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  • Temperature  (299)
  • Models, Molecular
  • American Association for the Advancement of Science (AAAS)  (518)
  • American Institute of Physics (AIP)
  • Periodicals Archive Online (PAO)
  • 2000-2004  (518)
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  • American Association for the Advancement of Science (AAAS)  (518)
  • American Institute of Physics (AIP)
  • Periodicals Archive Online (PAO)
  • Springer  (14)
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  • 101
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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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  • 102
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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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  • 103
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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
    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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  • 104
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    Biomolecular interactions at phospholipid-decorated surfaces of liquid crystals (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-20
    Description: The spontaneous assembly of phospholipids at planar interfaces between thermotropic liquid crystals and aqueous phases gives rise to patterned orientations of the liquid crystals that reflect the spatial and temporal organization of the phospholipids. Strong and weak specific-binding events involving proteins at these interfaces drive the reorganization of the phospholipids and trigger orientational transitions in the liquid crystals. Because these interfaces are fluid, processes involving the lateral organization of proteins (such as the formation of protein- and phospholipid-rich domains) are also readily imaged by the orientational response of the liquid crystal, as are stereospecific enzymatic events. These results provide principles for label-free monitoring of aqueous streams for molecular and biomolecular species without the need for complex instrumentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brake, Jeffrey M -- Daschner, Maren K -- Luk, Yan-Yeung -- Abbott, Nicholas L -- New York, N.Y. -- Science. 2003 Dec 19;302(5653):2094-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical and Biological Engineering, University of Wisconsin, Madison, 1415 Engineering Drive, Madison, WI 53706-1607, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14684814" target="_blank"〉PubMed〈/a〉
    Keywords: 1,2-Dipalmitoylphosphatidylcholine/chemistry ; Biphenyl Compounds/*chemistry ; Calcium ; Catalysis ; Crystallization ; Fluorescence ; Glass ; Gold ; Hydrolysis ; Micelles ; Nitriles/*chemistry ; Phosphatidylcholines/chemistry ; Phospholipases A/*metabolism ; Phospholipids/*chemistry ; Quaternary Ammonium Compounds/chemistry ; Silanes/chemistry ; Temperature ; Water/chemistry
    Print ISSN: 0036-8075
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  • 105
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    Response of a deciduous forest to the Mount Pinatubo eruption: enhanced photosynthesis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-29
    Description: Volcanic aerosols from the 1991 Mount Pinatubo eruption greatly increased diffuse radiation worldwide for the following 2 years. We estimated that this increase in diffuse radiation alone enhanced noontime photosynthesis of a deciduous forest by 23% in 1992 and 8% in 1993 under cloudless conditions. This finding indicates that the aerosol-induced increase in diffuse radiation by the volcano enhanced the terrestrial carbon sink and contributed to the temporary decline in the growth rate of atmospheric carbon dioxide after the eruption.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Lianhong -- Baldocchi, Dennis D -- Wofsy, Steve C -- Munger, J William -- Michalsky, Joseph J -- Urbanski, Shawn P -- Boden, Thomas A -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):2035-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Environmental Sciences Division, Building 1509, Oak Ridge National Laboratory, Oak Ridge, TN 37831-6335, USA. lianhong-gu@ornl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12663919" target="_blank"〉PubMed〈/a〉
    Keywords: Aerosols ; *Atmosphere ; *Carbon Dioxide/metabolism ; Climate ; *Ecosystem ; Mathematics ; Models, Statistical ; Nonlinear Dynamics ; Philippines ; *Photosynthesis ; Regression Analysis ; Scattering, Radiation ; Seasons ; Sunlight ; Temperature ; Trees/*metabolism ; *Volcanic Eruptions
    Print ISSN: 0036-8075
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  • 106
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    Comprehensive identification of human bZIP interactions with coiled-coil arrays (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-14
    Description: In eukaryotes, the combinatorial association of sequence-specific DNA binding proteins is essential for transcription. We have used protein arrays to test 492 pairings of a nearly complete set of coiled-coil strands from human basic-region leucine zipper (bZIP) transcription factors. We find considerable partnering selectivity despite the bZIPs' homologous sequences. The interaction data are of high quality, as assessed by their reproducibility, reciprocity, and agreement with previous observations. Biophysical studies in solution support the relative binding strengths observed with the arrays. New associations provide insights into the circadian clock and the unfolded protein response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, John R S -- Keating, Amy E -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2097-101. Epub 2003 Jun 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Basic-Leucine Zipper Transcription Factors ; Chromatography, High Pressure Liquid ; Circadian Rhythm ; Circular Dichroism ; Cyclic AMP Response Element-Binding Protein/chemistry/metabolism ; DNA-Binding Proteins/chemistry/isolation & purification/*metabolism ; Dimerization ; G-Box Binding Factors ; Humans ; *Leucine Zippers ; Peptides/chemistry/isolation & purification/metabolism ; *Protein Array Analysis ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Signal Transduction ; Temperature ; Thermodynamics ; Transcription Factors/*chemistry/isolation & purification/*metabolism
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  • 107
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    Coral reef death during the 1997 Indian Ocean Dipole linked to Indonesian wildfires (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-16
    Description: Geochemical anomalies and growth discontinuities in Porites corals from western Sumatra, Indonesia, record unanticipated reef mortality during anomalous Indian Ocean Dipole upwelling and a giant red tide in 1997. Sea surface temperature reconstructions show that although some past upwelling events have been stronger, there were no analogous episodes of coral mortality during the past 7000 years, indicating that the 1997 red tide was highly unusual. We show that iron fertilization by the 1997 Indonesian wildfires was sufficient to produce the extraordinary red tide, leading to reef death by asphyxiation. These findings highlight tropical wildfires as an escalating threat to coastal marine ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abram, Nerilie J -- Gagan, Michael K -- McCulloch, Malcolm T -- Chappell, John -- Hantoro, Wahyoe S -- New York, N.Y. -- Science. 2003 Aug 15;301(5635):952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research School of Earth Sciences, Australian National University, Canberra, ACT 0200, Australia. nerilie.abram@anu.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12920295" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/*growth & development ; Atmosphere ; Biomass ; Dinoflagellida/growth & development ; *Ecosystem ; *Eutrophication ; *Fires ; Indian Ocean ; Indonesia ; Iron ; Phytoplankton/growth & development ; Population Dynamics ; Temperature
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  • 108
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    Catalytic reduction of dinitrogen to ammonia at a single molybdenum center (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-05
    Description: Dinitrogen (N2) was reduced to ammonia at room temperature and 1 atmosphere with molybdenum catalysts that contain tetradentate [HIPTN3N]3- triamidoamine ligands (such as [HIPTN3N]Mo(N2), where [HIPTN3N]3- is [(3,5-(2,4,6-i-Pr3C6H2)2C6H3NCH2CH2)3N]3-) in heptane. Slow addition of the proton source [(2,6-lutidinium)(BAr'4), where Ar' is 3,5-(CF3)2C6H3]and reductant (decamethyl chromocene) was critical for achieving high efficiency ( approximately 66% in four turnovers). Numerous x-ray studies, along with isolation and characterization of six proposed intermediates in the catalytic reaction under noncatalytic conditions, suggest that N2 was reduced at a sterically protected, single molybdenum center that cycled from Mo(III) through Mo(VI) states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yandulov, Dmitry V -- Schrock, Richard R -- GM 31978/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 4;301(5629):76-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12843387" target="_blank"〉PubMed〈/a〉
    Keywords: Ammonia/*chemistry ; Atmospheric Pressure ; Catalysis ; Chromium/chemistry ; Electrons ; Ligands ; Magnetic Resonance Spectroscopy ; Molybdenum/*chemistry ; Nitrogen/*chemistry ; Nitrogenase/metabolism ; Organometallic Compounds/chemistry ; Oxidation-Reduction ; Protons ; Temperature
    Print ISSN: 0036-8075
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  • 109
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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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  • 110
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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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  • 111
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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
    Print ISSN: 0036-8075
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  • 112
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    DNA: a programmable force sensor (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-19
    Description: Direct quantification of biomolecular interaction by single-molecule force spectroscopy has evolved into a powerful tool for materials and life sciences. We introduce an approach in which the unbinding forces required to break intermolecular bonds are measured in a differential format by comparison with a known reference bond (here, a short DNA duplex). In addition to a marked increase in sensitivity and force resolution, which enabled us to resolve single-base pair mismatches, this concept allows for highly specific parallel assays. This option was exploited to overcome cross-reactions of antibodies in a protein biochip application.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albrecht, Christian -- Blank, Kerstin -- Lalic-Multhaler, Mio -- Hirler, Siegfried -- Mai, Thao -- Gilbert, Ilka -- Schiffmann, Susanne -- Bayer, Tom -- Clausen-Schaumann, Hauke -- Gaub, Hermann E -- New York, N.Y. -- Science. 2003 Jul 18;301(5631):367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nanotype GmbH, Lochhamer Schlag 12, 82166 Grafelfing, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12869761" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; *Base Pair Mismatch ; *Biosensing Techniques ; Carbocyanines ; Cross Reactions ; *DNA/chemistry/genetics/metabolism ; Dimethylpolysiloxanes ; Fluorescence ; Fluorescent Dyes ; Glass ; Humans ; Immunoassay ; Interleukin-5/analysis/immunology ; Mice ; Microscopy, Atomic Force ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Oligonucleotide Array Sequence Analysis ; *Protein Array Analysis ; Protein Binding ; Silicones ; Temperature ; Thermodynamics
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  • 113
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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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    Geographic barriers isolate endemic populations of hyperthermophilic archaea (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-26
    Description: Barriers to dispersal between populations allow them to diverge through local adaptation or random genetic drift. High-resolution multilocus sequence analysis revealed that, on a global scale, populations of hyperthermophilic microorganisms are isolated from one another by geographic barriers and have diverged over the course of their recent evolutionary history. The identification of a biogeographic pattern in the archaeon Sulfolobus challenges the current model of microbial biodiversity in which unrestricted dispersal constrains the development of global species richness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitaker, Rachel J -- Grogan, Dennis W -- Taylor, John W -- New York, N.Y. -- Science. 2003 Aug 15;301(5635):976-8. Epub 2003 Jul 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, CA 94720, USA. rwhitaker@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12881573" target="_blank"〉PubMed〈/a〉
    Keywords: Analysis of Variance ; Biological Evolution ; *Ecosystem ; Genes, Archaeal ; Genes, rRNA ; Genetic Drift ; Genetic Variation ; Genetics, Population ; Genotype ; Geography ; Geologic Sediments/*microbiology ; Hot Temperature ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Phylogeny ; Sequence Analysis, DNA ; Sulfolobus/genetics/isolation & purification/*physiology ; Temperature ; *Water Microbiology
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    Structural basis of a phototropin light switch (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-09-13
    Description: Phototropins are light-activated kinases important for plant responses to blue light. Light initiates signaling in these proteins by generating a covalent protein-flavin mononucleotide (FMN) adduct within sensory Per-ARNT-Sim (PAS) domains. We characterized the light-dependent changes of a phototropin PAS domain by solution nuclear magnetic resonance spectroscopy and found that an alpha helix located outside the canonical domain plays a key role in this activation process. Although this helix associates with the PAS core in the dark, photoinduced changes in the domain structure disrupt this interaction. We propose that this mechanism couples light-dependent bond formation to kinase activation and identifies a signaling pathway conserved among PAS domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harper, Shannon M -- Neil, Lori C -- Gardner, Kevin H -- CA90601/CA/NCI NIH HHS/ -- GM08297/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 12;301(5639):1541-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12970567" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Avena/*chemistry ; Cryptochromes ; Darkness ; *Drosophila Proteins ; *Eye Proteins ; Flavoproteins/*chemistry/metabolism ; *Light ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; *Photoreceptor Cells, Invertebrate ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, G-Protein-Coupled ; Signal Transduction
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    High plant diversity in Eocene South America: evidence from Patagonia (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-04-05
    Description: Tropical South America has the highest plant diversity of any region today, but this richness is usually characterized as a geologically recent development (Neogene or Pleistocene). From caldera-lake beds exposed at Laguna del Hunco in Patagonia, Argentina, paleolatitude approximately 47 degrees S, we report 102 leaf species. Radioisotopic and paleomagnetic analyses indicate that the flora was deposited 52 million years ago, the time of the early Eocene climatic optimum, when tropical plant taxa and warm, equable climates reached middle latitudes of both hemispheres. Adjusted for sample size, observed richness exceeds that of any other Eocene leaf flora, supporting an ancient history of high plant diversity in warm areas of South America.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilf, Peter -- Cuneo, N Ruben -- Johnson, Kirk R -- Hicks, Jason F -- Wing, Scott L -- Obradovich, John D -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):122-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geosciences, Pennsylvania State University, University Park, PA 16802, USA. pwilf@geosc.psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12677065" target="_blank"〉PubMed〈/a〉
