-strand RNA viruses such as poliovirus replicate their genomes on intracellular membranes of their eukaryotic hosts. Electron microscopy has revealed that purified poliovirus RNA-dependent RNA polymerase forms planar and tubular oligomeric arrays. The structural integrity of these arrays correlates with cooperative RNA binding and RNA elongation and is sensitive to mutations that disrupt intermolecular contacts predicted by the polymerase structure. Membranous vesicles isolated from poliovirus-infected cells contain structures consistent with the presence of two-dimensional polymerase arrays on their surfaces during infection. Therefore, host cytoplasmic membranes may function as physical foundations for two-dimensional polymerase arrays, conferring the advantages of surface catalysis to viral RNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyle, John M -- Bullitt, Esther -- Bienz, Kurt -- Kirkegaard, Karla -- AI-42119/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2218-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, 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/12077417" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Inclusion Bodies, Viral/metabolism/ultrastructure ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Poliovirus/*enzymology/physiology ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; RNA Replicase/*chemistry/isolation & purification/*metabolism/ultrastructure ; RNA, Viral/biosynthesis/*metabolism ; Viral Core Proteins/metabolism ; Virus Replication
    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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  • 5
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    Disrupted timing of discontinuous but not continuous movements by cerebellar lesions (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-31
    Description: Patients with cerebellar damage are known to exhibit deficits in the temporal control of movements. We report that these deficits are restricted to discontinuous movements. Cerebellar patients exhibited no deficit in temporal variability when producing continuous, rhythmic movements. We hypothesize that the temporal properties of continuous movements are emergent and reflect the operation of other control parameters not associated with the cerebellum. In contrast, discontinuous movements require an explicit representation of the temporal goal, a function of the cerebellum. The requirement for explicit temporal representation provides a parsimonious account of cerebellar involvement in a range of tasks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spencer, Rebecca M C -- Zelaznik, Howard N -- Diedrichsen, Jorn -- Ivry, Richard B -- NS17778/NS/NINDS NIH HHS/ -- NS30256/NS/NINDS NIH HHS/ -- NS40813/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 May 30;300(5624):1437-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, University of California, Berkeley, 3210 Tolman Hall #1650, Berkeley, CA 94720, USA. rspencer@socrates.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12775842" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Aged, 80 and over ; Cerebellar Diseases/*physiopathology ; Cerebellum/physiology/*physiopathology ; Female ; Humans ; Male ; Middle Aged ; *Motor Activity ; Movement ; *Psychomotor Performance ; Spinocerebellar Degenerations/*physiopathology ; 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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  • 6
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    Sustaining fisheries yields over evolutionary time scales (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-06
    Description: Fishery management plans ignore the potential for evolutionary change in harvestable biomass. We subjected populations of an exploited fish (Menidia menidia) to large, small, or random size-selective harvest of adults over four generations. Harvested biomass evolved rapidly in directions counter to the size-dependent force of fishing mortality. Large-harvested populations initially produced the highest catch but quickly evolved a lower yield than controls. Small-harvested populations did the reverse. These shifts were caused by selection of genotypes with slower or faster rates of growth. Management tools that preserve natural genetic variation are necessary for long-term sustainable yield.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conover, David O -- Munch, Stephan B -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Marine Sciences Research Center, State University of New York, Stony Brook, NY 11794-5000, USA. dconover@notes.cc.sunysb.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12098697" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Biomass ; Body Constitution ; Body Weight ; Conservation of Natural Resources ; *Fisheries ; Fishes/anatomy & histology/*genetics/*growth & development ; Genetic Variation ; Population Dynamics ; Regression Analysis ; *Selection, Genetic ; Time Factors
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  • 7
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    Casting metal nanowires within discrete self-assembled peptide nanotubes (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-26
    Description: Tubular nanostructures are suggested to have a wide range of applications in nanotechnology. We report our observation of the self-assembly of a very short peptide, the Alzheimer's beta-amyloid diphenylalanine structural motif, into discrete and stiff nanotubes. Reduction of ionic silver within the nanotubes, followed by enzymatic degradation of the peptide backbone, resulted in the production of discrete nanowires with a long persistence length. The same dipeptide building block, made of D-phenylalanine, resulted in the production of enzymatically stable nanotubes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reches, Meital -- Gazit, Ehud -- New York, N.Y. -- Science. 2003 Apr 25;300(5619):625-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12714741" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Amyloid beta-Peptides/chemistry ; Biosensing Techniques ; Birefringence ; Dipeptides/*chemistry ; Microscopy, Electron ; Microscopy, Electron, Scanning ; Molecular Sequence Data ; *Nanotechnology ; Oxidation-Reduction ; Protein Conformation ; Silver ; Solubility ; Spectroscopy, Fourier Transform Infrared
    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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  • 8
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    Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-19
    Description: Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Abeta peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kayed, Rakez -- Head, Elizabeth -- Thompson, Jennifer L -- McIntire, Theresa M -- Milton, Saskia C -- Cotman, Carl W -- Glabe, Charles G -- AG00538/AG/NIA NIH HHS/ -- AG16573/AG/NIA NIH HHS/ -- NS31230/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 18;300(5618):486-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12702875" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Alzheimer Disease/metabolism/pathology ; Amyloid/chemistry/toxicity ; Amyloid beta-Peptides/analysis/*chemistry/immunology/toxicity ; Animals ; Antibodies/immunology ; Antibody Specificity ; Biopolymers/analysis/chemistry/toxicity ; Brain/pathology ; Brain Chemistry ; Cell Survival ; Humans ; Microscopy, Confocal ; Microscopy, Electron ; Molecular Mimicry ; Neurofibrillary Tangles/chemistry ; Peptide Fragments/chemistry/immunology ; Protein Conformation ; Rabbits ; Solubility ; Tumor Cells, Cultured
    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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    Parkinson's disease. Coincidence or connection? (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, Richard -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):451-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964452" target="_blank"〉PubMed〈/a〉
    Keywords: Canada/epidemiology ; Cluster Analysis ; Environmental Exposure/adverse effects ; *Famous Persons ; Female ; History, 21st Century ; Humans ; Male ; Parkinson Disease/*epidemiology/etiology ; *Television ; Time Factors ; Virus Diseases/complications/epidemiology
    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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    Coordinated reactivation of distributed memory traces in primate neocortex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-21
    Description: Conversion of new memories into a lasting form may involve the gradual refinement and linking together of neural representations stored widely throughout neocortex. This consolidation process may require coordinated reactivation of distributed components of memory traces while the cortex is "offline," i.e., not engaged in processing external stimuli. Simultaneous neural ensemble recordings from four sites in the macaque neocortex revealed such coordinated reactivation. In motor, somatosensory, and parietal cortex (but not prefrontal cortex), the behaviorally induced correlation structure and temporal patterning of neural ensembles within and between regions were preserved, confirming a major tenet of the trace-reactivation theory of memory consolidation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, K L -- McNaughton, B L -- MH01565/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2070-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neural Systems, Memory, and Aging, University of Arizona, Tucson, AZ 85724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242447" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Cues ; Electrodes, Implanted ; Macaca mulatta ; Male ; Memory/*physiology ; Mental Recall/*physiology ; Motor Cortex/physiology ; Neocortex/*physiology ; Neurons/*physiology ; Parietal Lobe/physiology ; Prefrontal Cortex/physiology ; Somatosensory Cortex/physiology ; 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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  • 11
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    Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-12
    Description: Direct interaction between platelet receptor glycoprotein Ibalpha (GpIbalpha) and thrombin is required for platelet aggregation and activation at sites of vascular injury. Abnormal GpIbalpha-thrombin binding is associated with many pathological conditions,including occlusive arterial thrombosis and bleeding disorders. The crystal structure of the GpIbalpha-thrombin complex at 2.6 angstrom resolution reveals simultaneous interactions of GpIbalpha with exosite I of one thrombin molecule,and with exosite II of a second thrombin molecule. In the crystal lattice,the periodic arrangement of GpIbalpha-thrombin complexes mirrors a scaffold that could serve as a driving force for tight platelet adhesion. The details of these interactions reconcile GpIbalpha-thrombin binding modes that are presently controversial,highlighting two distinct interfaces that are potential targets for development of novel antithrombotic drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dumas, John J -- Kumar, Ravindra -- Seehra, Jasbir -- Somers, William S -- Mosyak, Lidia -- New York, N.Y. -- Science. 2003 Jul 11;301(5630):222-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical and Screening Sciences, Wyeth, 200 Cambridge Park Drive, Cambridge, MA 02140, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12855811" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Blood Platelets/chemistry/physiology ; Crystallization ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Platelet Adhesiveness ; *Platelet Aggregation ; Platelet Glycoprotein GPIb-IX Complex/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thrombin/*chemistry/*metabolism
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  • 12
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    Ecology. New count of old whales adds up to big debate (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lubick, Naomi -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):451.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12881542" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atlantic Ocean ; Conservation of Natural Resources ; DNA, Mitochondrial/genetics ; *Ecosystem ; Female ; Genetic Variation ; Genetics, Population ; Male ; Mutation ; Population Density ; Population Dynamics ; Time Factors ; *Whales/genetics
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  • 13
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    Cylindrical channels from concave helices (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Calladine, C R -- Pratap, V -- Chandran, V -- Mizuguchi, K -- Luisi, B F -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):661-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12561825" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; Escherichia coli Proteins/*chemistry ; Glycine/chemistry ; Ion Channels/*chemistry ; *Models, Molecular ; Protein Conformation ; Protein Structure, Secondary
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  • 14
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    Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-06
    Description: We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor.diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naber, Nariman -- Minehardt, Todd J -- Rice, Sarah -- Chen, Xiaoru -- Grammer, Jean -- Matuska, Marija -- Vale, Ronald D -- Kollman, Peter A -- Car, Roberto -- Yount, Ralph G -- Cooke, Roger -- Pate, Edward -- AR39643/AR/NIAMS NIH HHS/ -- AR42895/AR/NIAMS NIH HHS/ -- DK05915/DK/NIDDK NIH HHS/ -- GM29072/GM/NIGMS NIH HHS/ -- RR1081/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2003 May 2;300(5620):798-801.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California, San Francisco, CA 94143, USA. naber@itsa.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12730601" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/*metabolism ; Adenosine Diphosphate/analogs & derivatives/metabolism ; Adenosine Triphosphate/analogs & derivatives/metabolism ; Animals ; Binding Sites ; Computer Simulation ; Crystallography, X-Ray ; *Drosophila Proteins ; Drosophila melanogaster ; Electron Spin Resonance Spectroscopy ; Humans ; Hydrogen Bonding ; Hydrolysis ; Kinesin/*chemistry/*metabolism ; Microtubules/*metabolism ; Models, Molecular ; Molecular Motor Proteins/*chemistry/*metabolism ; Molecular Probes/metabolism ; Protein Conformation ; Spin Labels
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  • 15
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    Whales before whaling in the North Atlantic (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-26
    Description: It is well known that hunting dramatically reduced all baleen whale populations, yet reliable estimates of former whale abundances are elusive. Based on coalescent models for mitochondrial DNA sequence variation, the genetic diversity of North Atlantic whales suggests population sizes of approximately 240,000 humpback, 360,000 fin, and 265,000 minke whales. Estimates for fin and humpback whales are far greater than those previously calculated for prewhaling populations and 6 to 20 times higher than present-day population estimates. Such discrepancies suggest the need for a quantitative reevaluation of historical whale populations and a fundamental revision in our conception of the natural state of the oceans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roman, Joe -- Palumbi, Stephen R -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):508-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organismic and Evolutionary Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12881568" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atlantic Ocean ; Base Sequence ; Conservation of Natural Resources ; DNA, Mitochondrial/genetics ; *Ecosystem ; Female ; Genetic Variation ; Genetics, Population ; Male ; Molecular Sequence Data ; Population Density ; Population Dynamics ; Time Factors ; *Whales/classification/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Structural biology. Complex II is complex too (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hederstedt, Lars -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):671-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Organism Biology, Lund University, SE-22362 Lund, Sweden. lars.hederstedt@cob.lu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560540" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Anaerobiosis ; Binding Sites ; Crystallography, X-Ray ; Electron Transport ; Electron Transport Complex II ; Escherichia coli/*enzymology ; Flavin-Adenine Dinucleotide/metabolism ; Heme/chemistry/metabolism ; Models, Molecular ; Multienzyme Complexes/antagonists & inhibitors/*chemistry/*metabolism ; Oxidation-Reduction ; Oxidoreductases/antagonists & inhibitors/*chemistry/*metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Reactive Oxygen Species/metabolism ; Succinate Dehydrogenase/antagonists & inhibitors/*chemistry/*metabolism ; Succinic Acid/metabolism ; Ubiquinone/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Planetary Science. A-roving we will go, slowly (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2003 Sep 26;301(5641):1834.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14512597" target="_blank"〉PubMed〈/a〉
