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  • Articles  (209)
  • Rats  (70)
  • Phosphorylation  (58)
  • Models, Molecular  (50)
  • Temperature  (48)
  • American Association for the Advancement of Science (AAAS)  (209)
  • American Chemical Society
  • Blackwell Publishing Ltd
  • 1995-1999  (209)
  • 1980-1984
  • 1925-1929
  • 1997  (209)
  • 1929
  • 1928
  • Natural Sciences in General  (209)
  • Physics  (209)
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  • Articles  (209)
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  • American Association for the Advancement of Science (AAAS)  (209)
  • American Chemical Society
  • Blackwell Publishing Ltd
  • Springer  (3)
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  • 1995-1999  (209)
  • 1980-1984
  • 1925-1929
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  • 1
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    STATs and gene regulation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-12
    Description: STATs (signal transducers and activators of transcription) are a family of latent cytoplasmic proteins that are activated to participate in gene control when cells encounter various extracellular polypeptides. Biochemical and molecular genetic explorations have defined a single tyrosine phosphorylation site and, in a dimeric partner molecule, an Src homology 2 (SH2) phosphotyrosine-binding domain, a DNA interaction domain, and a number of protein-protein interaction domains (with receptors, other transcription factors, the transcription machinery, and perhaps a tyrosine phosphatase). Mouse genetics experiments have defined crucial roles for each known mammalian STAT. The discovery of a STAT in Drosophila, and most recently in Dictyostelium discoideum, implies an ancient evolutionary origin for this dual-function set of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Darnell, J E Jr -- AI32489/AI/NIAID NIH HHS/ -- AI34420/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 12;277(5332):1630-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9287210" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; *Gene Expression Regulation ; Humans ; Nuclear Proteins/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; *Signal Transduction ; Trans-Activators/chemistry/genetics/*metabolism ; *Transcriptional Activation ; src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Photochemically driven collapse of Titan's atmosphere (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: Saturn's giant moon Titan has a thick (1.5 bar) nitrogen atmosphere, which has a temperature structure that is controlled by the absorption of solar and thermal radiation by methane, hydrogen, and organic aerosols into which methane is irreversibly converted by photolysis. Previous studies of Titan's climate evolution have been done with the assumption that the methane abundance was maintained against photolytic depletion throughout Titan's history, either by continuous supply from the interior or by buffering by a surface or near surface reservoir. Radiative-convective and radiative-saturated equilibrium models of Titan's atmosphere show that methane depletion may have allowed Titan's atmosphere to cool so that nitrogen, its main constituent, condenses onto the surface, collapsing Titan into a Triton-like frozen state with a thin atmosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lorenz, R D -- McKay, C P -- Lunine, J I -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):642-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Planetary Sciences, Lunar and Planetary Laboratory, University of Arizona, Tucson 85721, USA.rlorenz@pl.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005844" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Evolution, Planetary ; *Extraterrestrial Environment ; *Methane ; *Nitrogen ; Photolysis ; *Saturn ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: The nuclear factor of activated T cells (NFAT) group of transcription factors is retained in the cytoplasm of quiescent cells. NFAT activation is mediated in part by induced nuclear import. This process requires calcium-dependent dephosphorylation of NFAT caused by the phosphatase calcineurin. The c-Jun amino-terminal kinase (JNK) phosphorylates NFAT4 on two sites. Mutational removal of the JNK phosphorylation sites caused constitutive nuclear localization of NFAT4. In contrast, JNK activation in calcineurin-stimulated cells caused nuclear exclusion of NFAT4. These findings show that the nuclear accumulation of NFAT4 promoted by calcineurin is opposed by the JNK signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chow, C W -- Rincon, M -- Cavanagh, J -- Dickens, M -- Davis, R J -- CA58396/CA/NCI NIH HHS/ -- CA65831/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1638-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374467" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; COS Cells ; Calcineurin/metabolism ; Calcineurin Inhibitors ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cell Nucleus/*metabolism ; Cyclosporine/pharmacology ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Mutation ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphorylation ; Protein Kinases/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    PtdIns(3,4,5)P3 gets its message across (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hemmings, B A -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):534.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, CH-4002 Basel, Switzerland. hemmings@fmi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254423" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Enzyme Activation ; Phosphatidylinositol Phosphates/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins/chemistry/*metabolism ; Proto-Oncogene Proteins c-akt ; Second Messenger Systems ; Signal Transduction
    Print ISSN: 0036-8075
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  • 5
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    Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: Angiogenesis is thought to depend on a precise balance of positive and negative regulation. Angiopoietin-1 (Ang1) is an angiogenic factor that signals through the endothelial cell-specific Tie2 receptor tyrosine kinase. Like vascular endothelial growth factor, Ang1 is essential for normal vascular development in the mouse. An Ang1 relative, termed angiopoietin-2 (Ang2), was identified by homology screening and shown to be a naturally occurring antagonist for Ang1 and Tie2. Transgenic overexpression of Ang2 disrupts blood vessel formation in the mouse embryo. In adult mice and humans, Ang2 is expressed only at sites of vascular remodeling. Natural antagonists for vertebrate receptor tyrosine kinases are atypical; thus, the discovery of a negative regulator acting on Tie2 emphasizes the need for exquisite regulation of this angiogenic receptor system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maisonpierre, P C -- Suri, C -- Jones, P F -- Bartunkova, S -- Wiegand, S J -- Radziejewski, C -- Compton, D -- McClain, J -- Aldrich, T H -- Papadopoulos, N -- Daly, T J -- Davis, S -- Sato, T N -- Yancopoulos, G D -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):55-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals Inc., 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204896" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiopoietin-1 ; Angiopoietin-2 ; Animals ; Blood Vessels/embryology/*metabolism ; Cells, Cultured ; Cloning, Molecular ; Embryo, Mammalian/metabolism ; Endothelial Growth Factors/genetics/metabolism ; Endothelium, Vascular/*cytology/metabolism ; Female ; Humans ; Ligands ; Lymphokines/genetics/metabolism ; Membrane Glycoproteins/antagonists & inhibitors/metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Neovascularization, Physiologic ; Phosphorylation ; Proteins/chemistry/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptor Protein-Tyrosine Kinases/*antagonists & inhibitors/metabolism ; Receptor, TIE-2 ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors
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  • 6
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    Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-18
    Description: The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, C J -- Hayer-Hartl, M -- Di Liberto, M -- Hartl, F -- Kuriyan, J -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):431-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, 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/9103205" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/*chemistry/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; *Escherichia coli Proteins ; HSP70 Heat-Shock Proteins/*chemistry/metabolism ; Heat-Shock Proteins/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Chaperones/*chemistry/metabolism ; Molecular Sequence Data ; *Protein Conformation ; Protein Structure, Secondary
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  • 7
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    Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: Exposure of the yeast Saccharomyces cerevisiae to high extracellular osmolarity induces the Sln1p-Ypd1p-Ssk1p two-component osmosensor to activate a mitogen-activated protein (MAP) kinase cascade composed of the Ssk2p and Ssk22p MAP kinase kinase kinases (MAPKKKs), the Pbs2p MAPKK, and the Hog1p MAPK. A second osmosensor, Sho1p, also activated Pbs2p and Hog1p, but did so through the Ste11p MAPKKK. Although Ste11p also participates in the mating pheromone-responsive MAPK cascade, there was no detectable cross talk between these two pathways. The MAPKK Pbs2p bound to the Sho1p osmosensor, the MAPKKK Ste11p, and the MAPK Hog1p. Thus, Pbs2p may serve as a scaffold protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Posas, F -- Saito, H -- GM50909/GM/NIGMS NIH HHS/ -- GM53415/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1702-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180081" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Enzyme Activation ; Genes, Fungal ; Genetic Complementation Test ; MAP Kinase Kinase Kinases ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Mutation ; Osmolar Concentration ; Osmotic Pressure ; Peptides/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; *Saccharomyces cerevisiae Proteins ; Signal Transduction
    Print ISSN: 0036-8075
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  • 8
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    Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine alpha-hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states. The anomalous signal of the endogenous coppers was used to determine the structure of the catalytic core of oxidized rat PHM with and without bound peptide substrate. These structures strongly suggest that the PHM reaction proceeds via activation of substrate by a copper-bound oxygen species. The mechanistic and structural insight gained from the PHM structures can be directly extended to dopamine beta-monooxygenase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prigge, S T -- Kolhekar, A S -- Eipper, B A -- Mains, R E -- Amzel, L M -- DK32949/DK/NIDDK NIH HHS/ -- GM44692/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1300-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360928" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Catalysis ; Copper/chemistry/metabolism ; Crystallography, X-Ray ; Dipeptides/metabolism ; Dopamine beta-Hydroxylase/chemistry/metabolism ; Electrons ; Hydroxylation ; Ligands ; Mixed Function Oxygenases/*chemistry/metabolism ; Models, Molecular ; *Multienzyme Complexes ; Oxidation-Reduction ; Oxygen/metabolism ; Peptides/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Rats
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  • 9
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    Proteins from scratch (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeGrado, W F -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):80-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. wdegrado@mail.med.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9340760" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; Amino Acid Sequence ; Computer Simulation ; DNA-Binding Proteins/chemical synthesis/*chemistry ; Models, Molecular ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Tertiary ; Software ; Thermodynamics ; Transcription Factors/chemical synthesis/*chemistry ; Zinc Fingers
    Print ISSN: 0036-8075
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  • 10
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    Activated acetic acid by carbon fixation on (Fe,Ni)S under primordial conditions (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-11
    Description: In experiments modeling the reactions of the reductive acetyl-coenzyme A pathway at hydrothermal temperatures, it was found that an aqueous slurry of coprecipitated NiS and FeS converted CO and CH3SH into the activated thioester CH3-CO-SCH3, which hydrolyzed to acetic acid. In the presence of aniline, acetanilide was formed. When NiS-FeS was modified with catalytic amounts of selenium, acetic acid and CH3SH were formed from CO and H2S alone. The reaction can be considered as the primordial initiation reaction for a chemoautotrophic origin of life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, C -- Wachtershauser, G -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):245-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organic Chemistry and Biochemistry, Technische Universitat Munchen, Lichtenbergstrasse 4, D-85747 Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9092471" target="_blank"〉PubMed〈/a〉
    Keywords: Acetic Acid/*chemistry ; Carbon Monoxide/*chemistry ; Catalysis ; Cobalt/chemistry ; *Evolution, Chemical ; Ferrous Compounds/*chemistry ; Hydrogen Sulfide/chemistry ; Hydrogen-Ion Concentration ; Hydrolysis ; Nickel/*chemistry ; *Origin of Life ; Oxidation-Reduction ; Sulfhydryl Compounds/chemistry ; Temperature
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  • 11
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    Prebiotic chemistry. Where smokers rule (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crabtree, R H -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):222.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University Chemistry Department, New Haven, CT 06520-8107, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9132945" target="_blank"〉PubMed〈/a〉
    Keywords: Acetate-CoA Ligase/metabolism ; Acetates/*chemistry ; Acetyl Coenzyme A/chemistry ; Carbon Monoxide/chemistry ; Catalysis ; *Evolution, Chemical ; Ferrous Compounds/chemistry ; Nickel/chemistry ; *Origin of Life ; Temperature
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  • 12
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    Requirement of guanosine triphosphate-bound ran for signal-mediated nuclear protein export (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: A leucine-rich nuclear export signal (NES) allows rapid export of proteins from cell nuclei. Microinjection studies revealed a role for the guanosine triphosphatase (GTPase) Ran in NES-mediated export. Nuclear injection of a Ran mutant (Thr24 --〉 Asn) blocked protein export but not import, whereas depletion of the Ran nucleotide exchange factor RCC1 blocked protein import but not export. However, injection of Ran GTPase-activating protein (RanGAP) into RCC1-depleted cell nuclei inhibited export. Coinjection with Ran mutants insensitive to RanGAP prevented this inhibition. Therefore, NES-mediated protein export appears to require a Ran-GTP complex but does not require Ran-dependent GTP hydrolysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richards, S A -- Carey, K L -- Macara, I G -- EST3207122/ES/NIEHS NIH HHS/ -- GM 50526/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1842-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Vermont, Burlington, VT 05405, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Carrier Proteins/metabolism ; *Cell Cycle Proteins ; Cell Line ; Cell Nucleus/*metabolism ; Cricetinae ; Cytoplasm ; DNA-Binding Proteins/metabolism ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/metabolism ; *GTPase-Activating Proteins ; Glutathione Transferase/metabolism ; Green Fluorescent Proteins ; *Guanine Nucleotide Exchange Factors ; Guanosine Triphosphate/*metabolism ; Luminescent Proteins/metabolism ; Mutation ; Nuclear Envelope/metabolism ; Nuclear Localization Signals ; Nuclear Proteins/genetics/*metabolism ; Receptors, Glucocorticoid/metabolism ; Recombinant Fusion Proteins/metabolism ; Temperature ; ran GTP-Binding Protein
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  • 13
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    Neurospora wc-1 and wc-2: transcription, photoresponses, and the origins of circadian rhythmicity (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-02
