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  • Cell Line  (349)
  • Binding Sites  (342)
  • *Ecosystem
  • American Association for the Advancement of Science (AAAS)  (692)
  • American Meteorological Society
  • MDPI Publishing
  • 1995-1999  (692)
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  • American Association for the Advancement of Science (AAAS)  (692)
  • American Meteorological Society
  • MDPI Publishing
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  • 201
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    Enzyme structure with two catalytic sites for double-sieve selection of substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyzes only the valylated products. For this two-step substrate selection, a "double-sieve" mechanism has already been proposed. The present crystal structures of the synthetase in complexes with L-isoleucine and L-valine demonstrate that the first sieve is on the aminoacylation domain containing the Rossmann fold, whereas the second, editing sieve exists on a globular beta-barrel domain that protrudes from the aminoacylation domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nureki, O -- Vassylyev, D G -- Tateno, M -- Shimada, A -- Nakama, T -- Fukai, S -- Konno, M -- Hendrickson, T L -- Schimmel, P -- Yokoyama, S -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Apr 24;280(5363):578-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9554847" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate ; Binding Sites ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Hydrogen Bonding ; Hydrolysis ; Isoleucine/*metabolism ; Isoleucine-tRNA Ligase/*chemistry/metabolism ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA, Transfer, Ile/metabolism ; Substrate Specificity ; Thermus thermophilus/enzymology ; Transfer RNA Aminoacylation ; Valine/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 202
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    Bioresources and "biopiracy" in Brazil (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silva, M -- New York, N.Y. -- Science. 1998 May 1;280(5364):657.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9599137" target="_blank"〉PubMed〈/a〉
    Keywords: Brazil ; *Ecosystem ; Legislation as Topic ; Ownership/*legislation & jurisprudence ; *Research
    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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  • 203
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    Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: The mechanisms by which Ebola virus evades detection and infects cells to cause hemorrhagic fever have not been defined, though its glycoprotein, synthesized in either a secreted or transmembrane form, is likely involved. Here the secreted glycoprotein was found to interact with neutrophils through CD16b, the neutrophil-specific form of the Fc gamma receptor III, whereas the transmembrane glycoprotein was found to interact with endothelial cells but not neutrophils. A murine retroviral vector pseudotyped with the transmembrane glycoprotein preferentially infected endothelial cells. Thus, the secreted glycoprotein inhibits early neutrophil activation, which likely affects the host response to infection, whereas binding of the transmembrane glycoprotein to endothelial cells may contribute to the hemorrhagic symptoms of this disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Z -- Delgado, R -- Xu, L -- Todd, R F -- Nabel, E G -- Sanchez, A -- Nabel, G J -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1034-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461435" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Ebolavirus/genetics/metabolism/*pathogenicity/physiology ; Endothelium, Vascular/cytology/*metabolism/virology ; Genes, Viral ; Genetic Vectors ; Glycoproteins/genetics/*metabolism/secretion ; Hemorrhagic Fever, Ebola/virology ; Humans ; L-Selectin/metabolism ; Membrane Glycoproteins/genetics/*metabolism ; Moloney murine leukemia virus/genetics/physiology ; Neutrophil Activation ; Neutrophils/immunology/*metabolism ; Receptors, IgG/metabolism ; Transfection ; Tumor Cells, Cultured ; Viral Matrix Proteins/genetics/*metabolism ; Viral Proteins/genetics/*metabolism/secretion
    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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  • 204
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    Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-30
    Description: The complement and immunoglobulin receptors are the major phagocytic receptors involved during infection. However, only immunoglobulin-dependent uptake results in a respiratory burst and an inflammatory response in macrophages. Rho guanosine triphosphatases (molecular switches that control the organization of the actin cytoskeleton) were found to be essential for both types of phagocytosis. Two distinct mechanisms of phagocytosis were identified: Type I, used by the immunoglobulin receptor, is mediated by Cdc42 and Rac, and type II, used by the complement receptor, is mediated by Rho. These results suggest a molecular basis for the different biological consequences that are associated with phagocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caron, E -- Hall, A -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1717-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory for Molecular Cell Biology, Cancer Research Campaign Oncogene and Signal Transduction Group, and Department of Biochemistry, 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/9831565" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Actins/metabolism ; Animals ; Antigens, CD/*immunology/metabolism ; *Bacterial Proteins ; Bacterial Toxins/pharmacology ; COS Cells ; Cell Cycle Proteins/metabolism ; Cell Line ; Enzyme Activation ; Erythrocytes/immunology ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/metabolism ; Macrophage-1 Antigen/*immunology/metabolism ; Macrophages/immunology ; Mice ; Opsonin Proteins ; *Phagocytosis ; Phagosomes/enzymology ; Receptors, IgG/*immunology/metabolism ; Transfection ; cdc42 GTP-Binding Protein ; rac GTP-Binding Proteins
    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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  • 205
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    Secret life of cytochrome bc1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, J L -- New York, N.Y. -- Science. 1998 Jul 3;281(5373):58-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA. smithj@bragg.bio.purdue.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9679019" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cattle ; Crystallization ; Crystallography, X-Ray ; Cytochromes c1/chemistry/metabolism ; Diffusion ; Dimerization ; Electron Transport ; Electron Transport Complex III/*chemistry/metabolism ; Hydrogen Bonding ; Iron-Sulfur Proteins/chemistry/metabolism ; Mitochondria, Heart/*enzymology ; Oxidation-Reduction ; *Protein Conformation ; Protein Structure, Secondary ; Protons ; Ubiquinone/analogs & derivatives/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 206
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    Genomic cis-regulatory logic: experimental and computational analysis of a sea urchin gene (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: The genomic regulatory network that controls gene expression ultimately determines form and function in each species. The operational nature of the regulatory programming specified in cis-regulatory DNA sequence was determined from a detailed functional analysis of a sea urchin control element that directs the expression of a gene in the endoderm during development. Spatial expression and repression, and the changing rate of transcription of this gene, are mediated by a complex and extended cis-regulatory system. The system may be typical of developmental cis-regulatory apparatus. All of its activities are integrated in the proximal element, which contains seven target sites for DNA binding proteins. A quantitative computational model of this regulatory element was constructed that explicitly reveals the logical interrelations hard-wired into the DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuh, C H -- Bolouri, H -- Davidson, E H -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1896-902.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, 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/9506933" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Adhesion Molecules/*genetics/physiology ; Computer Simulation ; DNA-Binding Proteins/metabolism ; Embryo, Nonmammalian/metabolism ; Endoderm/metabolism ; Gastrula/metabolism ; *Gene Expression Regulation, Developmental ; Lithium Chloride/pharmacology ; Models, Genetic ; Molecular Sequence Data ; Mutagenesis ; Promoter Regions, Genetic/genetics/*physiology ; Proteins/*genetics/physiology ; Sea Urchins/embryology/*genetics/metabolism ; *Transcription, Genetic/drug effects
    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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  • 207
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    Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-25
    Description: Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCzeta and PKCdelta in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1. PDK1-dependent phosphorylation of PKCdelta in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCdelta in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Le Good, J A -- Ziegler, W H -- Parekh, D B -- Alessi, D R -- Cohen, P -- Parker, P J -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748166" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Binding Sites ; Cell Line ; Chromones/pharmacology ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Isoenzymes/*metabolism ; Morpholines/pharmacology ; Phosphatidylcholines/pharmacology ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphatidylinositol Phosphates ; Phosphatidylserines/pharmacology ; Phosphorylation ; Protein Kinase C/*metabolism ; Protein Kinase C beta ; Protein-Serine-Threonine Kinases/*metabolism ; Recombinant Proteins/metabolism ; Tetradecanoylphorbol Acetate/pharmacology
    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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  • 208