    Keywords: Extraterrestrial Environment ; *Mars ; Space Flight ; *Spacecraft ; Time Factors
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  • 18
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    Genomics. Molecular prodigality (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bray, Dennis -- New York, N.Y. -- Science. 2003 Feb 21;299(5610):1189-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Cambridge CB2 3EJ, UK. d.bray@zoo.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12595679" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Antibody Diversity ; Escherichia coli Proteins/chemistry/genetics/metabolism ; Evolution, Molecular ; Genetic Variation ; Genomics ; Histones/chemistry/genetics/metabolism ; Humans ; Methylation ; Phenotype ; Potassium Channels/chemistry/genetics/metabolism ; Protein Conformation ; Protein Isoforms/chemistry/metabolism ; Protein Processing, Post-Translational ; Proteins/*chemistry/genetics/*metabolism ; Proteomics ; RNA Splicing ; Receptors, Cell Surface/chemistry/genetics/metabolism ; Selection, Genetic ; Troponin T/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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  • 19
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    Demography of dietary restriction and death in Drosophila (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-23
    Description: Dietary restriction (DR) increases life-span in organisms from yeast to mammals, presumably by slowing the accumulation of aging-related damage. Here we show that in Drosophila, DR extends life-span entirely by reducing the short-term risk of death. Two days after the application of DR at any age for the first time, previously fully fed flies are no more likely to die than flies of the same age that have been subjected to long-term DR. DR of mammals may also reduce short-term risk of death, and hence DR instigated at any age could generate a full reversal of mortality.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mair, William -- Goymer, Patrick -- Pletcher, Scott D -- Partridge, Linda -- New York, N.Y. -- Science. 2003 Sep 19;301(5640):1731-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14500985" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Animals ; *Caloric Restriction ; Demography ; *Diet ; Drosophila/*physiology ; Female ; *Longevity ; Male ; Mortality ; Reproduction ; Risk ; Temperature ; Time Factors
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  • 20
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    From anchovies to sardines and back: multidecadal change in the Pacific Ocean (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-11
    Description: In the Pacific Ocean, air and ocean temperatures, atmospheric carbon dioxide, landings of anchovies and sardines, and the productivity of coastal and open ocean ecosystems have varied over periods of about 50 years. In the mid-1970s, the Pacific changed from a cool "anchovy regime" to a warm "sardine regime." A shift back to an anchovy regime occurred in the middle to late 1990s. These large-scale, naturally occurring variations must be taken into account when considering human-induced climate change and the management of ocean living resources.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chavez, Francisco P -- Ryan, John -- Lluch-Cota, Salvador E -- Niquen C, Miguel -- New York, N.Y. -- Science. 2003 Jan 10;299(5604):217-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monterey Bay Aquarium Research Institute, 7700 Sandholdt Road, Moss Landing, CA 95039, USA. chfr@mbari.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12522241" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atmosphere ; Birds ; Carbon Dioxide ; *Climate ; *Ecosystem ; *Fishes ; Pacific Ocean ; *Seawater ; Temperature ; Time Factors
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  • 21
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    Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-10
    Description: Multidrug efflux pumps cause serious problems in cancer chemotherapy and treatment of bacterial infections. Yet high-resolution structures of ligand transporter complexes have previously been unavailable. We obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands. The structures show that three molecules of ligands bind simultaneously to the extremely large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions. Each ligand uses a slightly different subset of AcrB residues for binding. The bound ligand molecules often interact with each other, stabilizing the binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Edward W -- McDermott, Gerry -- Zgurskaya, Helen I -- Nikaido, Hiroshi -- Koshland, Daniel E Jr -- AI 09644/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2003 May 9;300(5621):976-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738864" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Infective Agents/chemistry/metabolism ; Anti-Infective Agents, Local/chemistry/metabolism ; Binding Sites ; Carrier Proteins/*chemistry/isolation & purification/*metabolism ; Cell Membrane/chemistry ; Chemistry, Physical ; Ciprofloxacin/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Dequalinium/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/isolation & purification/*metabolism ; Ethidium/chemistry/metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Membrane Proteins/*chemistry/isolation & purification/*metabolism ; Models, Molecular ; Multidrug Resistance-Associated Proteins ; Physicochemical Phenomena ; Protein Binding ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rhodamines/chemistry/metabolism ; Static Electricity
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  • 22
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    Facilitation of spinal NMDA receptor currents by spillover of synaptically released glycine (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-28
    Description: In the mammalian CNS, N-methyl-D-aspartate (NMDA) receptors serve prominent roles in many physiological and pathophysiological processes including pain transmission. For full activation, NMDA receptors require the binding of glycine. It is not known whether the brain uses changes in extracellular glycine to modulate synaptic NMDA responses. Here, we show that synaptically released glycine facilitates NMDA receptor currents in the superficial dorsal horn, an area critically involved in pain processing. During high presynaptic activity, glycine released from inhibitory interneurons escapes the synaptic cleft and reaches nearby NMDA receptors by so-called spillover. In vivo, this process may contribute to the development of inflammatory hyperalgesia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahmadi, Seifollah -- Muth-Selbach, Uta -- Lauterbach, Andreas -- Lipfert, Peter -- Neuhuber, Winfried L -- Zeilhofer, Hanns Ulrich -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2094-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Experimentelle und Klinische Pharmakologie und Toxikologie, Universitat Erlangen-Nurnberg, Fahrstrasse 17, D-91054 Erlangen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829784" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesics/pharmacology ; Animals ; Anterior Horn Cells/drug effects/metabolism ; Diffusion ; Electric Stimulation ; Evoked Potentials/drug effects ; Excitatory Postsynaptic Potentials/drug effects ; Glycine/*metabolism/pharmacology ; In Vitro Techniques ; Interneurons/metabolism ; Neural Inhibition/drug effects ; Opioid Peptides/pharmacology ; Pain Measurement ; Patch-Clamp Techniques ; Posterior Horn Cells/drug effects/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Serine/pharmacology ; Spinal Cord/drug effects/metabolism ; Synapses/*metabolism ; *Synaptic Transmission/drug effects ; Temperature
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  • 23
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    Derepression of BDNF transcription involves calcium-dependent phosphorylation of MeCP2 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-01
    Description: Mutations in MeCP2, which encodes a protein that has been proposed to function as a global transcriptional repressor, are the cause of Rett syndrome (RT T), an X-linked progressive neurological disorder. Although the selective inactivation of MeCP2 in neurons is sufficient to confer a Rett-like phenotype in mice, the specific functions of MeCP2 in postmitotic neurons are not known. We find that MeCP2 binds selectively to BDNF promoter III and functions to repress expression of the BDNF gene. Membrane depolarization triggers the calcium-dependent phosphorylation and release of MeCP2 from BDNF promoter III, thereby facilitating transcription. These studies indicate that MeCP2 plays a key role in the control of neuronal activity-dependent gene regulation and suggest that the deregulation of this process may underlie the pathology of RT T.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wen G -- Chang, Qiang -- Lin, Yingxi -- Meissner, Alexander -- West, Anne E -- Griffith, Eric C -- Jaenisch, Rudolf -- Greenberg, Michael E -- HD 18655/HD/NICHD NIH HHS/ -- NS28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):885-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children'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/14593183" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/*genetics ; Calcium/*metabolism ; Cell Membrane/physiology ; Cells, Cultured ; *Chromosomal Proteins, Non-Histone ; Cloning, Molecular ; CpG Islands ; DNA Methylation ; DNA-Binding Proteins/*metabolism ; Electrophoretic Mobility Shift Assay ; *Gene Expression Regulation ; Gene Silencing ; Histones/metabolism ; Methyl-CpG-Binding Protein 2 ; Methylation ; Mice ; Mice, Knockout ; Neurons/metabolism/physiology ; Phosphorylation ; Potassium Chloride/pharmacology ; Precipitin Tests ; Promoter Regions, Genetic ; Rats ; *Repressor Proteins ; Rett Syndrome/genetics ; *Transcription, Genetic
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  • 24
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    Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-23
    Description: Although critical for development, immunity, wound healing, and metastasis, integrins represent one of the few classes of plasma membrane receptors for which the basic signaling mechanism remains a mystery. We investigated cytoplasmic conformational changes in the integrin LFA-1 (alphaLbeta2) in living cells by measuring fluorescence resonance energy transfer between cyan fluorescent protein-fused and yellow fluorescent protein-fused alphaL and beta2 cytoplasmic domains. In the resting state these domains were close to each other, but underwent significant spatial separation upon either intracellular activation of integrin adhesiveness (inside-out signaling) or ligand binding (outside-in signaling). Thus, bidirectional integrin signaling is accomplished by coupling extracellular conformational changes to an unclasping and separation of the alpha and beta cytoplasmic domains, a distinctive mechanism for transmitting information across the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Minsoo -- Carman, Christopher V -- Springer, Timothy A -- CA31798/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 19;301(5640):1720-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CBR Institute for Biomedical Research, Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14500982" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Antigens, CD11a/*chemistry ; Antigens, CD18/*chemistry ; Bacterial Proteins ; Cell Adhesion ; Cell Membrane/*metabolism ; Chemokine CXCL12 ; Chemokines, CXC/metabolism ; Cytoplasm/*chemistry ; Dimerization ; Fluorescence Resonance Energy Transfer ; Green Fluorescent Proteins ; Humans ; Intercellular Adhesion Molecule-1/metabolism ; Ligands ; Luminescent Proteins ; Lymphocyte Function-Associated Antigen-1/chemistry/*metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, CXCR4/metabolism ; Recombinant Fusion Proteins/chemistry ; *Signal Transduction ; Talin/chemistry/metabolism ; Transfection ; Tumor Cells, Cultured
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  • 25
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    Experience strengthening transmission by driving AMPA receptors into synapses (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-08
    Description: The mechanisms underlying experience-dependent plasticity in the brain may depend on the AMPA subclass of glutamate receptors (AMPA-Rs). We examined the trafficking of AMPA-Rs into synapses in the developing rat barrel cortex. In vivo gene delivery was combined with in vitro recordings to show that experience drives recombinant GluR1, an AMPA-R subunit, into synapses formed between layer 4 and layer 2/3 neurons. Moreover, expression of the GluR1 cytoplasmic tail, a construct that inhibits synaptic delivery of endogenous AMPA-Rs during long-term potentiation, blocked experience-driven synaptic potentiation. In general, synaptic incorporation of AMPA-Rs in vivo conforms to rules identified in vitro and contributes to plasticity driven by natural stimuli in the mammalian brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, Takuya -- Svoboda, Karel -- Malinow, Roberto -- NS032827/NS/NINDS NIH HHS/ -- NS038259/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Mar 7;299(5612):1585-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jones Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12624270" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electrophysiology ; Gene Transfer Techniques ; Long-Term Potentiation ; *Neuronal Plasticity ; Neurons/*metabolism/virology ; Patch-Clamp Techniques ; Rats ; Receptors, AMPA/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sindbis Virus/genetics ; Somatosensory Cortex/*metabolism/virology ; Synapses/*metabolism ; *Synaptic Transmission ; Touch ; Vibrissae/physiology
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  • 26
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    A mutation in the C. elegans EXP-2 potassium channel that alters feeding behavior (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: The nematode pharynx has a potassium channel with unusual properties, which allows the muscles to repolarize quickly and with the proper delay. Here, the Caenorhabditis elegans exp-2 gene is shown to encode this channel. EXP-2 is a Kv-type (voltage-activated) potassium channel that has inward-rectifying properties resembling those of the structurally dissimilar human ether-a-go-go-related gene (HERG) channel. Null and gain-of-function mutations affect pharyngeal muscle excitability in ways that are consistent with the electrophysiological behavior of the channel, and thereby demonstrate a direct link between the kinetics of this unusual channel and behavior.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791429/" 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/PMC3791429/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, M W -- Fleischhauer, R -- Dent, J A -- Joho, R H -- Avery, L -- HL46154/HL/NHLBI NIH HHS/ -- NS28407/NS/NINDS NIH HHS/ -- R01 HL046154/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2501-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148, USA. wdavis@biology.utah.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617464" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Feeding Behavior ; Genes, Helminth ; Genes, Reporter ; Ion Channel Gating ; Kinetics ; Membrane Potentials ; Models, Molecular ; Muscles/metabolism ; Mutation ; Neurons/metabolism ; Oocytes/metabolism ; Pharyngeal Muscles/physiology ; Potassium Channels/chemistry/genetics/*physiology ; Protein Conformation ; RNA, Complementary/genetics ; Recombinant Fusion Proteins/biosynthesis ; Xenopus laevis
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    Molecular biology. Cancer fighter's modus operandi revealed (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-30