    Description: Circadian rhythmicity is universally associated with the ability to perceive light, and the oscillators ("clocks") giving rise to these rhythms, which are feedback loops based on transcription and translation, are reset by light. Although such loops must contain elements of positive and negative regulation, the clock genes analyzed to date-frq in Neurospora and per and tim in Drosophila-are associated only with negative feedback and their biochemical functions are largely inferred. The white collar-1 and white collar-2 genes, both global regulators of photoresponses in Neurospora, encode DNA binding proteins that contain PAS domains and are believed to act as transcriptional activators. Data shown here suggest that wc-1 is a clock-associated gene and wc-2 is a clock component; both play essential roles in the assembly or operation of the Neurospora circadian oscillator. Thus DNA binding and transcriptional activation can now be associated with a clock gene that may provide a positive element in the feedback loop. In addition, similarities between the PAS-domain regions of molecules involved in light perception and circadian rhythmicity in several organisms suggest an evolutionary link between ancient photoreceptor proteins and more modern proteins required for circadian oscillation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crosthwaite, S K -- Dunlap, J C -- Loros, J J -- GM 34985/GM/NIGMS NIH HHS/ -- MH01186/MH/NIMH NIH HHS/ -- MH44651/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1997 May 2;276(5313):763-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755-3844, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9115195" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Clocks/physiology ; Biological Evolution ; Circadian Rhythm/*physiology ; DNA, Fungal/metabolism ; DNA-Binding Proteins/chemistry/genetics/*physiology ; Feedback ; Fungal Proteins/genetics ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Light ; Molecular Sequence Data ; Neurospora crassa/genetics/*physiology ; Phytochrome/metabolism ; Signal Transduction ; Temperature ; Transcription Factors/chemistry/genetics/*physiology ; *Transcriptional Activation
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    Gene discovery offers tentative clues to Parkinson's (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):1973.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9221499" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; Chromosomes, Human, Pair 4 ; Genetic Markers ; Humans ; Lewy Bodies/chemistry ; Mice ; Mice, Transgenic ; Nerve Tissue Proteins/analysis/chemistry/*genetics ; Oxidative Stress ; Parkinson Disease/etiology/*genetics ; Point Mutation ; Protein Conformation ; Protein Folding ; Rats ; Synucleins
    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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  • 15
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    De novo protein design: fully automated sequence selection (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-06
    Description: The first fully automated design and experimental validation of a novel sequence for an entire protein is described. A computational design algorithm based on physical chemical potential functions and stereochemical constraints was used to screen a combinatorial library of 1.9 x 10(27) possible amino acid sequences for compatibility with the design target, a betabetaalpha protein motif based on the polypeptide backbone structure of a zinc finger domain. A BLAST search shows that the designed sequence, full sequence design 1 (FSD-1), has very low identity to any known protein sequence. The solution structure of FSD-1 was solved by nuclear magnetic resonance spectroscopy and indicates that FSD-1 forms a compact well-ordered structure, which is in excellent agreement with the design target structure. This result demonstrates that computational methods can perform the immense combinatorial search required for protein design, and it suggests that an unbiased and quantitative algorithm can be used in various structural contexts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dahiyat, B I -- Mayo, S L -- GM08346/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):82-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311930" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; Amino Acid Sequence ; Computer Simulation ; Crystallography, X-Ray ; DNA-Binding Proteins/chemical synthesis/*chemistry ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; Solutions ; Transcription Factors/chemical synthesis/*chemistry ; Zinc Fingers
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  • 16
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    NGF signals ride a trolley to nucleus (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9289850" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Axonal Transport ; Axons/*metabolism ; Cell Nucleus/metabolism ; Cells, Cultured ; Cyclic AMP Response Element-Binding Protein/metabolism ; Gene Expression Regulation ; Nerve Growth Factors/*metabolism ; Neurons/*metabolism ; Proto-Oncogene Proteins/metabolism ; Rats ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, trkA ; Receptors, Nerve Growth Factor/metabolism ; *Signal Transduction
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  • 17
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    Neurogenesis in postnatal rat spinal cord: a study in primary culture (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: Spinal cord injuries result in paralysis, because when damaged neurons die they are not replaced. Neurogenesis of electrophysiologically functional neurons occurred in spinal cord cultured from postnatal rats. In these cultures, the numbers of immunocytochemically identified neurons increased over time. Additionally, neurons identified immunocytochemically or electrophysiologically incorporated bromodeoxyuridine, confirming they had differentiated from mitotic cells in vitro. These findings suggest that postnatal spinal cord retains the capacity to generate functional neurons. The presence of neuronal precursor cells in postnatal spinal cord may offer new therapeutic approaches for restoration of function to individuals with spinal cord injuries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kehl, L J -- Fairbanks, C A -- Laughlin, T M -- Wilcox, G L -- DA07097/DA/NIDA NIH HHS/ -- DA07234/DA/NIDA NIH HHS/ -- DE00225/DE/NIDCR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):586-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Program in Neuroscience, University of Minnesota, Minneapolis, MN 55455, USA. 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9110976" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Bromodeoxyuridine/metabolism ; Cell Differentiation ; Cells, Cultured ; Culture Media ; Glial Fibrillary Acidic Protein/analysis ; Immunohistochemistry ; Mitosis ; Neurons/chemistry/*cytology/metabolism ; Phosphopyruvate Hydratase/analysis ; Rats ; Spinal Cord/chemistry/*cytology ; Tubulin/analysis
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  • 18
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    Mixed self-assembled monolayers in chemical separations (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-03
    Description: Chemical separations of many biomolecules and pharmaceuticals are limited by their electrostatic interaction with the surfaces of the separation medium. Mixed self-assembled monolayers of octadecyl and methyl chains organize into a dense, two-dimensionally cross-linked network over the chromatographic silica surface to reduce acid dissociation of the surface silanols. Molecular models predict that two-dimensional cross-linking is sterically possible for pure methylsiloxane monolayers, silicon-29 nuclear magnetic resonance measurements show that cross-linking predominates for mixed monolayers of primarily methylsiloxane, and chromatographic measurements confirm that electrostatic interactions are reduced when the monolayer is primarily methylsiloxane. Chromatographic separation of genetic variants of a highly charged protein, cytochrome c, demonstrates the promise of self-assembled monolayers in separations of biomolecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirth, M J -- Fairbank, R W -- Fatunmbi, H O -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):44-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8974384" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatography/*methods ; Cytochrome c Group/isolation & purification ; Electrochemistry ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Proteins/*isolation & purification ; Silica Gel ; Silicon Dioxide ; *Siloxanes/chemistry ; Surface Properties
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  • 19
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    Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-17
    Description: The proto-oncogene-encoded transcription factor c-Jun activates genes in response to a number of inducers that act through mitogen-activated protein kinase (MAPK) signal transduction pathways. The activation of c-Jun after phosphorylation by MAPK is accompanied by a reduction in c-Jun ubiquitination and consequent stabilization of the protein. These results illustrate the relevance of regulated protein degradation in the signal-dependent control of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Musti, A M -- Treier, M -- Bohmann, D -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):400-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstr. 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8994040" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Cycle Proteins/metabolism ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation ; JNK Mitogen-Activated Protein Kinases ; Mice ; *Mitogen-Activated Protein Kinases ; Phosphorylation ; Proto-Oncogene Proteins c-jun/*metabolism ; Signal Transduction ; Transfection ; Ubiquitins/*metabolism ; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Rat model for Gulf War syndrome? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1997 Nov 21;278(5342):1404.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411763" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Disease Models, Animal ; Hippocampus/*drug effects/metabolism ; Humans ; Isoflurophate/*toxicity ; Maze Learning/drug effects ; Military Personnel ; Nicotinic Antagonists/toxicity ; Persian Gulf Syndrome/*chemically induced/metabolism ; Rats ; Receptors, Nicotinic/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    Marijuana: harder than thought? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):1967-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9221496" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/drug effects/metabolism ; Animals ; Brain/*drug effects/metabolism ; *Cannabis ; Corticotropin-Releasing Hormone/*metabolism ; Dopamine/*metabolism ; Dronabinol/adverse effects/*pharmacology ; Humans ; Naloxone/pharmacology ; Nucleus Accumbens/drug effects/metabolism ; Rats ; Substance Withdrawal Syndrome/*metabolism ; Substance-Related Disorders/metabolism
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  • 22
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    Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: Long-term potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barria, A -- Muller, D -- Derkach, V -- Griffith, L C -- Soderling, T R -- NS27037/NS/NINDS NIH HHS/ -- R01 GM054408/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197267" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/analogs & derivatives/pharmacology ; 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Cell Line ; Enzyme Inhibitors/pharmacology ; Excitatory Amino Acid Antagonists/pharmacology ; Hippocampus/*metabolism ; Humans ; In Vitro Techniques ; *Long-Term Potentiation/drug effects ; Male ; Peptide Mapping ; Phosphorylation ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/*metabolism ; Synaptic Transmission/drug effects
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  • 23
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    Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beamer, L J -- Carroll, S F -- Eisenberg, D -- GM31299/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1861-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188532" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antimicrobial Cationic Peptides ; Binding Sites ; Blood Bactericidal Activity ; Blood Proteins/*chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Humans ; Lipopolysaccharides/metabolism ; *Membrane Proteins ; Models, Molecular ; Molecular Sequence Data ; Phosphatidylcholines/chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 24
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    Paleomagnetic evidence of a low-temperature origin of carbonate in the Martian meteorite ALH84001 (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-14
    Description: Indirect evidence for life on Mars has been reported from the study of meteorite ALH84001. The formation temperature of the carbonates is controversial; some estimates suggest 20 degrees to 80 degrees C, whereas others exceed 650 degrees C. Paleomagnetism can be used to distinguish between these possibilities because heating can remagnetize ferrimagnetic minerals. Study of two adjacent pyroxene grains from the crushed zone of ALH84001 shows that each possesses a stable natural remanent magnetization (NRM), implying that Mars had a substantial magnetic field when the grains cooled. However, NRM directions from these particles differ, implying that the meteorite has not been heated significantly since the formation of the internal crushed zone about 4 billion years ago. The carbonate globules postdate this brecciation, and thus formed at low temperatures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kirschvink, J L -- Maine, A T -- Vali, H -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1629-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geological and Planetary Sciences, California Institute of Technology, 170-25, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054354" target="_blank"〉PubMed〈/a〉
    Keywords: Carbonates/*chemistry ; Magnetics ; *Mars ; *Meteoroids ; Minerals/*chemistry ; Temperature
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  • 25
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    Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-04
    Description: On the basis of x-ray diffraction data to a resolution of 2.9 angstroms, atomic models of most protein components of the bovine cytochrome bc1 complex were built, including core 1, core 2, cytochrome b, subunit 6, subunit 7, a carboxyl-terminal fragment of cytochrome c1, and an amino-terminal fragment of the iron-sulfur protein. The positions of the four iron centers within the bc1 complex and the binding sites of the two specific respiratory inhibitors antimycin A and myxothiazol were identified. The membrane-spanning region of each bc1 complex monomer consists of 13 transmembrane helices, eight of which belong to cytochrome b. Closely interacting monomers are arranged as symmetric dimers and form cavities through which the inhibitor binding pockets can be accessed. The proteins core 1 and core 2 are structurally similar to each other and consist of two domains of roughly equal size and identical folding topology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xia, D -- Yu, C A -- Kim, H -- Xia, J Z -- Kachurin, A M -- Zhang, L -- Yu, L -- Deisenhofer, J -- GM 30721/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):60-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204897" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antimycin A/metabolism/pharmacology ; Binding Sites ; Cattle ; Crystallography, X-Ray ; Cytochrome b Group/chemistry ; Cytochromes c1/chemistry ; Dimerization ; Electron Transport Complex III/*chemistry/metabolism ; Intracellular Membranes/enzymology ; Iron/metabolism ; Methacrylates ; Mitochondria, Heart/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thiazoles/metabolism/pharmacology
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  • 26
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    Fast-action flicks draw chemists' rave reviews (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):1986-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9221502" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry ; Carbon Monoxide/chemistry/*metabolism ; *Electrons ; Iron/chemistry/*metabolism ; Lasers ; Models, Molecular ; Motion Pictures as Topic ; Myoglobin/chemistry/*metabolism ; *Photoreceptors, Microbial ; Synchrotrons ; *X-Ray Diffraction
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  • 27
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    Large porous particles for pulmonary drug delivery (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: A new type of inhalation aerosol, characterized by particles of small mass density and large size, permitted the highly efficient delivery of inhaled therapeutics into the systemic circulation. Particles with mass densities less than 0.4 gram per cubic centimeter and mean diameters exceeding 5 micrometers were inspired deep into the lungs and escaped the lungs' natural clearance mechanisms until the inhaled particles delivered their therapeutic payload. Inhalation of large porous insulin particles resulted in elevated systemic levels of insulin and suppressed systemic glucose levels for 96 hours, whereas small nonporous insulin particles had this effect for only 4 hours. High systemic bioavailability of testosterone was also achieved by inhalation delivery of porous particles with a mean diameter (20 micrometers) approximately 10 times that of conventional inhaled therapeutic particles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edwards, D A -- Hanes, J -- Caponetti, G -- Hrkach, J -- Ben-Jebria, A -- Eskew, M L -- Mintzes, J -- Deaver, D -- Lotan, N -- Langer, R -- GM26698/GM/NIGMS NIH HHS/ -- HD29125/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Pennsylvania State University, 204 Fenske Laboratory, University Park, PA 16802, USA. dxe11@psuv.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188534" target="_blank"〉PubMed〈/a〉