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    Populations as "species-in-waiting"? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, K M -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2031-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669956" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; *Ecosystem ; *Genetics, Population ; Mathematics ; Population Density
    Print ISSN: 0036-8075
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  • 209
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    Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-24
    Description: Selective protein kinase inhibitors were developed on the basis of the unexpected binding mode of 2,6,9-trisubstituted purines to the adenosine triphosphate-binding site of the human cyclin-dependent kinase 2 (CDK2). By iterating chemical library synthesis and biological screening, potent inhibitors of the human CDK2-cyclin A kinase complex and of Saccharomyces cerevisiae Cdc28p were identified. The structural basis for the binding affinity and selectivity was determined by analysis of a three-dimensional crystal structure of a CDK2-inhibitor complex. The cellular effects of these compounds were characterized in mammalian cells and yeast. In the latter case the effects were characterized on a genome-wide scale by monitoring changes in messenger RNA levels in treated cells with high-density oligonucleotide probe arrays. Purine libraries could provide useful tools for analyzing a variety of signaling and regulatory pathways and may lead to the development of new therapeutics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gray, N S -- Wodicka, L -- Thunnissen, A M -- Norman, T C -- Kwon, S -- Espinoza, F H -- Morgan, D O -- Barnes, G -- LeClerc, S -- Meijer, L -- Kim, S H -- Lockhart, D J -- Schultz, P G -- New York, N.Y. -- Science. 1998 Jul 24;281(5376):533-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9677190" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/*analogs & derivatives/chemistry/metabolism/pharmacology ; Binding Sites ; *CDC2-CDC28 Kinases ; CDC28 Protein Kinase, S cerevisiae/antagonists & inhibitors ; Cell Division/drug effects ; Crystallography, X-Ray ; Cyclin A/metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/*antagonists & inhibitors ; Drug Evaluation, Preclinical ; Flavonoids/chemistry/metabolism/pharmacology ; Gene Expression Regulation, Fungal/drug effects ; Genes, Fungal ; Humans ; Hydrogen Bonding ; Oligonucleotide Probes ; Phosphates/metabolism ; Piperidines/chemistry/metabolism/pharmacology ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Purines/chemical synthesis/chemistry/metabolism/*pharmacology ; RNA, Messenger/genetics/metabolism ; Saccharomyces cerevisiae/enzymology/genetics ; Structure-Activity Relationship ; Transcription, Genetic/drug effects ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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  • 210
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    An antimicrobial activity of cytolytic T cells mediated by granulysin (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-02
    Description: Cytolytic T lymphocytes (CTLs) kill intracellular pathogens by a granule-dependent mechanism. Granulysin, a protein found in granules of CTLs, reduced the viability of a broad spectrum of pathogenic bacteria, fungi, and parasites in vitro. Granulysin directly killed extracellular Mycobacterium tuberculosis, altering the membrane integrity of the bacillus, and, in combination with perforin, decreased the viability of intracellular M. tuberculosis. The ability of CTLs to kill intracellular M. tuberculosis was dependent on the presence of granulysin in cytotoxic granules, defining a mechanism by which T cells directly contribute to immunity against intracellular pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stenger, S -- Hanson, D A -- Teitelbaum, R -- Dewan, P -- Niazi, K R -- Froelich, C J -- Ganz, T -- Thoma-Uszynski, S -- Melian, A -- Bogdan, C -- Porcelli, S A -- Bloom, B R -- Krensky, A M -- Modlin, R L -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, UCLA School of Medicine, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9756476" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Differentiation, T-Lymphocyte/analysis/*immunology/pharmacology ; Cell Line ; Cell Membrane/ultrastructure ; Cells, Cultured ; Cytoplasmic Granules/immunology ; *Cytotoxicity, Immunologic ; Humans ; Macrophages/immunology/microbiology ; Membrane Glycoproteins/immunology/pharmacology ; Microscopy, Confocal ; Microscopy, Electron, Scanning ; Mycobacterium tuberculosis/*immunology/physiology/ultrastructure ; Perforin ; Pore Forming Cytotoxic Proteins ; Recombinant Proteins/pharmacology ; T-Lymphocytes, Cytotoxic/*immunology
    Print ISSN: 0036-8075
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  • 211
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    Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: Mechanosensitive ion channels play a critical role in transducing physical stresses at the cell membrane into an electrochemical response. The MscL family of large-conductance mechanosensitive channels is widely distributed among prokaryotes and may participate in the regulation of osmotic pressure changes within the cell. In an effort to better understand the structural basis for the function of these channels, the structure of the MscL homolog from Mycobacterium tuberculosis was determined by x-ray crystallography to 3.5 angstroms resolution. This channel is organized as a homopentamer, with each subunit containing two transmembrane alpha helices and a third cytoplasmic alpha helix. From the extracellular side, a water-filled opening approximately 18 angstroms in diameter leads into a pore lined with hydrophilic residues which narrows at the cytoplasmic side to an occluded hydrophobic apex that may act as the channel gate. This structure may serve as a model for other mechanosensitive channels, as well as the broader class of pentameric ligand-gated ion channels exemplified by the nicotinic acetylcholine receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, G -- Spencer, R H -- Lee, A T -- Barclay, M T -- Rees, D C -- GM18486/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2220-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, 147-75CH, 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/9856938" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cell Membrane/chemistry ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; *Escherichia coli Proteins ; *Ion Channel Gating ; Ion Channels/*chemistry/metabolism ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Mycobacterium tuberculosis/*chemistry ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Temperature
    Print ISSN: 0036-8075
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  • 212
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    Structure of human methionine aminopeptidase-2 complexed with fumagillin (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-13
    Description: The fungal metabolite fumagillin suppresses the formation of new blood vessels, and a fumagillin analog is currently in clinical trials as an anticancer agent. The molecular target of fumagillin is methionine aminopeptidase-2 (MetAP-2). A 1.8 A resolution crystal structure of free and inhibited human MetAP-2 shows a covalent bond formed between a reactive epoxide of fumagillin and histidine-231 in the active site of MetAP-2. Extensive hydrophobic and water-mediated polar interactions with other parts of fumagillin provide additional affinity. Fumagillin-based drugs inhibit MetAP-2 but not MetAP-1, and the three-dimensional structure also indicates the likely determinants of this specificity. The structural basis for fumagillin's potency and specificity forms the starting point for structure-based drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, S -- Widom, J -- Kemp, C W -- Crews, C M -- Clardy, J -- CA24487/CA/NCI NIH HHS/ -- CA59021/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1324-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉J. Clardy, Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, NY 14853-1301, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812898" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aminopeptidases/antagonists & inhibitors/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Cyclohexanes ; Fatty Acids, Unsaturated/chemistry/*metabolism/pharmacology ; Humans ; Hydrogen Bonding ; Metalloendopeptidases/antagonists & inhibitors/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Sequence Alignment ; Sesquiterpenes
    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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  • 213
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    Single-molecule enzymatic dynamics (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-04
    Description: Enzymatic turnovers of single cholesterol oxidase molecules were observed in real time by monitoring the emission from the enzyme's fluorescent active site, flavin adenine dinucleotide (FAD). Statistical analyses of single-molecule trajectories revealed a significant and slow fluctuation in the rate of cholesterol oxidation by FAD. The static disorder and dynamic disorder of reaction rates, which are essentially indistinguishable in ensemble-averaged experiments, were determined separately by the real-time single-molecule approach. A molecular memory phenomenon, in which an enzymatic turnover was not independent of its previous turnovers because of a slow fluctuation of protein conformation, was evidenced by spontaneous spectral fluctuation of FAD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, H P -- Xun, L -- Xie, X S -- New York, N.Y. -- Science. 1998 Dec 4;282(5395):1877-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pacific Northwest National Laboratory, William R. Wiley Environmental Molecular Sciences Laboratory, Richland, WA 99352, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9836635" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Brevibacterium/enzymology ; Cholesterol/*metabolism ; Cholesterol Oxidase/*metabolism ; Flavin-Adenine Dinucleotide/*metabolism ; Kinetics ; Microscopy, Fluorescence ; Oxidation-Reduction ; Probability ; Spectrometry, Fluorescence ; Stochastic Processes
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  • 214