    Keywords: Argentina ; Climate ; Ecology ; *Ecosystem ; *Fossils ; Geologic Sediments ; North America ; Plant Development ; Plant Leaves/anatomy & histology ; *Plants/classification ; Rain ; South America ; Temperature ; Tropical Climate
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    Self-assembly of proteins into designed networks (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-10-04
    Description: A C4-symmetric tetrameric aldolase was used to produce a quadratic network consisting of the enzyme as a rigid four-way connector and stiff streptavidin rods as spacers. Each aldolase subunit was furnished with a His6 tag for oriented binding to a planar surface and two tethered biotins for binding streptavidin in an oriented manner. The networks were improved by starting with composite units and also by binding to nickel-nitrilotriacetic acid-lipid monolayers. The mesh was adjustable in 5-nanometer increments. The production of a net with switchable mesh was initiated with the use of a calcium ion-containing beta-helix spacer that denatured on calcium ion depletion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ringler, Philippe -- Schulz, Georg E -- New York, N.Y. -- Science. 2003 Oct 3;302(5642):106-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Organische Chemie und Biochemie, Albert-Ludwigs-Universitat Freiburg, Albertstrasse 21, D-79104 Freiburg im Breisgau, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14526081" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde-Lyases/*chemistry/genetics/metabolism ; Binding Sites ; Biotin/chemistry/metabolism ; Calcium/metabolism ; Edetic Acid ; *Glycoside Hydrolases ; Lipids/chemistry ; Macromolecular Substances ; Metalloendopeptidases/chemistry/metabolism ; Microscopy, Electron ; Models, Molecular ; Mutation ; Nitrilotriacetic Acid ; Protein Conformation ; Protein Denaturation ; *Protein Engineering ; Protein Structure, Secondary ; Recombinant Fusion Proteins/chemistry ; Streptavidin/*chemistry ; beta-Galactosidase/*chemistry
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    A sublimation model for martian south polar ice features (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-02-15
    Description: In their pioneering work, Leighton and Murray argued that the Mars atmosphere, which at present is 95% carbon dioxide, is controlled by vapor equilibrium with a much larger polar reservoir of solid carbon dioxide. Here we argue that the polar reservoir is small and cannot function as a long-term buffer to the more massive atmosphere. Our work is based on modeling of the circular depressions commonly found on the south polar cap. We argue that a carbon dioxide ice layer about 8 meters thick is being etched away to reveal water ice underneath. This is consistent with thermal infrared data from the Mars Odyssey mission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Byrne, Shane -- Ingersoll, Andrew P -- New York, N.Y. -- Science. 2003 Feb 14;299(5609):1051-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geological and Planetary Sciences, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12586939" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Carbon Dioxide ; *Dry Ice ; *Ice ; *Mars ; *Models, Theoretical ; Seasons ; Temperature ; Water
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    Cell signaling. The BRCT domain: signaling with friends? (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caldecott, Keith W -- New York, N.Y. -- Science. 2003 Oct 24;302(5645):579-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genome Damage and Stability Center, University of Sussex, Brighton BN1 9RR, UK. k.w.caldecott@sussex.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14576410" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; BRCA1 Protein/*chemistry/*metabolism ; Carrier Proteins/chemistry/metabolism ; *Cell Cycle Proteins ; DNA Damage ; DNA Repair ; DNA-Binding Proteins/chemistry/metabolism ; E2F Transcription Factors ; Models, Molecular ; Nuclear Proteins ; Peptide Library ; Phosphopeptides/*metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Proteins/chemistry/*metabolism ; Proteomics ; RNA Helicases/chemistry/metabolism ; *Signal Transduction ; Transcription Factors/chemistry/metabolism
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    Antibody domain exchange is an immunological solution to carbohydrate cluster recognition (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-28
    Description: Human antibody 2G12 neutralizes a broad range of human immunodeficiency virus type 1 (HIV-1) isolates by binding an unusually dense cluster of carbohydrate moieties on the "silent" face of the gp120 envelope glycoprotein. Crystal structures of Fab 2G12 and its complexes with the disaccharide Manalpha1-2Man and with the oligosaccharide Man9GlcNAc2 revealed that two Fabs assemble into an interlocked VH domain-swapped dimer. Further biochemical, biophysical, and mutagenesis data strongly support a Fab-dimerized antibody as the prevalent form that recognizes gp120. The extraordinary configuration of this antibody provides an extended surface, with newly described binding sites, for multivalent interaction with a conserved cluster of oligomannose type sugars on the surface of gp120. The unique interdigitation of Fab domains within an antibody uncovers a previously unappreciated mechanism for high-affinity recognition of carbohydrate or other repeating epitopes on cell or microbial surfaces.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Calarese, Daniel A -- Scanlan, Christopher N -- Zwick, Michael B -- Deechongkit, Songpon -- Mimura, Yusuke -- Kunert, Renate -- Zhu, Ping -- Wormald, Mark R -- Stanfield, Robyn L -- Roux, Kenneth H -- Kelly, Jeffery W -- Rudd, Pauline M -- Dwek, Raymond A -- Katinger, Hermann -- Burton, Dennis R -- Wilson, Ian A -- AI33292/AI/NIAID NIH HHS/ -- GM46192/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2065-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/chemistry/immunology/metabolism ; Antibody Affinity ; Antibody Specificity ; Binding Sites, Antibody ; Cell Adhesion Molecules/metabolism ; Centrifugation, Density Gradient ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Disaccharides/chemistry/metabolism ; Epitopes ; HIV Antibodies/*chemistry/genetics/*immunology/metabolism ; HIV Envelope Protein gp120/*immunology ; HIV-1/*immunology ; Humans ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/*chemistry/genetics/*immunology/metabolism ; Immunoglobulin Heavy Chains/chemistry/immunology ; Immunoglobulin Light Chains/chemistry/immunology ; Immunoglobulin Variable Region/chemistry/immunology ; Lectins/chemistry/immunology/metabolism ; Lectins, C-Type/metabolism ; Ligands ; Mannans/chemistry/metabolism ; Mannosides/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Oligosaccharides/chemistry/*immunology/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Cell Surface/metabolism
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    Crystallographic and spectroscopic characterization of a nonheme Fe(IV)-O complex (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-02-15
    Description: Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rohde, Jan-Uwe -- In, Jun-Hee -- Lim, Mi Hee -- Brennessel, William W -- Bukowski, Michael R -- Stubna, Audria -- Munck, Eckard -- Nam, Wonwoo -- Que, Lawrence Jr -- GM-22701/GM/NIGMS NIH HHS/ -- GM-33162/GM/NIGMS NIH HHS/ -- GM-38767/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Feb 14;299(5609):1037-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12586936" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Chemistry, Physical ; Crystallization ; Crystallography, X-Ray ; Iron/*chemistry ; Ligands ; Models, Molecular ; Molecular Structure ; Oxidation-Reduction ; Oxygen/*chemistry ; Physicochemical Phenomena ; Spectrometry, Mass, Electrospray Ionization ; Spectroscopy, Mossbauer
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    Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-04-26
    Description: Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal transduction. We show that bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wood, Zachary A -- Poole, Leslie B -- Karplus, P Andrew -- ES00210/ES/NIEHS NIH HHS/ -- GM50389/GM/NIGMS NIH HHS/ -- R01 GM050389/GM/NIGMS NIH HHS/ -- R01 GM050389-10/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 25;300(5619):650-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97333, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12714747" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Bacteria/enzymology ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Cysteine/metabolism ; Disulfides/chemistry/metabolism ; Evolution, Molecular ; Humans ; Hydrogen Peroxide/*metabolism ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Peroxidases/*chemistry/*metabolism ; Peroxiredoxins ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Salmonella typhimurium/*enzymology ; Sequence Alignment ; *Signal Transduction ; Sulfenic Acids/metabolism ; Sulfinic Acids/metabolism ; Yeasts/enzymology
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    A conserved domain in axonal targeting of Kv1 (Shaker) voltage-gated potassium channels (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-08-02
    Description: Axonal voltage-gated potassium (Kv1) channels regulate action-potential invasion and hence transmitter release. Although evolutionarily conserved, what mediates their axonal targeting is not known. We found that Kv1 axonal targeting required its T1 tetramerization domain. When fused to unpolarized CD4 or dendritic transferrin receptor, T1 promoted their axonal surface expression. Moreover, T1 mutations eliminating Kvbeta association compromised axonal targeting, but not surface expression, of CD4-T1 fusion proteins. Thus, proper association of Kvbeta with the Kv1 T1 domain is essential for axonal targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Chen -- Jan, Yuh Nung -- Jan, Lily Yeh -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):646-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Departments of Physiology and Biochemistry, University of California, San Francisco, CA 94143-0725, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893943" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Substitution ; Animals ; Antigens, CD4/metabolism ; Axons/*metabolism ; Biopolymers ; COS Cells ; Cell Line ; Cell Membrane/metabolism ; Cell Polarity ; Cells, Cultured ; Dendrites/metabolism ; Endocytosis ; Hippocampus/cytology ; Humans ; Kv1.2 Potassium Channel ; Models, Molecular ; Mutagenesis ; Neurons/metabolism ; Potassium Channels/*chemistry/*metabolism ; *Potassium Channels, Voltage-Gated ; *Protein Structure, Tertiary ; Receptors, Transferrin/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Shaker Superfamily of Potassium Channels ; Shal Potassium Channels ; Transfection
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    Geology. Resources of the sea floor (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-02-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rona, Peter A -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):673-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Marine and Coastal Sciences and Department of Geological Sciences, Rutgers University, New Brunswick, NJ 08901, USA. rona@imcs.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560541" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Physiological Phenomena ; *Ecosystem ; *Geologic Sediments/chemistry/microbiology ; Geological Phenomena ; *Geology ; Hot Temperature ; International Cooperation ; Minerals/*analysis ; Mining ; Oceans and Seas ; *Seawater/microbiology ; Temperature ; United Nations ; Volcanic Eruptions
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    Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-12-13
    Description: The crystal structure at 4.8 angstrom resolution of the reaction center-light harvesting 1 (RC-LH1) core complex from Rhodopseudomonas palustris shows the reaction center surrounded by an oval LH1 complex that consists of 15 pairs of transmembrane helical alpha- and beta-apoproteins and their coordinated bacteriochlorophylls. Complete closure of the RC by the LH1 is prevented by a single transmembrane helix, out of register with the array of inner LH1 alpha-apoproteins. This break, located next to the binding site in the reaction center for the secondary electron acceptor ubiquinone (UQB), may provide a portal through which UQB can transfer electrons to cytochrome b/c1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roszak, Aleksander W -- Howard, Tina D -- Southall, June -- Gardiner, Alastair T -- Law, Christopher J -- Isaacs, Neil W -- Cogdell, Richard J -- New York, N.Y. -- Science. 2003 Dec 12;302(5652):1969-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14671305" target="_blank"〉PubMed〈/a〉
    Keywords: Apoproteins/chemistry ; Bacterial Proteins/*chemistry ; Bacteriochlorophyll A/chemistry ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Light-Harvesting Protein Complexes/*chemistry ; Macromolecular Substances ; Models, Molecular ; Photosynthetic Reaction Center Complex Proteins/*chemistry ; Protein Conformation ; Protein Structure, Secondary ; Rhodopseudomonas/*chemistry ; Ubiquinone/chemistry
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    Mars-like soils in the Atacama Desert, Chile, and the dry limit of microbial life (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-08
    Description: The Viking missions showed the martian soil to be lifeless and depleted in organic material and indicated the presence of one or more reactive oxidants. Here we report the presence of Mars-like soils in the extreme arid region of the Atacama Desert. Samples from this region had organic species only at trace levels and extremely low levels of culturable bacteria. Two samples from the extreme arid region were tested for DNA and none was recovered. Incubation experiments, patterned after the Viking labeled-release experiment but with separate biological and nonbiological isomers, show active decomposition of organic species in these soils by nonbiological processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Navarro-Gonzalez, Rafael -- Rainey, Fred A -- Molina, Paola -- Bagaley, Danielle R -- Hollen, Becky J -- de la Rosa, Jose -- Small, Alanna M -- Quinn, Richard C -- Grunthaner, Frank J -- Caceres, Luis -- Gomez-Silva, Benito -- McKay, Christopher P -- New York, N.Y. -- Science. 2003 Nov 7;302(5647):1018-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratorio de Quimica de Plasmas y Estudios Planetarios, Instituto de Ciencias Nucleares, Universidad Nacional Autonoma de Mexico, Circuito Exterior, Ciudad Universitaria, Apartado Postal 70-543, Mexico City, 04510, Mexico.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14605363" target="_blank"〉PubMed〈/a〉
    Keywords: Air Microbiology ; Alanine/chemistry/metabolism ; Bacteria/classification/*growth & development/isolation & purification/metabolism ; Benzene/analysis ; Biodiversity ; Chile ; Colony Count, Microbial ; DNA, Bacterial/analysis/genetics ; *Desert Climate ; Formates/analysis/chemistry/metabolism ; Gas Chromatography-Mass Spectrometry ; Genes, rRNA ; Glucose/chemistry/metabolism ; Mars ; Organic Chemicals/analysis ; Oxidation-Reduction ; Photochemistry ; Polymerase Chain Reaction ; *Soil Microbiology ; Stereoisomerism ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structure and mechanism of the lactose permease of Escherichia coli (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-02