    Keywords: *Administration, Inhalation ; Aerosols ; Animals ; Biological Availability ; Blood Glucose/analysis ; Bronchoalveolar Lavage ; *Drug Carriers ; Drug Compounding ; Insulin/administration & dosage/blood/pharmacokinetics ; *Lactic Acid ; *Lung ; Male ; Particle Size ; *Polyglycolic Acid ; *Polylysine ; *Polymers ; Rats ; Rats, Sprague-Dawley ; Testosterone/administration & dosage/blood/pharmacokinetics
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    In situ activation pattern of Drosophila EGF receptor pathway during development (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-22
    Description: Signaling cascades triggered by receptor tyrosine kinases (RTKs) participate in diverse developmental processes. The active state of these signaling pathways was monitored by examination of the in situ distribution of the active, dual phosphorylated form of mitogen-activated protein kinase (ERK) with a specific monoclonal antibody. Detection of the active state of the Drosophila epidermal growth factor receptor (DER) pathway allowed the visualization of gradients and boundaries of receptor activation, assessment of the distribution of activating ligands, and analysis of interplay with the inhibitory ligand Argos. This in situ approach can be used to monitor other receptor-triggered pathways in a wide range of organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabay, L -- Seger, R -- Shilo, B Z -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9262480" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Body Patterning ; Calcium-Calmodulin-Dependent Protein Kinases/immunology/*metabolism ; Cell Differentiation ; Drosophila/cytology/embryology/genetics/*metabolism ; *Drosophila Proteins ; *Epidermal Growth Factor ; Eye Proteins/metabolism ; Gene Expression Regulation, Developmental ; Genes, Insect ; Membrane Proteins/metabolism ; Mutation ; Nerve Tissue Proteins/metabolism ; Phosphorylation ; Photoreceptor Cells, Invertebrate/cytology/embryology ; Receptor, Epidermal Growth Factor/*metabolism ; *Signal Transduction
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    Receptor and betagamma binding sites in the alpha subunit of the retinal G protein transducin (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-17
    Description: Transmembrane receptors for hormones, neurotransmitters, light, and odorants mediate their cellular effects by activating heterotrimeric guanine nucleotide-binding proteins (G proteins). Crystal structures have revealed contact surfaces between G protein subunits, but not the surfaces or molecular mechanism through which Galphabetagamma responds to activation by transmembrane receptors. Such a surface was identified from the results of testing 100 mutant alpha subunits of the retinal G protein transducin for their ability to interact with rhodopsin. Sites at which alanine substitutions impaired this interaction mapped to two distinct Galpha surfaces: a betagamma-binding surface and a putative receptor-interacting surface. On the basis of these results a mechanism for receptor-catalyzed exchange of guanosine diphosphate for guanosine triphosphate is proposed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onrust, R -- Herzmark, P -- Chi, P -- Garcia, P D -- Lichtarge, O -- Kingsley, C -- Bourne, H R -- CA-54427/CA/NCI NIH HHS/ -- GM-27800/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):381-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143-0450, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8994033" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Compounds/pharmacology ; Animals ; Binding Sites ; COS Cells ; Fluorides/pharmacology ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Models, Molecular ; Mutation ; Phenotype ; *Protein Conformation ; Retinaldehyde/pharmacology ; Rhodopsin/*metabolism/pharmacology ; Rod Cell Outer Segment/metabolism ; Transducin/*chemistry/metabolism
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    Inducible expression and phosphorylation of coactivator BOB.1/OBF.1 in T cells (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: BOB.1/OBF.1 is a transcriptional coactivator that is constitutively expressed in B cells and interacts with the Oct1 and Oct2 transcription factors. Upon activation of Jurkat T cells and primary murine thymocytes with phorbol esters and ionomycin, BOB.1/OBF.1 expression and transactivation function were induced. BOB.1/OBF.1 was phosphorylated at Ser184 both in vivo and in vitro, and this modification was required for inducible activation. Mutation of Ser184 also diminished transactivation function in B cells, suggesting that the activating phosphorylation that is inducible in T cells is constitutively present in B cells. Thus, BOB.1/OBF.1 is a transcriptional coactivator that is critically regulated by posttranslational modifications to mediate cell type-specific gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwilling, S -- Dieckmann, A -- Pfisterer, P -- Angel, P -- Wirth, T -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):221-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MSZ, Institut fur Medizinische Strahlenkunde und Zellforschung, Universitat Wurzburg, Versbacher Strasse 5, 97078 Wurzburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211847" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/metabolism ; Cells, Cultured ; *DNA-Binding Proteins ; *Gene Expression Regulation ; HeLa Cells ; Homeodomain Proteins/metabolism ; Host Cell Factor C1 ; Humans ; Immunosuppressive Agents/pharmacology ; Ionomycin/pharmacology ; Jurkat Cells ; *Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Octamer Transcription Factor-1 ; Phosphorylation ; Phosphoserine/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/immunology/*metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Trans-Activators/genetics/*metabolism ; Transcription Factors/metabolism ; *Transcriptional Activation
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    Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25 (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-05
    Description: In response to DNA damage, mammalian cells prevent cell cycle progression through the control of critical cell cycle regulators. A human gene was identified that encodes the protein Chk1, a homolog of the Schizosaccharomyces pombe Chk1 protein kinase, which is required for the DNA damage checkpoint. Human Chk1 protein was modified in response to DNA damage. In vitro Chk1 bound to and phosphorylated the dual-specificity protein phosphatases Cdc25A, Cdc25B, and Cdc25C, which control cell cycle transitions by dephosphorylating cyclin-dependent kinases. Chk1 phosphorylates Cdc25C on serine-216. As shown in an accompanying paper by Peng et al. in this issue, serine-216 phosphorylation creates a binding site for 14-3-3 protein and inhibits function of the phosphatase. These results suggest a model whereby in response to DNA damage, Chk1 phosphorylates and inhibits Cdc25C, thus preventing activation of the Cdc2-cyclin B complex and mitotic entry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Y -- Wong, C -- Thoma, R S -- Richman, R -- Wu, Z -- Piwnica-Worms, H -- Elledge, S J -- GM17763/GM/NIGMS NIH HHS/ -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1497-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Marrs McLean Department of Biochemistry, Howard Hughes Medical Institute, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278511" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Amino Acid Sequence ; Animals ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/antagonists & inhibitors/*metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Cytoskeletal Proteins ; *DNA Damage ; *F-Box Proteins ; G2 Phase ; HeLa Cells ; Humans ; Mice ; *Mitosis ; Molecular Sequence Data ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Recombinant Fusion Proteins/metabolism ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Transfection ; *Tyrosine 3-Monooxygenase ; *Ubiquitin-Protein Ligases ; *cdc25 Phosphatases
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    Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: CD1 represents a third lineage of antigen-presenting molecules that are distantly related to major histocompatibility complex (MHC) molecules in the immune system. The crystal structure of mouse CD1d1, corresponding to human CD1d, at 2.8 resolution shows that CD1 adopts an MHC fold that is more closely related to that of MHC class I than to that of MHC class II. The binding groove, although significantly narrower, is substantially larger because of increased depth and it has only two major pockets that are almost completely hydrophobic. The extreme hydrophobicity and shape of the binding site are consistent with observations that human CD1b and CD1c can present mycobacterial cell wall antigens, such as mycolic acid and lipoarabinomannans. However, mouse CD1d1 can present very hydrophobic peptides, but must do so in a very different way from MHC class Ia and class II molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zeng, Z -- Castano, A R -- Segelke, B W -- Stura, E A -- Peterson, P A -- Wilson, I A -- CA-58896/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):339-45.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute for Chemical Biology at the Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219685" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigens, CD1/*chemistry/immunology/metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Glycolipids/chemistry/immunology/metabolism ; Histocompatibility Antigens Class I/chemistry ; Histocompatibility Antigens Class II/chemistry ; Humans ; Hydrogen Bonding ; Ligands ; Lipid Metabolism ; Lipids/chemistry/immunology ; Mice ; Models, Molecular ; *Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; T-Lymphocyte Subsets/immunology
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    Experiments in a Parkinson's rat model (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pallini, R -- Consales, A -- Lauretti, L -- Fernandez, E -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):389-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9518368" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dopamine/physiology ; Fluorescent Dyes/*metabolism ; *Genetic Therapy ; Genetic Vectors ; Glial Cell Line-Derived Neurotrophic Factor ; Nerve Degeneration ; Nerve Growth Factors/genetics ; Nerve Tissue Proteins/*genetics ; Neurons/metabolism/pathology ; *Neuroprotective Agents ; Oxidopamine/pharmacology ; Parkinson Disease/pathology/*therapy ; Rats ; *Stilbamidines ; Substantia Nigra/metabolism/*pathology
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    Toroidal structure of lambda-exonuclease (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-20
    Description: Structure determination at 2.4 angstrom resolution shows that lambda-exonuclease consists of three subunits that form a toroid. The central channel is funnel shaped, tapering from an inner diameter of about 30 angstroms at the wider end to 15 angstroms at the narrow end. This is adequate to accommodate the DNA substrate and thus provides a structural basis for the ability of the enzyme to sequentially hydrolyze thousands of nucleotides in a highly processive manner. The results also suggest the locations of the active sites and the constraints that limit cleavage to a single strand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kovall, R -- Matthews, B W -- GM20066/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1824-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, Howard Hughes Medical Institute, and Department of Physics, University of Oregon, Eugene, OR 97403, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295273" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/enzymology ; Binding Sites ; Crystallography, X-Ray ; DNA/genetics/*metabolism ; DNA, Single-Stranded/genetics/*metabolism ; DNA, Viral/genetics/metabolism ; Evolution, Molecular ; Exodeoxyribonucleases/*chemistry/genetics/metabolism ; Hydrolysis ; Magnesium/metabolism ; Models, Molecular ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombination, Genetic ; Viral Proteins
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    Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-21
    Description: Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal lipidation of Ras and several other cellular signal transduction proteins. The essential nature of this modification for proper function of these proteins has led to the emergence of FTase as a target for the development of new anticancer therapy. Inhibition of this enzyme suppresses the transformed phenotype in cultured cells and causes tumor regression in animal models. The crystal structure of heterodimeric mammalian FTase was determined at 2.25 angstrom resolution. The structure shows a combination of two unusual domains: a crescent-shaped seven-helical hairpin domain and an alpha-alpha barrel domain. The active site is formed by two clefts that intersect at a bound zinc ion. One cleft contains a nine-residue peptide that may mimic the binding of the Ras substrate; the other cleft is lined with highly conserved aromatic residues appropriate for binding the farnesyl isoprenoid with required specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, H W -- Boduluri, S R -- Moomaw, J F -- Casey, P J -- Beese, L S -- GM46372/GM/NIGMS NIH HHS/ -- GM52382/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1800-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9065406" target="_blank"〉PubMed〈/a〉
    Keywords: *Alkyl and Aryl Transferases ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Protein Conformation ; Protein Structure, Secondary ; Proteins/metabolism ; Sequence Alignment ; Transferases/*chemistry/genetics/metabolism ; Zinc/metabolism
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    Selective colorimetric detection of polynucleotides based on the distance-dependent optical properties of gold nanoparticles (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-22
    Description: A highly selective, colorimetric polynucleotide detection method based on mercaptoalkyloligonucleotide-modified gold nanoparticle probes is reported. Introduction of a single-stranded target oligonucleotide (30 bases) into a solution containing the appropriate probes resulted in the formation of a polymeric network of nanoparticles with a concomitant red-to-pinkish/purple color change. Hybridization was facilitated by freezing and thawing of the solutions, and the denaturation of these hybrid materials showed transition temperatures over a narrow range that allowed differentiation of a variety of imperfect targets. Transfer of the hybridization mixture to a reverse-phase silica plate resulted in a blue color upon drying that could be detected visually. The unoptimized system can detect about 10 femtomoles of an oligonucleotide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elghanian, R -- Storhoff, J J -- Mucic, R C -- Letsinger, R L -- Mirkin, C A -- GM 10265/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1078-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9262471" target="_blank"〉PubMed〈/a〉
    Keywords: *Biosensing Techniques ; Colorimetry ; *Gold ; Microchemistry ; *Nucleic Acid Hybridization ; *Oligonucleotide Probes ; Polydeoxyribonucleotides/*analysis ; Spectrophotometry ; Temperature
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    Microbiology's scarred revolutionary (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1997 May 2;276(5313):699-702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157549" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/*classification/genetics/physiology ; Bacteria/*classification/genetics ; Base Sequence ; Biological Evolution ; History, 20th Century ; Origin of Life ; *Phylogeny ; RNA, Bacterial/genetics ; RNA, Ribosomal/genetics ; Sequence Analysis, RNA ; Temperature ; United States
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    The early Mars climate question heats up (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasting, J F -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1245.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geoscience, Pennsylvania State University, State College 16802, USA. kasting@essc.psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411751" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Carbon Dioxide ; Climate ; Exobiology ; *Extraterrestrial Environment ; Greenhouse Effect ; Ice ; Infrared Rays ; *Mars ; Scattering, Radiation ; Temperature ; Water
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    The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-18