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    Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: Mitogen stimulation of cytoskeletal changes and c-jun amino-terminal kinases is mediated by Rac small guanine nucleotide-binding proteins. Vav, a guanosine diphosphate (GDP)-guanosine triphosphate (GTP) exchange factor for Rac that stimulates the exchange of bound GDP for GTP, bound to and was directly controlled by substrates and products of phosphoinositide (PI) 3-kinase. The PI 3-kinase substrate phosphatidylinositol-4,5-bisphosphate inhibited activation of Vav by the tyrosine kinase Lck, whereas the product phosphatidylinositol-3,4,5-trisphosphate enhanced phosphorylation and activation of Vav by Lck. Control of Vav in response to mitogens by the products of PI 3-kinase suggests a mechanism for Ras-dependent activation of Rac.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, J -- Luby-Phelps, K -- Das, B -- Shu, X -- Xia, Y -- Mosteller, R D -- Krishna, U M -- Falck, J R -- White, M A -- Broek, D -- CA50261/CA/NCI NIH HHS/ -- CA71443/CA/NCI NIH HHS/ -- GM31278/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):558-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA 90033-0800, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438848" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanine Nucleotide Exchange Factors ; Guanosine Diphosphate/*metabolism ; Guanosine Triphosphate/metabolism ; Inositol 1,4,5-Trisphosphate/metabolism/pharmacology ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/metabolism ; Mutagenesis, Site-Directed ; Oncogene Proteins/chemistry/*metabolism ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphatidylinositol 4,5-Diphosphate/metabolism/pharmacology ; Phosphatidylinositol Phosphates/metabolism/pharmacology ; Phosphatidylinositols/*metabolism/pharmacology ; Phosphorylation ; Proteins/metabolism ; Proto-Oncogene Proteins c-vav ; Rats ; rac GTP-Binding Proteins ; ras Guanine Nucleotide Exchange Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Pinning down cell division (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1883-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417635" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Cell Cycle Proteins ; *Cell Division ; Humans ; *Mitosis ; Models, Molecular ; Peptidylprolyl Isomerase/chemistry/*metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Proline/metabolism ; Protein Conformation ; Protein-Serine-Threonine Kinases/metabolism ; Yeasts/cytology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 216
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    Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: Pin1 is an essential and conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins). In response to their phosphorylation during mitosis, Pin1 binds and regulates members of a highly conserved set of proteins that overlaps with antigens recognized by the mitosis-specific monoclonal antibody MPM-2. Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Both Pin1 and MPM-2 selected similar phosphorylated serine-proline-containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Pin1 preferentially isomerized proline residues preceded by phosphorylated serine or threonine with up to 1300-fold selectivity compared with unphosphorylated peptides. Pin1 may thus regulate mitotic progression by catalyzing sequence-specific and phosphorylation-dependent proline isomerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yaffe, M B -- Schutkowski, M -- Shen, M -- Zhou, X Z -- Stukenberg, P T -- Rahfeld, J U -- Xu, J -- Kuang, J -- Kirschner, M W -- Fischer, G -- Cantley, L C -- Lu, K P -- GM56203/GM/NIGMS NIH HHS/ -- GM56230/GM/NIGMS NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1957-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395400" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/metabolism ; Antibodies, Monoclonal ; Binding Sites ; Carrier Proteins/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; DNA-Binding Proteins/metabolism ; Epitopes ; HeLa Cells ; Heat-Shock Proteins/metabolism ; Humans ; Isomerism ; *Mitosis ; Models, Molecular ; Oligopeptides/chemistry/*metabolism ; Peptide Library ; Peptidylprolyl Isomerase/chemistry/*metabolism ; Phosphoproteins/chemistry/immunology/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Proline/*metabolism ; Protein Conformation ; Recombinant Fusion Proteins/chemistry/metabolism ; Substrate Specificity ; Tacrolimus Binding Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 217
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    Correction of deafness in shaker-2 mice by an unconventional myosin in a BAC transgene (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: The shaker-2 mouse mutation, the homolog of human DFNB3, causes deafness and circling behavior. A bacterial artificial chromosome (BAC) transgene from the shaker-2 critical region corrected the vestibular defects, deafness, and inner ear morphology of shaker-2 mice. An unconventional myosin gene, Myo15, was discovered by DNA sequencing of this BAC. Shaker-2 mice were found to have an amino acid substitution at a highly conserved position within the motor domain of this myosin. Auditory hair cells of shaker-2 mice have very short stereocilia and a long actin-containing protrusion extending from their basal end. This histopathology suggests that Myo15 is necessary for actin organization in the hair cells of the cochlea.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Probst, F J -- Fridell, R A -- Raphael, Y -- Saunders, T L -- Wang, A -- Liang, Y -- Morell, R J -- Touchman, J W -- Lyons, R H -- Noben-Trauth, K -- Friedman, T B -- Camper, S A -- Z01 DC 00035/DC/NIDCD NIH HHS/ -- Z01 DC 00038/DC/NIDCD NIH HHS/ -- Z01 DC 02407/DC/NIDCD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 29;280(5368):1444-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, 4701 MSRB III, University of Michigan, 1500 West Medical Center Drive, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9603735" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Brain/metabolism ; Chromosomes, Bacterial ; Deafness/*genetics/pathology/therapy ; Ear, Inner/metabolism ; Female ; Genetic Complementation Test ; Hair Cells, Auditory/ultrastructure ; Humans ; Liver/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Mice, Transgenic ; Myosins/chemistry/*genetics/metabolism ; Phenotype ; Point Mutation ; Transgenes
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 218
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    Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-30
    Description: A combinatorial disulfide cross-linking strategy was used to prepare a stalled complex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer and a deoxynucleoside triphosphate (dNTP), and the crystal structure of the complex was determined at a resolution of 3.2 angstroms. The presence of a dideoxynucleotide at the 3'-primer terminus allows capture of a state in which the substrates are poised for attack on the dNTP. Conformational changes that accompany formation of the catalytic complex produce distinct clusters of the residues that are altered in viruses resistant to nucleoside analog drugs. The positioning of these residues in the neighborhood of the dNTP helps to resolve some long-standing puzzles about the molecular basis of resistance. The resistance mutations are likely to influence binding or reactivity of the inhibitors, relative to normal dNTPs, and the clustering of the mutations correlates with the chemical structure of the drug.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, H -- Chopra, R -- Verdine, G L -- Harrison, S C -- GM-18621/GM/NIGMS NIH HHS/ -- GM-39589/GM/NIGMS NIH HHS/ -- GM-44853/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1669-75.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831551" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/metabolism/*pharmacology ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; DNA Primers/chemistry/metabolism ; DNA, Viral/chemistry/metabolism ; Deoxyribonucleotides/chemistry/metabolism ; Dimerization ; Drug Resistance, Microbial ; HIV Reverse Transcriptase/*chemistry/genetics/metabolism ; HIV-1/*drug effects/enzymology ; Humans ; Hydrogen Bonding ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Protein Conformation ; Reverse Transcriptase Inhibitors/metabolism/*pharmacology ; Templates, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structure of the amino-terminal protein interaction domain of STAT-4 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: STATs (signal transducers and activators of transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. The crystal structure of an NH2-terminal conserved domain (N-domain) comprising the first 123 residues of STAT-4 was determined at 1.45 angstroms. The domain consists of eight helices that are assembled into a hook-like structure. The N-domain has been implicated in several protein-protein interactions affecting transcription, and it enables dimerized STAT molecules to polymerize and to bind DNA cooperatively. The structure shows that N-domains can interact through an extensive interface formed by polar interactions across one face of the hook. Mutagenesis of an invariant tryptophan residue at the heart of this interface abolished cooperative DNA binding by the full-length protein in vitro and reduced the transcriptional response after cytokine stimulation in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vinkemeier, U -- Moarefi, I -- Darnell, J E Jr -- Kuriyan, J -- AI32489/AI/NIAID NIH HHS/ -- AI34420/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1048-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology and Laboratories of Molecular Biophysics, The Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461439" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Crystallography, X-Ray ; DNA/metabolism ; DNA-Binding Proteins/*chemistry/genetics/metabolism ; Humans ; Hydrogen Bonding ; Interferon-gamma/pharmacology ; Models, Molecular ; Molecular Sequence Data ; Oligodeoxyribonucleotides/metabolism ; *Protein Conformation ; Protein Structure, Tertiary ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; Signal Transduction ; Trans-Activators/*chemistry/genetics/metabolism ; Transcription, Genetic ; Transfection ; src Homology Domains
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 220
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    Coupled gating between individual skeletal muscle Ca2+ release channels (ryanodine receptors) (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-07