    Description: Membrane transport proteins that transduce free energy stored in electrochemical ion gradients into a concentration gradient are a major class of membrane proteins. We report the crystal structure at 3.5 angstroms of the Escherichia coli lactose permease, an intensively studied member of the major facilitator superfamily of transporters. The molecule is composed of N- and C-terminal domains, each with six transmembrane helices, symmetrically positioned within the permease. A large internal hydrophilic cavity open to the cytoplasmic side represents the inward-facing conformation of the transporter. The structure with a bound lactose homolog, beta-D-galactopyranosyl-1-thio-beta-D-galactopyranoside, reveals the sugar-binding site in the cavity, and residues that play major roles in substrate recognition and proton translocation are identified. We propose a possible mechanism for lactose/proton symport (co-transport) consistent with both the structure and a large body of experimental data.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abramson, Jeff -- Smirnova, Irina -- Kasho, Vladimir -- Verner, Gillian -- Kaback, H Ronald -- Iwata, So -- DK51131: 08/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):610-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Imperial College London, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Binding Sites ; Biological Transport ; Cell Membrane/enzymology ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry/enzymology ; Escherichia coli Proteins/chemistry/genetics/metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Ion Transport ; Lactose/*metabolism ; Membrane Transport Proteins/*chemistry/genetics/*metabolism ; Models, Molecular ; *Monosaccharide Transport Proteins ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protons ; Substrate Specificity ; *Symporters ; Thiogalactosides/metabolism
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    Climate-driven increases in global terrestrial net primary production from 1982 to 1999 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: Recent climatic changes have enhanced plant growth in northern mid-latitudes and high latitudes. However, a comprehensive analysis of the impact of global climatic changes on vegetation productivity has not before been expressed in the context of variable limiting factors to plant growth. We present a global investigation of vegetation responses to climatic changes by analyzing 18 years (1982 to 1999) of both climatic data and satellite observations of vegetation activity. Our results indicate that global changes in climate have eased several critical climatic constraints to plant growth, such that net primary production increased 6% (3.4 petagrams of carbon over 18 years) globally. The largest increase was in tropical ecosystems. Amazon rain forests accounted for 42% of the global increase in net primary production, owing mainly to decreased cloud cover and the resulting increase in solar radiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nemani, Ramakrishna R -- Keeling, Charles D -- Hashimoto, Hirofumi -- Jolly, William M -- Piper, Stephen C -- Tucker, Compton J -- Myneni, Ranga B -- Running, Steven W -- New York, N.Y. -- Science. 2003 Jun 6;300(5625):1560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Forestry, University of Montana, Missoula, MT 59801, USA. nemani@ntsg.umt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791990" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Carbon/analysis ; Carbon Dioxide ; *Climate ; *Ecosystem ; Geography ; *Plant Development ; Rain ; Seasons ; Soil ; Sunlight ; Temperature ; Time Factors ; Tropical Climate ; Volcanic Eruptions
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Planetary science. A liquid core for Mars? (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dehant, Veronique -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):260-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690177" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Evolution, Planetary ; Gravitation ; *Mars ; Pressure ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Architecture of succinate dehydrogenase and reactive oxygen species generation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-01
    Description: The structure of Escherichia coli succinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone. It was found that the SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species (ROS) formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of ROS. Furthermore, symptoms of genetic disorders associated with mitochondrial SQR mutations may be a result of ROS formation resulting from impaired electron transport in the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yankovskaya, Victoria -- Horsefield, Rob -- Tornroth, Susanna -- Luna-Chavez, Cesar -- Miyoshi, Hideto -- Leger, Christophe -- Byrne, Bernadette -- Cecchini, Gary -- Iwata, So -- GM61606/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):700-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Division, VA Medical Center, San Francisco, CA 94121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560550" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Anaerobiosis ; Binding Sites ; Crystallography, X-Ray ; Dinitrophenols/chemistry/pharmacology ; Electron Transport ; Electron Transport Complex II ; Escherichia coli/*enzymology ; Flavin-Adenine Dinucleotide/metabolism ; Heme/chemistry ; Models, Molecular ; Multienzyme Complexes/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Mutation ; Oxidation-Reduction ; Oxidoreductases/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Reactive Oxygen Species/*metabolism ; Succinate Dehydrogenase/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Succinic Acid/metabolism ; Superoxides/metabolism ; Ubiquinone/chemistry/metabolism
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    Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-06
    Description: The earliest of a series of copper efflux genes in Escherichia coli are controlled by CueR, a member of the MerR family of transcriptional activators. Thermodynamic calibration of CueR reveals a zeptomolar (10(-21) molar) sensitivity to free Cu+, which is far less than one atom per cell. Atomic details of this extraordinary sensitivity and selectivity for +1transition-metal ions are revealed by comparing the crystal structures of CueR and a Zn2+-sensing homolog, ZntR. An unusual buried metal-receptor site in CueR restricts the metal to a linear, two-coordinate geometry and uses helix-dipole and hydrogen-bonding interactions to enhance metal binding. This binding mode is rare among metalloproteins but well suited for an ultrasensitive genetic switch.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changela, Anita -- Chen, Kui -- Xue, Yi -- Holschen, Jackie -- Outten, Caryn E -- O'Halloran, Thomas V -- Mondragon, Alfonso -- F32 DK61868/DK/NIDDK NIH HHS/ -- GM08382/GM/NIGMS NIH HHS/ -- GM38784/GM/NIGMS NIH HHS/ -- GM51350/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1383-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, 2205Tech Drive, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958362" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Binding Sites ; Copper/*metabolism ; Crystallization ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Dimerization ; Escherichia coli/*chemistry/genetics/metabolism ; Escherichia coli Proteins/*chemistry/genetics/*metabolism ; Helix-Turn-Helix Motifs ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Metals/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Secondary ; Sequence Alignment ; Thermodynamics ; Transcription Factors/chemistry/genetics/metabolism ; Transcriptional Activation ; Zinc/metabolism
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    Planetary science. Iceball Mars? (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):234-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690163" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Extraterrestrial Environment ; *Ice ; *Mars ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Planetary science. New front-runner for carving Martian gullies (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610263" target="_blank"〉PubMed〈/a〉
    Keywords: Eukaryota ; Exobiology ; Extraterrestrial Environment ; Ice ; *Mars ; *Snow ; Temperature ; *Water
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    Structural biology. Breaching the barrier (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Locher, Kaspar P -- Bass, Randal B -- Rees, Douglas C -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):603-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Zurich, Zurich CH-8093, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893929" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Biological Transport ; Cell Membrane/enzymology ; Crystallography, X-Ray ; Escherichia coli/chemistry/enzymology ; Escherichia coli Proteins/*chemistry/metabolism ; Glycerophosphates/metabolism ; Lactose/metabolism ; Membrane Transport Proteins/*chemistry/metabolism ; Models, Molecular ; *Monosaccharide Transport Proteins ; Phosphates/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Symporters
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Climate change. Will ocean fertilization work? (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buesseler, Ken O -- Boyd, Philip W -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):67-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA. kbuesseler@whoi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12677048" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Biomass ; *Carbon Dioxide/metabolism ; *Iron ; Oceans and Seas ; Photosynthesis ; Phytoplankton/*growth & development/metabolism ; *Seawater ; Temperature
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    Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-28
    Description: Interleukin-6 (IL-6) is an immunoregulatory cytokine that activates a cell-surface signaling assembly composed of IL-6, the IL-6 alpha-receptor (IL-6Ralpha), and the shared signaling receptor gp130. The 3.65 angstrom-resolution structure of the extracellular signaling complex reveals a hexameric, interlocking assembly mediated by a total of 10 symmetry-related, thermodynamically coupled interfaces. Assembly of the hexameric complex occurs sequentially: IL-6 is first engaged by IL-6Ralpha and then presented to gp130in the proper geometry to facilitate a cooperative transition into the high-affinity, signaling-competent hexamer. The quaternary structures of other IL-6/IL-12 family signaling complexes are likely constructed by means of a similar topological blueprint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boulanger, Martin J -- Chow, Dar-chone -- Brevnova, Elena E -- Garcia, K Christopher -- AI51321/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology and Department of Structural Biology, Stanford University School of Medicine, Fairchild D319, 299 Campus Drive, Stanford, CA 94305-5124, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829785" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/*chemistry/*metabolism ; Binding Sites ; Crystallography, X-Ray ; Cytokine Receptor gp130 ; Humans ; Interleukin-6/*chemistry/*metabolism ; Macromolecular Substances ; Membrane Glycoproteins/*chemistry/*metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Interleukin-6/*chemistry/*metabolism ; Signal Transduction ; Thermodynamics
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    DNA: one teacher's reflection (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kennedy, Donald -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):213.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690152" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; DNA/chemistry/genetics/*history ; Gene Expression ; History, 20th Century ; History, 21st Century ; Models, Molecular ; Molecular Biology/education/*history ; Nucleic Acid Conformation
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    Comment on "Climate and management contributions to recent trends in U.S. agricultural yields" (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Lianhong -- New York, N.Y. -- Science. 2003 Jun 6;300(5625):1505; author reply 1505.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Environmental Science Division, Oak Ridge National Laboratory, Oak Ridge, TN 37830, USA. lianhong-gu@ornl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791966" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture/*methods/statistics & numerical data ; *Climate ; Crops, Agricultural/*growth & development ; Linear Models ; Soybeans/*growth & development ; Statistics as Topic ; Sunlight ; Temperature ; United States ; Weather ; Zea mays/*growth & development
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    Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-25
    Description: Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key membrane traffic regulators in eukaryotic cells whose function is governed by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using a combination of chemical synthesis and protein engineering, we generated and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of the complex was solved to 1.5 angstrom resolution and provides a structural basis for the ability of RabGDI to inhibit the release of nucleotide by Rab proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provides a molecular basis for understanding a RabGDI mutant that causes mental retardation in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rak, Alexey -- Pylypenko, Olena -- Durek, Thomas -- Watzke, Anja -- Kushnir, Susanna -- Brunsveld, Lucas -- Waldmann, Herbert -- Goody, Roger S -- Alexandrov, Kirill -- New York, N.Y. -- Science. 2003 Oct 24;302(5645):646-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physical Biochemistry, Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14576435" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography, X-Ray ; Guanine Nucleotide Dissociation Inhibitors/*chemistry/genetics/metabolism ; Guanosine Diphosphate/chemistry/metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Lipid Metabolism ; Magnesium/chemistry/metabolism ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; Protein Prenylation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; rab GTP-Binding Proteins/*chemistry/metabolism
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    Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-27
    Description: Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin filaments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the filament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lilic, Mirjana -- Galkin, Vitold E -- Orlova, Albina -- VanLoock, Margaret S -- Egelman, Edward H -- Stebbins, C Erec -- New York, N.Y. -- Science. 2003 Sep 26;301(5641):1918-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Microbiology, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14512630" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/metabolism ; Actins/*metabolism ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Binding Sites ; Crystallography, X-Ray ; Image Processing, Computer-Assisted ; Microfilament Proteins/*chemistry/genetics/*metabolism ; Microscopy, Electron ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Salmonella typhimurium/chemistry/*metabolism ; Sequence Deletion ; Subtilisin/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Geochemistry. Minerals cooked up in the laboratory call ancient microfossils into question (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2003 Nov 14;302(5648):1134.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14615504" target="_blank"〉PubMed〈/a〉
    Keywords: Australia ; Barium/chemistry ; Carbonates/chemistry ; *Fossils ; Geologic Sediments/*chemistry ; Life ; Organic Chemicals/chemistry ; Silicon Dioxide/chemistry ; Temperature
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  • 142
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    Protein conformational dynamics probed by single-molecule electron transfer (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-11