    Description: The three-dimensional structure of the complex between human H-Ras bound to guanosine diphosphate and the guanosine triphosphatase (GTPase)-activating domain of the human GTPase-activating protein p120GAP (GAP-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. The structure shows the partly hydrophilic and partly hydrophobic nature of the communication between the two molecules, which explains the sensitivity of the interaction toward both salts and lipids. An arginine side chain (arginine-789) of GAP-334 is supplied into the active site of Ras to neutralize developing charges in the transition state. The switch II region of Ras is stabilized by GAP-334, thus allowing glutamine-61 of Ras, mutation of which activates the oncogenic potential, to participate in catalysis. The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations. Glycine-12 in the transition state mimic is within van der Waals distance of both arginine-789 of GAP-334 and glutamine-61 of Ras, and even its mutation to alanine would disturb the arrangements of residues in the transition state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheffzek, K -- Ahmadian, M R -- Kabsch, W -- Wiesmuller, L -- Lautwein, A -- Schmitz, F -- Wittinghofer, A -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):333-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur molekulare Physiologie, Abteilung Strukturelle Biologie, Rheinlanddamm 201, 44139 Dortmund, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219684" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Compounds/chemistry/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalysis ; Cell Transformation, Neoplastic ; Crystallography, X-Ray ; Enzyme Activation ; Fluorides/chemistry/metabolism ; GTP Phosphohydrolases/chemistry/*metabolism ; GTP-Binding Proteins/chemistry/metabolism ; GTPase-Activating Proteins ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Protein Conformation ; Protein Structure, Secondary ; Proteins/*chemistry/*metabolism ; Signal Transduction ; ras GTPase-Activating Proteins ; ras Proteins/chemistry/genetics/*metabolism
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    Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: Small structural perturbations in the enzyme isocitrate dehydrogenase (IDH) were made in order to evaluate the contribution of precise substrate alignment to the catalytic power of an enzyme. The reaction trajectory of IDH was modified (i) after the adenine moiety of nicotinamide adenine dinucleotide phosphate was changed to hypoxanthine (the 6-amino was changed to 6-hydroxyl), and (ii) by replacing Mg2+, which has six coordinating ligands, with Ca2+, which has eight coordinating ligands. Both changes make large (10(-3) to 10(-5)) changes in the reaction velocity but only small changes in the orientation of the substrates (both distance and angle) as revealed by cryocrystallographic trapping of active IDH complexes. The results provide evidence that orbital overlap produced by optimal orientation of reacting orbitals plays a major quantitative role in the catalytic power of enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mesecar, A D -- Stoddard, B L -- Koshland, D E Jr -- GM49857/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):202-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, Stanley Hall, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211842" target="_blank"〉PubMed〈/a〉
    Keywords: Cadmium/metabolism ; Calcium/metabolism ; Catalysis ; Chemistry, Physical ; Crystallography, X-Ray ; Hydrogen Bonding ; Isocitrate Dehydrogenase/*chemistry/*metabolism ; Kinetics ; Ligands ; Magnesium/metabolism ; Models, Molecular ; Mutagenesis, Site-Directed ; NAD/analogs & derivatives/metabolism ; NADP/metabolism ; Physicochemical Phenomena ; *Protein Conformation
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    A neural substrate of prediction and reward (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-14
    Description: The capacity to predict future events permits a creature to detect, model, and manipulate the causal structure of its interactions with its environment. Behavioral experiments suggest that learning is driven by changes in the expectations about future salient events such as rewards and punishments. Physiological work has recently complemented these studies by identifying dopaminergic neurons in the primate whose fluctuating output apparently signals changes or errors in the predictions of future salient and rewarding events. Taken together, these findings can be understood through quantitative theories of adaptive optimizing control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, W -- Dayan, P -- Montague, P R -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1593-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology, University of Fribourg, CH-1700 Fribourg, Switzerland. Wolfram.Schultz@unifr.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054347" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Computer Simulation ; Conditioning (Psychology) ; Cues ; Dopamine/*physiology ; *Learning ; Mesencephalon/*physiology ; *Models, Neurological ; Neurons/*physiology ; Rats ; *Reward
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  • 42
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    Conversion by Peyer's patch lymphocytes of human enterocytes into M cells that transport bacteria (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: The epithelium that lines the gut is impermeable to macromolecules and microorganisms, except in Peyer's patches (PPs), where the lymphoid follicle-associated epithelium (FAE) contains M cells that transport antigens and microorganisms. A cultured system that reproduces the main characteristics of FAE and M cells was established by cultivation of PP lymphocytes with the differentiated human intestinal cell line Caco-2. Lymphocytes settled into the epithelial monolayer, inducing reorganization of the brush border and a temperature-dependent transport of particles and Vibrio cholerae. This model system could prove useful for intestinal physiology, vaccine research, and drug delivery studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerneis, S -- Bogdanova, A -- Kraehenbuhl, J P -- Pringault, E -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):949-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Institute for Experimental Cancer Research, and Institute of Biochemistry, University of Lausanne, CH-1066 Epalinges-Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252325" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; *Bacterial Translocation ; Caco-2 Cells ; Carrier Proteins/analysis ; Cell Polarity ; Coculture Techniques ; Fluorescein-5-isothiocyanate ; Humans ; *Immunity, Mucosal ; Intestinal Mucosa/*cytology/*immunology/microbiology ; Lymphocytes/*immunology ; Mice ; Mice, Inbred BALB C ; Microfilament Proteins/analysis ; Microspheres ; Microvilli/chemistry/ultrastructure ; Peyer's Patches/cytology/*immunology ; Sucrase-Isomaltase Complex/analysis ; T-Lymphocytes/immunology ; Temperature ; Vibrio cholerae/*metabolism
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    Researchers get their first good look at the nucleosome (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-11-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Featherstone, C -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1763-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9324764" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; Crystallography, X-Ray ; DNA/*chemistry ; Histones/*chemistry ; Models, Molecular ; Nucleic Acid Conformation ; Nucleosomes/*chemistry ; *Protein Conformation ; Protein Folding ; Transcription, Genetic
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  • 44
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    Solution structure of 3-oxo-delta5-steroid isomerase (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-18
    Description: The three-dimensional structure of the enzyme 3-oxo-delta5-steroid isomerase (E.C. 5.3.3.1), a 28-kilodalton symmetrical dimer, was solved by multidimensional heteronuclear magnetic resonance spectroscopy. The two independently folded monomers pack together by means of extensive hydrophobic and electrostatic interactions. Each monomer comprises three alpha helices and a six-strand mixed beta-pleated sheet arranged to form a deep hydrophobic cavity. Catalytically important residues Tyr14 (general acid) and Asp38 (general base) are located near the bottom of the cavity and positioned as expected from mechanistic hypotheses. An unexpected acid group (Asp99) is also located in the active site adjacent to Tyr14, and kinetic and binding studies of the Asp99 to Ala mutant demonstrate that Asp99 contributes to catalysis by stabilizing the intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Z R -- Ebrahimian, S -- Zawrotny, M E -- Thornburg, L D -- Perez-Alvarado, G C -- Brothers, P -- Pollack, R M -- Summers, M F -- GM38155/GM/NIGMS NIH HHS/ -- GM49082/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103200" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Androstenedione/metabolism ; Binding Sites ; Dimerization ; Estradiol/metabolism ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; *Protein Conformation ; Protein Structure, Secondary ; Solutions ; Steroid Isomerases/*chemistry/genetics/metabolism
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  • 45
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    Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-28
    Description: Signal transmission by many cell surface receptors results in the activation of phosphoinositide (PI) 3-kinases that phosphorylate the 3' position of polyphosphoinositides. From a screen for mouse proteins that bind phosphoinositides, the protein GRP1was identified. GRP1 binds phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4, 5)P3] through a pleckstrin homology (PH) domain and displays a region of high sequence similarity to the yeast Sec7 protein. The PH domain of the closely related protein cytohesin-1, which, through its Sec7 homology domain, regulates integrin beta2 and catalyzes guanine nucleotide exchange of the small guanine nucleotide-binding protein ARF1, was also found to specifically bind PtdIns(3,4,5)P3. GRP1 and cytohesin-1 appear to connect receptor-activated PI 3-kinase signaling pathways with proteins that mediate biological responses such as cell adhesion and membrane trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klarlund, J K -- Guilherme, A -- Holik, J J -- Virbasius, J V -- Chawla, A -- Czech, M P -- DK30648/DK/NIDDK NIH HHS/ -- DK30898/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1927-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, 373 Plantation Street, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072969" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Adipocytes/chemistry ; Amino Acid Sequence ; Animals ; Antigens, CD18/metabolism ; Blood Proteins/*chemistry ; Brain Chemistry ; Cell Adhesion Molecules/chemistry/*metabolism ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; DNA, Complementary ; Fungal Proteins/*chemistry ; GTP-Binding Proteins/metabolism ; *Guanine Nucleotide Exchange Factors ; Humans ; Mice ; Molecular Sequence Data ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/*metabolism ; *Phosphoproteins ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction
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  • 46
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    Src structure crystallizes 20 years of oncogene research (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Featherstone, C -- New York, N.Y. -- Science. 1997 Feb 21;275(5303):1066.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054006" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography, X-Ray ; Models, Molecular ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein-Tyrosine Kinases/chemistry ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins c-hck ; Proto-Oncogene Proteins pp60(c-src)/*chemistry/metabolism ; Tyrosine/chemistry/metabolism ; *src Homology Domains
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  • 47
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    Fyn-kinase as a determinant of ethanol sensitivity: relation to NMDA-receptor function (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-24
    Description: Animals vary in their sensitivity to ethanol, a trait at least partly determined by genetic factors. In order to identify possible responsible genes, mice lacking Fyn, a non-receptor type tyrosine kinase, were investigated. These mice were hypersensitive to the hypnotic effect of ethanol. The administration of ethanol enhanced tyrosine phosphorylation of the N-methyl-D-aspartate receptor (NMDAR) in the hippocampus of control mice but not in Fyn-deficient mice. An acute tolerance to ethanol inhibition of NMDAR-mediated excitatory postsynaptic potentials in hippocampal slices developed in control mice but not in Fyn-deficient mice. These results indicate that Fyn affects behavioral, biochemical, and physiological responses to ethanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyakawa, T -- Yagi, T -- Kitazawa, H -- Yasuda, M -- Kawai, N -- Tsuboi, K -- Niki, H -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):698-701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Neurobiology of Emotion, Brain Science Institute, RIKEN, Hirosawa, Wako-shi, Saitama-ken 351-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Central Nervous System Depressants/*pharmacology ; Ethanol/*pharmacology ; Excitatory Postsynaptic Potentials/drug effects ; Flurazepam/pharmacology ; Hippocampus/metabolism ; Hypnotics and Sedatives/pharmacology ; In Vitro Techniques ; Male ; Mice ; Mice, Knockout ; Motor Activity/*drug effects ; N-Methylaspartate/pharmacology ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/deficiency/genetics/*metabolism ; Proto-Oncogene Proteins/deficiency/genetics/*metabolism ; Proto-Oncogene Proteins c-fyn ; Receptors, N-Methyl-D-Aspartate/*metabolism
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  • 48
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    Direct observation of cooling of heme upon photodissociation of carbonmonoxy myoglobin (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-23
    Description: The formation of vibrationally excited heme upon photodissociation of carbonmonoxy myoglobin and its subsequent vibrational energy relaxation was monitored by picosecond anti-Stokes resonance Raman spectroscopy. The anti-Stokes intensity of the nu4 band showed immediate generation of vibrationally excited hemes and biphasic decay of the excited populations. The best fit to double exponentials gave time constants of 1.9 +/- 0.6 and 16 +/- 9 picoseconds for vibrational population decay and 3.0 +/- 1.0 and 25 +/- 14 picoseconds for temperature relaxation of the photolyzed heme when a Boltzmann distribution was assumed. The decay of the nu4 anti-Stokes intensity was accompanied by narrowing and frequency upshift of the Stokes counterpart. This direct monitoring of the cooling dynamics of the heme cofactor within the globin matrix allows the characterization of the vibrational energy flow through the protein moiety and to the water bath.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mizutani, Y -- Kitagawa, T -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):443-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Science, Okazaki National Research Institutes, Myodaiji, Okazaki 444, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334299" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Monoxide/chemistry ; Heme/*chemistry ; Myoglobin/*chemistry ; Photolysis ; Photons ; Spectrum Analysis, Raman ; Temperature ; Thermodynamics
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    Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-18
    Description: Most cases of early-onset familial Alzheimer's disease (FAD) are caused by mutations in the genes encoding the presenilin 1 (PS1) and PS2 proteins, both of which undergo regulated endoproteolytic processing. During apoptosis, PS1 and PS2 were shown to be cleaved at sites distal to their normal cleavage sites by a caspase-3 family protease. In cells expressing PS2 containing the asparagine-141 FAD mutant, the ratio of alternative to normal PS2 cleavage fragments was increased relative to wild-type PS2-expressing cells, suggesting a potential role for apoptosis-associated cleavage of presenilins in the pathogenesis of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, T W -- Pettingell, W H -- Jung, Y K -- Kovacs, D M -- Tanzi, R E -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics and Aging Unit, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219695" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism/pathology ; Amino Acid Chloromethyl Ketones/pharmacology ; Amino Acid Substitution ; Animals ; *Apoptosis ; Caspase 3 ; *Caspases ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation ; Etoposide/pharmacology ; Membrane Proteins/chemistry/genetics/*metabolism ; Mutation ; Oligopeptides/pharmacology ; Phosphorylation ; Presenilin-1 ; Presenilin-2 ; Rats ; Staurosporine/pharmacology ; Tumor Cells, Cultured
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  • 50
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    daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-15