    Description: Excitation-contraction coupling in skeletal muscle requires the release of intracellular calcium ions (Ca2+) through ryanodine receptor (RyR1) channels in the sarcoplasmic reticulum. Half of the RyR1 channels are activated by voltage-dependent Ca2+ channels in the plasma membrane. In planar lipid bilayers, RyR1 channels exhibited simultaneous openings and closings, termed "coupled gating." Addition of the channel accessory protein FKBP12 induced coupled gating, and removal of FKBP12 uncoupled channels. Coupled gating provides a mechanism by which RyR1 channels that are not associated with voltage-dependent Ca2+ channels can be regulated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, S O -- Ondrias, K -- Marks, A R -- R01A139794/PHS HHS/ -- R01HL56180/HL/NHLBI NIH HHS/ -- R03TW00949/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):818-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Cardiology Program, Divisions of Cardiology and Circulatory Physiology, Department of Medicine, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694652" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Calcium Channels/metabolism ; Carrier Proteins/metabolism ; Cell Line ; DNA-Binding Proteins/metabolism ; Heat-Shock Proteins/metabolism ; *Ion Channel Gating/drug effects ; Lipid Bilayers ; Muscle, Skeletal/metabolism ; Polyenes/pharmacology ; Probability ; Rabbits ; Recombinant Proteins/metabolism ; Ryanodine/metabolism ; Ryanodine Receptor Calcium Release Channel/*metabolism ; Sarcoplasmic Reticulum/*metabolism ; Sirolimus ; Spodoptera ; Tacrolimus Binding Proteins
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  • 221
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    Promotion of trophoblast stem cell proliferation by FGF4 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-16
    Description: The trophoblast cell lineage is essential for the survival of the mammalian embryo in utero. This lineage is specified before implantation into the uterus and is restricted to form the fetal portion of the placenta. A culture of mouse blastocysts or early postimplantation trophoblasts in the presence of fibroblast growth factor 4 (FGF4) permitted the isolation of permanent trophoblast stem cell lines. These cell lines differentiated to other trophoblast subtypes in vitro in the absence of FGF4 and exclusively contributed to the trophoblast lineage in vivo in chimeras.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, S -- Kunath, T -- Hadjantonakis, A K -- Nagy, A -- Rossant, J -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2072-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851926" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/cytology ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Lineage ; Chimera ; Culture Media, Conditioned ; Embryo, Mammalian/cytology ; Female ; Fibroblast Growth Factor 4 ; Fibroblast Growth Factors/*pharmacology/physiology ; Fibroblasts/cytology ; Gene Expression Regulation, Developmental ; Genetic Markers ; Karyotyping ; Male ; Mice ; Models, Biological ; Proto-Oncogene Proteins/*pharmacology/physiology ; Signal Transduction ; Stem Cells/*cytology/metabolism ; Trophoblasts/*cytology/metabolism
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    Structure of nitric oxide synthase oxygenase dimer with pterin and substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitric oxide. Pterin binding refolds the central interface region, recruits new structural elements, creates a 30 angstrom deep active-center channel, and causes a 35 degrees helical tilt to expose a heme edge and the adjacent residue tryptophan-366 for likely reductase domain interactions and caveolin inhibition. Heme propionate interactions with pterin and L-Arg suggest that pterin has electronic influences on heme-bound oxygen. L-Arginine binds to glutamic acid-371 and stacks with heme in an otherwise hydrophobic pocket to aid activation of heme-bound oxygen by direct proton donation and thereby differentiate the two chemical steps of nitric oxide synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crane, B R -- Arvai, A S -- Ghosh, D K -- Wu, C -- Getzoff, E D -- Stuehr, D J -- Tainer, J A -- HL58883/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2121-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical 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/9516116" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine/chemistry/*metabolism ; Binding Sites ; Biopterin/*analogs & derivatives/chemistry/metabolism ; Citrulline/analogs & derivatives/chemistry/metabolism ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Isoenzymes/chemistry/metabolism ; Ligands ; Macrophages/enzymology ; Mice ; Models, Molecular ; Nitric Oxide/biosynthesis ; Nitric Oxide Synthase/*chemistry/metabolism ; Nitric Oxide Synthase Type II ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Thiourea/analogs & derivatives/chemistry/metabolism
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    Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-04
    Description: Mitochondrial cytochrome bc1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. Refined crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme. The "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme. The mitochondrial targeting presequence of the "Rieske" protein (subunit 9) is lodged between the two "core" subunits at the matrix side of the complex. These "core" subunits are related to the matrix processing peptidase, and the structure unveils how mitochondrial targeting presequences are recognized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iwata, S -- Lee, J W -- Okada, K -- Lee, J K -- Iwata, M -- Rasmussen, B -- Link, T A -- Ramaswamy, S -- Jap, B K -- New York, N.Y. -- Science. 1998 Jul 3;281(5373):64-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720, USA. iwata@xray.bmc.uu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9651245" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cattle ; Crystallization ; Crystallography, X-Ray ; Cytochrome b Group/chemistry/metabolism ; Cytochromes c1/chemistry/metabolism ; Electron Transport ; Electron Transport Complex III/*chemistry/metabolism ; Enzyme Inhibitors/metabolism ; Hydrogen Bonding ; Hydroquinones/metabolism ; Intracellular Membranes/enzymology ; Iron-Sulfur Proteins/chemistry/metabolism ; Methacrylates ; Mitochondria, Heart/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; *Protein Conformation ; Protein Structure, Secondary ; Thiazoles/metabolism
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  • 224
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    A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-25
    Description: The entry of primate immunodeficiency viruses into target cells depends on a sequential interaction of the gp120 envelope glycoprotein with the cellular receptors, CD4 and members of the chemokine receptor family. The gp120 third variable (V3) loop has been implicated in chemokine receptor binding, but the use of the CCR5 chemokine receptor by diverse primate immunodeficiency viruses suggests the involvement of an additional, conserved gp120 element. Through the use of gp120 mutants, a highly conserved gp120 structure was shown to be critical for CCR5 binding. This structure is located adjacent to the V3 loop and contains neutralization epitopes induced by CD4 binding. This conserved element may be a useful target for pharmacologic or prophylactic intervention in human immunodeficiency virus (HIV) infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rizzuto, C D -- Wyatt, R -- Hernandez-Ramos, N -- Sun, Y -- Kwong, P D -- Hendrickson, W A -- Sodroski, J -- AI 40895/AI/NIAID NIH HHS/ -- AI 41851/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1949-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9632396" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Antigens, CD4/metabolism ; Binding Sites ; Crystallization ; HIV Antibodies/immunology ; HIV Envelope Protein gp120/*chemistry/genetics/immunology/*metabolism ; HIV-1/*chemistry/immunology ; Humans ; Models, Molecular ; Peptide Fragments/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Receptors, CCR5/*metabolism ; Recombinant Proteins/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 225
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    The tetrameric structure of a glutamate receptor channel (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: The subunit stoichiometry of several ligand-gated ion channel receptors is still unknown. A counting method was developed to determine the number of subunits in one family of brain glutamate receptors. Successful application of this method in an HEK cell line provides evidence that ionotropic glutamate receptors share a tetrameric structure with the voltage-gated potassium channels. The average conductance of these channels depends on how many subunits are occupied by an agonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenmund, C -- Stern-Bach, Y -- Stevens, C F -- NS 12961/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Workgroup Cellular Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616121" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cell Line ; Electric Conductivity ; Excitatory Amino Acid Agonists/metabolism ; Excitatory Amino Acid Antagonists/metabolism ; Humans ; Ligands ; Macromolecular Substances ; Models, Biological ; Patch-Clamp Techniques ; Quinoxalines/metabolism ; Quisqualic Acid/metabolism ; Receptors, AMPA/agonists/antagonists & inhibitors/*chemistry/*metabolism ; Receptors, Glutamate/chemistry/metabolism ; Receptors, Kainic Acid/agonists/antagonists & inhibitors/*chemistry/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism
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    Chain reactions linking acorns to gypsy moth outbreaks and Lyme disease risk (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: In eastern U.S. oak forests, defoliation by gypsy moths and the risk of Lyme disease are determined by interactions among acorns, white-footed mice, moths, deer, and ticks. Experimental removal of mice, which eat moth pupae, demonstrated that moth outbreaks are caused by reductions in mouse density that occur when there are no acorns. Experimental acorn addition increased mouse density. Acorn addition also increased densities of black-legged ticks, evidently by attracting deer, which are key tick hosts. Mice are primarily responsible for infecting ticks with the Lyme disease agent. The results have important implications for predicting and managing forest health and human health.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, C G -- Ostfeld, R S -- Richard, M P -- Schauber, E M -- Wolff, J O -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1023-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Ecosystem Studies (IES), Post Office Box AB, Millbrook, NY 12545, USA. clivegjones@compuserve.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachnid Vectors/growth & development/microbiology/physiology ; Borrelia burgdorferi Group/physiology ; *Disease Reservoirs ; *Ecosystem ; Forestry ; Humans ; Ixodes/growth & development/microbiology/*physiology ; Larva/microbiology/physiology ; Lyme Disease/*epidemiology/transmission ; Metamorphosis, Biological ; Moths/*physiology ; Peromyscus/microbiology/*parasitology/physiology ; Population Dynamics ; Pupa/physiology ; Risk Factors ; *Trees
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    Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: The preferred antitubercular drug isoniazid specifically targets a long-chain enoyl-acyl carrier protein reductase (InhA), an enzyme essential for mycolic acid biosynthesis in Mycobacterium tuberculosis. Despite the widespread use of this drug for more than 40 years, its precise mode of action has remained obscure. Data from x-ray crystallography and mass spectrometry reveal that the mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of InhA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rozwarski, D A -- Grant, G A -- Barton, D H -- Jacobs, W R Jr -- Sacchettini, J C -- AI-36849/AI/NIAID NIH HHS/ -- GM-45859/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):98-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417034" target="_blank"〉PubMed〈/a〉
    Keywords: Antitubercular Agents/metabolism/*pharmacology ; Bacterial Proteins ; Binding Sites ; Biotransformation ; Crystallography, X-Ray ; Drug Resistance, Microbial ; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) ; Fatty Acid Synthases/antagonists & inhibitors/chemistry/genetics/metabolism ; Isoniazid/metabolism/*pharmacology ; Mass Spectrometry ; Models, Molecular ; Mutation ; Mycobacterium tuberculosis/*drug effects/enzymology ; Mycolic Acids/metabolism ; NAD/chemistry/*metabolism ; Oxidoreductases/*antagonists & inhibitors/chemistry/genetics/metabolism
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  • 228
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    Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: Syntaxins are thought to function during vesicular transport as receptors on the target membrane and to contribute to the specificity of membrane docking and fusion by interacting with vesicle-associated receptors. Here, syntaxin 5 (Syn5) was shown to be an integral component of endoplasmic reticulum-derived transport vesicles. This pool, but not the target, Golgi-associated Syn5 pool, was essential for the assembly of vesicular-tubular pre-Golgi intermediates and the delivery of cargo to the Golgi. The requirement for vesicle-associated Syn5 in transport suggests a reevaluation of the basis for operation of the early secretory pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowe, T -- Dascher, C -- Bannykh, S -- Plutner, H -- Balch, W E -- CA58689/CA/NCI NIH HHS/ -- GM 42336/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):696-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445473" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Antibodies ; Biological Transport ; Carrier Proteins/metabolism ; Cell Line ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/*metabolism/ultrastructure ; Mannose-Binding Lectins ; Membrane Fusion ; *Membrane Glycoproteins ; Membrane Proteins/immunology/*metabolism ; N-Ethylmaleimide-Sensitive Proteins ; Organelles/metabolism ; Qa-SNARE Proteins ; Qb-SNARE Proteins ; Qc-SNARE Proteins ; R-SNARE Proteins ; Rats ; SNARE Proteins ; *Vesicular Transport Proteins ; Vesicular stomatitis Indiana virus/physiology ; Viral Envelope Proteins/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 229
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    Natural ligand of mouse CD1d1: cellular glycosylphosphatidylinositol (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: Mouse CD1d1, a member of the CD1 family of evolutionarily conserved major histocompatibility antigen-like molecules, controls the differentiation and function of a T lymphocyte subset, NK1+ natural T cells, proposed to regulate immune responses. The CD1d1 crystal structure revealed a large hydrophobic binding site occupied by a ligand of unknown chemical nature. Mass spectrometry and metabolic radiolabeling were used to identify cellular glycosylphosphatidylinositol as a major natural ligand of CD1d1. CD1d1 bound glycosylphosphatidylinositol through its phosphatidylinositol aspect with high affinity. Glycosylphosphatidylinositol or another glycolipid could be a candidate natural ligand for CD1d1-restricted T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joyce, S -- Woods, A S -- Yewdell, J W -- Bennink, J R -- De Silva, A D -- Boesteanu, A -- Balk, S P -- Cotter, R J -- Brutkiewicz, R R -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1541-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, Milton S. Hershey Medical Center, Hershey, PA 17033-0850, USA. sjoyce@bcmic.hmc.psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9488653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD1/chemistry/isolation & purification/*metabolism ; Binding Sites ; Glycosylphosphatidylinositols/chemistry/*metabolism ; Ligands ; Mass Spectrometry ; Mice ; Solubility ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; T-Lymphocyte Subsets/immunology
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  • 230
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    A marine natural product inhibitor of kinesin motors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-02
    Description: Members of the kinesin superfamily of motor proteins are essential for mitotic and meiotic spindle organization, chromosome segregation, organelle and vesicle transport, and many other processes that require microtubule-based transport. A compound, adociasulfate-2, was isolated from a marine sponge, Haliclona (also known as Adocia) species, that inhibited kinesin activity by targeting its motor domain and mimicking the activity of the microtubule. Thus, the kinesin-microtubule interaction site could be a useful target for small molecule modulators, and adociasulfate-2 should serve as an archetype for specific inhibitors of kinesin functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sakowicz, R -- Berdelis, M S -- Ray, K -- Blackburn, C L -- Hopmann, C -- Faulkner, D J -- Goldstein, L S -- New York, N.Y. -- Science. 1998 Apr 10;280(5361):292-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Division of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0683, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9535660" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/antagonists & inhibitors ; Adenosine Triphosphate/metabolism ; Animals ; Binding Sites ; Cell Division/drug effects ; Drosophila/embryology ; Enzyme Inhibitors/chemistry/*isolation & purification/*pharmacology ; HeLa Cells ; Humans ; Kinesin/*antagonists & inhibitors/metabolism ; Kinetics ; Microtubules/*metabolism ; Mitosis/drug effects ; Porifera/*chemistry ; Sulfuric Acid Esters/chemistry/*isolation & purification/*pharmacology
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  • 231
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    Discrete start sites for DNA synthesis in the yeast ARS1 origin (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: Sites of DNA synthesis initiation have been detected at the nucleotide level in a yeast origin of bidirectional replication with the use of replication initiation point mapping. The ARS1 origin of Saccharomyces cerevisiae showed a transition from discontinuous to continuous DNA synthesis in an 18-base pair region (nucleotides 828 to 845) from within element B1 toward B2, adjacent to the binding site for the origin recognition complex, the putative initiator protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bielinsky, A K -- Gerbi, S A -- GM 35929/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cell Biology and Biochemistry, Division of Biology and Medicine, Brown University, Providence, RI 02912, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417033" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; DNA Helicases/metabolism ; DNA Primers ; *DNA Replication ; DNA, Fungal/*biosynthesis ; *DNA-Binding Proteins ; Molecular Sequence Data ; *Replication Origin ; Saccharomyces cerevisiae/*metabolism ; Trans-Activators/metabolism
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    Attenuation of virulence by disruption of the Mycobacterium tuberculosis erp gene (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: The virulence of the mycobacteria that cause tuberculosis depends on their ability to multiply in mammalian hosts. Disruption of the bacterial erp gene, which encodes the exported repetitive protein, impaired multiplication of M. tuberculosis and M. bovis Bacille Calmette-Guerin in cultured macrophages and mice. Reintroduction of erp into the mutants restored their ability to multiply. These results indicate that erp contributes to the virulence of M. tuberculosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berthet, F X -- Lagranderie, M -- Gounon, P -- Laurent-Winter, C -- Ensergueix, D -- Chavarot, P -- Thouron, F -- Maranghi, E -- Pelicic, V -- Portnoi, D -- Marchal, G -- Gicquel, B -- AI 35207/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):759-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite de Genetique Mycobacterienne, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784137" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BCG Vaccine ; Bacterial Proteins/analysis/genetics/*physiology ; Cell Line ; Genes, Bacterial ; Genetic Complementation Test ; Immunohistochemistry ; Lung/microbiology ; Macrophages/microbiology ; Membrane Proteins/analysis/genetics/*physiology ; Mice ; Mice, Inbred BALB C ; Mutation ; Mycobacterium bovis/genetics/growth & development ; Mycobacterium tuberculosis/genetics/growth & ; development/metabolism/*pathogenicity ; Phagosomes/microbiology ; Recombinant Fusion Proteins ; Tuberculosis/microbiology ; Vaccines, Attenuated ; Virulence/genetics
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  • 233