    Description: Electron transfer is used as a probe for angstrom-scale structural changes in single protein molecules. In a flavin reductase, the fluorescence of flavin is quenched by a nearby tyrosine residue by means of photo-induced electron transfer. By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, we were able to observe the variation of flavin-tyrosine distance over time. We could then determine the potential of mean force between the flavin and the tyrosine, and a correlation analysis revealed conformational fluctuation at multiple time scales spanning from hundreds of microseconds to seconds. This phenomenon suggests the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Haw -- Luo, Guobin -- Karnchanaphanurach, Pallop -- Louie, Tai-Man -- Rech, Ivan -- Cova, Sergio -- Xun, Luying -- Xie, X Sunney -- R01GM61577-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 10;302(5643):262-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14551431" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Catalysis ; Chemistry, Physical ; Computer Simulation ; Electrons ; Escherichia coli/enzymology ; FMN Reductase/*chemistry/genetics/metabolism ; Flavin Mononucleotide/*chemistry/metabolism ; Flavin-Adenine Dinucleotide/*chemistry/metabolism ; Flavins ; Fluorescence ; Hydrogen Bonding ; Likelihood Functions ; Mathematics ; Models, Molecular ; Mutagenesis, Site-Directed ; Photons ; Physicochemical Phenomena ; Protein Conformation ; Serine ; Spectrometry, Fluorescence ; Temperature ; Thermodynamics ; Tyrosine
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    Phosphadioxirane: a peroxide from an ortho-substituted arylphosphine and singlet dioxygen (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-11
    Description: We prepared the primary adduct for the reaction of singlet dioxygen (1O2) with an arylphosphine by using the sterically hindered arylphosphine tris(o-methoxyphenyl)phosphine. The resulting phosphadioxirane has a dioxygen molecule triangularly bound to the phosphorus atom. Olefin trapping experiments show that the phosphadioxirane can undergo nonradical oxygen atom-transfer reactions. Under protic conditions, two different intermediates are formed during the reaction of singlet dioxygen with tris(o-methoxyphenyl)phosphine, namely, the corresponding hydroperoxy arylphosphine and a hydroxy phosphorane. Experiments with other arylphosphines possessing different electronic and steric properties demonstrate that the relative stability of the tris(o-methoxyphenyl)phosphadioxirane is due to both steric and electronic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, David G -- Gao, Ruomei -- Celaje, Jeff -- Chung, Ha-Yong -- Selke, Matthias -- GM 08101/GM/NIGMS NIH HHS/ -- GM 64104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 10;302(5643):259-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, California State University, Los Angeles, Los Angeles, CA 90032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14551430" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Epoxy Compounds/*chemistry ; Heterocyclic Compounds, 1-Ring/*chemistry ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Organophosphorus Compounds/*chemistry ; Oxidation-Reduction ; Oxygen/chemistry ; Peroxides/*chemistry ; Phosphines/chemistry ; Phosphorus ; Physicochemical Phenomena ; Singlet Oxygen/chemistry ; Temperature
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  • 144
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    Fluid core size of Mars from detection of the solar tide (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-08
    Description: The solar tidal deformation of Mars, measured by its k2 potential Love number, has been obtained from an analysis of Mars Global Surveyor radio tracking. The observed k2 of 0.153 +/- 0.017 is large enough to rule out a solid iron core and so indicates that at least the outer part of the core is liquid. The inferred core radius is between 1520 and 1840 kilometers and is independent of many interior properties, although partial melt of the mantle is one factor that could reduce core size. Ice-cap mass changes can be deduced from the seasonal variations in air pressure and the odd gravity harmonic J3, given knowledge of cap mass distribution with latitude. The south cap seasonal mass change is about 30 to 40% larger than that of the north cap.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoder, C F -- Konopliv, A S -- Yuan, D N -- Standish, E M -- Folkner, W M -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):299-303. Epub 2003 Mar 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jet Propulsion Laboratory, California Institute of Technology, Pasadena, CA 91109, USA. Charles.F.Yoder@jpl.nasa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12624177" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Dry Ice ; Gravitation ; *Mars ; Mathematics ; Pressure ; Rotation ; Temperature
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    Comment on "Global biodiversity, biochemical kinetics, and the energetic-equivalence rule" (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Storch, David -- New York, N.Y. -- Science. 2003 Jan 17;299(5605):346; author reply 346.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biodiversity and Macroecology Group, Department of Animal and Plant Sciences, University of Sheffield, Sheffield S10 2TN, UK, and Center for Theoretical Study, Charles University, Jilska 1, 110 00 Prague, Czech Republic. storch@cts.cuni.cz〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12531999" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Constitution ; *Ecosystem ; Kinetics ; *Models, Biological ; Population Density ; Temperature ; Thermodynamics
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    Importance of surface morphology in interstellar H2 formation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-13
    Description: Detailed laboratory experiments on the formation of HD from atom recombination on amorphous solid water films show that this process is extremely efficient in a temperature range of 8 to 20 kelvin, temperatures relevant for H2 formation on dust grain surfaces in the interstellar medium (ISM). The fate of the 4.5 electron volt recombination energy is highly dependent on film morphology. These results suggest that grain morphology, rather than the detailed chemical nature of the grain surface, is most important in determining the energy content of the H2 as it is released from the grain into the ISM.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hornekaer, L -- Baurichter, A -- Petrunin, V V -- Field, D -- Luntz, A C -- New York, N.Y. -- Science. 2003 Dec 12;302(5652):1943-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of Southern Denmark, Denmark. hornekaer@fysik.sdu.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14671297" target="_blank"〉PubMed〈/a〉
    Keywords: Astronomical Phenomena ; *Astronomy ; *Cosmic Dust ; Extraterrestrial Environment ; Hydrogen/*chemistry ; Spectrum Analysis ; Temperature ; Thermodynamics ; Water
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    Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-15
    Description: A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also called 3CLpro), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) Mpro and for an inhibitor complex of porcine coronavirus [transmissible gastroenteritis virus (TGEV)] Mpro, and we constructed a homology model for SARS coronavirus (SARS-CoV) Mpro. The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV Mpro-mediated cleavage of a TGEV Mpro substrate. Molecular modeling suggests that available rhinovirus 3Cpro inhibitors may be modified to make them useful for treating SARS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anand, Kanchan -- Ziebuhr, John -- Wadhwani, Parvesh -- Mesters, Jeroen R -- Hilgenfeld, Rolf -- New York, N.Y. -- Science. 2003 Jun 13;300(5626):1763-7. Epub 2003 May 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry, University of Lubeck, D-23538 Lubeck, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12746549" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Chloromethyl Ketones/chemistry/metabolism ; Amino Acid Sequence ; *Antiviral Agents ; Binding Sites ; Catalytic Domain ; Coronavirus 229E, Human/*enzymology ; Crystallization ; Crystallography, X-Ray ; Cysteine Endopeptidases/*chemistry/metabolism ; Cysteine Proteinase Inhibitors/chemistry/metabolism ; Dimerization ; *Drug Design ; Humans ; Isoxazoles/chemistry/metabolism/pharmacology ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pyrrolidinones/chemistry/metabolism/pharmacology ; Recombinant Proteins/chemistry/metabolism ; SARS Virus/*drug effects/*enzymology ; Sequence Alignment ; Sequence Homology, Amino Acid ; Severe Acute Respiratory Syndrome/drug therapy ; Transmissible gastroenteritis virus/enzymology
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    Chemistry. Seeing is believing (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knowles, Jeremy -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):2002-3. Epub 2003 Mar 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA. jeremy_knowles@harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12637674" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Catalysis ; Chemistry, Physical ; Crystallization ; Crystallography, X-Ray ; Glucose-6-Phosphate/*analogs & derivatives/chemistry/metabolism ; Glucosephosphates/chemistry/metabolism ; Hydrogen Bonding ; Phosphoglucomutase/*chemistry/*metabolism ; Phosphoranes/chemistry ; Phosphorus/*chemistry ; Phosphorylation ; Physicochemical Phenomena ; Temperature
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    Design of a novel globular protein fold with atomic-level accuracy (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-25
    Description: A major challenge of computational protein design is the creation of novel proteins with arbitrarily chosen three-dimensional structures. Here, we used a general computational strategy that iterates between sequence design and structure prediction to design a 93-residue alpha/beta protein called Top7 with a novel sequence and topology. Top7 was found experimentally to be folded and extremely stable, and the x-ray crystal structure of Top7 is similar (root mean square deviation equals 1.2 angstroms) to the design model. The ability to design a new protein fold makes possible the exploration of the large regions of the protein universe not yet observed in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhlman, Brian -- Dantas, Gautam -- Ireton, Gregory C -- Varani, Gabriele -- Stoddard, Barry L -- Baker, David -- New York, N.Y. -- Science. 2003 Nov 21;302(5649):1364-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14631033" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Sequence ; Circular Dichroism ; Computational Biology ; Computer Graphics ; Computer Simulation ; Crystallization ; Crystallography, X-Ray ; Databases, Protein ; Models, Molecular ; Molecular Sequence Data ; Monte Carlo Method ; Nuclear Magnetic Resonance, Biomolecular ; *Protein Conformation ; Protein Denaturation ; *Protein Engineering ; *Protein Folding ; Protein Structure, Secondary ; Proteins/*chemistry ; *Software ; Solubility ; Temperature ; Thermodynamics
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    Climate change. Consensus on ecological impacts remains elusive (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jensen, Mari N -- New York, N.Y. -- Science. 2003 Jan 3;299(5603):38.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12511629" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Climate ; *Ecosystem ; *Greenhouse Effect ; Meta-Analysis as Topic ; Models, Statistical ; *Plant Physiological Phenomena ; Research Design ; Selection Bias ; Statistics as Topic ; Temperature
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    Self-assembled silica-carbonate structures and detection of ancient microfossils (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-15
    Description: We have synthesized inorganic micron-sized filaments, whose microstucture consists of silica-coated nanometer-sized carbonate crystals, arranged with strong orientational order. They exhibit noncrystallographic, curved, helical morphologies, reminiscent of biological forms. The filaments are similar to supposed cyanobacterial microfossils from the Precambrian Warrawoona chert formation in Western Australia, reputed to be the oldest terrestrial microfossils. Simple organic hydrocarbons, whose sources may also be abiotic and indeed inorganic, readily condense onto these filaments and subsequently polymerize under gentle heating to yield kerogenous products. Our results demonstrate that abiotic and morphologically complex microstructures that are identical to currently accepted biogenic materials can be synthesized inorganically.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia-Ruiz, J M -- Hyde, S T -- Carnerup, A M -- Christy, A G -- Van Kranendonk, M J -- Welham, N J -- New York, N.Y. -- Science. 2003 Nov 14;302(5648):1194-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto Andaluz de Ciencias de la Tierra, Consejo Superior de Investigaciones Cientificas Universidad de Granada, Facultad de Ciencias, Campus de Fuentenueva 18002, Granada, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14615534" target="_blank"〉PubMed〈/a〉
    Keywords: Australia ; Barium/chemistry ; Carbonates/*chemistry ; Crystallization ; Cyanobacteria ; Exobiology ; Formaldehyde/chemistry ; *Fossils ; Geologic Sediments/*chemistry ; Hydrocarbons/*chemistry ; Hydrogen-Ion Concentration ; Life ; Microscopy, Electron ; Microscopy, Electron, Scanning ; Molecular Conformation ; Phenol/chemistry ; Silicon Dioxide/*chemistry ; Temperature ; X-Ray Diffraction
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  • 152
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    Long-term region-wide declines in Caribbean corals (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-07-19
    Description: We report a massive region-wide decline of corals across the entire Caribbean basin, with the average hard coral cover on reefs being reduced by 80%, from about 50% to 10% cover, in three decades. Our meta-analysis shows that patterns of change in coral cover are variable across time periods but largely consistent across subregions, suggesting that local causes have operated with some degree of synchrony on a region-wide scale. Although the rate of coral loss has slowed in the past decade compared to the 1980s, significant declines are persisting. The ability of Caribbean coral reefs to cope with future local and global environmental change may be irretrievably compromised.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardner, Toby A -- Cote, Isabelle M -- Gill, Jennifer A -- Grant, Alastair -- Watkinson, Andrew R -- New York, N.Y. -- Science. 2003 Aug 15;301(5635):958-60. Epub 2003 Jul 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12869698" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/*growth & development ; Caribbean Region ; Disasters ; *Ecosystem ; Eukaryota/growth & development ; Population Dynamics ; Temperature ; Time Factors
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    Fluids from aging ocean crust that support microbial life (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-04
    Description: Little is known about the potential for life in the vast, low-temperature (〈100 degrees C) reservoir of fluids within mid-ocean ridge flank and ocean basin crust. Recently, an overpressured 300-meter-deep borehole was fitted with an experimental seal (CORK) delivering crustal fluids to the sea floor for discrete and large-volume sampling and characterization. Results demonstrate that the 65 degrees C fluids from 3.5-million-year-old ocean crust support microbial growth. Ribosomal RNA gene sequence data indicate the presence of diverse Bacteria and Archaea, including gene clones of varying degrees of relatedness to known nitrate reducers (with ammonia production), thermophilic sulfate reducers, and thermophilic fermentative heterotrophs, all consistent with fluid chemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cowen, James P -- Giovannoni, Stephen J -- Kenig, Fabien -- Johnson, H Paul -- Butterfield, David -- Rappe, Michael S -- Hutnak, Michael -- Lam, Phyllis -- New York, N.Y. -- Science. 2003 Jan 3;299(5603):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oceanography, School of Ocean and Earth Science and Technology, University of Hawaii, Honolulu, HI 96822, USA. jcowen@soest.hawaii.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12511653" target="_blank"〉PubMed〈/a〉