    Description: A C. elegans neurosecretory signaling system regulates whether animals enter the reproductive life cycle or arrest development at the long-lived dauer diapause stage. daf-2, a key gene in the genetic pathway that mediates this endocrine signaling, encodes an insulin receptor family member. Decreases in DAF-2 signaling induce metabolic and developmental changes, as in mammalian metabolic control by the insulin receptor. Decreased DAF-2 signaling also causes an increase in life-span. Life-span regulation by insulin-like metabolic control is analogous to mammalian longevity enhancement induced by caloric restriction, suggesting a general link between metabolism, diapause, and longevity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K D -- Tissenbaum, H A -- Liu, Y -- Ruvkun, G -- R01AG14161/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):942-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252323" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/chemistry/*genetics/growth & development/metabolism ; Caenorhabditis elegans Proteins ; Chromosome Mapping ; Conserved Sequence ; Energy Intake ; *Genes, Helminth ; Glucose/metabolism ; Humans ; Insulin/metabolism ; Larva/genetics/growth & development/metabolism ; Longevity/*genetics ; Molecular Sequence Data ; Mutation ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Receptor, IGF Type 1/chemistry/genetics ; Receptor, Insulin/chemistry/*genetics/metabolism ; Signal Transduction
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    Iron-sulfur clusters: nature's modular, multipurpose structures (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-01
    Description: Iron-sulfur proteins are found in all life forms. Most frequently, they contain Fe2S2, Fe3S4, and Fe4S4 clusters. These modular clusters undergo oxidation-reduction reactions, may be inserted or removed from proteins, can influence protein structure by preferential side chain ligation, and can be interconverted. In addition to their electron transfer function, iron-sulfur clusters act as catalytic centers and sensors of iron and oxygen. Their most common oxidation states are paramagnetic and present significant challenges for understanding the magnetic properties of mixed valence systems. Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beinert, H -- Holm, R H -- Munck, E -- 5-K06 GM 18442/GM/NIGMS NIH HHS/ -- GM 12394/GM/NIGMS NIH HHS/ -- GM 34812/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Aug 1;277(5326):653-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Enzyme Research and the Department of Biochemistry, University of Wisconsin, Madison, WI 53705, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9235882" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Electron Spin Resonance Spectroscopy ; Electron Transport ; Iron/chemistry/*metabolism ; Iron-Sulfur Proteins/chemistry/*metabolism ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Oxidation-Reduction ; Spectroscopy, Mossbauer ; Sulfur/chemistry/*metabolism
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  • 52
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    Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-31
    Description: The regulation of the serine-threonine kinase Akt by lipid products of phosphoinositide 3-kinase (PI 3-kinase) was investigated. Akt activity was found to correlate with the amount of phosphatidylinositol-3,4-bisphosphate (PtdIns-3,4-P2) in vivo, and synthetic PtdIns-3,4-P2 activated Akt both in vitro and in vivo. Binding of PtdIns-3,4-P2 occurred within the Akt pleckstrin homology (PH) domain and facilitated dimerization of Akt. Akt mutated in the PH domain was not activated by PI 3-kinase in vivo or by PtdIns-3, 4-P2 in vitro, and it was impaired in binding to PtdIns-3,4-P2. Examination of the binding to other phosphoinositides revealed that they bound to the Akt PH domain with much lower affinity than did PtdIns-3,4-P2 and failed to increase Akt activity. Thus, Akt is apparently regulated by the direct interaction of PtdIns-3,4-P2 with the Akt PH domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Franke, T F -- Kaplan, D R -- Cantley, L C -- Toker, A -- GM41890/GM/NIGMS NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- R01 GM041890/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):665-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, National Cancer Institute-Frederick Cancer Research Facility and Development Center (NCI-FCRFDC), Frederick, MD 21702, USA. tfranke@bidmc.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005852" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; COS Cells ; Dimerization ; Enzyme Activation ; Mice ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/*metabolism/pharmacology ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Platelet-Derived Growth Factor/pharmacology ; Point Mutation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-akt ; Recombinant Fusion Proteins/chemistry/metabolism
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    NMDA channel regulation by channel-associated protein tyrosine kinase Src (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: The N-methyl-D-aspartate (NMDA) receptor mediates synaptic transmission and plasticity in the central nervous system (CNS) and is regulated by tyrosine phosphorylation. In membrane patches excised from mammalian central neurons, the endogenous tyrosine kinase Src was shown to regulate the activity of NMDA channels. The action of Src required a sequence [Src(40-58)] within the noncatalytic, unique domain of Src. In addition, Src coprecipitated with NMDA receptor proteins. Finally, endogenous Src regulated the function of NMDA receptors at synapses. Thus, NMDA receptor regulation by Src may be important in development, plasticity, and pathology in the CNS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, X M -- Askalan, R -- Keil, G J 2nd -- Salter, M W -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):674-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Hospital for Sick Children, Department of Physiology, University of Toronto, Toronto, Ontario, M5G 1X8 Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005855" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Ion Channel Gating ; Ion Channels/*metabolism ; Molecular Sequence Data ; N-Methylaspartate/metabolism ; Neurons/*metabolism ; Oligopeptides/pharmacology ; Patch-Clamp Techniques ; Phosphorylation ; Phosphotyrosine/metabolism ; Rats ; Rats, Wistar ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Spinal Cord/cytology ; Synapses/*metabolism ; Synaptic Transmission ; src-Family Kinases/chemistry/*metabolism
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    Fear of hope (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, W -- New York, N.Y. -- Science. 1997 Sep 26;277(5334):1907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9333941" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology ; Cell Transplantation ; Genetic Therapy ; Humans ; Immunotherapy ; *Nerve Regeneration ; Neuroglia/*transplantation ; Olfactory Bulb/cytology/transplantation ; Rats ; Spinal Cord Injuries/surgery/*therapy
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    Feeling a protein's motion (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrenstein, D -- New York, N.Y. -- Science. 1997 Aug 1;277(5326):637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254428" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriorhodopsins/*chemistry ; Biophysical Phenomena ; Biophysics ; Chemistry, Physical ; Lasers ; Microscopy, Atomic Force ; Models, Molecular ; Physicochemical Phenomena ; *Protein Conformation
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    Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-05
    Description: Arrest of the cell cycle at the G2 checkpoint, induced by DNA damage, requires inhibitory phosphorylation of the kinase Cdc2 in both fission yeast and human cells. The kinase Wee1 and the phosphatase Cdc25, which regulate Cdc2 phosphorylation, were evaluated as targets of Chk1, a kinase essential for the checkpoint. Fission yeast cdc2-3w Deltacdc25 cells, which express activated Cdc2 and lack Cdc25, were responsive to Wee1 but insensitive to Chk1 and irradiation. Expression of large amounts of Chk1 produced the same phenotype as did loss of the cdc25 gene in cdc2-3w cells. Cdc25 associated with Chk1 in vivo and was phosphorylated when copurified in Chk1 complexes. These findings identify Cdc25, but not Wee1, as a target of the DNA damage checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Furnari, B -- Rhind, N -- Russell, P -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278510" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/*metabolism ; Cell Division ; *DNA Damage ; DNA Helicases/metabolism ; Fungal Proteins/*metabolism ; G2 Phase ; Gamma Rays ; Genes, Fungal ; *Mitosis ; Models, Biological ; Mutation ; *Nuclear Proteins ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/genetics/*metabolism/radiation effects ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Temperature ; *ras-GRF1
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    The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-18
    Description: Engagement of antigen and immunoglobulin receptors on hematopoietic cells is directly coupled to activation of nonreceptor protein tyrosine kinases (PTKs) that then phosphorylate critical intracellular substrates. In mast cells stimulated through the FcvarepsilonRI receptor, activation of several PTKs including Syk leads to degranulation and release of such mediators of the allergic response as histamine and serotonin. Regulation of Syk function occurred through interaction with the Cbl protein, itself a PTK substrate in this system. Overexpression of Cbl led to inhibition of Syk and suppression of serotonin release from mast cells, demonstrating its ability to inhibit a nonreceptor tyrosine kinase. Complex adaptor proteins such as Cbl can directly regulate the functions of the proteins they bind.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ota, Y -- Samelson, L E -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):418-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-5430, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103201" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Degranulation ; Enzyme Precursors/antagonists & inhibitors/*metabolism ; Genetic Vectors ; Intracellular Signaling Peptides and Proteins ; Mast Cells/*metabolism ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-cbl ; Rats ; Receptors, IgE/metabolism ; Receptors, IgG/metabolism ; Recombinant Proteins/metabolism ; Serotonin/metabolism ; Signal Transduction ; Tumor Cells, Cultured ; *Ubiquitin-Protein Ligases ; Vaccinia virus
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    Detection of soft X-rays and a sensitive search for noble gases in comet Hale-Bopp (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-05
    Description: An image of comet Hale-Bopp (C/1995 O1) in soft x-rays reveals a central emission offset from the nucleus, as well as an extended emission feature that does not correlate with the dust jets seen at optical wavelengths. Neon was found to be depleted in the cometary ice by more than a factor of 25 relative to solar abundance, which suggests that ices in Hale-Bopp formed at (or later experienced) temperatures higher than 25 kelvin. A helium line emission at a wavelength of 584 angstroms was detected and may be attributable to charge transfer of solar wind alpha particles in the cometary coma. Ionized oxygen and another helium line contribute to an emission observed at 538 angstroms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krasnopolsky, V A -- Mumma, M J -- Abbott, M -- Flynn, B C -- Meech, K J -- Yeomans, D K -- Feldman, P D -- Cosmovici, C B -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1488-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Catholic University of America, Washington, DC 20064, USA. ys2VK@lepvax.gsfc.nasa.gov 20771, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278508" target="_blank"〉PubMed〈/a〉
    Keywords: Cosmic Dust ; Helium/*analysis ; Ice ; *Meteoroids ; Neon/*analysis ; Oxygen/*analysis ; Temperature ; X-Rays
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    Signaling vascular morphogenesis and maintenance (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanahan, D -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):48-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California at San Francisco, San Francisco, CA 94143-0534, USA. dougvhanahan@biochem.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9229772" target="_blank"〉PubMed〈/a〉
    Keywords: Angiopoietin-1 ; Angiopoietin-2 ; Animals ; Apoptosis ; Blood Vessels/*embryology/growth & development/metabolism ; Cell Division ; Endothelial Growth Factors/metabolism ; Endothelium, Vascular/*cytology/metabolism ; Lymphokines/metabolism ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Knockout ; Morphogenesis ; *Neovascularization, Physiologic ; Phosphorylation ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptor, TIE-2 ; Receptors, Growth Factor/metabolism ; Receptors, Vascular Endothelial Growth Factor ; *Signal Transduction ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor Receptor-1 ; Vascular Endothelial Growth Factors
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    Water on the sun: line assignments based on variational calculations (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-18
    Description: The infrared spectrum of hot water observed in a sunspot has been assigned. The high temperature of the sunspot (3200 K) gave rise to a highly congested pure rotational spectrum in the 10-micrometer region that involved energy levels at least halfway to dissociation. Traditional spectroscopy, based on perturbation theory, is inadequate for this problem. Instead, accurate variational solutions of the vibration-rotation Schrodinger equation were used to make assignments, revealing unexpected features, including rotational difference bands and fewer degeneracies than anticipated. These results indicate that a shift away from perturbation theory to first principles calculations is necessary in order to assign spectra of hot polyatomic molecules such as water.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Polyansky, O L -- Zobov, N F -- Viti, S -- Tennyson, J -- Bernath, P F -- Wallace, L -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):346-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Astronomy, University College London, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219686" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Physicochemical Phenomena ; *Solar Activity ; *Solar System ; Spectrophotometry, Infrared ; Temperature ; Water/*analysis/chemistry
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    PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-07
    Description: Protein dephosphorylation by phosphatase PP1 plays a central role in mediating the effects of insulin on glucose and lipid metabolism. A PP1C-targeting protein expressed in 3T3-L1 adipocytes (called PTG, for protein targeting to glycogen) was cloned and characterized. PTG was expressed predominantly in insulin-sensitive tissues. In addition to binding and localizing PP1C to glycogen, PTG formed complexes with phosphorylase kinase, phosphorylase a, and glycogen synthase, the primary enzymes involved in the hormonal regulation of glycogen metabolism. Overexpression of PTG markedly increased basal and insulin-stimulated glycogen synthesis in Chinese hamster ovary cells overexpressing the insulin receptor, which do not express endogenous PTG. These results suggest that PTG is critical for glycogen metabolism, possibly functioning as a molecular scaffold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Printen, J A -- Brady, M J -- Saltiel, A R -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1475-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Michigan School of Medicine, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9045612" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; CHO Cells ; Carrier Proteins/chemistry/genetics/*metabolism ; Cloning, Molecular ; Cricetinae ; DNA, Complementary/genetics ; Glycogen/biosynthesis/*metabolism ; Glycogen Synthase/metabolism ; Insulin/pharmacology ; *Intracellular Signaling Peptides and Proteins ; Mice ; Molecular Sequence Data ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylase Kinase/metabolism ; Phosphorylase a/metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 1 ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Transfection
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    Ground-based thermal infrared observations of comet Hale-Bopp (C/1995 O1) during 1996 (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-28
    Description: Thermal infrared (IR) imaging and spectroscopy of comet Hale-Bopp (C/1995 O1) during June, August, and September 1996 traced the development of the dust coma several months before perihelion. Images revealed nightly variations in the brightness of the inner coma from 1 to 12 June that were correlated with the appearance of a northward-pointing jet. The central IR flux increased by a factor of 8 between 1 June and 30 September, and the September data showed IR jets that corresponded to similar structures that were visible in reflected sunlight at shorter wavelengths. At all epochs, 8- to 13-micrometer spectra of the central coma revealed a strong silicate emission feature, including an 11.2-micrometer feature indicative of crystalline olivine, even when the comet was at a heliocentric distance of 4.1 astronomical units.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hayward, T L -- Hanner, M S -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1907-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Radiophysics and Space Research, Cornell University, Ithaca, NY 14853, USA. hayward@astrosun.tn.cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072961" target="_blank"〉PubMed〈/a〉