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    Biotic transitions in global marine diversity (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-26
    Description: Long-term transitions in the composition of Earth's marine biota during the Phanerozoic have historically been explained in two different ways. One view is that they were mediated through biotic interactions among organisms played out over geologic time. The other is that mass extinctions transcended any such interactions and governed diversity over the long term by resetting the relative diversities of higher taxa. However, a growing body of evidence suggests that macroevolutionary processes effecting biotic transitions during background times were not fundamentally different from those operating during mass extinctions. Physical perturbations at many geographic scales combined to produce the long-term trajectory of Phanerozoic diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, A I -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1157-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology, University of Cincinnati, OH 45221-0013, USA. arnold.miller@uc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9716540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Earth (Planet) ; *Ecosystem ; Fossils ; Marine Biology/*classification/statistics & numerical data ; Paleontology/*classification/statistics & numerical data
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    Of mice and moths--and Lyme disease? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, J -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):984-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9490486" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachnid Vectors/microbiology/physiology ; Borrelia burgdorferi Group/physiology ; Disease Reservoirs ; *Ecosystem ; Ixodes/microbiology/*physiology ; Lyme Disease/*epidemiology/transmission ; Moths/*physiology ; New York/epidemiology ; Peromyscus/parasitology/*physiology ; Population Dynamics ; Pupa/physiology ; Risk Factors ; *Trees
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 235
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    Glutamate receptor activation: a four-step program (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, C -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1547-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02254-9100, USA. cmiller@brandeis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9644020" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Electric Conductivity ; Excitatory Amino Acid Agonists/metabolism ; Excitatory Amino Acid Antagonists/metabolism ; Macromolecular Substances ; Patch-Clamp Techniques ; Receptors, Glutamate/*chemistry/*metabolism
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  • 236
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    MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-11
    Description: Signal transduction is controlled both by regulation of enzyme activation and by organization of enzymatic complexes with nonenzymatic adapters, scaffolds, and anchor proteins. The extracellular signal-regulated kinase (ERK) cascade is one of several evolutionarily conserved mitogen-activated protein (MAP) kinase cascades important in the regulation of growth, apoptosis, and differentiation. A two-hybrid screen was conducted to identify nonenzymatic components of this signaling cascade that might be important in regulating its activity. A protein called MP1 (MEK Partner 1) was identified that bound specifically to MEK1 and ERK1 and facilitated their activation. When overexpressed in cultured cells, MP1 enhanced activation of ERK1 and activation of a reporter driven by the transcription factor Elk-1. Expression of MP1 in cells increased binding of ERK1 to MEK1. MP1 apparently functions as an adapter to enhance the efficiency of the MAP kinase cascade.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaeffer, H J -- Catling, A D -- Eblen, S T -- Collier, L S -- Krauss, A -- Weber, M J -- CA39076/CA/NCI NIH HHS/ -- GM47332/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1668-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Cancer Center, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733512" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Carrier Proteins/*metabolism ; Cell Line ; *DNA-Binding Proteins ; Enzyme Activation ; MAP Kinase Kinase 1 ; MAP Kinase Kinase 2 ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-raf/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; *Transcription Factors ; Transcriptional Activation ; Transfection ; ets-Domain Protein Elk-1
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  • 237
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    Aspirin-like molecules that covalently inactivate cyclooxygenase-2 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Many of aspirin's therapeutic effects arise from its acetylation of cyclooxygenase-2 (COX-2), whereas its antithrombotic and ulcerogenic effects result from its acetylation of COX-1. Here, aspirin-like molecules were designed that preferentially acetylate and irreversibly inactivate COX-2. The most potent of these compounds was o-(acetoxyphenyl)hept-2-ynyl sulfide (APHS). Relative to aspirin, APHS was 60 times as reactive against COX-2 and 100 times as selective for its inhibition; it also inhibited COX-2 in cultured macrophages and colon cancer cells and in the rat air pouch in vivo. Such compounds may lead to the development of aspirin-like drugs for the treatment or prevention of immunological and proliferative diseases without gastrointestinal or hematologic side effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalgutkar, A S -- Crews, B C -- Rowlinson, S W -- Garner, C -- Seibert, K -- Marnett, L J -- CA47479/CA/NCI NIH HHS/ -- CA68485/CA/NCI NIH HHS/ -- ES00267/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1998 May 22;280(5367):1268-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉A.B. Hancock Jr. Memorial Laboratory for Cancer Research, Vanderbilt Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596581" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetylene/*analogs & derivatives/chemical synthesis/chemistry/pharmacology ; Alkynes ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/*chemical ; synthesis/chemistry/pharmacology ; Aspirin/chemistry/pharmacology ; Binding Sites ; Cell Division/drug effects ; Cell Line ; Colonic Neoplasms/enzymology/pathology ; Cyclooxygenase 2 ; Cyclooxygenase 2 Inhibitors ; Cyclooxygenase Inhibitors/*chemical synthesis/chemistry/pharmacology ; Dinoprostone/biosynthesis ; Drug Design ; Humans ; Indomethacin/pharmacology ; Isoenzymes/chemistry/genetics/*metabolism ; Macrophages/enzymology ; Membrane Proteins ; Mutagenesis, Site-Directed ; Prostaglandin D2/biosynthesis ; Prostaglandin-Endoperoxide Synthases/chemistry/genetics/*metabolism ; Rats ; Rats, Inbred Lew ; Sulfides/*chemical synthesis/chemistry/pharmacology ; Thromboxane B2/biosynthesis ; Tumor Cells, Cultured
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    Harnessing the biosynthetic code: combinations, permutations, and mutations (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-02
    Description: Polyketides and non-ribosomal peptides are two large families of complex natural products that are built from simple carboxylic acid or amino acid monomers, respectively, and that have important medicinal or agrochemical properties. Despite the substantial differences between these two classes of natural products, each is synthesized biologically under the control of exceptionally large, multifunctional proteins termed polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs) that contain repeated, coordinated groups of active sites called modules, in which each module is responsible for catalysis of one complete cycle of polyketide or polypeptide chain elongation and associated functional group modifications. It has recently become possible to use molecular genetic methodology to alter the number, content, and order of such modules and, in so doing, to alter rationally the structure of the resultant products. This review considers the promise and challenges inherent in the combinatorial manipulation of PKS and NRPS structure in order to generate entirely "unnatural" products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cane, D E -- Walsh, C T -- Khosla, C -- CA66736/CA/NCI NIH HHS/ -- GM20011/GM/NIGMS NIH HHS/ -- GM22172/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):63-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Box H, Brown University, Providence, RI 02912-9108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9756477" target="_blank"〉PubMed〈/a〉
    Keywords: Apoenzymes/metabolism ; Binding Sites ; Multienzyme Complexes/chemistry/genetics/*metabolism ; *Peptide Biosynthesis ; Peptide Synthases/chemistry/genetics/*metabolism ; Peptides/chemistry ; *Protein Engineering
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Extension of life-span by introduction of telomerase into normal human cells (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: Normal human cells undergo a finite number of cell divisions and ultimately enter a nondividing state called replicative senescence. It has been proposed that telomere shortening is the molecular clock that triggers senescence. To test this hypothesis, two telomerase-negative normal human cell types, retinal pigment epithelial cells and foreskin fibroblasts, were transfected with vectors encoding the human telomerase catalytic subunit. In contrast to telomerase-negative control clones, which exhibited telomere shortening and senescence, telomerase-expressing clones had elongated telomeres, divided vigorously, and showed reduced straining for beta-galactosidase, a biomarker for senescence. Notably, the telomerase-expressing clones have a normal karyotype and have already exceeded their normal life-span by at least 20 doublings, thus establishing a causal relationship between telomere shortening and in vitro cellular senescence. The ability to maintain normal human cells in a phenotypically youthful state could have important applications in research and medicine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bodnar, A G -- Ouellette, M -- Frolkis, M -- Holt, S E -- Chiu, C P -- Morin, G B -- Harley, C B -- Shay, J W -- Lichtsteiner, S -- Wright, W E -- AG05747/AG/NIA NIH HHS/ -- AG07992/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geron Corporation, Menlo Park, CA 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454332" target="_blank"〉PubMed〈/a〉