    Keywords: Ammonia/analysis/metabolism ; Archaea/cytology/*genetics/isolation & purification/physiology ; Bacteria/cytology/*growth & development/isolation & purification/metabolism ; Bacterial Physiological Phenomena ; Carboxylic Acids/metabolism ; Electrons ; Fermentation ; Genes, rRNA ; Geologic Sediments/*microbiology ; Hydrocarbons/metabolism ; Hydrogen/metabolism ; Hydrogen Sulfide/analysis/metabolism ; Nitrates/analysis/metabolism ; Nitrogen Fixation ; Oxidation-Reduction ; Pacific Ocean ; Phylogeny ; Seawater/chemistry/*microbiology ; Sulfates/analysis/metabolism ; Temperature
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    Ecology. An intimate knowledge of trees (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2003 Apr 25;300(5619):566-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12714718" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Carbon Dioxide/metabolism ; Costa Rica ; *Ecology ; Ecosystem ; *Greenhouse Effect ; History, 20th Century ; History, 21st Century ; Publishing ; Temperature ; *Trees/growth & development/metabolism ; *Tropical Climate ; United States
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  • 155
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    Molecular architecture of the multiprotein splicing factor SF3b (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-10
    Description: The splicing factor SF3b is a multiprotein complex essential for the accurate excision of introns from pre-messenger RNA. As an integral component of the U2 small nuclear ribonucleoprotein (snRNP) and the U11/U12 di-snRNP, SF3b is involved in the recognition of the pre-messenger RNA's branch site within the major and minor spliceosomes. We have determined the three-dimensional structure of the human SF3b complex by single-particle electron cryomicroscopy at a resolution of less than 10 angstroms, allowing identification of protein domains with known structural folds. The best fit of a modeled RNA-recognition motif indicates that the protein p14 is located in the central cavity of the complex. The 22 tandem helical repeats of the protein SF3b155 are located in the outer shell of the complex enclosing p14.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golas, Monika M -- Sander, Bjoern -- Will, Cindy L -- Luhrmann, Reinhard -- Stark, Holger -- New York, N.Y. -- Science. 2003 May 9;300(5621):980-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738865" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Cryoelectron Microscopy ; HeLa Cells ; Humans ; Image Processing, Computer-Assisted ; Macromolecular Substances ; Models, Molecular ; Multiprotein Complexes ; Phosphoproteins/*chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Precursors/chemistry/metabolism ; RNA Splicing ; *RNA-Binding Proteins ; Repetitive Sequences, Amino Acid ; Ribonucleoprotein, U2 Small Nuclear/*chemistry ; Spliceosomes/chemistry/metabolism
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    BAR domains as sensors of membrane curvature: the amphiphysin BAR structure (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-12-03
    Description: The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peter, Brian J -- Kent, Helen M -- Mills, Ian G -- Vallis, Yvonne -- Butler, P Jonathan G -- Evans, Philip R -- McMahon, Harvey T -- New York, N.Y. -- Science. 2004 Jan 23;303(5657):495-9. Epub 2003 Nov 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) 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/14645856" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/chemistry/genetics/metabolism ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; COP-Coated Vesicles/metabolism ; Carrier Proteins/chemistry/genetics/metabolism ; Cell Membrane/chemistry/metabolism ; Clathrin/metabolism ; Clathrin-Coated Vesicles/metabolism ; Coated Vesicles/chemistry/*metabolism ; Crystallography, X-Ray ; *Cytoskeletal Proteins ; Dimerization ; Drosophila/chemistry ; Drosophila Proteins/*chemistry/*metabolism ; GTPase-Activating Proteins/chemistry/metabolism ; Liposomes/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nerve Tissue Proteins/*chemistry/genetics/*metabolism ; Nuclear Proteins/chemistry/metabolism ; Phosphoproteins/chemistry/metabolism ; Protein Binding ; Protein Structure, Secondary ; *Protein Structure, Tertiary
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    Kinesin walks hand-over-hand (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-12-20
    Description: Kinesin is a processive motor that takes 8.3-nm center-of-mass steps along microtubules for each adenosine triphosphate hydrolyzed. Whether kinesin moves by a "hand-over-hand" or an "inchworm" model has been controversial. We have labeled a single head of the kinesin dimer with a Cy3 fluorophore and localized the position of the dye to within 2 nm before and after a step. We observed that single kinesin heads take steps of 17.3 +/- 3.3 nm. A kinetic analysis of the dwell times between steps shows that the 17-nm steps alternate with 0-nm steps. These results strongly support a hand-over-hand mechanism, and not an inchworm mechanism. In addition, our results suggest that kinesin is bound by both heads to the microtubule while it waits for adenosine triphosphate in between steps.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yildiz, Ahmet -- Tomishige, Michio -- Vale, Ronald D -- Selvin, Paul R -- AR42895/AR/NIAMS NIH HHS/ -- AR44420/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):676-8. Epub 2003 Dec 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14684828" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate ; Carbocyanines ; Dimerization ; Fluorescence ; Fluorescent Dyes ; Humans ; Kinesin/chemistry/genetics/*metabolism ; Kinetics ; Microtubules/*metabolism ; *Models, Biological ; Models, Molecular ; Molecular Motor Proteins/chemistry/genetics/*metabolism ; Mutation ; Protein Conformation
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  • 158
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    Morphology and composition of the surface of Mars: Mars Odyssey THEMIS results (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: The Thermal Emission Imaging System (THEMIS) on Mars Odyssey has produced infrared to visible wavelength images of the martian surface that show lithologically distinct layers with variable thickness, implying temporal changes in the processes or environments during or after their formation. Kilometer-scale exposures of bedrock are observed; elsewhere airfall dust completely mantles the surface over thousands of square kilometers. Mars has compositional variations at 100-meter scales, for example, an exposure of olivine-rich basalt in the walls of Ganges Chasma. Thermally distinct ejecta facies occur around some craters with variations associated with crater age. Polar observations have identified temporal patches of water frost in the north polar cap. No thermal signatures associated with endogenic heat sources have been identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christensen, Philip R -- Bandfield, Joshua L -- Bell, James F 3rd -- Gorelick, Noel -- Hamilton, Victoria E -- Ivanov, Anton -- Jakosky, Bruce M -- Kieffer, Hugh H -- Lane, Melissa D -- Malin, Michael C -- McConnochie, Timothy -- McEwen, Alfred S -- McSween, Harry Y Jr -- Mehall, Greg L -- Moersch, Jeffery E -- Nealson, Kenneth H -- Rice, James W Jr -- Richardson, Mark I -- Ruff, Steven W -- Smith, Michael D -- Titus, Timothy N -- Wyatt, Michael B -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2056-61. Epub 2003 Jun 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geological Sciences, Arizona State University, Tempe, AZ 85287-6305, USA. phil.christensen@asu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791998" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Dioxide ; Extraterrestrial Environment ; Geologic Sediments ; Geological Phenomena ; Geology ; *Mars ; Seasons ; Temperature ; Water
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    Deep-sea science. Cool corals become hot topic (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malakoff, David -- New York, N.Y. -- Science. 2003 Jan 10;299(5604):195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12522232" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa/physiology ; Conservation of Natural Resources ; Ecosystem ; International Cooperation ; Oceans and Seas ; Seawater ; Temperature
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    A nebular origin for chondritic fine-grained phyllosilicates (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-01-25
    Description: Hydrated minerals occur in accretionary rims around chondrules in CM chondrites. Previous models suggested that these phyllosilicates did not form by gas-solid reactions in the canonical solar nebula. We propose that chondrule-forming shock waves in icy regions of the nebula produced conditions that allowed rapid mineral hydration. The time scales for phyllosilicate formation are similar to the time it takes for a shocked system to cool from the temperature of phyllosilicate stability to that of water ice condensation. This scenario allows for simultaneous formation of chondrules and their fine-grained accretionary rims.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ciesla, Fred J -- Lauretta, Dante S -- Cohen, Barbara A -- Hood, Lon L -- New York, N.Y. -- Science. 2003 Jan 24;299(5606):549-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Planetary Sciences, Lunar and Planetary Laboratory, University of Arizona, 1629 East University Boulevard, Tucson, AZ 85721, USA. fciesla@lpl.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12543970" target="_blank"〉PubMed〈/a〉
    Keywords: Ice ; *Meteoroids ; Pressure ; *Silicates ; Temperature ; Thermodynamics ; *Water
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  • 161
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    Helical conformation of alkanes in a hydrophobic cavitand (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-30
    Description: Alkanes adopt extended conformations in solution that minimize steric interactions and maximize surface area. Folding can reduce the amount of hydrophobic surface exposed to solvent, but sterically unfavorable gauche interactions result. However, we found that the alkyl chains of two common surfactants in aqueous solution adopt helical conformations when bound within a synthetic receptor. The receptor recognizes the helical alkane better than the extended conformation, even though 2 to 3 kilocalories per mole of strain is introduced. The proper filling of space and burial of hydrophobic surface drive the molecular recognition between the receptor and the coiled alkane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trembleau, Laurent -- Rebek, Julius Jr -- GM 27932/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 29;301(5637):1219-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skaggs Institute for Chemical Biology and Department of Chemistry, 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/12947192" target="_blank"〉PubMed〈/a〉
    Keywords: Alkanes/*chemistry ; Benzimidazoles/*chemistry ; Chemistry, Physical ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Conformation ; Phosphorylcholine/*analogs & derivatives/*chemistry ; Physicochemical Phenomena ; Sodium Dodecyl Sulfate/*chemistry ; Solutions ; Surface Properties ; Surface-Active Agents/*chemistry ; Temperature ; Thermodynamics
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    Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-10-04
    Description: The cytochrome b6f complex provides the electronic connection between the photosystem I and photosystem II reaction centers of oxygenic photosynthesis and generates a transmembrane electrochemical proton gradient for adenosine triphosphate synthesis. A 3.0 angstrom crystal structure of the dimeric b6f complex from the thermophilic cyanobacterium Mastigocladus laminosus reveals a large quinone exchange cavity, stabilized by lipid, in which plastoquinone, a quinone-analog inhibitor, and a novel heme are bound. The core of the b6f complex is similar to the analogous respiratory cytochrome bc1 complex, but the domain arrangement outside the core and the complement of prosthetic groups are strikingly different. The motion of the Rieske iron-sulfur protein extrinsic domain, essential for electron transfer, must also be different in the b6f complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurisu, Genji -- Zhang, Huamin -- Smith, Janet L -- Cramer, William A -- GM-38323/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Nov 7;302(5647):1009-14. Epub 2003 Oct 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, 915 West State Street, Purdue University, West Lafayette, IN 47907-2054, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14526088" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Cyanobacteria/*chemistry/metabolism ; Cytochrome b6f Complex/*chemistry/metabolism ; Cytochromes f/chemistry/metabolism ; Dimerization ; Electron Transport ; Electron Transport Complex III/chemistry/metabolism ; Heme/chemistry ; Hydrophobic and Hydrophilic Interactions ; Iron-Sulfur Proteins/chemistry/metabolism ; Lipid Bilayers ; Models, Molecular ; *Photosynthesis ; Plastoquinone/chemistry/metabolism ; Polyenes/chemistry/metabolism ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Protons
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    Antibody multispecificity mediated by conformational diversity (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre-steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉James, Leo C -- Roversi, Pietro -- Tawfik, Dan S -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1362-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge CB2 2HQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610298" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4-Dinitrophenol/immunology ; Amino Acid Sequence ; Antibodies, Monoclonal/chemistry/immunology ; Antibody Diversity ; *Antibody Specificity ; Antigen-Antibody Complex ; Antigen-Antibody Reactions ; Antigens/*immunology ; Binding Sites, Antibody ; Cross Reactions ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Haptens/immunology ; Hydrogen Bonding ; Immunoglobulin E/*chemistry/*immunology ; Immunoglobulin Fragments/chemistry/immunology ; Isomerism ; Kinetics ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Peptide Library ; Protein Conformation ; Recombinant Proteins/immunology
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    Ecological consequences of a century of warming in Lake Tanganyika (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-06-28
    Description: Deep tropical lakes are excellent climate monitors because annual mixing is shallow and flushing rates are low, allowing heat to accumulate during climatic warming. We describe effects of warming on Lake Tanganyika: A sharpened density gradient has slowed vertical mixing and reduced primary production. Increased warming rates during the coming century may continue to slow mixing and further reduce productivity in Lake Tanganyika and other deep tropical lakes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verburg, Piet -- Hecky, Robert E -- Kling, Hedy -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):505-7. Epub 2003 Jun 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Waterloo, Waterloo, ON N2L 3G1, Canada. pverburg@scimail.uwaterloo.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829786" target="_blank"〉PubMed〈/a〉