    Keywords: Cosmic Dust ; Iron Compounds/analysis ; Magnesium Compounds/analysis ; *Meteoroids ; Silicates/analysis ; Spectrum Analysis ; Temperature
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    Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-05-09
    Description: Timely deactivation of kinase cascades is crucial to the normal control of cell signaling and is partly accomplished by protein phosphatase 2A (PP2A). The catalytic (alpha) subunit of the serine-threonine kinase casein kinase 2 (CK2) bound to PP2A in vitro and in mitogen-starved cells; binding required the integrity of a sequence motif common to CK2alpha and SV40 small t antigen. Overexpression of CK2alpha resulted in deactivation of mitogen-activated protein kinase kinase (MEK) and suppression of cell growth. Moreover, CK2alpha inhibited the transforming activity of oncogenic Ras, but not that of constitutively activated MEK. Thus, CK2alpha may regulate the deactivation of the mitogen-activated protein kinase pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heriche, J K -- Lebrin, F -- Rabilloud, T -- Leroy, D -- Chambaz, E M -- Goldberg, Y -- New York, N.Y. -- Science. 1997 May 9;276(5314):952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Commissariat a l'Energie Atomique, Departement de Biologie Moleculaire et Structurale, Laboratoire de Biochimie des Regulations Cellulaires Endocrines, Unite 244, F-38054 Grenoble Cedex 9, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9139659" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Antigens, Polyomavirus Transforming ; Binding Sites ; Casein Kinase II ; Cell Division ; Cell Transformation, Neoplastic ; MAP Kinase Kinase 1 ; Mice ; *Mitogen-Activated Protein Kinase Kinases ; Mutation ; Okadaic Acid/pharmacology ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Protein Phosphatase 2 ; Protein-Serine-Threonine Kinases/*metabolism/pharmacology ; Protein-Tyrosine Kinases/metabolism/pharmacology ; Recombinant Fusion Proteins/metabolism ; Transfection ; ras Proteins/pharmacology
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    A synaptically controlled, associative signal for Hebbian plasticity in hippocampal neurons (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-10
    Description: The role of back-propagating dendritic action potentials in the induction of long-term potentiation (LTP) was investigated in CA1 neurons by means of dendritic patch recordings and simultaneous calcium imaging. Pairing of subthreshold excitatory postsynaptic potentials (EPSPs) with back-propagating action potentials resulted in an amplification of dendritic action potentials and evoked calcium influx near the site of synaptic input. This pairing also induced a robust LTP, which was reduced when EPSPs were paired with non-back-propagating action potentials or when stimuli were unpaired. Action potentials thus provide a synaptically controlled, associative signal to the dendrites for Hebbian modifications of synaptic strength.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Magee, J C -- Johnston, D -- MH44754/MH/NIMH NIH HHS/ -- NS09482/NS/NINDS NIH HHS/ -- NS11535/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Jan 10;275(5297):209-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA. jmagee@ptp.bcm.tmc.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8985013" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Animals ; Axons/physiology ; Calcium/metabolism ; Calcium Channel Blockers/pharmacology ; Calcium Channels/drug effects/physiology ; Dendrites/*physiology ; Feedback ; In Vitro Techniques ; Long-Term Potentiation/drug effects/*physiology ; Patch-Clamp Techniques ; Pyramidal Cells/drug effects/*physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/*physiology ; *Synaptic Transmission/drug effects ; Tetrodotoxin/pharmacology
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    Low-temperature carbonate concretions in the Martian meteorite ALH84001: evidence from stable isotopes and mineralogy (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-14
    Description: The martian meteorite ALH84001 contains small, disk-shaped concretions of carbonate with concentric chemical and mineralogical zonation. Oxygen isotope compositions of these concretions, measured by ion microprobe, range from delta18O = +9.5 to +20.5 per thousand. Most of the core of one concretion is homogeneous (16.7 +/- 1.2 per thousand) and over 5 per thousand higher in delta18O than a second concretion. Orthopyroxene that hosts the secondary carbonates is isotopically homogeneous (delta18O = 4.6 +/- 1.2 per thousand). Secondary SiO2 has delta18O = 20.4 per thousand. Carbon isotope ratios measured from the core of one concretion average delta13C = 46 +/- 8 per thousand, consistent with formation on Mars. The isotopic variations and mineral compositions offer no evidence for high temperature (〉650 degrees C) carbonate precipitation and suggest non-equilibrium processes at low temperatures (〈 approximately 300 degrees C).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valley, J W -- Eiler, J M -- Graham, C M -- Gibson, E K -- Romanek, C S -- Stolper, E M -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1633-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology and Geophysics, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054355" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Isotopes ; Carbonates/*chemistry ; Chemical Precipitation ; *Mars ; *Meteoroids ; Minerals/chemistry ; Oxygen Isotopes ; Silicon Dioxide/chemistry ; Temperature
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    Oxygen on Ganymede: laboratory studies (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-06-20
    Description: To test proposals for the origin of oxygen absorption bands in the visible reflectance spectrum of Ganymede, the reflectance of condensed films of pure oxygen (O2) and O2-water mixtures and the evolution of O2 from the films as a function of temperature were determined. Absorption band shapes and positions for oxygen at 26 kelvin were similar to those reported for Ganymede, whereas those for the mixtures were slightly shifted. The band intensity dropped by more than two orders of magnitude when the ice mixture was warmed to 100 kelvin, although about 20 percent of the O2 remained trapped in the ice, which suggested that at these temperatures O2 molecules dissolve in the ice rather than aggregate in clusters or bubbles. The experiments suggest that the absorption bands in Ganymede's spectrum were not produced in the relatively warm surface of the satellite but in a much colder source. Solid O2 may exist in a cold subsurface layer or in an atmospheric haze.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vidal, R A -- Bahr, D -- Baragiola, R A -- Peters, M -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Atomic and Surface Physics, University of Virginia, Thornton Hall, Charlottesville, VA 22901, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188525" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Extraterrestrial Environment ; *Jupiter ; Oxygen/*analysis ; Spectrum Analysis ; Temperature
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    Direct measurement of angles between bond vectors in high-resolution NMR (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-23
    Description: Angles between two interatomic vectors are measured for structure elucidation in solution nuclear magnetic resonance (NMR). The angles can be determined directly by using the effects of dipole-dipole cross-correlated relaxation of double-quantum and zero-quantum coherences. The measured rates can be directly related to the angular geometry without need for calibration of a Karplus-type curve, as is the case for scalar coupling measurements, and depend only on the rotational correlation time of the molecule as an empirical parameter. This makes the determination of torsional angles independent from the measurement of coupling constants. The two interatomic vectors can in principle be arbitrarily far apart. The method was demonstrated on the measurement of the peptide backbone angle psi in the protein rhodniin, which is difficult to determine in solution by NMR spectroscopy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reif, B -- Hennig, M -- Griesinger, C -- New York, N.Y. -- Science. 1997 May 23;276(5316):1230-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Organische Chemie, Marie-Curie-Strasse 11, Universitat Frankfurt, D-60439 Frankfurt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157875" target="_blank"〉PubMed〈/a〉
    Keywords: Antithrombins/*chemistry ; Insect Proteins/*chemistry ; Magnetic Resonance Spectroscopy/*methods ; Models, Molecular ; Protein Conformation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The cis-trans paradox of integrase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jayaram, M -- New York, N.Y. -- Science. 1997 Apr 4;276(5309):49-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas at Austin, Austin, TX 78712, USA. jayaram@almach.cc.utexas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9122709" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/*enzymology ; Binding Sites ; Crystallography, X-Ray ; DNA/*metabolism ; DNA Nucleotidyltransferases/chemistry/metabolism ; DNA, Circular/metabolism ; Integrases/*chemistry/metabolism ; Models, Molecular ; *Protein Conformation ; Recombinases ; *Recombination, Genetic ; Tyrosine/metabolism ; Virus Integration
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A bitter battle over insulin gene (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1028-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9289846" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; California ; *Cloning, Molecular ; DNA, Recombinant ; Drug Industry ; *Genetic Research ; *Genetic Vectors ; Guideline Adherence/legislation & jurisprudence ; Humans ; Insulin/*genetics ; National Institutes of Health (U.S.) ; *Patents as Topic ; *Plasmids ; Rats ; Recombinant Proteins ; Scientific Misconduct/*legislation & jurisprudence ; United States ; Universities
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-24
    Description: BAD is a distant member of the Bcl-2 family that promotes cell death. Phosphorylation of BAD prevents this. BAD phosphorylation induced by interleukin-3 (IL-3) was inhibited by specific inhibitors of phosphoinositide 3-kinase (PI 3-kinase). Akt, a survival-promoting serine-threonine protein kinase, was activated by IL-3 in a PI 3-kinase-dependent manner. Active, but not inactive, forms of Akt were found to phosphorylate BAD in vivo and in vitro at the same residues that are phosphorylated in response to IL-3. Thus, the proapoptotic function of BAD is regulated by the PI 3-kinase-Akt pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉del Peso, L -- Gonzalez-Garcia, M -- Page, C -- Herrera, R -- Nunez, G -- CA-64556/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):687-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381178" target="_blank"〉PubMed〈/a〉
    Keywords: Androstadienes/pharmacology ; Animals ; Apoptosis ; Carrier Proteins/*metabolism ; Cell Line ; Chromones/pharmacology ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Interleukin-3/*pharmacology ; Mice ; Morpholines/pharmacology ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; bcl-Associated Death Protein ; bcl-X Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecules give new insights into deadliest brain cancers (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1226.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411748" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brevican ; Carrier Proteins/genetics/*physiology ; Chloride Channels/*physiology ; Chondroitin Sulfate Proteoglycans ; Glioma/*metabolism/*pathology/therapy ; Humans ; Lectins, C-Type ; Neoplasm Invasiveness ; Nerve Tissue Proteins/genetics/*physiology ; Neuroglia/metabolism ; Rats ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Triton's distorted atmosphere (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-23
    Description: A stellar-occultation light curve for Triton shows asymmetry that can be understood if Triton's middle atmosphere is distorted from spherical symmetry. Although a globally oblate model can explain the data, the inferred atmospheric flattening is so large that it could be caused only by an unrealistic internal mass distribution or highly supersonic zonal winds. Cyclostrophic winds confined to a jet near Triton's northern or southern limbs (or both) could also be responsible for the details of the light curve, but such winds are required to be slightly supersonic. Hazes and clouds in the atmosphere are unlikely to have caused the asymmetry in the light curve.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elliot, J L -- Stansberry, J A -- Olkin, C B -- Agner, M A -- Davies, M E -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):436-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth, Atmospheric, and Planetary Sciences and Department of Physics, Building 54-422, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139-4307, USA. jle@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334297" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Extraterrestrial Environment ; Gravitation ; *Neptune ; Optics and Photonics ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-21
    Description: Inactivation of the adenomatous polyposis coli (APC) tumor suppressor gene initiates colorectal neoplasia. One of the biochemical activities associated with the APC protein is down-regulation of transcriptional activation mediated by beta-catenin and T cell transcription factor 4 (Tcf-4). The protein products of mutant APC genes present in colorectal tumors were found to be defective in this activity. Furthermore, colorectal tumors with intact APC genes were found to contain activating mutations of beta-catenin that altered functionally significant phosphorylation sites. These results indicate that regulation of beta-catenin is critical to APC's tumor suppressive effect and that this regulation can be circumvented by mutations in either APC or beta-catenin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morin, P J -- Sparks, A B -- Korinek, V -- Barker, N -- Clevers, H -- Vogelstein, B -- Kinzler, K W -- CA57345/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1787-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Johns Hopkins Oncology Center, 424 North Bond Street, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9065402" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Colonic Neoplasms/*genetics/metabolism ; Cytoskeletal Proteins/*genetics/*metabolism ; Gene Expression Regulation, Neoplastic ; *Genes, APC ; Genes, Reporter ; Germ-Line Mutation ; Humans ; Mutation ; Phosphorylation ; Signal Transduction ; TCF Transcription Factors ; *Trans-Activators ; Transcription Factor 7-Like 2 Protein ; Transcription Factors/*metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; beta Catenin
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    The Mars Pathfinder atmospheric structure investigation/meteorology (ASI/MET) experiment (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: The Mars Pathfinder atmospheric structure investigation/meteorology (ASI/MET) experiment measured the vertical density, pressure, and temperature structure of the martian atmosphere from the surface to 160 km, and monitored surface meteorology and climate for 83 sols (1 sol = 1 martian day = 24.7 hours). The atmospheric structure and the weather record are similar to those observed by the Viking 1 lander (VL-1) at the same latitude, altitude, and season 21 years ago, but there are differences related to diurnal effects and the surface properties of the landing site. These include a cold nighttime upper atmosphere; atmospheric temperatures that are 10 to 12 degrees kelvin warmer near the surface; light slope-controlled winds; and dust devils, identified by their pressure, wind, and temperature signatures. The results are consistent with the warm, moderately dusty atmosphere seen by VL-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schofield, J T -- Barnes, J R -- Crisp, D -- Haberle, R M -- Larsen, S -- Magalhaes, J A -- Murphy, J R -- Seiff, A -- Wilson, G -- New York, N.Y. -- Science. 1997 Dec 5;278(5344):1752-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉J. T. Schofield and D. Crisp, Jet Propulsion Laboratory, California Institute of Technology, 4800 Oak Grove Drive, Pasadena, CA 91109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9388169" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; Carbon Dioxide ; *Extraterrestrial Environment ; *Mars ; Pressure ; Temperature ; Wind