    Keywords: Biomarkers ; Catalysis ; *Cell Aging ; *Cell Division ; Cell Line ; Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA-Binding Proteins ; Fibroblasts/cytology ; Homeostasis ; Humans ; Karyotyping ; Phenotype ; Pigment Epithelium of Eye/cytology ; Proteins/genetics/*metabolism ; *Rna ; RNA-Directed DNA Polymerase/genetics/metabolism ; Stem Cells/cytology/enzymology ; Telomerase/genetics/*metabolism ; Telomere/metabolism/*physiology/ultrastructure ; Transfection ; Tumor Cells, Cultured ; beta-Galactosidase/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: Myotonic dystrophy (DM) is caused by a CTG expansion in the 3' untranslated region of the DM gene. One model of DM pathogenesis suggests that RNAs from the expanded allele create a gain-of-function mutation by the inappropriate binding of proteins to the CUG repeats. Data presented here indicate that the conserved heterogeneous nuclear ribonucleoprotein, CUG-binding protein (CUG-BP), may mediate the trans-dominant effect of the RNA. CUG-BP was found to bind to the human cardiac troponin T (cTNT) pre-messenger RNA and regulate its alternative splicing. Splicing of cTNT was disrupted in DM striated muscle and in normal cells expressing transcripts that contain CUG repeats. Altered expression of genes regulated posttranscriptionally by CUG-BP therefore may contribute to DM pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philips, A V -- Timchenko, L T -- Cooper, T A -- AR 44387/AR/NIAMS NIH HHS/ -- HL45565/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 May 1;280(5364):737-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563950" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; CELF1 Protein ; Cell Line ; Cell Nucleus/metabolism ; Exons ; Humans ; Introns ; Muscle, Skeletal/cytology/embryology/metabolism ; Mutation ; Myotonic Dystrophy/*genetics/metabolism ; Myotonin-Protein Kinase ; Phosphorylation ; Protein-Serine-Threonine Kinases/*genetics ; RNA Precursors/metabolism ; RNA, Messenger/*genetics/metabolism ; RNA-Binding Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Ribonucleoproteins/genetics/*metabolism ; Transcription, Genetic ; Transfection ; *Trinucleotide Repeats ; Troponin/genetics ; Troponin T
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    Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: Eps15 homology (EH) domains are eukaryotic signaling modules that recognize proteins containing Asn-Pro-Phe (NPF) sequences. The structure of the central EH domain of Eps15 has been solved by heteronuclear magnetic resonance spectroscopy. The fold consists of a pair of EF hand motifs, the second of which binds tightly to calcium. The NPF peptide is bound in a hydrophobic pocket between two alpha helices, and binding is mediated by a critical aromatic interaction as revealed by structure-based mutagenesis. The fold is predicted to be highly conserved among 30 identified EH domains and provides a structural basis for defining EH-mediated events in protein trafficking and growth factor signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Beer, T -- Carter, R E -- Lobel-Rice, K E -- Sorkin, A -- Overduin, M -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1357-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, CO 80262, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721102" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/metabolism ; Calcium-Binding Proteins/*chemistry/metabolism ; Helix-Loop-Helix Motifs ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Oligopeptides/chemistry/*metabolism ; Phosphoproteins/*chemistry/metabolism ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Signal Transduction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Segregation of transcription and replication sites into higher order domains (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-04
    Description: Microscopy shows that individual sites of DNA replication and transcription of mammalian nuclei segregate into sets of roughly 22 and 16 higher order domains, respectively. Each domain set displayed a distinct network-like appearance, including regions of individual domains and interdigitation of domains between the two networks. These data support a dynamic mosaic model for the higher order arrangement of genomic function inside the cell nuclei.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wei, X -- Samarabandu, J -- Devdhar, R S -- Siegel, A J -- Acharya, R -- Berezney, R -- GM 23922/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1502-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9727975" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Cell Line ; Cell Nucleolus/metabolism/ultrastructure ; Cell Nucleus/*metabolism/ultrastructure ; *DNA Replication ; *Genome ; Genome, Human ; Humans ; Image Processing, Computer-Assisted ; Mice ; Microscopy, Confocal ; Models, Biological ; S Phase ; *Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Inhibition of the hammerhead ribozyme cleavage reaction by site-specific binding of Tb (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: Terbium(III) [Tb(III)] was shown to inhibit the hammerhead ribozyme by competing with a single magnesium(II) ion. X-ray crystallography revealed that the Tb(III) ion binds to a site adjacent to an essential guanosine in the catalytic core of the ribozyme, approximately 10 angstroms from the cleavage site. Synthetic modifications near this binding site yielded an RNA substrate that was resistant to Tb(III) binding and capable of being cleaved, even in the presence of up to 20 micromolar Tb(III). It is suggested that the magnesium(II) ion thought to bind at this site may act as a switch, affecting the conformational changes required to achieve the transition state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feig, A L -- Scott, W G -- Uhlenbeck, O C -- GM-36944/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):81-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417029" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Binding, Competitive ; Catalysis ; Crystallography, X-Ray ; Magnesium/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; RNA, Catalytic/*antagonists & inhibitors/chemistry/*metabolism ; Terbium/*metabolism/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Lyme disease and the passenger pigeon? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blockstein, D E -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1831,1833.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9537894" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Columbidae ; *Ecosystem ; Feeding Behavior ; Lyme Disease/*epidemiology ; Peromyscus ; Population Dynamics ; *Trees
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    Visualization of single RNA transcripts in situ (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: Fluorescence in situ hybridization (FISH) and digital imaging microscopy were modified to allow detection of single RNA molecules. Oligodeoxynucleotide probes were synthesized with five fluorochromes per molecule, and the light emitted by a single probe was calibrated. Points of light in exhaustively deconvolved images of hybridized cells gave fluorescent intensities and distances between probes consistent with single messenger RNA molecules. Analysis of beta-actin transcription sites after serum induction revealed synchronous and cyclical transcription from single genes. The rates of transcription initiation and termination and messenger RNA processing could be determined by positioning probes along the transcription unit. This approach extends the power of FISH to yield quantitative molecular information on a single cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Femino, A M -- Fay, F S -- Fogarty, K -- Singer, R H -- GM 54887/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Apr 24;280(5363):585-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Structural Biology and Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9554849" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Animals ; Cell Line ; Fluorescein-5-isothiocyanate ; *In Situ Hybridization, Fluorescence ; Kinetics ; Oligonucleotide Probes ; RNA Processing, Post-Transcriptional ; RNA, Messenger/*analysis/*genetics/metabolism ; Rats ; *Transcription, Genetic
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    A viral mechanism for inhibition of the cellular phosphatase calcineurin (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-24
    Description: The transcription factor NFAT (nuclear factor of activated T cells) controls the expression of many immunomodulatory proteins. African swine fever virus inhibits proinflammatory cytokine expression in infected macrophages, and a viral protein A238L was found to display the activity of the immunosuppressive drug cyclosporin A by inhibiting NFAT-regulated gene transcription in vivo. This it does by binding the catalytic subunit of calcineurin and inhibiting calcineurin phosphatase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miskin, J E -- Abrams, C C -- Goatley, L C -- Dixon, L K -- New York, N.Y. -- Science. 1998 Jul 24;281(5376):562-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Animal Health, Pirbright Laboratory, Pirbright, Surrey, GU24 0NF, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9677199" target="_blank"〉PubMed〈/a〉
    Keywords: African Swine Fever Virus/*physiology ; Amino Acid Sequence ; Animals ; Binding Sites ; Calcineurin/metabolism ; *Calcineurin Inhibitors ; Cell Nucleus/metabolism ; Cells, Cultured ; Cercopithecus aethiops ; Cyclosporine/pharmacology ; DNA-Binding Proteins/genetics/*metabolism ; Genes, Reporter ; Macrophages, Alveolar/*virology ; Molecular Sequence Data ; NF-kappa B/metabolism ; NFATC Transcription Factors ; *Nuclear Proteins ; Recombinant Proteins/metabolism ; Swine ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic ; Vero Cells ; Viral Proteins/genetics/*metabolism
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    Bifurcation of lipid and protein kinase signals of PI3Kgamma to the protein kinases PKB and MAPK (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-09