    Description: Researchers have deciphered how a promising cancer drug acts like a smart bomb, homing in on only a very narrow range of its potential targets in the cell. The compound, known as STI-571, has shown remarkable success in early clinical trials on patients with chronic myelogenous leukemia. Now, in work reported on page 1938, scientists reveal just how the compound works--information that could aid in the design of similar cancer therapies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1857-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11012350" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/chemistry/*therapeutic use ; Benzamides ; Catalytic Domain/drug effects ; Clinical Trials as Topic ; Enzyme Activation/drug effects ; Enzyme Inhibitors/therapeutic use ; Humans ; Imatinib Mesylate ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/*drug therapy/enzymology ; *Piperazines ; Protein Conformation ; Protein-Tyrosine Kinases/antagonists & inhibitors/chemistry ; Proto-Oncogene Proteins c-abl/*antagonists & inhibitors ; Pyrimidines/chemistry/*therapeutic use
    Print ISSN: 0036-8075
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  • 28
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    A structural model of transcription elongation (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-01
    Description: The path of the nucleic acids through a transcription elongation complex was tracked by mapping cross-links between bacterial RNA polymerase (RNAP) and transcript RNA or template DNA onto the x-ray crystal structure. In the resulting model, the downstream duplex DNA is nestled in a trough formed by the beta' subunit and enclosed on top by the beta subunit. In the RNAP channel, the RNA/DNA hybrid extends from the enzyme active site, along a region of the beta subunit harboring rifampicin resistance mutations, to the beta' subunit "rudder." The single-stranded RNA is then extruded through another channel formed by the beta-subunit flap domain. The model provides insight into the functional properties of the transcription complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korzheva, N -- Mustaev, A -- Kozlov, M -- Malhotra, A -- Nikiforov, V -- Goldfarb, A -- Darst, S A -- GM30717/GM/NIGMS NIH HHS/ -- GM49242/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):619-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Public Health Research Institute, 455 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10915625" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cross-Linking Reagents ; Crystallography, X-Ray ; DNA/chemistry/genetics/*metabolism ; DNA Primers ; DNA-Directed RNA Polymerases/*chemistry/genetics/metabolism ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligoribonucleotides/chemistry/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Messenger/chemistry/genetics/*metabolism ; Templates, Genetic ; Thermus/enzymology ; *Transcription, Genetic
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    Neuroscience. Early insult rewires pain circuits (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-12
    Description: On page 628, neuroscientists report that painful stimuli delivered to rats shortly after birth permanently rewire the spinal cord circuits that respond to pain. Not only do the circuits contain more axons, but the axons extend to more areas of the spinal cord than they normally would. The results should help convince skeptics of the importance of managing pain in human infants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Helmuth, L -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):521-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10939955" target="_blank"〉PubMed〈/a〉
    Keywords: Afferent Pathways ; Aging ; Animals ; Animals, Newborn ; Axons/*physiology ; Hindlimb/innervation ; Humans ; Infant, Newborn ; Inflammation/physiopathology ; *Pain ; Pain Threshold ; Rats ; Sciatic Nerve/*anatomy & histology/physiology ; Spinal Cord/*cytology
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    Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-15
    Description: Murine T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain gammadelta T cell receptors (TCRs) in the absence of other components. The crystal structure of T22b at 3.1 angstroms reveals similarities to MHC class I molecules, but one side of the normal peptide-binding groove is severely truncated, which allows direct access to the beta-sheet floor. Potential gammadelta TCR-binding sites can be inferred from functional mapping of T10 and T22 point mutants and allelic variants. Thus, T22 represents an unusual variant of the MHC-like fold and indicates that gammadelta and alphabeta TCRs interact differently with their respective MHC ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wingren, C -- Crowley, M P -- Degano, M -- Chien, Y -- Wilson, I A -- AI33431/AI/NIAID NIH HHS/ -- CA58896/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):310-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute for Chemical 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/10634787" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Substitution ; Animals ; Binding Sites ; Crystallography, X-Ray ; Glycosylation ; Histocompatibility Antigens Class I/*chemistry ; Hydrogen Bonding ; Ligands ; Mice ; Models, Molecular ; Point Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry/immunology/metabolism ; Receptors, Antigen, T-Cell, gamma-delta/immunology/*metabolism ; Surface Properties ; beta 2-Microglobulin/chemistry
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    Hierarchical self-assembly of F-actin and cationic lipid complexes: stacked three-layer tubule networks (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-17
    Description: We describe a distinct type of spontaneous hierarchical self-assembly of cytoskeletal filamentous actin (F-actin), a highly charged polyelectrolyte, and cationic lipid membranes. On the mesoscopic length scale, confocal microscopy reveals ribbonlike tubule structures that connect to form a network of tubules on the macroscopic scale (more than 100 micrometers). Within the tubules, on the 0.5- to 50-nanometer length scale, x-ray diffraction reveals an unusual structure consisting of osmotically swollen stacks of composite membranes with no direct analog in simple amphiphilic systems. The composite membrane is composed of three layers, a lipid bilayer sandwiched between two layers of actin, and is reminiscent of multilayered bacterial cell walls that exist far from equilibrium. Electron microscopy reveals that the actin layer consists of laterally locked F-actin filaments forming an anisotropic two-dimensional tethered crystal that appears to be the origin of the tubule formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G C -- Tang, J X -- Lin, A -- Li, Y -- Janmey, P A -- Safinya, C R -- AR38910/AR/NIAMS NIH HHS/ -- GM59288/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 16;288(5473):2035-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Materials Department, University of California, Santa Barbara, CA 93106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10856215" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*chemistry/ultrastructure ; Anisotropy ; Cations ; Crystallization ; Electrochemistry ; Electrolytes ; Fatty Acids, Monounsaturated/chemistry ; Freeze Fracturing ; Lipid Bilayers/*chemistry ; Microscopy, Confocal ; Microscopy, Electron ; Molecular Conformation ; Protein Conformation ; Quaternary Ammonium Compounds/chemistry ; X-Ray Diffraction
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    Reversal of antipsychotic-induced working memory deficits by short-term dopamine D1 receptor stimulation (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-03-17
    Description: Chronic blockade of dopamine D2 receptors, a common mechanism of action for antipsychotic drugs, down-regulates D1 receptors in the prefrontal cortex and, as shown here, produces severe impairments in working memory. These deficits were reversed in monkeys by short-term coadministration of a D1 agonist, ABT 431, and this improvement was sustained for more than a year after cessation of D1 treatment. These findings indicate that pharmacological modulation of the D1 signaling pathway can produce long-lasting changes in functional circuits underlying working memory. Resetting this pathway by brief exposure to the agonist may provide a valuable strategy for therapeutic intervention in schizophrenia and other dopamine dysfunctional states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castner, S A -- Williams, G V -- Goldman-Rakic, P S -- P01DA10160/DA/NIDA NIH HHS/ -- P50MH44866/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 17;287(5460):2020-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neurobiology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10720329" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antipsychotic Agents/*pharmacology ; Cyclic AMP/metabolism ; Dopamine/metabolism ; Dopamine Agonists/*pharmacology ; Dopamine Antagonists/pharmacology ; Down-Regulation ; Female ; Haloperidol/*pharmacology ; Haplorhini ; Memory/*drug effects ; Prefrontal Cortex/drug effects/metabolism ; Psychomotor Performance/drug effects ; Pyridines/*pharmacology ; Receptors, Dopamine D1/agonists/*metabolism ; Signal Transduction ; Tetrahydronaphthalenes/*pharmacology ; Time Factors
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    Neuroimaging evidence for dissociable forms of repetition priming (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-02-26
    Description: Repetition priming has been characterized neurophysiologically as a decreased response following stimulus repetition. The present study used event-related functional magnetic resonance imaging to investigate whether this repetition-related response is sensitive to stimulus familiarity. A right fusiform region exhibited an attenuated response to the repetition of familiar stimuli, both faces and symbols, but exhibited an enhanced response to the repetition of unfamiliar stimuli. Moreover, both repetition effects were modulated by lag between successive presentations. Further experiments replicated the interactions between repetition, familiarity, and lag and demonstrated the persistence of these effects over multiple repetitions. Priming-related responses are therefore not unitary but depend on the presence or absence of preexisting stimulus representations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henson, R -- Shallice, T -- Dolan, R -- New York, N.Y. -- Science. 2000 Feb 18;287(5456):1269-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Department of Cognitive Neurology, Institute of Neurology, Institute of Cognitive Neuroscience and Department of Psychology, University College London, London WC1E 6BT, UK. r.henson@ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10678834" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Brain Mapping ; Face ; Female ; Humans ; Magnetic Resonance Imaging ; Male ; Memory/*physiology ; *Pattern Recognition, Visual ; Regression Analysis ; Temporal Lobe/*physiology ; Time Factors
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    Role for rapid dendritic protein synthesis in hippocampal mGluR-dependent long-term depression (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-05-20
    Description: A hippocampal pyramidal neuron receives more than 10(4) excitatory glutamatergic synapses. Many of these synapses contain the molecular machinery for messenger RNA translation, suggesting that the protein complement (and thus function) of each synapse can be regulated on the basis of activity. Here, local postsynaptic protein synthesis, triggered by synaptic activation of metabotropic glutamate receptors, was found to modify synaptic transmission within minutes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, K M -- Kayser, M S -- Bear, M F -- New York, N.Y. -- Science. 2000 May 19;288(5469):1254-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Neuroscience, Brown University, Providence, RI 02912, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10818003" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/pharmacology ; Animals ; Anisomycin/pharmacology ; Dendrites/drug effects/*metabolism ; Electric Stimulation ; Excitatory Amino Acid Antagonists/pharmacology ; Hippocampus/*metabolism/physiology ; Methoxyhydroxyphenylglycol/analogs & derivatives/pharmacology ; Nerve Tissue Proteins/antagonists & inhibitors/*biosynthesis/genetics ; Neural Inhibition/drug effects/*physiology ; Protein Biosynthesis/drug effects ; Protein Synthesis Inhibitors/pharmacology ; RNA, Messenger/metabolism ; Rats ; Receptors, Metabotropic Glutamate/*physiology ; Synaptic Transmission/drug effects/physiology ; Xanthenes/pharmacology
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    Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-10
    Description: Cyclic nucleotides are second messengers that are essential in vision, muscle contraction, neurotransmission, exocytosis, cell growth, and differentiation. These molecules are degraded by a family of enzymes known as phosphodiesterases, which serve a critical function by regulating the intracellular concentration of cyclic nucleotides. We have determined the three-dimensional structure of the catalytic domain of phosphodiesterase 4B2B to 1.77 angstrom resolution. The active site has been identified and contains a cluster of two metal atoms. The structure suggests the mechanism of action and basis for specificity and will provide a framework for structure-assisted drug design for members of the phosphodiesterase family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, R X -- Hassell, A M -- Vanderwall, D -- Lambert, M H -- Holmes, W D -- Luther, M A -- Rocque, W J -- Milburn, M V -- Zhao, Y -- Ke, H -- Nolte, R T -- AI33072/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 9;288(5472):1822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Chemistry, Department of Molecular Sciences, Glaxo Wellcome Research and Development, Research Triangle Park, NC 27709, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10846163" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/*chemistry/*metabolism ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/chemistry/*metabolism ; Cyclic GMP/chemistry/metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Hydrogen Bonding ; Hydrolysis ; Metals/metabolism ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Substrate Specificity
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    Learning-induced LTP in neocortex (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-10-20
    Description: The hypothesis that learning occurs through long-term potentiation (LTP)- and long-term depression (LTD)-like mechanisms is widely held but unproven. This hypothesis makes three assumptions: Synapses are modifiable, they modify with learning, and they strengthen through an LTP-like mechanism. We previously established the ability for synaptic modification and a synaptic strengthening with motor skill learning in horizontal connections of the rat motor cortex (MI). Here we investigated whether learning strengthened these connections through LTP. We demonstrated that synapses in the trained MI were near the ceiling of their modification range, compared with the untrained MI, but the range of synaptic modification was not affected by learning. In the trained MI, LTP was markedly reduced and LTD was enhanced. These results are consistent with the use of LTP to strengthen synapses during learning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rioult-Pedotti, M S -- Friedman, D -- Donoghue, J P -- NS27164/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2000 Oct 20;290(5491):533-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Brown University, Providence, RI 02912, USA. mengia_rioult@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11039938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electric Stimulation ; Female ; Learning/*physiology ; Long-Term Potentiation/*physiology ; Models, Neurological ; Motor Cortex/*physiology ; Motor Skills ; Neuronal Plasticity ; Rats ; Rats, Sprague-Dawley ; Synapses/*physiology ; Synaptic Transmission
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    Neurobiology. Receptors as kissing cousins (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milligan, G -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):65-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Scotland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10766637" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases/metabolism ; Animals ; Cell Line ; Cerebral Cortex/metabolism ; Corpus Striatum/metabolism ; Dimerization ; Energy Transfer ; Fluorescence ; GTP-Binding Proteins/*metabolism ; Ligands ; Rats ; Receptor Cross-Talk ; Receptors, Dopamine D1/metabolism ; Receptors, Dopamine D2/agonists/*metabolism ; Receptors, Dopamine D5 ; Receptors, GABA-A/metabolism ; Receptors, Somatostatin/agonists/*metabolism ; Signal Transduction ; Somatostatin/metabolism