    Keywords: Africa South of the Sahara ; Animals ; Biomass ; *Ecosystem ; Environment ; *Fresh Water/chemistry ; Greenhouse Effect ; Light ; Mollusca/physiology ; Oxygen/analysis ; Phosphorus/analysis ; Phytoplankton/physiology ; Seasons ; Silicon Dioxide/analysis ; Sulfur Compounds/analysis ; Temperature ; Time Factors ; *Tropical Climate
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    The structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-03
    Description: The sterol regulatory element-binding protein 2 (SREBP-2), a nuclear transcription factor that is essential for cholesterol metabolism, enters the nucleus through a direct interaction of its helix-loop-helix leucine zipper domain with importin-beta. We show the crystal structure of importin-beta complexed with the active form of SREBP-2. Importin-beta uses characteristic long helices like a pair of chopsticks to interact with an SREBP-2 dimer. Importin-beta changes its conformation to reveal a pseudo-twofold symmetry on its surface structure so that it can accommodate a symmetric dimer molecule. Importin-beta may use a similar strategy to recognize other dimeric cargoes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Soo Jae -- Sekimoto, Toshihiro -- Yamashita, Eiki -- Nagoshi, Emi -- Nakagawa, Atsushi -- Imamoto, Naoko -- Yoshimura, Masato -- Sakai, Hiroaki -- Chong, Khoon Tee -- Tsukihara, Tomitake -- Yoneda, Yoshihiro -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1571-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Graduate School of Frontier Biosciences, Osaka University, Yamadaoka 2-2, Suita, Osaka 565-0871, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645851" target="_blank"〉PubMed〈/a〉
    Keywords: *Active Transport, Cell Nucleus ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Nucleus/metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/*metabolism ; Dimerization ; Helix-Loop-Helix Motifs ; Humans ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Molecular Sequence Data ; Nuclear Localization Signals ; Nuclear Pore/metabolism ; Protein Binding ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sterol Regulatory Element Binding Protein 2 ; Transcription Factors/*chemistry/*metabolism ; beta Karyopherins/*chemistry/*metabolism ; ran GTP-Binding Protein/metabolism
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    Phase change and the regulation of developmental timing in plants (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-07-19
    Description: Plants produce different types of organs at different times in shoot development. Along with the major changes in organ morphology that take place during developmental transitions, more gradual patterns of variation occur. The identity of organs produced at a particular position on the shoot is determined by interactions between several independently regulated, temporally coordinated processes. Two of these processes are organ production and the specification of organ identity. Coordination of these processes is accomplished in part by a thermal clock and by signal transduction pathways that mediate the response of plants to light.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poethig, R Scott -- New York, N.Y. -- Science. 2003 Jul 18;301(5631):334-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Science Institute, Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA. spoethig@sas.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12869752" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Clocks/*physiology ; Cell Differentiation ; Gene Expression Regulation, Plant ; Genes, Plant ; Light ; Photoperiod ; *Plant Development ; Plant Shoots/*growth & development ; Plants/genetics ; Signal Transduction ; Temperature
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    Planetary science. The surface of Mars: not just dust and rocks (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golombek, Matthew P -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2043-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jet Propulsion Laboratory, California Institute of Technology, Pasadena, CA 91109, USA. mgolombek@jpl.nasa.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829771" target="_blank"〉PubMed〈/a〉
    Keywords: Evolution, Planetary ; Extraterrestrial Environment ; Geologic Sediments ; Geological Phenomena ; Geology ; *Mars ; Temperature
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    Steroid control of longevity in Drosophila melanogaster (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-03-01
    Description: Ecdysone, the major steroid hormone of Drosophila melanogaster, is known for its role in development and reproduction. Flies that are heterozygous for mutations of the ecdysone receptor exhibit increases in life-span and resistance to various stresses, with no apparent deficit in fertility or activity. A mutant involved in the biosynthesis of ecdysone displays similar effects, which are suppressed by feeding ecdysone to the flies. These observations demonstrate the importance of the ecdysone hormonal pathway, a new player in regulating longevity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simon, Anne F -- Shih, Cindy -- Mack, Antha -- Benzer, Seymour -- AG16630/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1407-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 156-29, California Institute of Technology, 1201 California Boulevard, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610309" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Weight ; Crosses, Genetic ; Drosophila melanogaster/genetics/growth & development/*physiology ; Ecdysone/biosynthesis/*physiology ; Ecdysterone/administration & dosage/pharmacology ; Female ; Fertility ; Genes, Insect ; Ligands ; *Longevity ; Male ; Mutation ; Oxidative Stress ; Phototropism ; Receptors, Steroid/genetics/*physiology ; Starvation ; Temperature
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    Oceanic Rossby waves acting as a "hay rake" for ecosystem floating by-products (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-04
    Description: Recent satellite observations of Rossby waves and chlorophyll anomalies propagating in subtropical gyres have suggested that wave-induced upwelling could stimulate photosynthesis. Instead, we show that chlorophyll maxima are located in abnormally warm water, in Rossby wave-induced convergences. This excludes inputs of nutrients from deeper water. We argue that the sea color anomalies are not caused by chlorophyll but by floating particles evolved from the ecosystem and accumulated by Rossby waves, acting as "marine hay rakes," in convergence zones. Such processes may be determinant for the distribution of living organisms in oligotrophic areas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dandonneau, Yves -- Vega, Andres -- Loisel, Hubert -- du Penhoat, Yves -- Menkes, Christophe -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉IRD, IPSL/Laboratoire d'Oceanographie Dynamique et de Climatologie, 75252 Paris 05, France. yd@lodyc.jussieu.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645844" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Chlorophyll/*analysis ; Color ; Computer Simulation ; *Ecosystem ; Light ; Oceanography/*methods ; Optics and Photonics ; Pacific Ocean ; *Phytoplankton ; Scattering, Radiation ; *Seawater ; Spacecraft ; Temperature ; Water Movements ; Wind
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    Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-02
    Description: The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single-binding site, alternating-access mechanism through a rocker-switch type of movement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Yafei -- Lemieux, M Joanne -- Song, Jinmei -- Auer, Manfred -- Wang, Da-Neng -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):616-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893936" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biological Transport ; Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry/enzymology ; Escherichia coli Proteins/chemistry/metabolism ; Glycerophosphates/*metabolism ; Helix-Turn-Helix Motifs ; Mass Spectrometry ; Membrane Transport Proteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Periplasm/metabolism ; Phosphates/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Watching a protein as it functions with 150-ps time-resolved x-ray crystallography (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-21
    Description: We report picosecond time-resolved x-ray diffraction from the myoglobin (Mb) mutant in which Leu29 is replaced by Phe (L29Fmutant). The frame-by-frame structural evolution, resolved to 1.8 angstroms, allows one to literally "watch" the protein as it executes its function. Time-resolved mid-infrared spectroscopy of flash-photolyzed L29F MbCO revealed a short-lived CO intermediate whose 140-ps lifetime is shorter than that found in wild-type protein by a factor of 1000. The electron density maps of the protein unveil transient conformational changes far more dramatic than the structural differences between the carboxy and deoxy states and depict the correlated side-chain motion responsible for rapidly sweeping CO away from its primary docking site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schotte, Friedrich -- Lim, Manho -- Jackson, Timothy A -- Smirnov, Aleksandr V -- Soman, Jayashree -- Olson, John S -- Phillips, George N Jr -- Wulff, Michael -- Anfinrud, Philip A -- AR40252/AR/NIAMS NIH HHS/ -- GM35649/GM/NIGMS NIH HHS/ -- HL47020/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 20;300(5627):1944-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney 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/12817148" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Binding Sites ; Carbon Monoxide/chemistry/metabolism ; Crystallography, X-Ray/*methods ; Fourier Analysis ; Heme/chemistry ; Ligands ; Models, Molecular ; Mutagenesis, Site-Directed ; Myoglobin/*chemistry/genetics/*metabolism ; Photolysis ; Protein Conformation ; Spectrophotometry, Infrared ; Time Factors ; Whales
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    A new class of bacterial RNA polymerase inhibitor affects nucleotide addition (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-25
    Description: RNA polymerase (RNAP) is the central enzyme of gene expression. Despite availability of crystal structures, details of its nucleotide addition cycle remain obscure. We describe bacterial RNAP inhibitors (the CBR703 series) whose properties illuminate this mechanism. These compounds inhibit known catalytic activities of RNAP (nucleotide addition, pyrophosphorolysis, and Gre-stimulated transcript cleavage) but not translocation of RNA or DNA when translocation is uncoupled from catalysis. CBR703-resistance substitutions occur on an outside surface of RNAP opposite its internal active site. We propose that CBR703 compounds inhibit nucleotide addition allosterically by hindering movements of active site structures that are linked to the CBR703 binding site through a bridge helix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Artsimovitch, Irina -- Chu, Clement -- Lynch, A Simon -- Landick, Robert -- GM38660/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 24;302(5645):650-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14576436" target="_blank"〉PubMed〈/a〉
    Keywords: Amidines/chemistry/isolation & purification/metabolism/*pharmacology ; Binding Sites ; Catalysis ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/*antagonists & ; inhibitors/chemistry/genetics/*metabolism ; Drug Resistance, Bacterial ; Enzyme Inhibitors/chemistry/isolation & purification/metabolism/pharmacology ; Escherichia coli/*drug effects/genetics ; Exodeoxyribonucleases/metabolism ; Hydroxylamines/chemistry/isolation & purification/metabolism/*pharmacology ; Models, Molecular ; Mutation ; Nucleotides/*metabolism ; Phenylurea Compounds/chemistry/isolation & purification/metabolism/pharmacology ; Piperazines/chemistry/isolation & purification/pharmacology ; Promoter Regions, Genetic/drug effects ; Protein Conformation ; Protein Structure, Secondary ; Pyrazoles/chemistry/isolation & purification/pharmacology ; RNA, Bacterial/*biosynthesis ; Templates, Genetic ; Transcription, Genetic/*drug effects
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    Planetary science. Learning to think like Martians (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zuber, Maria T -- New York, N.Y. -- Science. 2003 Dec 5;302(5651):1694-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth, Atmospheric and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. zuber@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14657483" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Carbon Dioxide ; Dry Ice ; Extraterrestrial Environment ; Ice ; *Mars ; Seasons ; Temperature
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    Programmed adsorption and release of proteins in a microfluidic device (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-19
    Description: A microfluidic device has been developed that can adsorb proteins from solution, hold them with negligible denaturation, and release them on command. The active element in the device is a 4-nanometer-thick polymer film that can be thermally switched between an antifouling hydrophilic state and a protein-adsorbing state that is more hydrophobic. This active polymer has been integrated into a microfluidic hot plate that can be programmed to adsorb and desorb protein monolayers in less than 1 second. The rapid response characteristics of the device can be manipulated for proteomic functions, including preconcentration and separation of soluble proteins on an integrated fluidics chip.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, Dale L -- Manginell, Ronald P -- Samara, Michael A -- Kim, Byung-Il -- Bunker, Bruce C -- New York, N.Y. -- Science. 2003 Jul 18;301(5631):352-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sandia National Laboratory, Post Office Box 5800, Albuquerque, NM 87185-1413, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12869757" target="_blank"〉PubMed〈/a〉
    Keywords: Acrylic Resins ; Adsorption ; Biochemistry/instrumentation/*methods ; Cytochrome c Group/chemistry ; Hemoglobins/chemistry ; Hydrophobic and Hydrophilic Interactions ; Microchemistry ; Miniaturization ; Proteins/*chemistry ; Serum Albumin, Bovine/chemistry ; Spectrophotometry, Ultraviolet ; Temperature
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    Chemistry. The motions of an enzyme soloist (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-10-11
    Description: Dynamics of proteins are crucial to their function. In his Perspective, Orrit stresses the advantages of studying these dynamics with single-molecule methods--which require no synchronization--rather than with conventional ensemble measurements. He highlights the report by Yang et al., who follow the fluorescence of a single enzyme molecule. Electron transfer from the fluorophore to a quencher induces fluctuations of the fluorescence lifetime along with the fluorophore-quencher distance. The wide range of characteristic times of those fluctuations reveals the complexity of the protein's potential energy landscape. As a new molecular ruler, electron transfer complements other single-molecule methods such as energy transfer (FRET) for distances shorter than a few nanometers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orrit, Michel -- New York, N.Y. -- Science. 2003 Oct 10;302(5643):239-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NanoOptics and Spins, Leiden Institute of Physics, Leiden University, Post Office Box 9504, Netherlands. orrit@molphys.leidenuniv.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14551425" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Chemistry, Physical ; Electrons ; Escherichia coli/enzymology ; FMN Reductase/*chemistry/genetics/metabolism ; Flavin Mononucleotide/*chemistry/metabolism ; Flavin-Adenine Dinucleotide/*chemistry/metabolism ; Flavins/chemistry ; Fluorescence ; Hydrogen Bonding ; Lasers ; Likelihood Functions ; Mathematics ; Mutation ; Photons ; Physicochemical Phenomena ; *Protein Conformation ; Serine/chemistry ; Spectrometry, Fluorescence ; Temperature ; Thermodynamics ; Tyrosine