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    Seeing the synapse (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelner, K L -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):547.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148416" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Calcium-Binding Proteins ; Cells, Cultured ; Electric Stimulation ; Hippocampus ; Membrane Glycoproteins/metabolism ; Membrane Proteins/metabolism ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Neurotransmitter Agents/*metabolism ; R-SNARE Proteins ; Rats ; Recombinant Fusion Proteins/metabolism ; Synapses/*metabolism ; Synaptic Transmission ; Synaptotagmins
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    Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-12-31
    Description: Methyl-coenzyme M reductase (MCR), the enzyme responsible for the microbial formation of methane, is a 300-kilodalton protein organized as a hexamer in an alpha2beta2gamma2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum, determined at 1.45 angstrom resolution for the inactive enzyme state MCRox1-silent, reveals that two molecules of the nickel porphinoid coenzyme F430 are embedded between the subunits alpha, alpha', beta, and gamma and alpha', alpha, beta', and gamma', forming two identical active sites. Each site is accessible for the substrate methyl-coenzyme M through a narrow channel locked after binding of the second substrate coenzyme B. Together with a second structurally characterized enzyme state (MCRsilent) containing the heterodisulfide of coenzymes M and B, a reaction mechanism is proposed that uses a radical intermediate and a nickel organic compound.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ermler, U -- Grabarse, W -- Shima, S -- Goubeaud, M -- Thauer, R K -- New York, N.Y. -- Science. 1997 Nov 21;278(5342):1457-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biophysik, Heinrich-Hoffmann-Strabetae 7, 60528 Frankfurt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9367957" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Coenzymes/chemistry/metabolism ; Crystallography, X-Ray ; Disulfides/chemistry/metabolism ; Hydrogen/metabolism ; Hydrogen Bonding ; Ligands ; Mesna/analogs & derivatives/chemistry/metabolism ; Metalloporphyrins/chemistry/metabolism ; Methane/*metabolism ; Methanobacterium/*enzymology ; Models, Molecular ; Nickel/chemistry/metabolism ; Oxidation-Reduction ; Oxidoreductases/*chemistry/*metabolism ; Phosphothreonine/analogs & derivatives/chemistry/metabolism ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary
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    The year of the dendrite (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sejnowski, T J -- New York, N.Y. -- Science. 1997 Jan 10;275(5297):178-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute at the Salk Institute for Biological Studies, University of California, San Diego, CA 92186, USA. terry@salk.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8999546" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/metabolism ; Cerebral Cortex/cytology/*physiology ; Dendrites/*physiology ; Ion Channels ; Long-Term Potentiation ; Neuronal Plasticity ; Pyramidal Cells/*physiology ; Rats ; Synapses/physiology ; Synaptic Transmission
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    Calcium waves in retinal glial cells (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-02-07
    Description: Calcium signals were recorded from glial cells in acutely isolated rat retina to determine whether Ca2+ waves occur in glial cells of intact central nervous system tissue. Chemical (adenosine triphosphate), electrical, and mechanical stimulation of astrocytes initiated increases in the intracellular concentration of Ca2+ that propagated at approximately 23 micrometers per second through astrocytes and Muller cells as intercellular waves. The Ca2+ waves persisted in the absence of extracellular Ca2+ but were largely abolished by thapsigargin and intracellular heparin, indicating that Ca2+ was released from intracellular stores. The waves did not evoke changes in cell membrane potential but traveled synchronously in astrocytes and Muller cells, suggesting a functional linkage between these two types of glial cells. Such glial Ca2+ waves may constitute an extraneuronal signaling pathway in the central nervous system.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2410141/" 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/PMC2410141/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, E A -- Zahs, K R -- EY04077/EY/NEI NIH HHS/ -- EY10383/EY/NEI NIH HHS/ -- R01 EY004077/EY/NEI NIH HHS/ -- R01 EY004077-19/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1997 Feb 7;275(5301):844-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Minnesota, 435 Delaware Street, SE, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9012354" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Animals ; Astrocytes/*metabolism ; Calcium/*metabolism ; Calcium Channels/metabolism ; Electric Stimulation ; Heparin/pharmacology ; In Vitro Techniques ; Inositol 1,4,5-Trisphosphate Receptors ; Kinetics ; Membrane Potentials ; Neuroglia/*metabolism ; Physical Stimulation ; Rats ; Receptors, Cytoplasmic and Nuclear/metabolism ; Retina/*cytology/metabolism ; Signal Transduction ; Stimulation, Chemical ; Thapsigargin/pharmacology
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    Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3 (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-28
    Description: The transcription factor NF-AT responds to Ca2+-calcineurin signals by translocating to the nucleus, where it participates in the activation of early immune response genes. Calcineurin dephosphorylates conserved serine residues in the amino terminus of NF-AT, resulting in nuclear import. Purification of the NF-AT kinase revealed that it is composed of a priming kinase activity and glycogen synthase kinase-3 (GSK-3). GSK-3 phosphorylates conserved serines necessary for nuclear export, promotes nuclear exit, and thereby opposes Ca2+-calcineurin signaling. Because GSK-3 responds to signals initiated by Wnt and other ligands, NF-AT family members could be effectors of these pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beals, C R -- Sheridan, C M -- Turck, C W -- Gardner, P -- Crabtree, G R -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1930-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Developmental Biology, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; Brain/enzymology ; COS Cells ; Calcineurin ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Calmodulin-Binding Proteins/metabolism ; Cell Nucleus/*metabolism ; Cloning, Molecular ; Cyclic AMP-Dependent Protein Kinases/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Glycogen Synthase Kinase 3 ; Glycogen Synthase Kinases ; Humans ; Molecular Sequence Data ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Rats ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factors/genetics/*metabolism ; Transfection
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    How cells get the right chromosomes (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-31
    Description: When cells divide, the chromosomes must be delivered flawlessly to the daughter cells. Missing or extra chromosomes can result in birth defects and cancer. Chance events are the starting point for chromosome delivery, which makes the process prone to error. Errors are avoided by diverse uses of mechanical tension from mitotic forces. Tension stabilizes the proper chromosome configuration, controls a cell cycle checkpoint, and changes chromosome chemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nicklas, R B -- GM-13745/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):632-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, LSRC Building, Duke University, Box 91000, Durham, NC 27708-1000, USA. bnicklas@acpub.duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005842" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes/*metabolism ; Humans ; Kinetochores/*metabolism ; *Meiosis ; Microtubules/*metabolism ; *Mitosis ; Nuclear Proteins/metabolism ; Phosphorylation ; Selection, Genetic ; Spindle Apparatus/*metabolism ; Stress, Mechanical
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    Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-14
    Description: Nitrogen regulatory protein C (NtrC) contacts a bacterial RNA polymerase from distant enhancers by means of DNA loops and activates transcription by allowing polymerase to gain access to the template DNA strand. It was shown that NtrC from Salmonella typhimurium must build large oligomers to activate transcription. In contrast to eukaryotic enhancer-binding proteins, most of which must bind directly to DNA, some NtrC dimers were bound solely by protein-protein interactions. NtrC oligomers were visualized with scanning force microscopy. Evidence of their functional importance was provided by showing that some inactive non-DNA-binding and DNA-binding mutant forms of NtrC can cooperate to activate transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wyman, C -- Rombel, I -- North, A K -- Bustamante, C -- Kustu, S -- GM17078/GM/NIGMS NIH HHS/ -- GM32543/GM/NIGMS NIH HHS/ -- GM38361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1658-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054362" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; *Bacterial Proteins ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Dimerization ; Enhancer Elements, Genetic ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; Promoter Regions, Genetic ; RNA Polymerase Sigma 54 ; Salmonella typhimurium/genetics/metabolism ; Sigma Factor/*metabolism ; *Trans-Activators ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; *Transcriptional Activation
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    Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-12
    Description: An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two interstrand loops forming a helical subdomain atop the sandwich. The residues in the helical region, but not in the beta sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fass, D -- Davey, R A -- Hamson, C A -- Kim, P S -- Cunningham, J M -- Berger, J M -- New York, N.Y. -- Science. 1997 Sep 12;277(5332):1662-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9287219" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carrier Proteins/metabolism ; Crystallography, X-Ray ; Friend murine leukemia virus/*chemistry ; Glycoproteins/*chemistry ; *Membrane Glycoproteins ; Membrane Proteins/metabolism ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; *Protein Structure, Secondary ; Receptors, Virus/metabolism ; Viral Envelope Proteins/*chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 83
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    Brightness speeds search for structures great and small (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1997 Aug 29;277(5330):1217-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9297237" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriorhodopsins/chemistry ; Bluetongue virus/chemistry/ultrastructure ; Crystallization ; *Crystallography, X-Ray ; Manganese/analysis ; Models, Molecular ; Muscle Contraction ; Muscle Fibers, Skeletal/physiology ; Photons ; Plant Roots/chemistry ; *Protein Conformation ; Proteins/*chemistry ; *Synchrotrons ; X-Ray Diffraction
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  • 84
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    A cyanobacterial phytochrome two-component light sensory system (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-05
    Description: The biliprotein phytochrome regulates plant growth and developmental responses to the ambient light environment through an unknown mechanism. Biochemical analyses demonstrate that phytochrome is an ancient molecule that evolved from a more compact light sensor in cyanobacteria. The cyanobacterial phytochrome Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of a small response regulator, Rcp1 (response regulator for cyanobacterial phytochrome), encoded by the adjacent gene, thus implicating protein phosphorylation-dephosphorylation in the initial step of light signal transduction by phytochrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeh, K C -- Wu, S H -- Murphy, J T -- Lagarias, J C -- 1 P41 RR06009/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278513" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; Cloning, Molecular ; Cyanobacteria/chemistry/genetics/*metabolism ; Genes, Bacterial ; *Light ; Molecular Sequence Data ; Operon ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; Proteins ; Recombinant Fusion Proteins/chemistry/metabolism ; Sequence Deletion ; Signal Transduction
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  • 85
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    Expression cloning in the test tube (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, R W -- Lustig, K D -- Stukenberg, P T -- McGarry, T J -- Kirschner, M W -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):973-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. king@bcmp.med.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9281074" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis ; Cloning, Molecular/*methods ; DNA, Complementary/genetics ; Enzymes/metabolism ; Gene Expression ; Mitosis ; Phosphorylation ; Plasmids ; Protein Processing, Post-Translational ; Proteins/genetics/*metabolism
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  • 86
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    Martian 'microbes' cover their tracks (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, R A -- New York, N.Y. -- Science. 1997 Apr 4;276(5309):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9122703" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria ; *Carbonates/analysis/chemistry ; *Exobiology ; Extraterrestrial Environment ; Ferrosoferric Oxide ; Fossils ; *Iron/analysis/chemistry ; *Mars ; *Meteoroids ; *Oxides/analysis/chemistry ; Temperature
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  • 87
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    Curing rat glioblastoma: immunotherapy or graft rejection? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beutler, A S -- Banck, M S -- Aguzzi, A -- New York, N.Y. -- Science. 1997 Apr 4;276(5309):20-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9122700" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Glioblastoma/*immunology/*therapy ; *Graft Rejection ; Histocompatibility Antigens/*immunology ; Insulin-Like Growth Factor I/*genetics ; Major Histocompatibility Complex ; Neoplasm Transplantation ; RNA, Antisense/*therapeutic use ; Rats ; Transplantation, Homologous ; Tumor Cells, Cultured
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  • 88
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    Removal of osteoclast bone resorption products by transcytosis (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-04-11
    Description: Osteoclasts are multinucleated cells responsible for bone resorption. During the resorption cycle, osteoclasts undergo dramatic changes in their polarity, and resorbing cells reveal four functionally and structurally different membrane domains. Bone degradation products, both organic and inorganic, were endocytosed from the ruffled border membrane. They were then found to be transported in vesicles through the cell to the plasma membrane domain, located in the middle of the basal membrane, where they were liberated into the extracellular space. These results explain how resorbing osteoclasts can simultaneously remove large amounts of matrix degradation products and penetrate into bone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Salo, J -- Lehenkari, P -- Mulari, M -- Metsikko, K -- Vaananen, H K -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):270-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Biocenter, University of Oulu, Kajaanintie 52 A, 90220 Oulu, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9092479" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; Biological Transport ; Biotin/metabolism ; Bone Matrix/*metabolism ; *Bone Resorption ; Cattle ; Cell Membrane/metabolism/ultrastructure ; Cell Polarity ; Cells, Cultured ; Endocytosis ; Extracellular Space/metabolism ; Microscopy, Confocal ; Microscopy, Electron ; Minerals/metabolism ; Organelles/metabolism ; Osteocalcin/metabolism ; Osteoclasts/*metabolism/ultrastructure ; Rats ; Tetracycline/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: The signal transduction pathway or pathways linking extracellular signals to myogenesis are poorly defined. Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. This indicates that muscle-specific gene expression is necessary but not sufficient to commit differentiated myocytes to myotubes and suggests a function for the MAPKs during the early and late stages of skeletal muscle differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, A M -- Tonks, N K -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Demerec Building, 1 Bungtown Road, Post Office Box 100, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360925" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Cell Cycle Proteins ; Cell Differentiation ; Cell Division ; Cell Line ; Cloning, Molecular ; Culture Media ; Cyclin D1/genetics ; Dual Specificity Phosphatase 1 ; Gene Expression Regulation, Developmental ; Immediate-Early Proteins/genetics/*metabolism ; JNK Mitogen-Activated Protein Kinases ; Mice ; Mitogen-Activated Protein Kinase 1/antagonists & inhibitors/*metabolism ; *Mitogen-Activated Protein Kinases ; Mitogens/pharmacology ; Muscle Proteins/*genetics ; Muscle, Skeletal/*cytology/*enzymology/metabolism ; *Phosphoprotein Phosphatases ; Phosphorylation ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Tetracycline/pharmacology ; Transcription, Genetic