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    A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-07-06
    Description: A conserved domain in the extracellular region of the 60- and 80-kilodalton tumor necrosis factor receptors (TNFRs) was identified that mediates specific ligand-independent assembly of receptor trimers. This pre-ligand-binding assembly domain (PLAD) is physically distinct from the domain that forms the major contacts with ligand, but is necessary and sufficient for the assembly of TNFR complexes that bind TNF-alpha and mediate signaling. Other members of the TNFR superfamily, including TRAIL receptor 1 and CD40, show similar homotypic association. Thus, TNFRs and related receptors appear to function as preformed complexes rather than as individual receptor subunits that oligomerize after ligand binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, F K -- Chun, H J -- Zheng, L -- Siegel, R M -- Bui, K L -- Lenardo, M J -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2351-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Antigens, CD/chemistry/metabolism ; Apoptosis ; Binding Sites ; Cross-Linking Reagents ; Dimerization ; Energy Transfer ; Fluorescence ; Humans ; Ligands ; Macromolecular Substances ; Mutation ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Tumor Necrosis Factor/*chemistry/*metabolism ; Receptors, Tumor Necrosis Factor, Type I ; Receptors, Tumor Necrosis Factor, Type II ; Recombinant Fusion Proteins/chemistry/metabolism ; *Signal Transduction ; Succinimides ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/*metabolism
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    Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-20
    Description: Ectodysplasin, a member of the tumor necrosis factor family, is encoded by the anhidrotic ectodermal dysplasia (EDA) gene. Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA-A1 and EDA-A2 are two isoforms of ectodysplasin that differ only by an insertion of two amino acids. This insertion functions to determine receptor binding specificity, such that EDA-A1 binds only the receptor EDAR, whereas EDA-A2 binds only the related, but distinct, X-linked ectodysplasin-A2 receptor (XEDAR). In situ binding and organ culture studies indicate that EDA-A1 and EDA-A2 are differentially expressed and play a role in epidermal morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, M -- Wang, L C -- Hymowitz, S G -- Schilbach, S -- Lee, J -- Goddard, A -- de Vos, A M -- Gao, W Q -- Dixit, V M -- New York, N.Y. -- Science. 2000 Oct 20;290(5491):523-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11039935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites ; Cell Line ; DNA-Binding Proteins/metabolism ; Ectodermal Dysplasia/genetics ; Ectodysplasins ; Epidermis/embryology/*metabolism ; Humans ; *I-kappa B Proteins ; In Situ Hybridization ; Ligands ; Membrane Proteins/*chemistry/*metabolism ; Mice ; Models, Molecular ; Molecular Sequence Data ; Morphogenesis ; NF-kappa B/metabolism ; Phosphorylation ; Point Mutation ; Protein Conformation ; Proteins/metabolism ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 6 ; Transfection
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    Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-08-19
    Description: In thioredoxin reductase (TrxR) from Escherichia coli, cycles of reduction and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend on rate-limiting rearrangements of the FAD and NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) domains. We describe the structure of the flavin-reducing conformation of E. coli TrxR at a resolution of 3.0 angstroms. The orientation of the two domains permits reduction of FAD by NADPH and oxidation of the enzyme dithiol by the protein substrate, thioredoxin. The alternate conformation, described by Kuriyan and co-workers, permits internal transfer of reducing equivalents from reduced FAD to the active-site disulfide. Comparison of these structures demonstrates that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lennon, B W -- Williams, C H Jr -- Ludwig, M L -- GM16429/GM/NIGMS NIH HHS/ -- GM18723/GM/NIGMS NIH HHS/ -- GM21444/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1190-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947986" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Crystallography, X-Ray ; Escherichia coli/*enzymology ; Flavin-Adenine Dinucleotide/metabolism ; Hydrogen Bonding ; Models, Molecular ; NADP/metabolism ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Tertiary ; Thioredoxin-Disulfide Reductase/*chemistry/*metabolism ; Thioredoxins/metabolism
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    Dynamically controlled protein tunneling paths in photosynthetic reaction centers (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-06
    Description: Marcus theory has explained how thermal nuclear motions modulate the energy gap between donor and acceptor sites in protein electron transfer reactions. Thermal motions, however, may also modulate electron tunneling between these reactions. Here we identify a new mechanism of nuclear dynamics amplification that plays a central role when interference among the dominant tunneling pathway tubes is destructive. In these cases, tunneling takes place in protein conformations far from equilibrium that minimize destructive interference. As an example, we demonstrate how this dynamical amplification mechanism affects certain reaction rates in the photosynthetic reaction center and therefore may be critical for biological function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balabin, I A -- Onuchic, J N -- GM48043/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of California at San Diego, La Jolla, CA 92093-0319, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021791" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Computer Simulation ; Crystallography, X-Ray ; Darkness ; *Electrons ; Hydrogen Bonding ; Light ; Pheophytins/chemistry/metabolism ; Photosynthetic Reaction Center Complex Proteins/*chemistry/*metabolism ; Physicochemical Phenomena ; Protein Conformation ; Quinones/chemistry/metabolism ; Thermodynamics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Perspectives: drug delivery. Regulating export of ER cargo (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aridor, M -- Balch, W E -- New York, N.Y. -- Science. 2000 Feb 4;287(5454):816-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10691557" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Cell Line ; Drug Delivery Systems ; Endoplasmic Reticulum/*metabolism/secretion ; Golgi Apparatus/metabolism ; Growth Hormone/chemistry/metabolism/secretion ; Immunophilins/chemistry/metabolism ; Insulin/chemistry/metabolism/secretion ; Ligands ; Mice ; Models, Biological ; Protein Conformation ; Protein Engineering ; Protein Folding ; Recombinant Fusion Proteins/*chemistry/*metabolism/secretion ; Tacrolimus Binding Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    "Fluorescent timer": protein that changes color with time (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-25
    Description: We generated a mutant of the red fluorescent protein drFP583. The mutant (E5) changes its fluorescence from green to red over time. The rate of color conversion is independent of protein concentration and therefore can be used to trace time-dependent expression. We used in vivo labeling with E5 to measure expression from the heat shock-dependent promoter in Caenorhabditis elegans and from the Otx-2 promoter in developing Xenopus embryos. Thus, E5 is a "fluorescent timer" that can be used to monitor both activation and down-regulation of target promoters on the whole-organism scale.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Terskikh, A -- Fradkov, A -- Ermakova, G -- Zaraisky, A -- Tan, P -- Kajava, A V -- Zhao, X -- Lukyanov, S -- Matz, M -- Kim, S -- Weissman, I -- Siebert, P -- 1 RO3 TW01362-01/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1585-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Medicine, Stanford University, Stanford, CA 94305, USA. Alexey.Terskikh@Stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11090358" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/embryology/metabolism ; Caenorhabditis elegans/embryology/genetics ; Cell Line ; Color ; Fluorescence ; Gene Expression Profiling/*methods ; *Gene Expression Regulation ; Gene Expression Regulation, Developmental ; Heat-Shock Proteins/genetics ; *Homeodomain Proteins ; Humans ; Luminescent Proteins/*chemistry/*genetics/metabolism ; Mutation ; Nerve Tissue Proteins/genetics ; Otx Transcription Factors ; *Promoter Regions, Genetic ; Temperature ; Time Factors ; Trans-Activators/genetics ; Xenopus laevis/embryology
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    Waiting for organ transplantation. Institute of Medicine Committee on Organ Transplantation (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, R D -- Meltzer, D -- Duan, N -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):237-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Illinois at Chicago, Chicago, IL 60612, USA. rdgib@uic.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10660422" target="_blank"〉PubMed〈/a〉
    Keywords: *Government Regulation ; Health Policy ; Humans ; Institute of Medicine (U.S.) ; *Liver Transplantation/mortality ; *Organ Transplantation/mortality ; *Patient Selection ; *Resource Allocation ; Time Factors ; *Tissue and Organ Procurement/legislation & jurisprudence/standards ; United States
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    Seeing the herpesvirus capsid at 8.5 A (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-08
    Description: Human herpesviruses are large and structurally complex viruses that cause a variety of diseases. The three-dimensional structure of the herpesvirus capsid has been determined at 8.5 angstrom resolution by electron cryomicroscopy. More than 30 putative alpha helices were identified in the four proteins that make up the 0.2 billion-dalton shell. Some of these helices are located at domains that undergo conformational changes during capsid assembly and DNA packaging. The unique spatial arrangement of the heterotrimer at the local threefold positions accounts for the asymmetric interactions with adjacent capsid components and the unusual co-dependent folding of its subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Z H -- Dougherty, M -- Jakana, J -- He, J -- Rixon, F J -- Chiu, W -- New York, N.Y. -- Science. 2000 May 5;288(5467):877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10797014" target="_blank"〉PubMed〈/a〉
    Keywords: Capsid/*chemistry/*ultrastructure ; Capsid Proteins ; Cryoelectron Microscopy ; Herpesvirus 1, Human/chemistry/*ultrastructure ; Image Processing, Computer-Assisted ; Models, Molecular ; Molecular Weight ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Evolution. Parasites make scaredy-rats foolhardy (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmer, C -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):525-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10939959" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; Biological Evolution ; *Fear ; Female ; Humans ; Male ; *Personality ; Rats ; Toxoplasma/*physiology ; Toxoplasmosis, Animal/parasitology/*psychology ; Toxoplasmosis, Cerebral/parasitology/*psychology
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    The structural basis of ribosome activity in peptide bond synthesis (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-11
    Description: Using the atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with two substrate analogs, we establish that the ribosome is a ribozyme and address the catalytic properties of its all-RNA active site. Both substrate analogs are contacted exclusively by conserved ribosomal RNA (rRNA) residues from domain V of 23S rRNA; there are no protein side-chain atoms closer than about 18 angstroms to the peptide bond being synthesized. The mechanism of peptide bond synthesis appears to resemble the reverse of the acylation step in serine proteases, with the base of A2486 (A2451 in Escherichia coli) playing the same general base role as histidine-57 in chymotrypsin. The unusual pK(a) (where K(a) is the acid dissociation constant) required for A2486 to perform this function may derive in part from its hydrogen bonding to G2482 (G2447 in E. coli), which also interacts with a buried phosphate that could stabilize unusual tautomers of these two bases. The polypeptide exit tunnel is largely formed by RNA but has significant contributions from proteins L4, L22, and L39e, and its exit is encircled by proteins L19, L22, L23, L24, L29, and L31e.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nissen, P -- Hansen, J -- Ban, N -- Moore, P B -- Steitz, T A -- GM22778/GM/NIGMS NIH HHS/ -- GM54216/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 11;289(5481):920-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry and Department of Chemistry, Yale University, and Howard Hughes Medical Institute, New Haven, CT 06520-8114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10937990" target="_blank"〉PubMed〈/a〉
    Keywords: Archaeal Proteins/chemistry/metabolism ; Base Pairing ; Base Sequence ; Binding Sites ; Catalysis ; Crystallization ; Evolution, Molecular ; Haloarcula marismortui/chemistry/metabolism/ultrastructure ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligonucleotides/metabolism ; *Peptide Biosynthesis ; Peptides/metabolism ; Peptidyl Transferases/antagonists & inhibitors/chemistry/*metabolism ; Phosphates/chemistry/metabolism ; Protein Conformation ; Puromycin/metabolism ; RNA, Archaeal/chemistry/metabolism ; RNA, Catalytic/*chemistry/*metabolism ; RNA, Ribosomal, 23S/*chemistry/*metabolism ; RNA, Transfer/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Ribosomal Proteins/chemistry/metabolism ; Ribosomes/chemistry/*metabolism
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    Structural mechanism for STI-571 inhibition of abelson tyrosine kinase (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-09-16
    Description: The inadvertent activation of the Abelson tyrosine kinase (Abl) causes chronic myelogenous leukemia (CML). A small-molecule inhibitor of Abl (STI-571) is effective in the treatment of CML. We report the crystal structure of the catalytic domain of Abl, complexed to a variant of STI-571. Critical to the binding of STI-571 is the adoption by the kinase of an inactive conformation, in which a centrally located "activation loop" is not phosphorylated. The conformation of this loop is distinct from that in active protein kinases, as well as in the inactive form of the closely related Src kinases. These results suggest that compounds that exploit the distinctive inactivation mechanisms of individual protein kinases can achieve both high affinity and high specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schindler, T -- Bornmann, W -- Pellicena, P -- Miller, W T -- Clarkson, B -- Kuriyan, J -- GM29362/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1938-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10988075" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/chemistry/*pharmacology ; Benzamides ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Activation ; Enzyme Inhibitors/chemistry/*pharmacology ; Humans ; Imatinib Mesylate ; Mice ; Models, Molecular ; Phosphorylation ; *Piperazines ; Protein Conformation ; Proto-Oncogene Proteins c-abl/*antagonists & inhibitors/chemistry/metabolism ; Pyrimidines/chemistry/*pharmacology ; Recombinant Fusion Proteins ; Structure-Activity Relationship
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    A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-25