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    Equatorial retention of the contractile actin ring by microtubules during cytokinesis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: In most eukaryotes cytokinesis is brought about by a contractile actin ring located at the division plane. Here, in fission yeast the actin ring was found to be required to generate late-mitotic microtubular structures located at the division plane, and these in turn maintained the medial position of the actin ring. When these microtubular structures were disrupted, the actin ring migrated away from the cell middle in a membrane traffic-dependent manner, resulting in asymmetrical cell divisions that led to genomic instability. We propose that these microtubular structures contribute to a checkpoint control that retains the equatorial position of the ring when progression through cytokinesis is delayed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pardo, Mercedes -- Nurse, Paul -- New York, N.Y. -- Science. 2003 Jun 6;300(5625):1569-74.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Cycle Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, UK. mercedes.pardo@cancer.org.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791993" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*physiology ; Anaphase ; Benzimidazoles/pharmacology ; Bicyclo Compounds, Heterocyclic/pharmacology ; *Carbamates ; Cell Cycle Proteins/physiology ; Cell Division/*physiology ; Cell Nucleus/physiology ; Cytoskeletal Proteins/physiology ; Interphase ; Microtubule-Organizing Center/physiology/ultrastructure ; Microtubules/*physiology/ultrastructure ; Mitosis ; Mutation ; Recombinant Fusion Proteins/metabolism ; Schizosaccharomyces/cytology/genetics/*physiology ; Schizosaccharomyces pombe Proteins/genetics/metabolism/physiology ; Temperature ; Thiazoles/pharmacology ; Thiazolidines ; Tubulin/metabolism
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    Visualizing tmRNA entry into a stalled ribosome (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-05
    Description: Bacterial ribosomes stalled on defective messenger RNAs (mRNAs) are rescued by tmRNA, an approximately 300-nucleotide-long molecule that functions as both transfer RNA (tRNA) and mRNA. Translation then switches from the defective message to a short open reading frame on tmRNA that tags the defective nascent peptide chain for degradation. However, the mechanism by which tmRNA can enter and move through the ribosome is unknown. We present a cryo-electron microscopy study at approximately 13 to 15 angstroms of the entry of tmRNA into the ribosome. The structure reveals how tmRNA could move through the ribosome despite its complicated topology and also suggests roles for proteins S1 and SmpB in the function of tmRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valle, Mikel -- Gillet, Reynald -- Kaur, Sukhjit -- Henne, Anke -- Ramakrishnan, V -- Frank, Joachim -- GM 44973/GM/NIGMS NIH HHS/ -- GM29169/GM/NIGMS NIH HHS/ -- GM55440/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):127-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Wadsworth Center, Health Research, Inc., Empire State Plaza, Albany, NY 12201-0509, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12677067" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine ; Anticodon ; Bacterial Proteins/metabolism ; Codon ; Codon, Terminator ; Cryoelectron Microscopy ; Guanosine Triphosphate/metabolism ; Image Processing, Computer-Assisted ; Models, Molecular ; *Nucleic Acid Conformation ; Open Reading Frames ; Peptide Elongation Factor Tu/metabolism ; Protein Biosynthesis ; Pyridones/pharmacology ; RNA, Bacterial/*chemistry/*metabolism ; RNA, Messenger/chemistry/metabolism ; RNA, Transfer/chemistry/metabolism ; RNA-Binding Proteins/chemistry/metabolism ; Ribosomal Proteins/chemistry/metabolism ; Ribosomes/*metabolism ; Thermus thermophilus/chemistry/genetics/*metabolism
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    On the origins of morphological complexity in block copolymer surfactants (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-19
    Description: Amphiphilic compounds such as lipids and surfactants are fundamental building blocks of soft matter. We describe experiments with poly(1,2-butadiene-b-ethylene oxide) (PB-PEO) diblock copolymers, which form Y-junctions and three-dimensional networks in water at weight fractions of PEOintermediate to those associated with vesicle and wormlike micelle morphologies. Fragmentation of the network produces a nonergodic array of complex reticulated particles that have been imaged by cryogenic transmission electron microscopy. Data obtained with two sets of PB-PEOcompounds indicate that this type of self-assembly appears above a critical molecular weight. These block copolymers represent versatile amphiphiles, mimicking certain low molecular weight three-component (surfactant/water/oil) microemulsions, without addition of a separate hydrophobe.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jain, Sumeet -- Bates, Frank S -- 1R21EB00989-01/EB/NIBIB NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 18;300(5618):460-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12702869" target="_blank"〉PubMed〈/a〉
    Keywords: Butadienes/*chemistry ; Chemistry, Physical ; Cryoelectron Microscopy ; Macromolecular Substances ; Micelles ; Molecular Structure ; Molecular Weight ; Physicochemical Phenomena ; Polyethylene/*chemistry ; Polymers/*chemistry ; Solubility ; Surface-Active Agents/*chemistry ; Temperature ; Thermodynamics ; Viscosity ; Water
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    DNA's cast of thousands (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):282-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690186" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Chromatin/chemistry/metabolism ; DNA/chemistry/*history/metabolism ; DNA Replication ; DNA-Directed DNA Polymerase/chemistry/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Gene Expression Regulation ; *Genetic Code ; Histones/metabolism ; History, 20th Century ; Humans ; Models, Molecular ; Molecular Biology/*history ; Molecular Structure ; Nucleic Acid Conformation ; Proteins/metabolism ; RNA, Messenger/genetics/metabolism ; Templates, Genetic ; Transcription Factors/metabolism
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    Spatiotemporal rescue of memory dysfunction in Drosophila (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-06
    Description: We have developed a method for temporal and regional gene expression targeting (TARGET) in Drosophila and show the simultaneous spatial and temporal rescue of a memory defect. The transient expression of the rutabaga-encoded adenylyl cyclase in the mushroom bodies of the adult brain was necessary and sufficient to rescue the rutabaga memory deficit, which rules out a developmental brain defect in the etiology of this deficit and demonstrates an acute role for rutabaga in memory formation in these neurons. The TARGET system offers general utility in simultaneously addressing issues of when and where gene products are required.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGuire, Sean E -- Le, Phuong T -- Osborn, Alexander J -- Matsumoto, Kunihiro -- Davis, Ronald L -- GM63929/GM/NIGMS NIH HHS/ -- NS19904/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Dec 5;302(5651):1765-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular 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/14657498" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*genetics/*metabolism ; Animals ; Animals, Genetically Modified ; Cloning, Molecular ; DNA-Binding Proteins ; Drosophila/genetics/growth & development/*physiology ; Drosophila Proteins/*genetics/*metabolism ; *Gene Expression ; Genotype ; Green Fluorescent Proteins ; Luminescent Proteins/genetics/metabolism ; Memory/*physiology ; Mushroom Bodies/*physiology ; Neuronal Plasticity ; Phenotype ; Repressor Proteins/genetics/metabolism ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Temperature ; Transcription Factors/genetics/metabolism ; Transgenes
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    Structural biology. Learning to speak the language of proteins (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, David T -- New York, N.Y. -- Science. 2003 Nov 21;302(5649):1347-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Computer Science and Department of Biochemistry and Molecular Biology, University College, London WC1E 6BT, UK. dtj@cs.ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14631028" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Sequence ; Computational Biology ; Computer Graphics ; Computer Simulation ; Crystallography, X-Ray ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; *Protein Conformation ; *Protein Engineering ; *Protein Folding ; Proteins/*chemistry ; *Software
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 182
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    Glacial refugia: hotspots but not melting pots of genetic diversity (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: Glacial refuge areas are expected to harbor a large fraction of the intraspecific biodiversity of the temperate biota. To test this hypothesis, we studied chloroplast DNA variation in 22 widespread European trees and shrubs sampled in the same forests. Most species had genetically divergent populations in Mediterranean regions, especially those with low seed dispersal abilities. However, the genetically most diverse populations were not located in the south but at intermediate latitudes, a likely consequence of the admixture of divergent lineages colonizing the continent from separate refugia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petit, Remy J -- Aguinagalde, Itziar -- de Beaulieu, Jacques-Louis -- Bittkau, Christiane -- Brewer, Simon -- Cheddadi, Rachid -- Ennos, Richard -- Fineschi, Silvia -- Grivet, Delphine -- Lascoux, Martin -- Mohanty, Aparajita -- Muller-Starck, Gerhard -- Demesure-Musch, Brigitte -- Palme, Anna -- Martin, Juan Pedro -- Rendell, Sarah -- Vendramin, Giovanni G -- New York, N.Y. -- Science. 2003 Jun 6;300(5625):1563-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Recherche Agronomique, UMR Biodiversite, Genes et Ecosystemes, F-33612 Cestas, France. petit@pierroton.inra.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791991" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/*genetics ; DNA, Chloroplast/*genetics ; *Ecosystem ; Europe ; *Genetic Variation ; Genetics, Population ; Geography ; Haplotypes ; Seeds ; Temperature ; Trees/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Samples of stars beyond the solar system: silicate grains in interplanetary dust (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: We have identified six circumstellar silicate grains within interplanetary dust particles (IDPs). Their extrasolar origins are demonstrated by their extremely anomalous oxygen isotopic compositions. Three 17O-rich grains appear to originate from red giant or asymptotic giant branch stars. One 16O-rich grain may be from a metal-poor star. Two 16O-poor grains have unknown stellar sources. One of the grains is forsterite, and two are amorphous silicate "GEMS" (glass with embedded metal and sulfides), which is consistent with astronomical identifications of crystalline and amorphous silicates in the outflows of evolved stars. These observations suggest cometary origins of these IDPs and underscore the perplexing absence of silicates among circumstellar dust grains from meteorites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Messenger, Scott -- Keller, Lindsay P -- Stadermann, Frank J -- Walker, Robert M -- Zinner, Ernst -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):105-8. Epub 2003 Feb 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Space Sciences and Physics Department, Washington University, St. Louis, MO 63130, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610229" target="_blank"〉PubMed〈/a〉
    Keywords: Astronomical Phenomena ; *Astronomy ; Carbon ; *Cosmic Dust ; Meteoroids ; *Oxygen Isotopes ; *Silicates ; Solar System ; Temperature
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  • 184
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    Kinesin moves by an asymmetric hand-over-hand mechanism (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-06
    Description: Kinesin is a double-headed motor protein that moves along microtubules in 8-nanometer steps. Two broad classes of model have been invoked to explain kinesin movement: hand-over-hand and inchworm. In hand-over-hand models, the heads exchange leading and trailing roles with every step, whereas no such exchange is postulated for inchworm models, where one head always leads. By measuring the stepwise motion of individual enzymes, we find that some kinesin molecules exhibit a marked alternation in the dwell times between sequential steps, causing these motors to "limp" along the microtubule. Limping implies that kinesin molecules strictly alternate between two different conformations as they step, indicative of an asymmetric, hand-over-hand mechanism.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1523256/" 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/PMC1523256/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Asbury, Charles L -- Fehr, Adrian N -- Block, Steven M -- R01 GM051453/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Dec 19;302(5653):2130-4. Epub 2003 Dec 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14657506" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Computer Simulation ; Decapodiformes/enzymology ; Dimerization ; Drosophila Proteins/chemistry/physiology ; Drosophila melanogaster/*enzymology ; Humans ; Kinesin/*chemistry/*physiology ; Kinetics ; Microspheres ; Microtubules/metabolism ; Models, Molecular ; Molecular Motor Proteins/*chemistry/*physiology ; Movement ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Rotation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 185
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    Atmospheric science. Pinatubo, diffuse light, and the carbon cycle (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farquhar, Graham D -- Roderick, Michael L -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):1997-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cooperative Research Centre for Greenhouse Accounting, Research School of Biological Sciences, Institute of Advanced Studies, Australian National University, Canberra ACT 0200, Australia. michael.roderick@anu.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12663904" target="_blank"〉PubMed〈/a〉
    Keywords: *Atmosphere ; *Carbon Dioxide/metabolism ; Climate ; Philippines ; *Photosynthesis ; Scattering, Radiation ; Sunlight ; Temperature ; Trees/*metabolism ; *Volcanic Eruptions
    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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  • 186
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    Planetary science. Peering into stardust (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tielens, A G G M -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):68-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Space Organization of the Netherlands (SRON)-Kapteyn Astronomical Institute, 9700 AV Groningen, Netherlands. tielens@astro.rug.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12677049" target="_blank"〉PubMed〈/a〉
    Keywords: Astronomical Phenomena ; *Astronomy ; Carbon ; *Cosmic Dust ; Meteoroids ; *Oxygen Isotopes ; *Silicates ; Solar System ; Temperature
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  • 187
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    Heat and biodiversity (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huston, Michael A -- New York, N.Y. -- Science. 2003 Jan 24;299(5606):512-3; author reply 512-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12546005" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Ecosystem ; Geography ; Models, Biological ; Plant Physiological Phenomena ; Temperature ; Trees ; Tropical Climate