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  • 90
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    The importance of a well-groomed child (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sapolsky, R M -- New York, N.Y. -- Science. 1997 Sep 12;277(5332):1620-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Stanford University, Stanford, CA 94305, USA. sapolsky@leland.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9312858" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Newborn ; *Behavior, Animal ; Corticotropin-Releasing Hormone/metabolism ; Female ; Glucocorticoids/secretion ; *Grooming ; *Handling (Psychology) ; Hippocampus/physiology ; Humans ; *Maternal Behavior ; Rats ; Receptors, Glucocorticoid/metabolism
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  • 91
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    How does the brain organize memories? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eichenbaum, H -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):330-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, Boston University, Boston, MA 02215, USA. hbe@bu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9518364" target="_blank"〉PubMed〈/a〉
    Keywords: Amnesia/physiopathology/psychology ; Animals ; Brain Mapping ; Cerebral Cortex/*physiology ; Cues ; Haplorhini ; Hippocampus/*physiology ; Humans ; *Memory ; Neural Pathways ; Neurons/physiology ; Rats
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  • 92
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    Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-11-05
    Description: The carboxyl-terminal domain, residues 146 to 231, of the human immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required for capsid dimerization and viral assembly. This domain contains a stretch of 20 residues, called the major homology region (MHR), which is conserved across retroviruses and is essential for viral assembly, maturation, and infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal that the globular domain is composed of four helices and an extended amino-terminal strand. CA(146-231) dimerizes through parallel packing of helix 2 across a dyad. The MHR is distinct from the dimer interface and instead forms an intricate hydrogen-bonding network that interconnects strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamble, T R -- Yoo, S -- Vajdos, F F -- von Schwedler, U K -- Worthylake, D K -- Wang, H -- McCutcheon, J P -- Sundquist, W I -- Hill, C P -- R01 AI40333/AI/NIAID NIH HHS/ -- R01 AI43036/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):849-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346481" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Capsid/*chemistry/genetics ; Cell Line ; Cloning, Molecular ; Cloning, Organism ; Crystallography, X-Ray ; Dimerization ; HIV-1/*chemistry/genetics/physiology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptidylprolyl Isomerase/chemistry ; *Protein Conformation ; Virus Replication
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  • 93
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    Regulation of gliogenesis in the central nervous system by the JAK-STAT signaling pathway (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-23
    Description: A mechanism by which members of the ciliary neurotrophic factor (CNTF)-leukemia inhibitory factor cytokine family regulate gliogenesis in the developing mammalian central nervous system was characterized. Activation of the CNTF receptor promoted differentiation of cerebral cortical precursor cells into astrocytes and inhibited differentiation of cortical precursors along a neuronal lineage. Although CNTF stimulated both the Janus kinase-signal transducer and activator of transcription (JAK-STAT) and Ras-mitogen-activated protein kinase signaling pathways in cortical precursor cells, the JAK-STAT signaling pathway selectively enhanced differentiation of these precursors along a glial lineage. These findings suggest that cytokine activation of the JAK-STAT signaling pathway may be a mechanism by which cell fate is controlled during mammalian development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonni, A -- Sun, Y -- Nadal-Vicens, M -- Bhatt, A -- Frank, D A -- Rozovsky, I -- Stahl, N -- Yancopoulos, G D -- Greenberg, M E -- NIHP30-HD 18655/HD/NICHD NIH HHS/ -- R01 CA43855/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):477-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, and Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334309" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; Astrocytes/*cytology/drug effects/metabolism ; Cell Differentiation ; Cell Division ; Cell Lineage ; Cells, Cultured ; Cerebral Cortex/*cytology/embryology ; Ciliary Neurotrophic Factor ; Cytokine Receptor gp130 ; DNA-Binding Proteins/*metabolism ; Dimerization ; Glial Fibrillary Acidic Protein/biosynthesis ; Growth Inhibitors/metabolism/pharmacology ; *Interleukin-6 ; Janus Kinase 1 ; Leukemia Inhibitory Factor ; Leukemia Inhibitory Factor Receptor alpha Subunit ; Lymphokines/metabolism/pharmacology ; Membrane Glycoproteins/metabolism ; Nerve Growth Factors/pharmacology ; Nerve Tissue Proteins/metabolism/pharmacology ; Platelet-Derived Growth Factor/pharmacology ; Protein-Tyrosine Kinases/*metabolism ; Rats ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cytokine/metabolism ; Receptors, Nerve Growth Factor/metabolism ; Receptors, OSM-LIF ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; *Signal Transduction ; Stem Cells/cytology ; Trans-Activators/*metabolism
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  • 94
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    Postsynaptic glutamate transport at the climbing fiber-Purkinje cell synapse (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-05
    Description: The role of postsynaptic, neuronal glutamate transporters in terminating signals at central excitatory synapses is not known. Stimulation of a climbing fiber input to cerebellar Purkinje cells was shown to generate an anionic current mediated by glutamate transporters. The kinetics of transporter currents were resolved by pulses of glutamate to outside-out membrane patches from Purkinje cells. Comparison of synaptic transporter currents to transporter currents expressed in Xenopus oocytes suggests that postsynaptic uptake at the climbing fiber synapse removes at least 22 percent of released glutamate. These neuronal transporter currents arise from synchronous activation of transporters that greatly outnumber activated AMPA receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Otis, T S -- Kavanaugh, M P -- Jahr, C E -- NS21419/NS/NINDS NIH HHS/ -- NS33270/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1515-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, L-474, Oregon Health Sciences University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278516" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Transport System X-AG ; Animals ; Aspartic Acid/analogs & derivatives/pharmacology ; Biological Transport ; Carrier Proteins/*metabolism ; Dicarboxylic Acids/pharmacology ; Glutamate Plasma Membrane Transport Proteins ; Glutamic Acid/*metabolism ; In Vitro Techniques ; Kinetics ; Nerve Fibers/*metabolism ; Oocytes ; Patch-Clamp Techniques ; Purkinje Cells/*metabolism ; Pyrrolidines/pharmacology ; Rats ; Receptors, AMPA/metabolism ; Receptors, Glutamate/*metabolism ; *Symporters ; Synapses/*metabolism ; *Synaptic Transmission ; Xenopus
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  • 95
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    Structure of a protein photocycle intermediate by millisecond time-resolved crystallography (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-07
    Description: The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's phenolic oxygen. Resulting changes in shape, hydrogen bonding, and electrostatic potential at the protein surface form a likely basis for signal transduction. The structural results suggest a general framework for the interpretation of protein photocycles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Genick, U K -- Borgstahl, G E -- Ng, K -- Ren, Z -- Pradervand, C -- Burke, P M -- Srajer, V -- Teng, T Y -- Schildkamp, W -- McRee, D E -- Moffat, K -- Getzoff, E D -- GM36452/GM/NIGMS NIH HHS/ -- GM37684/GM/NIGMS NIH HHS/ -- RR07707/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1471-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, 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/9045611" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/physiology ; Binding Sites ; Chromatiaceae ; Crystallography, X-Ray ; Electrochemistry ; Hydrogen Bonding ; Isomerism ; Light ; Models, Molecular ; *Photoreceptors, Microbial ; *Protein Conformation ; Signal Transduction ; Spectrum Analysis
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: Structural changes in the extracellular matrix are necessary for cell migration during tissue remodeling and tumor invasion. Specific cleavage of laminin-5 (Ln-5) by matrix metalloprotease-2 (MMP2) was shown to induce migration of breast epithelial cells. MMP2 cleaved the Ln-5 gamma2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giannelli, G -- Falk-Marzillier, J -- Schiraldi, O -- Stetler-Stevenson, W G -- Quaranta, V -- CA47858/CA/NCI NIH HHS/ -- DE10063/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):225-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast/*cytology/metabolism ; Cell Adhesion ; Cell Adhesion Molecules/*metabolism ; Cell Division ; Cell Line ; *Cell Movement ; Cell Size ; Collagenases/metabolism ; Epithelial Cells ; Epithelium/metabolism ; Extracellular Matrix/*metabolism ; Female ; Fibrinolysin/metabolism ; Gelatinases/antagonists & inhibitors/*metabolism ; Humans ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Metalloendopeptidases/antagonists & inhibitors/*metabolism ; Mice ; Phenylalanine/analogs & derivatives/pharmacology ; Protease Inhibitors/pharmacology ; Rats ; Recombinant Fusion Proteins/metabolism ; Skin Neoplasms/metabolism/pathology ; Thiophenes/pharmacology
    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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  • 97
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    Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: In the absence of costimulation, T cells activated through their antigen receptor become unresponsive (anergic) and do not transcribe the gene encoding interleukin-2 (IL-2) when restimulated with antigen. Anergic alloantigen-specific human T cells contained phosphorylated Cbl that coimmunoprecipitated with Fyn. The adapter protein CrkL was associated with both phosphorylated Cbl and the guanidine nucleotide-releasing factor C3G, which catalyzes guanosine triphosphate (GTP) exchange on Rap1. Active Rap1 (GTP-bound form) was present in anergic cells. Forced expression of low amounts of Rap1-GTP in Jurkat T cells recapitulated the anergic defect and blocked T cell antigen receptor (TCR)- and CD28-mediated IL-2 gene transcription. Therefore, Rap1 functions as a negative regulator of TCR-mediated IL-2 gene transcription and may be responsible for the specific defect in IL-2 production in T cell anergy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boussiotis, V A -- Freeman, G J -- Berezovskaya, A -- Barber, D L -- Nadler, L M -- AI 35225/AI/NIAID NIH HHS/ -- AI39671/AI/NIAID NIH HHS/ -- HL 54785/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):124-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA. vassiliki_boussiotis@macmailgw.dfci.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311917" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Antigens, CD28/immunology ; *Clonal Anergy ; GTP-Binding Proteins/*metabolism ; Gene Expression Regulation ; Guanine Nucleotide Exchange Factors ; Guanosine Triphosphate/metabolism ; Humans ; Interleukin-2/*genetics ; Jurkat Cells ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-cbl ; Proto-Oncogene Proteins c-fyn ; Receptors, Antigen, T-Cell/immunology ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; T-Lymphocytes/*immunology/metabolism ; *Transcription, Genetic ; Transfection ; *Ubiquitin-Protein Ligases ; rap GTP-Binding Proteins ; ras Guanine Nucleotide Exchange Factors ; ras Proteins/metabolism ; src Homology Domains
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Defective TNF-alpha-induced apoptosis in STAT1-null cells due to low constitutive levels of caspases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Signal transducers and activators of transcription (STATs) enhance transcription of specific genes in response to cytokines and growth factors. STAT1 is also required for efficient constitutive expression of the caspases Ice, Cpp32, and Ich-1 in human fibroblasts. As a consequence, STAT1-null cells are resistant to apoptosis by tumor necrosis factor alpha (TNF-alpha). Reintroduction of STAT1alpha restored both TNF-alpha-induced apoptosis and the expression of Ice, Cpp32, and Ich-1. Variant STAT1 proteins carrying point mutations that inactivate domains required for STAT dimer formation nevertheless restored protease expression and sensitivity to apoptosis, indicating that the functions of STAT1 required for these activities are different from those that mediate induced gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumar, A -- Commane, M -- Flickinger, T W -- Horvath, C M -- Stark, G R -- P01 CA62220/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1630-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Lerner Research Institute, The Cleveland Clinic Foundation, Cleveland, OH 44195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374464" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Caspase 1 ; Caspase 2 ; Caspase 3 ; *Caspases ; Cell Line ; Cysteine Endopeptidases/genetics/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dactinomycin/pharmacology ; Dimerization ; Gene Expression Regulation, Enzymologic ; Humans ; Interferon-gamma/pharmacology ; Phosphorylation ; Point Mutation ; Proteins/genetics/*metabolism ; STAT1 Transcription Factor ; Signal Transduction ; Trans-Activators/chemistry/genetics/*metabolism ; Transfection ; Tumor Necrosis Factor-alpha/*pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-28
    Description: Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain alphabeta structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boyington, J C -- Gladyshev, V N -- Khangulov, S V -- Stadtman, T C -- Sun, P D -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Structure, National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), Rockville, MD 20852, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036855" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbon Dioxide/metabolism ; Catalysis ; Crystallography, X-Ray ; Electron Transport ; Escherichia coli/enzymology ; Ferrous Compounds/*chemistry ; Formate Dehydrogenases/*chemistry/metabolism ; Formates/*metabolism ; Guanine Nucleotides/chemistry/metabolism ; Hydrogen Bonding ; Hydrogenase/*chemistry/metabolism ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Molybdenum/chemistry/metabolism ; Multienzyme Complexes/*chemistry/metabolism ; Nitrites/chemistry ; Oxidation-Reduction ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protons ; Pterins/chemistry/metabolism ; Selenocysteine/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Structural basis for ligand-regulated oligomerization of AraC (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-18
    Description: The crystal structure of the arabinose-binding and dimerization domain of the Escherchia coli gene regulatory protein AraC was determined in the presence and absence of L-arabinose. The 1.5 angstrom structure of the arabinose-bound molecule shows that the protein adopts an unusual fold, binding sugar within a beta barrel and completely burying the arabinose with the amino-terminal arm of the protein. Dimer contacts in the presence of arabinose are mediated by an antiparallel coiled-coil. In the 2.8 angstrom structure of the uncomplexed protein, the amino-terminal arm is disordered, uncovering the sugar-binding pocket and allowing it to serve as an oligomerization interface. The ligand-gated oligomerization as seen in AraC provides the basis of a plausible mechanism for modulating the protein's DNA-looping properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soisson, S M -- MacDougall-Shackleton, B -- Schleif, R -- Wolberger, C -- GM18277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):421-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103202" target="_blank"〉PubMed〈/a〉
    Keywords: AraC Transcription Factor ; Arabinose/metabolism ; *Bacterial Proteins ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/*metabolism ; Dimerization ; Hydrogen Bonding ; Ligands ; Models, Molecular ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Repressor Proteins/*chemistry/metabolism ; *Transcription Factors
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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