    Description: Susceptibility to murine and human insulin-dependent diabetes mellitus correlates strongly with major histocompatibility complex (MHC) class II I-A or HLA-DQ alleles that lack an aspartic acid at position beta57. I-Ag7 lacks this aspartate and is the only class II allele expressed by the nonobese diabetic mouse. The crystal structure of I-Ag7 was determined at 2.6 angstrom resolution as a complex with a high-affinity peptide from the autoantigen glutamic acid decarboxylase (GAD) 65. I-Ag7 has a substantially wider peptide-binding groove around beta57, which accounts for distinct peptide preferences compared with other MHC class II alleles. Loss of Asp(beta57) leads to an oxyanion hole in I-Ag7 that can be filled by peptide carboxyl residues or, perhaps, through interaction with the T cell receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corper, A L -- Stratmann, T -- Apostolopoulos, V -- Scott, C A -- Garcia, K C -- Kang, A S -- Wilson, I A -- Teyton, L -- CA58896/CA/NCI NIH HHS/ -- DK55037/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):505-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical 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/10775108" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Aspartic Acid/chemistry ; Crystallography, X-Ray ; Diabetes Mellitus, Type 1/*immunology ; Drosophila melanogaster ; *Genes, MHC Class II ; Glutamate Decarboxylase/metabolism ; Histocompatibility Antigens Class II/*chemistry/genetics/metabolism ; Humans ; Hydrogen Bonding ; Mice ; Mice, Inbred NOD ; Models, Molecular ; Molecular Sequence Data ; Peptide Library ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell/metabolism ; Recombinant Proteins/chemistry/metabolism
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    Structure of the RNA polymerase domain of E. coli primase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-31
    Description: All cellular organisms use specialized RNA polymerases called "primases" to synthesize RNA primers for the initiation of DNA replication. The high-resolution crystal structure of a primase, comprising the catalytic core of the Escherichia coli DnaG protein, was determined. The core structure contains an active-site architecture that is unrelated to other DNA or RNA polymerase palm folds, but is instead related to the "toprim" fold. On the basis of the structure, it is likely that DnaG binds nucleic acid in a groove clustered with invariant residues and that DnaG is positioned within the replisome to accept single-stranded DNA directly from the replicative helicase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keck, J L -- Roche, D D -- Lynch, A S -- Berger, J M -- New York, N.Y. -- Science. 2000 Mar 31;287(5462):2482-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, 229 Stanley Hall, no. 3206, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10741967" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; DNA Helicases/chemistry/metabolism ; DNA Primase/*chemistry/*metabolism ; DNA Replication ; DNA, Bacterial/metabolism ; DNA, Single-Stranded/*metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Escherichia coli/*enzymology/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/biosynthesis ; Recombinant Proteins/chemistry/metabolism ; Templates, Genetic
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    Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-26
    Description: Polyadenylate [poly(A)] polymerase (PAP) catalyzes the addition of a polyadenosine tail to almost all eukaryotic messenger RNAs (mRNAs). The crystal structure of the PAP from Saccharomyces cerevisiae (Pap1) has been solved to 2.6 angstroms, both alone and in complex with 3'-deoxyadenosine triphosphate (3'-dATP). Like other nucleic acid polymerases, Pap1 is composed of three domains that encircle the active site. The arrangement of these domains, however, is quite different from that seen in polymerases that use a template to select and position their incoming nucleotides. The first two domains are functionally analogous to polymerase palm and fingers domains. The third domain is attached to the fingers domain and is known to interact with the single-stranded RNA primer. In the nucleotide complex, two molecules of 3'-dATP are bound to Pap1. One occupies the position of the incoming base, prior to its addition to the mRNA chain. The other is believed to occupy the position of the 3' end of the mRNA primer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bard, J -- Zhelkovsky, A M -- Helmling, S -- Earnest, T N -- Moore, C L -- Bohm, A -- R01 GM57218-01A2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1346-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958780" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Deoxyadenine Nucleotides/*chemistry/*metabolism ; Hydrogen Bonding ; Manganese/metabolism ; Models, Molecular ; Mutation ; Polynucleotide Adenylyltransferase/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/metabolism ; RNA, Messenger/metabolism ; Ribosomal Protein S6 ; Ribosomal Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*enzymology
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    Determining the 3D structure of HIV-1 protease (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-06-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kent, S -- Marshall, G R -- Wlodawer, A -- New York, N.Y. -- Science. 2000 Jun 2;288(5471):1590.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10858137" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; HIV Protease/chemical synthesis/*chemistry/metabolism ; Ligands ; Protein Conformation ; Recombinant Proteins/chemistry
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    Laboratory animals. Researchers fight plan to regulate mice, birds (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malakoff, D -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):23.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11183138" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Testing Alternatives/*legislation & jurisprudence ; Animal Welfare/*legislation & jurisprudence ; Animals ; *Animals, Laboratory ; Birds ; Mice ; Rats ; United States ; United States Department of Agriculture/*legislation & jurisprudence
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    Neurobiology. A new clue to how alcohol damages brains (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):947-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10691562" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Benzodiazepines/adverse effects/toxicity ; Brain/cytology/*drug effects/growth & development ; Ethanol/blood/*toxicity ; Female ; Humans ; Infant, Newborn ; Nerve Degeneration ; Neurons/cytology/*drug effects ; Pregnancy ; Rats ; Receptors, GABA/*drug effects/metabolism ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/*drug effects/metabolism
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    Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-10
    Description: Reciprocal gene activation and restriction during cell type differentiation from a common lineage is a hallmark of mammalian organogenesis. A key question, then, is whether a critical transcriptional activator of cell type-specific gene targets can also restrict expression of the same genes in other cell types. Here, we show that whereas the pituitary-specific POU domain factor Pit-1 activates growth hormone gene expression in one cell type, the somatotrope, it restricts its expression from a second cell type, the lactotrope. This distinction depends on a two-base pair spacing in accommodation of the bipartite POU domains on a conserved growth hormone promoter site. The allosteric effect on Pit-1, in combination with other DNA binding factors, results in the recruitment of a corepressor complex, including nuclear receptor corepressor N-CoR, which, unexpectedly, is required for active long-term repression of the growth hormone gene in lactotropes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scully, K M -- Jacobson, E M -- Jepsen, K -- Lunyak, V -- Viadiu, H -- Carriere, C -- Rose, D W -- Hooshmand, F -- Aggarwal, A K -- Rosenfeld, M G -- R01 DK18477/DK/NIDDK NIH HHS/ -- R01 DK54802/DK/NIDDK NIH HHS/ -- R01 GM49327/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 10;290(5494):1127-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Endocrinology and Metabolism, School of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11073444" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Base Sequence ; Binding Sites ; Cell Line ; Conserved Sequence ; Crystallization ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Female ; *Gene Expression Regulation ; Genes, Reporter ; Growth Hormone/*genetics ; Male ; Mice ; Mice, Transgenic ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/genetics/metabolism ; Nuclear Receptor Co-Repressor 1 ; Pituitary Gland/cytology/*metabolism ; Prolactin/*genetics ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Tertiary ; Rats ; Repressor Proteins/chemistry/genetics/*metabolism ; Transcription Factor Pit-1 ; Transcription Factors/chemistry/genetics/*metabolism ; Transcriptional Activation
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    Unfolding pathways of individual bacteriorhodopsins (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-07
    Description: Atomic force microscopy and single-molecule force spectroscopy were combined to image and manipulate purple membrane patches from Halobacterium salinarum. Individual bacteriorhodopsin molecules were first localized and then extracted from the membrane; the remaining vacancies were imaged again. Anchoring forces between 100 and 200 piconewtons for the different helices were found. Upon extraction, the helices were found to unfold. The force spectra revealed the individuality of the unfolding pathways. Helices G and F as well as helices E and D always unfolded pairwise, whereas helices B and C occasionally unfolded one after the other. Experiments with cleaved loops revealed the origin of the individuality: stabilization of helix B by neighboring helices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oesterhelt, F -- Oesterhelt, D -- Pfeiffer, M -- Engel, A -- Gaub, H E -- Muller, D J -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):143-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CeNS and Lehrstuhl fur angewandte Physik, Ludwig Maximilians-Universitat Munchen, Amalienstrasse 54, 80799 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10753119" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriorhodopsins/*chemistry/genetics ; Cysteine/chemistry ; Halobacterium salinarum/*chemistry ; Membrane Proteins/*chemistry/genetics ; *Microscopy, Atomic Force ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Protein Structure, Secondary ; Purple Membrane/*chemistry ; Serine Endopeptidases/metabolism ; Spectrum Analysis
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    Crystal structure of the ribonucleoprotein core of the signal recognition particle (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-26
    Description: The signal recognition particle (SRP), a protein-RNA complex conserved in all three kingdoms of life, recognizes and transports specific proteins to cellular membranes for insertion or secretion. We describe here the 1.8 angstrom crystal structure of the universal core of the SRP, revealing protein recognition of a distorted RNA minor groove. Nucleotide analog interference mapping demonstrates the biological importance of observed interactions, and genetic results show that this core is functional in vivo. The structure explains why the conserved residues in the protein and RNA are required for SRP assembly and defines a signal sequence recognition surface composed of both protein and RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Batey, R T -- Rambo, R P -- Lucast, L -- Rha, B -- Doudna, J A -- New York, N.Y. -- Science. 2000 Feb 18;287(5456):1232-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10678824" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Base Pairing ; Binding Sites ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli/chemistry/genetics/metabolism ; *Escherichia coli Proteins ; Guanosine Triphosphate/metabolism ; Hydrogen Bonding ; Magnesium/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Potassium/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Bacterial/*chemistry/genetics/metabolism ; Signal Recognition Particle/*chemistry/metabolism ; Transformation, Bacterial ; Water/metabolism
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    Requirement for DARPP-32 in progesterone-facilitated sexual receptivity in female rats and mice (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-02-11
    Description: DARPP-32, a dopamine- and adenosine 3',5'-monophosphate (cAMP)-regulated phosphoprotein (32 kilodaltons in size), is an obligate intermediate in progesterone (P)-facilitated sexual receptivity in female rats and mice. The facilitative effect of P on sexual receptivity in female rats was blocked by antisense oligonucleotides to DARPP-32. Homozygous mice carrying a null mutation for the DARPP-32 gene exhibited minimal levels of P-facilitated sexual receptivity when compared to their wild-type littermates. P significantly increased hypothalamic cAMP levels and cAMP-dependent protein kinase activity. These increases were not inhibited by a D1 subclass dopamine receptor antagonist. P also enhanced phosphorylation of DARPP-32 on threonine 34 in the hypothalamus of mice. DARPP-32 activation is thus an obligatory step in progestin receptor regulation of sexual receptivity in rats and mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mani, S K -- Fienberg, A A -- O'Callaghan, J P -- Snyder, G L -- Allen, P B -- Dash, P K -- Moore, A N -- Mitchell, A J -- Bibb, J -- Greengard, P -- O'Malley, B W -- MH49662/MH/NIMH NIH HHS/ -- MH57442/MH/NIMH NIH HHS/ -- NS 35457/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1053-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA. smani@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669419" target="_blank"〉PubMed〈/a〉
    Keywords: 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine/pharmacology ; Animals ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dopamine/pharmacology ; Dopamine Agonists/pharmacology ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Female ; Hypothalamus/metabolism ; Injections, Intraventricular ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; *Nerve Tissue Proteins ; Oligonucleotides, Antisense/pharmacology ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; Posture ; Progesterone/*pharmacology ; Proteins/genetics/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Progesterone/metabolism ; Serotonin/pharmacology ; Sexual Behavior, Animal/*drug effects ; Signal Transduction
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    An early taste of things to come (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marcus, M -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1878.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11012357" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn/physiology ; Embryonic and Fetal Development ; Female ; *Food Preferences/physiology ; Humans ; Rats ; *Taste
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    Climate change. Recent reductions in China's greenhouse gas emissions (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Streets, D G -- Jiang, K -- Hu, X -- Sinton, J E -- Zhang, X Q -- Xu, D -- Jacobson, M Z -- Hansen, J E -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1835-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Decision and Information Sciences Division, Argonne National Laboratory, Argonne, IL 60439, USA. dstreets@anl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729288" target="_blank"〉PubMed〈/a〉
    Keywords: Bioelectric Energy Sources/economics ; Carbon Dioxide/*metabolism ; China ; Coal/economics ; *Conservation of Energy Resources/economics ; Electricity ; *Energy-Generating Resources/economics ; *Greenhouse Effect ; Methane/metabolism ; Time Factors ; Wood
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    Active disruption of an RNA-protein interaction by a DExH/D RNA helicase (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-01-06
    Description: All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate-dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jankowsky, E -- Gross, C H -- Shuman, S -- Pyle, A M -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11141562" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions/metabolism ; Acid Anhydride Hydrolases/chemistry/*metabolism ; Adenosine Triphosphate/metabolism ; Base Sequence ; Binding Sites ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleoside-Triphosphatase ; Protein Binding ; Protein Conformation ; RNA/chemistry/*metabolism ; RNA Helicases/chemistry/*metabolism ; *RNA-Binding Proteins ; Ribonucleoprotein, U1 Small Nuclear/*metabolism
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    Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-04-21