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 188
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    Wildlife. In search of the ivory gull (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krajick, Kevin -- New York, N.Y. -- Science. 2003 Sep 26;301(5641):1840-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14512601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arctic Regions ; Behavior, Animal ; *Birds ; Canada ; *Cold Climate ; Conservation of Natural Resources ; *Ecosystem ; Environment ; Ice ; Population Density ; Temperature
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  • 189
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    Crystal structure of the potassium channel KirBac1.1 in the closed state (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-10
    Description: The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuo, Anling -- Gulbis, Jacqueline M -- Antcliff, Jennifer F -- Rahman, Tahmina -- Lowe, Edward D -- Zimmer, Jochen -- Cuthbertson, Jonathan -- Ashcroft, Frances M -- Ezaki, Takayuki -- Doyle, Declan A -- New York, N.Y. -- Science. 2003 Jun 20;300(5627):1922-6. Epub 2003 May 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738871" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Burkholderia pseudomallei/*chemistry ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrophobic and Hydrophilic Interactions ; *Ion Channel Gating ; Ion Transport ; Models, Molecular ; Molecular Sequence Data ; Potassium/metabolism ; Potassium Channels, Inwardly Rectifying/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 190
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    Single-molecule measurement of protein folding kinetics (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-08-30
    Description: In order to investigate the behavior of single molecules under conditions far from equilibrium, we have coupled a microfabricated laminar-flow mixer to a confocal optical system. This combination enables time-resolved measurement of Forster resonance energy transfer after an abrupt change in solution conditions. Observations of a small protein show the evolution of the intramolecular distance distribution as folding progresses. This technique can expose subpopulations, such as unfolded protein under conditions favoring the native structure, that would be obscured in equilibrium experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lipman, Everett A -- Schuler, Benjamin -- Bakajin, Olgica -- Eaton, William A -- New York, N.Y. -- Science. 2003 Aug 29;301(5637):1233-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Building 5, Room 104, National Institutes of Health, Bethesda, MD 20892-0520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12947198" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry ; Cold Temperature ; Diffusion ; Energy Transfer ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Kinetics ; Models, Molecular ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Thermodynamics ; Thermotoga maritima/*chemistry
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  • 191
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    A four-base paired genetic helix with expanded size (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-11-01
    Description: We describe a new molecular class of genetic-pairing system that has a native DNA backbone but has all four base pairs replaced by new, larger pairs. The base pairs include size-expanded analogs of thymine and of adenine, both extended by the width of a benzene ring (2.4 A). The expanded-diameter double helices are more thermodynamically stable than the Watson-Crick helix, likely because of enhanced base stacking. Structural data confirm a right-handed, double-stranded, and base-paired helical form. Because of the larger base size, all the pairs of this helical system are fluorescent, which suggests practical applications in detection of natural DNA and RNA. Our findings establish that there is no apparent structural or thermodynamic prohibition against genetic systems having sizes different from the natural one.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Haibo -- Gao, Jianmin -- Lynch, Stephen R -- Saito, Y David -- Maynard, Lystranne -- Kool, Eric T -- GM52956/GM/NIGMS NIH HHS/ -- GM63587/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593180" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/*analogs & derivatives/chemistry ; *Base Pairing ; Base Sequence ; Benzene/chemistry ; Circular Dichroism ; Hydrogen Bonding ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; *Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/*chemistry ; Temperature ; Thermodynamics ; Thymine/*analogs & derivatives/chemistry
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  • 192
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    Ecology. Global climate change strikes a tropical lake (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Livingstone, Daniel A -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):468-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and the Division of Earth and Ocean Science, Duke University, Durham, NC 27708, USA. livingst@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12881557" target="_blank"〉PubMed〈/a〉
    Keywords: Africa South of the Sahara ; Animals ; Conservation of Natural Resources ; Diatoms/physiology ; *Ecosystem ; Environment ; Fishes/physiology ; *Fresh Water/chemistry ; Greenhouse Effect ; Mollusca/physiology ; Photosynthesis ; Plankton/physiology ; Seasons ; Temperature ; Time Factors ; *Tropical Climate
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  • 193
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    Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-05-24
    Description: The phosphorylation of heptahelical receptors by heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is a universal regulatory mechanism that leads to desensitization of G protein signaling and to the activation of alternative signaling pathways. We determined the crystallographic structure of bovine GRK2 in complex with G protein beta1gamma2 subunits. Our results show how the three domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective activities and recruit the enzyme to the cell membrane in an orientation that not only facilitates receptor phosphorylation, but also allows for the simultaneous inhibition of signaling by Galpha and Gbetagamma subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lodowski, David T -- Pitcher, Julie A -- Capel, W Darrell -- Lefkowitz, Robert J -- Tesmer, John J G -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2003 May 23;300(5623):1256-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12764189" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cattle ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Cyclic AMP-Dependent Protein Kinases/*chemistry/*metabolism ; *GTP-Binding Protein beta Subunits ; *GTP-Binding Protein gamma Subunits ; Heterotrimeric GTP-Binding Proteins/*chemistry/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Signal Transduction ; beta-Adrenergic Receptor Kinases
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  • 194
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    High deleterious genomic mutation rate in stationary phase of Escherichia coli (2003)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2003-12-04
    Description: In natural habitats, bacteria spend most of their time in some form of growth arrest. Little is known about deleterious mutations in such stages, and consequently there is limited understanding of what evolutionary events occur. In a deleterious mutation accumulation experiment in prolonged stationary phase of Escherichia coli, about 0.03 slightly deleterious mutations were observed per genome per day. This is over an order of magnitude higher than extrapolations from fast-growing cells, but in line with inferences from observations in adaptive stationary phase mutation experiments. These findings may affect understanding of bacterial evolution and the emergence of bacterial pathogenicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loewe, Laurence -- Textor, Volker -- Scherer, Siegfried -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1558-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbial Ecology Group, Department of Biosciences, Technische Universitat Munchen, Weihenstephaner Berg 3, 85354 Freising, Germany. Laurence.Loewe@evolutionary-research.net〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645846" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Escherichia coli/*genetics/*growth & development ; *Genome, Bacterial ; Likelihood Functions ; *Mutation ; Phenotype ; Selection, Genetic ; Temperature ; Time Factors
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    Acclimation capacity underlies susceptibility to climate change (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stillman, Jonathon H -- New York, N.Y. -- Science. 2003 Jul 4;301(5629):65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hopkins Marine Station, Stanford University, Ocean-view Boulevard, Pacific Grove, CA 93950, USA. jstillman@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12843385" target="_blank"〉PubMed〈/a〉
    Keywords: *Acclimatization ; Animals ; Anomura/*physiology ; Biological Evolution ; California ; *Climate ; *Ecosystem ; *Environment ; Heart/physiology ; Heart Rate ; Mexico ; Oregon ; Pacific Ocean ; Phylogeny ; Species Specificity ; Temperature
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  • 196
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    Gating the selectivity filter in ClC chloride channels (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-22
    Description: ClC channels conduct chloride (Cl-) ions across cell membranes and thereby govern the electrical activity of muscle cells and certain neurons, the transport of fluid and electrolytes across epithelia, and the acidification of intracellular vesicles. The structural basis of ClC channel gating was studied. Crystal structures of wild-type and mutant Escherichia coli ClC channels bound to a monoclonal Fab fragment reveal three Cl- binding sites within the 15-angstrom neck of an hourglass-shaped pore. The Cl- binding site nearest the extracellular solution can be occupied either by a Cl- ion or by a glutamate carboxyl group. Mutations of this glutamate residue in Torpedo ray ClC channels alter gating in electrophysiological assays. These findings reveal a form of gating in which the glutamate carboxyl group closes the pore by mimicking a Cl- ion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dutzler, Raimund -- Campbell, Ernest B -- MacKinnon, Roderick -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):108-12. Epub 2003 Mar 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, 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/12649487" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Antibodies, Monoclonal/immunology ; Binding Sites ; Chloride Channels/*chemistry/genetics/immunology/*physiology ; Chlorides/*metabolism ; Crystallography, X-Ray ; Dimerization ; Escherichia coli/chemistry/metabolism ; Escherichia coli Proteins/chemistry/genetics/immunology/metabolism ; Glutamates/chemistry/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Immunoglobulin Fab Fragments/immunology ; *Ion Channel Gating ; Models, Molecular ; Oocytes ; Patch-Clamp Techniques ; Point Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Torpedo ; Xenopus
    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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  • 197
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    Agriculture. Study shows richer harvests owe much to climate (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2003 Feb 14;299(5609):997.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12586915" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture/*methods ; *Climate ; Crops, Agricultural/*growth & development ; Developing Countries ; Models, Statistical ; Soybeans/*growth & development ; Temperature ; United States ; Zea mays/*growth & development
    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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  • 198
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    Structural biology. A menage a trois in two configurations (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sadler, J Evan -- New York, N.Y. -- Science. 2003 Jul 11;301(5630):177-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Washington University, St. Louis, MO 63110, USA. esadler@im.wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12855796" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Blood Coagulation ; Blood Platelets/chemistry/metabolism ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Models, Molecular ; Platelet Aggregation ; Platelet Glycoprotein GPIb-IX Complex/chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Thrombin/*chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 199
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    Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-12
    Description: Thrombin bound to platelets contributes to stop bleeding and, in pathological conditions, may cause vascular thrombosis. We have determined the structure of platelet glycoprotein Ibalpha (GpIbalpha) bound to thrombin at 2.3 angstrom resolution and defined two sites in GpIbalpha that bind to exosite II and exosite I of two distinct alpha-thrombin molecules, respectively. GpIbalpha occupancy may be sequential, as the site binding to alpha-thrombin exosite I appears to be cryptic in the unoccupied receptor but exposed when a first thrombin molecule is bound through exosite II. These interactions may modulate alpha-thrombin function by mediating GpIbalpha clustering and cleavage of protease-activated receptors, which promote platelet activation, while limiting fibrinogen clotting through blockade of exosite I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celikel, Reha -- McClintock, Richard A -- Roberts, James R -- Mendolicchio, G Loredana -- Ware, Jerry -- Varughese, Kottayil I -- Ruggeri, Zaverio M -- HL-31950/HL/NHLBI NIH HHS/ -- HL-42846/HL/NHLBI NIH HHS/ -- HL-48728/HL/NHLBI NIH HHS/ -- HL-55375/HL/NHLBI NIH HHS/ -- R01 HL042846/HL/NHLBI NIH HHS/ -- RR0833/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 11;301(5630):218-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Thrombosis and Hemostasis, 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/12855810" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Blood Coagulation ; Blood Platelets/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Fibrinogen/metabolism ; Humans ; Hydrogen Bonding ; Ligands ; Models, Molecular ; Mutation ; Platelet Aggregation ; Platelet Glycoprotein GPIb-IX Complex/*chemistry/genetics/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Thrombin/*chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 200
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    Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-15
    Description: Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karlsson, Andreas -- Parales, Juanito V -- Parales, Rebecca E -- Gibson, David T -- Eklund, Hans -- Ramaswamy, S -- GM29909/GM/NIGMS NIH HHS/ -- GM62904/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Feb 14;299(5609):1039-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Swedish University of Agricultural Sciences, Box 590, Biomedical Center, 75124 Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12586937" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Chemistry, Physical ; Crystallization ; Crystallography, X-Ray ; Dioxygenases ; Hydroxylation ; Indoles/metabolism ; Iron/chemistry/*metabolism ; Models, Chemical ; Models, Molecular ; Molecular Structure ; Multienzyme Complexes/*chemistry/*metabolism ; Naphthalenes ; Oxidation-Reduction ; Oxygen/chemistry/*metabolism ; Oxygenases/*chemistry/*metabolism ; Physicochemical Phenomena ; Protein Conformation ; Protons ; Pseudomonas/enzymology ; Stereoisomerism
    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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