    Description: Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cramer, P -- Bushnell, D A -- Kornberg, R D -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 8;292(5523):1863-76. Epub 2001 Apr 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11313498" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; DNA, Fungal/chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Magnesium/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; RNA Polymerase II/*chemistry/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Fungal/biosynthesis/chemistry/metabolism ; RNA, Messenger/biosynthesis/chemistry/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; Transcription Factors/metabolism ; *Transcription, Genetic
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    Impact of polymer tether length on multiple ligand-receptor bond formation (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-07-21
    Description: The promoters of cell adhesion are ligands, which are often attached to flexible tethers that bind to surface receptors on adjacent cells. Using a combination of Monte Carlo simulations, diffusion reaction theory, and direct experiments (surface force measurements) of the biotin-streptavidin system, we have quantified polymer chain dynamics and the kinetics and spatial range of tethered ligand-receptor binding. The results show that the efficiency of strong binding does not depend solely on the molecular architecture or binding energy of the receptor-ligand pair, nor on the equilibrium configuration of the polymer tether, but rather on its "rare" extended conformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeppesen, C -- Wong, J Y -- Kuhl, T L -- Israelachvili, J N -- Mullah, N -- Zalipsky, S -- Marques, C M -- GM-17876/GM/NIGMS NIH HHS/ -- GM-47334/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jul 20;293(5529):465-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Materials Research Laboratory, Department of Chemical Engineering, University of California, Santa Barbara, CA 93106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11463908" target="_blank"〉PubMed〈/a〉
    Keywords: Biotin/*chemistry/metabolism ; Chemistry, Physical ; Diffusion ; Kinetics ; Ligands ; Mathematics ; Monte Carlo Method ; Physicochemical Phenomena ; Polyethylene Glycols ; Polymers/*chemistry ; Protein Conformation ; Streptavidin/*chemistry/metabolism ; Surface Properties ; Thermodynamics
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    Interaction of the response regulator ARR4 with phytochrome B in modulating red light signaling (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-03
    Description: The Arabidopsis thaliana response regulator 4, expressed in response to phytochrome B action, specifically interacts with the extreme amino-terminus of the photoreceptor. The response regulator 4 stabilizes the active Pfr form of phytochrome B in yeast and in planta, thus elevates the level of the active photoreceptor in vivo. Accordingly, transgenic Arabidopsis plants overexpressing the response regulator 4 display hypersensitivity to red light but not to light of other wavelengths. We propose that the response regulator 4 acts as an output element of a two-component system that modulates red light signaling on the level of the phytochrome B photoreceptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sweere, U -- Eichenberg, K -- Lohrmann, J -- Mira-Rodado, V -- Baurle, I -- Kudla, J -- Nagy, F -- Schafer, E -- Harter, K -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biologie II / Botanik, Universitat Freiburg, Schanzlestrasse 1, 79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691995" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism/radiation effects ; Arabidopsis Proteins/genetics/*metabolism ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Darkness ; Genes, Plant ; *Light ; Phenotype ; Phosphorylation ; *Photoreceptor Cells ; Phytochrome/chemistry/*metabolism ; Phytochrome B ; Plants, Genetically Modified ; Protein Conformation ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; *Transcription Factors ; Two-Hybrid System Techniques ; Yeasts/genetics/metabolism
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    A transcriptional switch mediated by cofactor methylation (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-11-10
    Description: We describe a molecular switch based on the controlled methylation of nucleosome and the transcriptional cofactors, the CREB-binding proteins (CBP)/p300. The CBP/p300 methylation site is localized to an arginine residue that is essential for stabilizing the structure of the KIX domain, which mediates CREB recruitment. Methylation of KIX by coactivator-associated arginine methyltransferase 1 (CARM1) blocks CREB activation by disabling the interaction between KIX and the kinase inducible domain (KID) of CREB. Thus, CARM1 functions as a corepressor in cyclic adenosine monophosphate signaling pathway via its methyltransferase activity while acting as a coactivator for nuclear hormones. These results provide strong in vivo and in vitro evidence that histone methylation plays a key role in hormone-induced gene activation and define cofactor methylation as a new regulatory mechanism in hormone signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, W -- Chen, H -- Du, K -- Asahara, H -- Tini, M -- Emerson, B M -- Montminy, M -- Evans, R M -- 9R01DK57978/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, Department of Biological Chemistry, University of California Davis Cancer Center/Basic Science, Sacramento, CA 95817, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701890" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Apoptosis ; Cell Line ; Cyclic AMP Response Element-Binding Protein/metabolism ; Dimerization ; E1A-Associated p300 Protein ; *Gene Expression Regulation ; Genes, Reporter ; Histone Acetyltransferases ; Histones/metabolism ; Methylation ; Molecular Sequence Data ; Nerve Growth Factor/pharmacology ; Nuclear Proteins/chemistry/*metabolism ; PC12 Cells ; Protein Structure, Tertiary ; Protein-Arginine N-Methyltransferases/*metabolism ; Rats ; Receptors, Retinoic Acid/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Somatostatin/genetics ; Trans-Activators/chemistry/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Transfection ; Tretinoin/metabolism/pharmacology
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    Taking cell-matrix adhesions to the third dimension (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-11-27
    Description: Adhesions between fibroblastic cells and extracellular matrix have been studied extensively in vitro, but little is known about their in vivo counterparts. Here, we characterized the composition and function of adhesions in three-dimensional (3D) matrices derived from tissues or cell culture. "3D-matrix adhesions" differ from focal and fibrillar adhesions characterized on 2D substrates in their content of alpha5beta1 and alphavbeta3 integrins, paxillin, other cytoskeletal components, and tyrosine phosphorylation of focal adhesion kinase (FAK). Relative to 2D substrates, 3D-matrix interactions also display enhanced cell biological activities and narrowed integrin usage. These distinctive in vivo 3D-matrix adhesions differ in structure, localization, and function from classically described in vitro adhesions, and as such they may be more biologically relevant to living organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cukierman, E -- Pankov, R -- Stevens, D R -- Yamada, K M -- New York, N.Y. -- Science. 2001 Nov 23;294(5547):1708-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11721053" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; *Cell Adhesion/drug effects ; Cell Culture Techniques/methods ; Cell Division ; Cell Movement ; Cell Size ; Cells, Cultured ; Culture Techniques/methods ; Cycloheximide/pharmacology ; Cytoskeletal Proteins/metabolism ; Extracellular Matrix/chemistry/metabolism ; Fibroblasts/chemistry/*cytology/*metabolism ; Fibronectins/metabolism ; Fluorescent Antibody Technique, Indirect ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Focal Adhesions/chemistry/metabolism ; Glutaral/metabolism ; Humans ; Imaging, Three-Dimensional/*methods ; Integrins/metabolism ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Conformation ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Time Factors
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    Molecular mechanisms of the biological clock in cultured fibroblasts (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-17
    Description: In mammals, the central circadian pacemaker resides in the hypothalamic suprachiasmatic nucleus (SCN), but circadian oscillators also exist in peripheral tissues. Here, using wild-type and cryptochrome (mCry)-deficient cell lines derived from mCry mutant mice, we show that the peripheral oscillator in cultured fibroblasts is identical to the oscillator in the SCN in (i) temporal expression profiles of all known clock genes, (ii) the phase of the various mRNA rhythms (i.e., antiphase oscillation of Bmal1 and mPer genes), (iii) the delay between maximum mRNA levels and appearance of nuclear mPER1 and mPER2 protein, (iv) the inability to produce oscillations in the absence of functional mCry genes, and (v) the control of period length by mCRY proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yagita, K -- Tamanini, F -- van Der Horst, G T -- Okamura, H -- New York, N.Y. -- Science. 2001 Apr 13;292(5515):278-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Brain Science, Department of Brain Sciences, Kobe University Graduate School of Medicine, Chuo-ku, Kobe 650-0017, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11303101" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Biological Clocks/*genetics ; CLOCK Proteins ; Cell Cycle Proteins ; Cell Line ; Cell Nucleus/metabolism ; Circadian Rhythm/*genetics ; Cryptochromes ; *DNA-Binding Proteins ; *Drosophila Proteins ; Endothelin-1/pharmacology ; *Eye Proteins ; Fibroblasts/*physiology ; Flavoproteins/genetics/metabolism ; Gene Expression Profiling ; *Gene Expression Regulation ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; *Photoreceptor Cells, Invertebrate ; RNA, Messenger/genetics/metabolism ; Rats ; Receptors, G-Protein-Coupled ; Suprachiasmatic Nucleus/metabolism ; Time Factors ; Trans-Activators/genetics/metabolism ; Transcription Factors/genetics/metabolism
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    Ribosome structure. The ribosome in action (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dahlberg, A E -- New York, N.Y. -- Science. 2001 May 4;292(5518):868-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology and Medicine, Brown University, Providence, RI 02912, USA. albert_dahlberg@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11341282" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/pharmacology ; Anticodon ; Base Pairing ; Binding Sites ; Codon ; Crystallography, X-Ray ; *Protein Biosynthesis ; Protein Conformation ; RNA, Bacterial/chemistry/metabolism ; RNA, Messenger/chemistry/*metabolism ; RNA, Ribosomal/chemistry/metabolism ; RNA, Transfer/chemistry/*metabolism ; RNA, Transfer, Amino Acid-Specific/chemistry/*metabolism ; Ribosomal Proteins/chemistry/metabolism ; Ribosomes/chemistry/*metabolism/*ultrastructure ; Thermus thermophilus/genetics/metabolism/ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Virology. The origin and control of pandemic influenza (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laver, G -- Garman, E -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1776-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Australian National University, Canberra 2601, ACT, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546857" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiviral Agents/therapeutic use ; Chickens/*virology ; Drug Industry/methods ; Drug Resistance, Microbial ; Enzyme Inhibitors/therapeutic use ; Guanidines ; HN Protein/chemistry/genetics/metabolism ; Hong Kong/epidemiology ; Humans ; Influenza A virus/*enzymology/genetics/immunology/*pathogenicity ; Influenza Vaccines/biosynthesis/economics/immunology ; Influenza, Human/diagnosis/drug therapy/*epidemiology/*prevention & control ; Models, Molecular ; Mutation/genetics ; Neuraminidase/antagonists & inhibitors/chemistry/genetics/metabolism ; Protein Conformation ; Pyrans ; RNA, Viral/analysis/genetics ; Reassortant Viruses/enzymology/genetics/immunology/pathogenicity ; Sialic Acids/therapeutic use ; Zanamivir
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    Short-term trials and long-term effects (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daniels, S R -- New York, N.Y. -- Science. 2001 Sep 28;293(5539):2392-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11579936" target="_blank"〉PubMed〈/a〉
    Keywords: Antihypertensive Agents/*therapeutic use ; *Controlled Clinical Trials as Topic ; Follow-Up Studies ; Humans ; Hypertension/*drug therapy ; Meta-Analysis as Topic ; *Placebos/adverse effects ; Time Factors
    Print ISSN: 0036-8075
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    Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-25
    Description: beta-Amyloid plaques and neurofibrillary tangles (NFTs) are the defining neuropathological hallmarks of Alzheimer's disease, but their pathophysiological relation is unclear. Injection of beta-amyloid Abeta42 fibrils into the brains of P301L mutant tau transgenic mice caused fivefold increases in the numbers of NFTs in cell bodies within the amygdala from where neurons project to the injection sites. Gallyas silver impregnation identified NFTs that contained tau phosphorylated at serine 212/threonine 214 and serine 422. NFTs were composed of twisted filaments and occurred in 6-month-old mice as early as 18 days after Abeta42 injections. Our data support the hypothesis that Abeta42 fibrils can accelerate NFT formation in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gotz, J -- Chen, F -- van Dorpe, J -- Nitsch, R M -- New York, N.Y. -- Science. 2001 Aug 24;293(5534):1491-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Psychiatry Research, University of Zurich, August Forel Strasse 1, 8008 Zurich, Switzerland. goetz@bli.unizh.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11520988" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Alzheimer Disease/metabolism/*pathology ; Amygdala/*pathology ; Amyloid beta-Peptides/administration & dosage/*metabolism ; Animals ; Brain/*pathology ; Epitopes ; Female ; Fluorescent Antibody Technique ; Humans ; Male ; Mice ; Mice, Transgenic ; Microscopy, Immunoelectron ; Mutation ; Neurofibrillary Tangles/*metabolism/pathology ; Peptide Fragments/administration & dosage/*metabolism ; Phosphorylation ; Plaque, Amyloid/*metabolism/pathology ; Protein Conformation ; Protein Isoforms ; Sex Characteristics ; tau Proteins/chemistry/genetics/immunology/*metabolism
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    Molecular imaging. Virus infects cell: live and uncut (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckman, M -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1803.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729272" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/*virology ; Cytoplasm/*virology ; Dependovirus/*physiology ; Fluorescence ; Genetic Vectors/physiology ; Host-Parasite Interactions/physiology ; Humans ; Microscopy, Fluorescence/methods ; Spectrometry, Fluorescence/*methods ; Time Factors
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    Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkbeta (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-05
    Description: We show that high doses of salicylates reverse hyperglycemia, hyperinsulinemia, and dyslipidemia in obese rodents by sensitizing insulin signaling. Activation or overexpression of the IkappaB kinase beta (IKKbeta) attenuated insulin signaling in cultured cells, whereas IKKbeta inhibition reversed insulin resistance. Thus, IKKbeta, rather than the cyclooxygenases, appears to be the relevant molecular target. Heterozygous deletion (Ikkbeta+/-) protected against the development of insulin resistance during high-fat feeding and in obese Lep(ob/ob) mice. These findings implicate an inflammatory process in the pathogenesis of insulin resistance in obesity and type 2 diabetes mellitus and identify the IKKbeta pathway as a target for insulin sensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, M -- Konstantopoulos, N -- Lee, J -- Hansen, L -- Li, Z W -- Karin, M -- Shoelson, S E -- AI43477/AI/NIAID NIH HHS/ -- DK45493/DK/NIDDK NIH HHS/ -- DK51729/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 31;293(5535):1673-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11533494" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Aspirin/administration & dosage/*pharmacology ; Blood Glucose/metabolism ; Cell Line ; Dietary Fats/*administration & dosage ; Gene Deletion ; Gene Targeting ; Glucose Tolerance Test ; I-kappa B Kinase ; Insulin/administration & dosage/blood/*metabolism/pharmacology ; *Insulin Resistance ; Lipids/blood ; Liver/metabolism ; Male ; Mice ; Mice, Obese ; Muscles/metabolism ; Obesity/metabolism/*physiopathology ; Phosphorylation ; Prostaglandin-Endoperoxide Synthases/genetics/metabolism ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/genetics/*metabolism ; Rats ; Rats, Zucker ; Receptor, Insulin/metabolism ; Signal Transduction ; Sodium Salicylate/administration & dosage/*pharmacology ; Tumor Necrosis Factor-alpha/pharmacology
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    X-ray crystallography. Transcription enzyme structure solved (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 2001 Apr 20;292(5516):411-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11330276" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; Humans ; Models, Molecular ; Molecular Weight ; Protein Conformation ; RNA/biosynthesis/genetics ; RNA Polymerase II/*chemistry/metabolism ; *Transcription, Genetic ; Yeasts/*enzymology
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    Prevention of chemotherapy-induced alopecia in rats by CDK inhibitors (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-01-06
    Description: Most traditional cytotoxic anticancer agents ablate the rapidly dividing epithelium of the hair follicle and induce alopecia (hair loss). Inhibition of cyclin-dependent kinase 2 (CDK2), a positive regulator of eukaryotic cell cycle progression, may represent a therapeutic strategy for prevention of chemotherapy-induced alopecia (CIA) by arresting the cell cycle and reducing the sensitivity of the epithelium to many cell cycle-active antitumor agents. Potent small-molecule inhibitors of CDK2 were developed using structure-based methods. Topical application of these compounds in a neonatal rat model of CIA reduced hair loss at the site of application in 33 to 50% of the animals. Thus, inhibition of CDK2 represents a potentially useful approach for the prevention of CIA in cancer patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S T -- Benson, B G -- Bramson, H N -- Chapman, D E -- Dickerson, S H -- Dold, K M -- Eberwein, D J -- Edelstein, M -- Frye, S V -- Gampe Jr, R T -- Griffin, R J -- Harris, P A -- Hassell, A M -- Holmes, W D -- Hunter, R N -- Knick, V B -- Lackey, K -- Lovejoy, B -- Luzzio, M J -- Murray, D -- Parker, P -- Rocque, W J -- Shewchuk, L -- Veal, J M -- Walker, D H -- Kuyper, L F -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Glaxo Wellcome Research and Development, Research Triangle Park, NC 27709, USA. std41085@glaxowellcome.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11141566" target="_blank"〉PubMed〈/a〉
    Keywords: Alopecia/*chemically induced/*prevention & control ; Animals ; Animals, Newborn ; Antineoplastic Agents/*toxicity ; Antineoplastic Combined Chemotherapy Protocols/toxicity ; Apoptosis/drug effects ; *CDC2-CDC28 Kinases ; Cell Cycle/drug effects ; Cell Line ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/*antagonists & inhibitors/metabolism ; Cyclophosphamide/toxicity ; Cytoprotection/drug effects ; DNA/biosynthesis ; Doxorubicin/toxicity ; Drug Design ; Enzyme Inhibitors/chemical synthesis/chemistry/*pharmacology ; Epithelium/drug effects ; Etoposide/toxicity ; Hair Follicle/cytology/*drug effects ; Humans ; Indoles/chemical synthesis/chemistry/*pharmacology ; Mice ; Mice, SCID ; Phosphorylation ; Protein-Serine-Threonine Kinases/*antagonists & inhibitors/metabolism ; Rats ; Retinoblastoma Protein/metabolism ; Scalp/transplantation ; Sulfonamides/chemical synthesis/chemistry/*pharmacology ; Transplantation, Heterologous
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    An experiment for all seasons (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, J -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):624-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474094" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture ; Animals ; Databases, Factual ; *Ecology ; *Ecosystem ; Government Agencies ; International Cooperation ; Internet ; Plants ; Research Support as Topic ; Software ; Time Factors ; Trees ; Weather
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    Structural biology. Actin' up (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De La Cruz, E M -- Pollard, T D -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):616-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474090" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Depolymerizing Factors ; Actins/*chemistry/*metabolism ; Adenosine Diphosphate/chemistry/*metabolism ; Adenosine Triphosphate/chemistry/metabolism ; Biopolymers/chemistry/metabolism ; *Contractile Proteins ; Crystallography, X-Ray ; Hydrolysis ; Microfilament Proteins/metabolism ; Phosphates/metabolism ; Profilins ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Rhodamines/metabolism ; Thymosin/metabolism
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    Neuroscience. A kinase to dampen the effects of cocaine? (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, A -- Tsai, L H -- New York, N.Y. -- Science. 2001 Apr 13;292(5515):236-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Harvard Medical School and Howard Hughes Medical Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11305318" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cocaine/*pharmacology ; Corpus Striatum/*drug effects/metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Cyclin-Dependent Kinase 5 ; Cyclin-Dependent Kinases/antagonists & inhibitors/genetics/*metabolism ; Dopamine/metabolism ; Dopamine Uptake Inhibitors/*pharmacology ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Mice ; Mice, Knockout ; Motor Activity/drug effects ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Phosphoprotein Phosphatases/antagonists & inhibitors/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-fos/metabolism ; Rats ; Signal Transduction
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    Bioinformatics. Reality simulation--observe while it happens (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berendsen, H J -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2304-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands. berendsen@chem.rug.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743188" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Aquaporin 1 ; Aquaporins/chemistry/*metabolism ; Bacterial Outer Membrane Proteins/chemistry/*metabolism ; Cell Membrane Permeability ; *Computational Biology ; *Computer Simulation ; *Escherichia coli Proteins ; Hydrogen Bonding ; Kinetics ; Lipid Bilayers ; *Models, Biological ; Permeability ; Static Electricity ; Time Factors ; Water/*metabolism
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    Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-02
    Description: The GGAs are a multidomain protein family implicated in protein trafficking between the Golgi and endosomes. Here, the VHS domain of GGA2 was shown to bind to the acidic cluster-dileucine motif in the cytoplasmic tail of the cation-independent mannose 6-phosphate receptor (CI-MPR). Receptors with mutations in this motif were defective in lysosomal enzyme sorting. The hinge domain of GGA2 bound clathrin, suggesting that GGA2 could be a link between cargo molecules and clathrin-coated vesicle assembly. Thus, GGA2 binding to the CI-MPR is important for lysosomal enzyme targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, Y -- Doray, B -- Poussu, A -- Lehto, V P -- Kornfeld, S -- R01 CA-08759/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 1;292(5522):1716-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11387476" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Vesicular Transport ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; *Carrier Proteins ; Cations ; Clathrin/metabolism ; Dipeptides/chemistry/metabolism ; L Cells (Cell Line) ; Lysosomes/*enzymology ; Mice ; Molecular Sequence Data ; Mutation ; Protein Sorting Signals ; Protein Structure, Tertiary ; *Protein Transport ; Proteins/chemistry/genetics/*metabolism ; Rats ; Receptor, IGF Type 2/*chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Solubility ; Transcription Factor AP-1/metabolism ; Transport Vesicles/metabolism ; Two-Hybrid System Techniques ; trans-Golgi Network/metabolism
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    Divining a forest's future from its past (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, J -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):626.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474096" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbon Dioxide ; Disasters ; Ecology ; *Ecosystem ; Financing, Government ; Government Agencies ; Massachusetts ; Research Support as Topic ; Time Factors ; *Trees
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    Real-time single-molecule imaging of the infection pathway of an adeno-associated virus (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: We describe a method, based on single-molecule imaging, that allows the real-time visualization of the infection pathway of single viruses in living cells, each labeled with only one fluorescent dye molecule. The tracking of single viruses removes ensemble averaging. Diffusion trajectories with high spatial and time resolution show various modes of motion of adeno-associated viruses (AAV) during their infection pathway into living HeLa cells: (i) consecutive virus touching at the cell surface and fast endocytosis; (ii) free and anomalous diffusion of the endosome and the virus in the cytoplasm and the nucleus; and (iii) directed motion by motor proteins in the cytoplasm and in nuclear tubular structures. The real-time visualization of the infection pathway of single AAVs shows a much faster infection than was generally observed so far.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seisenberger, G -- Ried, M U -- Endress, T -- Buning, H -- Hallek, M -- Brauchle, C -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1929-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department Chemie, Ludwig-Maximilians-Universitat Munchen, Butenandtstrasse 11, D-81377 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729319" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Biological Transport ; Cell Nucleus/*virology ; Cell Survival ; Cytoplasm/*virology ; Dependovirus/*physiology ; Diffusion ; Endocytosis ; Endosomes/virology ; Fluorescence ; Fluorescent Dyes/metabolism ; Genetic Vectors/physiology ; HeLa Cells ; Host-Parasite Interactions/physiology ; Humans ; Microscopy, Fluorescence/*methods ; Molecular Motor Proteins/metabolism ; Movement ; Nocodazole/pharmacology ; Spectrometry, Fluorescence/*methods ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Visualizing science. New imaging tools put the art back into science (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, A -- New York, N.Y. -- Science. 2001 May 11;292(5519):1044-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11352044" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Computer Graphics ; *Computer Simulation ; Computers ; Fractals ; Image Processing, Computer-Assisted/*methods ; Internet ; Microscopy, Video ; Motion Pictures as Topic ; Publishing ; Reproducibility of Results ; Software ; 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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    Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-28
    Description: The protective antigen moiety of anthrax toxin translocates the toxin's enzymic moieties to the cytosol of mammalian cells by a mechanism that depends on its ability to heptamerize and insert into membranes. We identified dominant-negative mutants of protective antigen that co-assemble with the wild-type protein and block its ability to translocate the enzymic moieties across membranes. These mutants strongly inhibited toxin action in cell culture and in an animal intoxication model, suggesting that they could be useful in therapy of anthrax.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sellman, B R -- Mourez, M -- Collier, R J -- 5T32AI07410/AI/NIAID NIH HHS/ -- R37-AI22021/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):695-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11326092" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthrax/*drug therapy ; *Antigens, Bacterial ; Bacterial Toxins/*antagonists & inhibitors/*genetics/metabolism/toxicity ; CHO Cells ; Cell Membrane/metabolism ; Cricetinae ; Endocytosis ; Genes, Dominant ; Male ; *Mutation ; Protein Transport ; Rats ; Rats, Inbred F344 ; Receptors, Peptide/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Endangered right whales on the southeastern Bering Sea shelf (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tynan, C T -- DeMaster, D P -- Peterson, W T -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1894.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Northwest Fisheries Science Center (NWFSC), National Oceanic and Atmospheric Administration (NOAA), Seattle, WA 98112, USA. Cynthia.Tynan@noaa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729308" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Migration ; Animals ; *Ecosystem ; *Environment ; Food Chain ; *Geography ; Pacific Ocean ; Seawater ; Survival Rate ; Temperature ; Time Factors ; Whales/*physiology
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  • 86
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    Where the grass never stops growing (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pickrell, J -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):625.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474095" target="_blank"〉PubMed〈/a〉
    Keywords: Ecology ; *Ecosystem ; England ; *Fertilizers ; Poaceae/*growth & development ; Time Factors
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  • 87
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    Control of synapse number by glia (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-07
    Description: Although astrocytes constitute nearly half of the cells in our brain, their function is a long-standing neurobiological mystery. Here we show by quantal analyses, FM1-43 imaging, immunostaining, and electron microscopy that few synapses form in the absence of glial cells and that the few synapses that do form are functionally immature. Astrocytes increase the number of mature, functional synapses on central nervous system (CNS) neurons by sevenfold and are required for synaptic maintenance in vitro. We also show that most synapses are generated concurrently with the development of glia in vivo. These data demonstrate a previously unknown function for glia in inducing and stabilizing CNS synapses, show that CNS synapse number can be profoundly regulated by nonneuronal signals, and raise the possibility that glia may actively participate in synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullian, E M -- Sapperstein, S K -- Christopherson, K S -- Barres, B A -- NS10784/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University School of Medicine, Department of Neurobiology, Fairchild Science Building, Stanford, CA 94305-5125, USA. emu@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158678" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/*physiology ; Calcium/metabolism ; *Calcium-Binding Proteins ; Cell Communication ; Cells, Cultured ; Coculture Techniques ; Excitatory Postsynaptic Potentials ; Fluorescent Dyes/metabolism ; Glutamic Acid/pharmacology ; Ionomycin/pharmacology ; Membrane Glycoproteins/metabolism ; Microscopy, Electron ; Nerve Tissue Proteins/metabolism ; Neuronal Plasticity ; Patch-Clamp Techniques ; Pyridinium Compounds/metabolism ; Quaternary Ammonium Compounds/metabolism ; Rats ; Rats, Sprague-Dawley ; Retinal Ganglion Cells/*physiology/ultrastructure ; Superior Colliculi/embryology/growth & development/ultrastructure ; Synapses/*physiology/ultrastructure ; Synaptic Transmission ; Synaptic Vesicles/metabolism ; Synaptophysin/metabolism ; Synaptotagmins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Botany. Patience yields secrets of seed longevity (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, K -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1884-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11245184" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/growth & development/*physiology ; Ecosystem ; Seasons ; Seeds/growth & development/*physiology ; Time Factors
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  • 89
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    Disasters. Volcano fatalities--lessons from the historical record (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simkin, T -- Siebert, L -- Blong, R -- New York, N.Y. -- Science. 2001 Jan 12;291(5502):255.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Museum of Natural History, Smithsonian Institution, Washington, DC 20560-0119, USA. simkin@nmnh.si.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11253213" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; *Mortality ; Time Factors ; Volcanic Eruptions/*statistics & numerical data
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  • 90
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    AIDS research. HIV inhibitor blocks virus from cell (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Helmuth, L -- New York, N.Y. -- Science. 2001 Jan 12;291(5502):229.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11253826" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; Anti-HIV Agents/chemistry/*metabolism ; Antigens, CD4/metabolism ; CD4-Positive T-Lymphocytes/metabolism/virology ; Carrier Proteins/chemistry/*metabolism ; Drug Design ; HIV/*metabolism ; HIV Envelope Protein gp41/chemistry/*metabolism ; Humans ; *Membrane Fusion ; *Peptides ; Protein Conformation ; Protein Engineering ; Protein Folding
    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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  • 91
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    Changes in forest biomass carbon storage in China between 1949 and 1998 (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-26
    Description: The location and mechanisms responsible for the carbon sink in northern mid-latitude lands are uncertain. Here, we used an improved estimation method of forest biomass and a 50-year national forest resource inventory in China to estimate changes in the storage of living biomass between 1949 and 1998. Our results suggest that Chinese forests released about 0.68 petagram of carbon between 1949 and 1980, for an annual emission rate of 0.022 petagram of carbon. Carbon storage increased significantly after the late 1970s from 4.38 to 4.75 petagram of carbon by 1998, for a mean accumulation rate of 0.021 petagram of carbon per year, mainly due to forest expansion and regrowth. Since the mid-1970s, planted forests (afforestation and reforestation) have sequestered 0.45 petagram of carbon, and their average carbon density increased from 15.3 to 31.1 megagrams per hectare, while natural forests have lost an additional 0.14 petagram of carbon, suggesting that carbon sequestration through forest management practices addressed in the Kyoto Protocol could help offset industrial carbon dioxide emissions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fang, J -- Chen, A -- Peng, C -- Zhao, S -- Ci, L -- New York, N.Y. -- Science. 2001 Jun 22;292(5525):2320-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Urban and Environmental Science, and Key Laboratory for Earth Surface Processes of the Ministry of Education, Peking University, Beijing 100871, China. jyfang@urban.pku.edu.cn〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423660" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomass ; *Carbon ; Carbon Dioxide ; China ; Conservation of Natural Resources ; Forestry ; Time Factors ; *Trees
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    Dendrodendritic inhibition through reversal of dopamine transport (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-29
    Description: Synapses in the central nervous system are usually defined by presynaptic exocytotic release sites and postsynaptic differentiations. We report here a demonstration of dendrodendritic inhibition that does not engage a conventional synapse. Using amperometric and patch-clamp recordings in rat brain slices of the substantia nigra, we found that blockade of the dopamine transporter abolished the dendritic release of dopamine and the resulting self-inhibition. These findings demonstrate that dendrodendritic autoinhibition entails the carrier-mediated release of dopamine rather than conventional exocytosis. This suggests that some widely used antidepressants that inhibit the dopamine transporter may benefit patients in the early stages of Parkinson's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falkenburger, B H -- Barstow, K L -- Mintz, I M -- R01-3445/PHS HHS/ -- New York, N.Y. -- Science. 2001 Sep 28;293(5539):2465-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Experimental Therapeutics, Boston University Medical Center, Boston, MA 02118, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11577238" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport/drug effects ; Calcium/metabolism ; Carrier Proteins/antagonists & inhibitors/*metabolism ; Dendrites/*metabolism ; Dopamine/*metabolism ; Dopamine D2 Receptor Antagonists ; Dopamine Plasma Membrane Transport Proteins ; Electric Stimulation ; Electrophysiology ; Evoked Potentials/drug effects ; Excitatory Postsynaptic Potentials ; Exocytosis ; Glutamic Acid/pharmacology ; Humans ; In Vitro Techniques ; *Membrane Glycoproteins ; Membrane Potentials ; *Membrane Transport Proteins ; *Nerve Tissue Proteins ; Neural Inhibition ; Neurons/metabolism ; Parkinson Disease/drug therapy/metabolism ; Patch-Clamp Techniques ; Piperazines/pharmacology ; Rats ; Receptors, Dopamine D2/metabolism ; Sodium/metabolism ; Substantia Nigra/cytology/*metabolism ; Subthalamic Nucleus/physiology
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  • 93
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    Impulsive choice induced in rats by lesions of the nucleus accumbens core (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-26
    Description: Impulsive choice is exemplified by choosing a small or poor reward that is available immediately, in preference to a larger but delayed reward. Impulsive choice contributes to drug addiction, attention-deficit/hyperactivity disorder, mania, and personality disorders, but its neuroanatomical basis is unclear. Here, we show that selective lesions of the nucleus accumbens core induce persistent impulsive choice in rats. In contrast, damage to two of its afferents, the anterior cingulate cortex and medial prefrontal cortex, had no effect on this capacity. Thus, dysfunction of the nucleus accumbens core may be a key element in the neuropathology of impulsivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cardinal, R N -- Pennicott, D R -- Sugathapala, C L -- Robbins, T W -- Everitt, B J -- G9537855/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2001 Jun 29;292(5526):2499-501. Epub 2001 May 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Psychology, University of Cambridge, Downing Street, Cambridge CB2 3EB, UK. rudolf.cardinal@pobox.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11375482" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Attention ; Attention Deficit Disorder with Hyperactivity ; Behavior, Animal ; Brain Mapping ; *Choice Behavior ; Disease Models, Animal ; Gyrus Cinguli/physiology ; *Impulsive Behavior ; Motor Activity ; Nucleus Accumbens/*physiology/surgery ; Prefrontal Cortex/physiology ; Random Allocation ; Rats ; Reinforcement (Psychology) ; Reward
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    Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-12
    Description: Dendritic cell specific intracellular adhesion molecule-3 (ICAM-3) grabbing nonintegrin (DC-SIGN), a C-type lectin present on the surface of dendritic cells, mediates the initial interaction of dendritic cells with T cells by binding to ICAM-3. DC-SIGN and DC-SIGNR, a related receptor found on the endothelium of liver sinusoids, placental capillaries, and lymph nodes, bind to oligosaccharides that are present on the envelope of human immunodeficiency virus (HIV), an interaction that strongly promotes viral infection of T cells. Crystal structures of carbohydrate-recognition domains of DC-SIGN and of DC-SIGNR bound to oligosaccharide, in combination with binding studies, reveal that these receptors selectively recognize endogenous high-mannose oligosaccharides and may represent a new avenue for developing HIV prophylactics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feinberg, H -- Mitchell, D A -- Drickamer, K -- Weis, W I -- GM50565/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 7;294(5549):2163-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, 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/11739956" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylglucosamine/chemistry/metabolism ; Calcium/metabolism ; Carbohydrate Conformation ; Carbohydrate Sequence ; Carrier Proteins/chemistry/metabolism ; *Cell Adhesion Molecules ; Collectins ; Crystallization ; Crystallography, X-Ray ; Glycoproteins/chemistry/metabolism ; HIV Envelope Protein gp120/chemistry/metabolism ; Humans ; Hydrogen Bonding ; Lectins/*chemistry/*metabolism ; *Lectins, C-Type ; Ligands ; Mannose/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides/chemistry/*metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Cell Surface/*chemistry/*metabolism
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    Chemistry. Nota bene: know thine enemy (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, O -- New York, N.Y. -- Science. 2001 Nov 9;294(5545):1298.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701920" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Bacterial ; *Bacillus anthracis ; Bacterial Toxins/chemistry/*metabolism ; Crystallography, X-Ray ; Endocytosis ; Hydrogen-Ion Concentration ; Macrophages/metabolism/microbiology ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Phagocytosis ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Cell Surface/chemistry/*metabolism ; Receptors, Peptide/chemistry/*metabolism
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  • 96
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    Gene therapy. Safer and virus-free? (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferber, D -- New York, N.Y. -- Science. 2001 Nov 23;294(5547):1638-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11721029" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biolistics ; Blood Pressure ; Clinical Trials as Topic ; Coronary Artery Disease/genetics/therapy ; DNA/administration & dosage/genetics ; Electroporation ; Gene Expression ; Gene Transfer Techniques/*trends ; Genetic Therapy/*methods/trends ; Genetic Vectors/*administration & dosage/*adverse effects/genetics ; Hemophilia A/genetics/therapy ; Humans ; Injections, Intra-Arterial ; Melanoma/genetics/therapy ; Microinjections ; Muscular Dystrophies/genetics/therapy ; Organ Specificity ; Plasmids/administration & dosage/genetics ; RNA/administration & dosage/genetics ; Time Factors ; Transfection ; Transgenes/genetics ; Viruses/genetics/pathogenicity
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  • 97
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    Relapse to cocaine-seeking after hippocampal theta burst stimulation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-12
    Description: Treatment efforts for cocaine addiction are hampered by high relapse rates. To map brain areas underlying relapse, we used electrical brain stimulation and intracranial injection of pharmacological compounds after extinction of cocaine self-administration behavior in rats. Electrical stimulation of the hippocampus containing glutamatergic fibers, but not the medial forebrain bundle containing dopaminergic fibers, elicited cocaine-seeking behavior dependent on glutamate in the ventral tegmental area. This suggests a role for glutamatergic neurotransmission in relapse to cocaine abuse. The medial forebrain bundle electrodes supported intense electrical self-stimulation. These findings suggest a dissociation of neural systems subserving positive reinforcement (self-stimulation) and incentive motivation (relapse).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vorel, S R -- Liu, X -- Hayes, R J -- Spector, J A -- Gardner, E L -- New York, N.Y. -- Science. 2001 May 11;292(5519):1175-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Department of Psychiatry and Behavioral Sciences, Albert Einstein College of Medicine, Bronx, NY 10461, USA. robvorel@hotmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11349151" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cocaine/administration & dosage/pharmacology ; Cocaine-Related Disorders/*physiopathology/prevention & control ; Conditioning, Operant/drug effects/physiology ; Dopamine/physiology ; Electric Stimulation ; Electrodes ; Excitatory Amino Acid Agonists/pharmacology ; Excitatory Amino Acid Antagonists/pharmacology ; Extinction, Psychological/drug effects/physiology ; Glutamic Acid/*physiology ; Hippocampus/cytology/*physiology ; Injections, Intravenous ; Kynurenic Acid/pharmacology ; Medial Forebrain Bundle/cytology/drug effects/physiology ; Memory/physiology ; N-Methylaspartate/pharmacology ; Rats ; Rats, Long-Evans ; Recurrence ; Reward ; Self Administration ; Synaptic Transmission/drug effects ; *Theta Rhythm ; Ventral Tegmental Area/cytology/drug effects/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 98
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    Crystal structure of an initiation factor bound to the 30S ribosomal subunit (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-03
    Description: Initiation of translation at the correct position on messenger RNA is essential for accurate protein synthesis. In prokaryotes, this process requires three initiation factors: IF1, IF2, and IF3. Here we report the crystal structure of a complex of IF1 and the 30S ribosomal subunit. Binding of IF1 occludes the ribosomal A site and flips out the functionally important bases A1492 and A1493 from helix 44 of 16S RNA, burying them in pockets in IF1. The binding of IF1 causes long-range changes in the conformation of H44 and leads to movement of the domains of 30S with respect to each other. The structure explains how localized changes at the ribosomal A site lead to global alterations in the conformation of the 30S subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, A P -- Clemons, W M Jr -- Brodersen, D E -- Morgan-Warren, R J -- Hartsch, T -- Wimberly, B T -- Ramakrishnan, V -- GM 44973/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jan 19;291(5503):498-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11228145" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Binding Sites ; Crystallography, X-Ray ; Eukaryotic Initiation Factor-1/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; RNA, Ribosomal, 16S/*chemistry/metabolism ; RNA, Transfer/metabolism ; Ribosomal Proteins/*chemistry/metabolism ; Ribosomes/*chemistry/metabolism ; Thermus thermophilus/*chemistry
    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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  • 99
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    Neurobiology. Total recall-the memory of addiction (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nestler, E J -- New York, N.Y. -- Science. 2001 Jun 22;292(5525):2266-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry and Center for Basic Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390--9070, USA. eric.nestler@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423644" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/drug effects/physiology/physiopathology ; Calcium/metabolism ; Calcium Signaling ; Cocaine/*pharmacology ; Cocaine-Related Disorders/*physiopathology ; Dopamine/metabolism ; Glutamic Acid/metabolism ; Hippocampus/physiology ; *Long-Term Potentiation ; Memory/*physiology ; Neurons/*drug effects/physiology ; Rats ; Receptors, AMPA/metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synaptic Transmission/drug effects ; Ventral Tegmental Area/*drug effects/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 100
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    Paleoclimate. Dating--vive la difference (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adkins, J -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1844-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Institute of Technology, Pasadena, CA 91125, USA. jess@gps.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729292" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atlantic Ocean ; *Atmosphere ; Calibration ; Carbon/metabolism ; Carbon Dioxide/metabolism ; Carbon Radioisotopes/metabolism ; Cold Climate ; Cosmic Radiation ; Geologic Sediments/*analysis/chemistry/parasitology ; Greenland ; Half-Life ; Ice ; Plankton/metabolism ; *Seawater ; Temperature ; Time Factors ; Volcanic Eruptions
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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