    Description: Phosphoinositide 3-kinases (PI3Ks) activate protein kinase PKB (also termed Akt), and PI3Kgamma activated by heterotrimeric guanosine triphosphate-binding protein can stimulate mitogen-activated protein kinase (MAPK). Exchange of a putative lipid substrate-binding site generated PI3Kgamma proteins with altered or aborted lipid but retained protein kinase activity. Transiently expressed, PI3Kgamma hybrids exhibited wortmannin-sensitive activation of MAPK, whereas a catalytically inactive PI3Kgamma did not. Membrane-targeted PI3Kgamma constitutively produced phosphatidylinositol 3,4, 3,4,5-trisphosphate and activated PKB but not MAPK. Moreover, stimulation of MAPK in response to lysophosphatidic acid was blocked by catalytically inactive PI3Kgamma but not by hybrid PI3Kgammas. Thus, two major signals emerge from PI3Kgamma: phosphoinositides that target PKB and protein phosphorylation that activates MAPK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bondeva, T -- Pirola, L -- Bulgarelli-Leva, G -- Rubio, I -- Wetzker, R -- Wymann, M P -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):293-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Unit "Molecular Cell Biology," University of Jena, D-07747 Jena, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9765155" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Androstadienes/pharmacology ; Animals ; Binding Sites ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Membrane/enzymology ; Cercopithecus aethiops ; Enzyme Activation ; Lysophospholipids/pharmacology ; MAP Kinase Kinase 1 ; Mitogen-Activated Protein Kinase 1 ; *Mitogen-Activated Protein Kinase Kinases ; Molecular Sequence Data ; Myelin Basic Protein/metabolism ; Phosphatidylinositol 3-Kinases/genetics/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Recombinant Proteins/metabolism ; Signal Transduction ; Transfection
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    Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energy-transducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms, respectively. FhuA is a beta barrel composed of 22 antiparallel beta strands. In contrast to the typical trimeric arrangement found in porins, FhuA is monomeric. Located within the beta barrel is a structurally distinct domain, the "cork," which mainly consists of a four-stranded beta sheet and four short alpha helices. A single lipopolysaccharide molecule is noncovalently associated with the membrane-embedded region of the protein. Upon binding of ferrichrome-iron, conformational changes are transduced to the periplasmic pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence homologies and mutagenesis data are used to propose a structural mechanism for TonB-dependent siderophore-mediated transport across the outer membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, A D -- Hofmann, E -- Coulton, J W -- Diederichs, K -- Welte, W -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2215-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec, Canada H3A 2B4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856937" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Biological Transport, Active ; Cell Membrane/chemistry/metabolism ; Crystallography, X-Ray ; Diffusion ; Escherichia coli/*chemistry/metabolism ; *Escherichia coli Proteins ; Ferric Compounds/*metabolism ; Ferrichrome/*metabolism ; Hydrogen Bonding ; Ligands ; Lipopolysaccharides/*metabolism ; Membrane Proteins/chemistry/metabolism ; Models, Molecular ; *Protein Conformation ; Protein Structure, Secondary ; Receptors, Virus/*chemistry/metabolism ; Signal Transduction
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    Prototype of a heme chaperone essential for cytochrome c maturation (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-26
    Description: Heme, the iron-containing cofactor essential for the activity of many enzymes, is incorporated into its target proteins by unknown mechanisms. Here, an Escherichia coli hemoprotein, CcmE, was shown to bind heme in the bacterial periplasm by way of a single covalent bond to a histidine. The heme was then released and delivered to apocytochrome c. Thus, CcmE can be viewed as a heme chaperone guiding heme to its appropriate biological partner and preventing illegitimate complex formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulz, H -- Hennecke, H -- Thony-Meyer, L -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1197-200.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mikrobiologisches Institut, Eidgenossische Technische Hochschule, Schmelzbergstrasse 7, CH-8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9712585" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apoproteins/metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Cytochrome c Group/*metabolism ; Cytochromes c ; Escherichia coli/genetics/*metabolism ; Heme/*metabolism ; Histidine/metabolism ; Mass Spectrometry ; Membrane Proteins/chemistry/genetics/*metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism
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    Sieves in sequence (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fersht, A R -- New York, N.Y. -- Science. 1998 Apr 24;280(5363):541.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Centre for Protein Engineering, Cambridge CB2 1EW, UK. arf10@cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9575099" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Binding Sites ; Escherichia coli/enzymology ; Hydrolysis ; Isoleucine/chemistry/*metabolism ; Isoleucine-tRNA Ligase/*chemistry/metabolism ; Substrate Specificity ; Thermus thermophilus/enzymology ; Transfer RNA Aminoacylation ; Valine/chemistry/*metabolism
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    A family of cAMP-binding proteins that directly activate Rap1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: cAMP (3',5' cyclic adenosine monophosphate) is a second messenger that in eukaryotic cells induces physiological responses ranging from growth, differentiation, and gene expression to secretion and neurotransmission. Most of these effects have been attributed to the binding of cAMP to cAMP-dependent protein kinase A (PKA). Here, a family of cAMP-binding proteins that are differentially distributed in the mammalian brain and body organs and that exhibit both cAMP-binding and guanine nucleotide exchange factor (GEF) domains is reported. These cAMP-regulated GEFs (cAMP-GEFs) bind cAMP and selectively activate the Ras superfamily guanine nucleotide binding protein Rap1A in a cAMP-dependent but PKA-independent manner. Our findings suggest the need to reformulate concepts of cAMP-mediated signaling to include direct coupling to Ras superfamily signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawasaki, H -- Springett, G M -- Mochizuki, N -- Toki, S -- Nakaya, M -- Matsuda, M -- Housman, D E -- Graybiel, A M -- P01 CA42063/CA/NCI NIH HHS/ -- P01 HL41484/HL/NHLBI NIH HHS/ -- R01 HD28341/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2275-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology (MIT), Cambridge, MA, 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856955" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Adrenal Glands/metabolism ; Adult ; Amino Acid Sequence ; Animals ; Brain/metabolism ; Cell Line ; Colforsin/pharmacology ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Fetus/metabolism ; GTP-Binding Proteins/*metabolism ; Gene Expression ; Guanine Nucleotide Exchange Factors ; Humans ; In Situ Hybridization ; Molecular Sequence Data ; Phosphorylation ; Proteins/chemistry/genetics/*metabolism ; Rats ; Second Messenger Systems ; Sequence Deletion ; Signal Transduction ; rap GTP-Binding Proteins ; ras Guanine Nucleotide Exchange Factors
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    Ribozyme architectural diversity made visible (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westhof, E -- Michel, F -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):251-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie Moleculaire et Cellulaire du CNRS, Strasbourg, France. westhof@ibmc.u-strasbg.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841389" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Pairing ; Binding Sites ; Crystallography, X-Ray ; Hepatitis Delta Virus/*genetics ; Introns ; *Models, Molecular ; *Nucleic Acid Conformation ; RNA, Catalytic/*chemistry ; RNA, Protozoan/chemistry ; RNA, Viral/chemistry ; Tetrahymena/*genetics
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    Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: An oligomer of the Sec61 trimeric complex is thought to form the protein-conducting channel for protein transport across the endoplasmic reticulum. A purified yeast Sec61 complex bound to monomeric yeast ribosomes as an oligomer in a saturable fashion. Cryo-electron microscopy of the ribosome-Sec61 complex and a three-dimensional reconstruction showed that the Sec61 oligomer is attached to the large ribosomal subunit by a single connection. Moreover, a funnel-shaped pore in the Sec61 oligomer aligned with the exit of a tunnel traversing the large ribosomal subunit, strongly suggesting that both structures function together in the translocation of proteins across the endoplasmic reticulum membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckmann, R -- Bubeck, D -- Grassucci, R -- Penczek, P -- Verschoor, A -- Blobel, G -- Frank, J -- 1R01 GM29169/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 19;278(5346):2123-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Laboratory of Cell Biology, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. beckmar@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9405348" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Biological Transport ; Endoplasmic Reticulum, Rough/metabolism ; Fungal Proteins/chemistry/metabolism/ultrastructure ; Image Processing, Computer-Assisted ; Macromolecular Substances ; Membrane Proteins/chemistry/metabolism/*ultrastructure ; Membrane Transport Proteins ; Microscopy, Electron ; Ribosomes/chemistry/metabolism/*ultrastructure ; Saccharomyces cerevisiae/chemistry/ultrastructure ; Saccharomyces cerevisiae Proteins
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    NMR maps giant molecules as they fold and flutter (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1014-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381198" target="_blank"〉PubMed〈/a〉
    Keywords: Apoproteins/*chemistry ; Binding Sites ; Folic Acid/analogs & derivatives/metabolism ; Folic Acid Antagonists/metabolism ; Hydrogen-Ion Concentration ; *Magnetic Resonance Spectroscopy ; Models, Molecular ; Myoglobin/*chemistry ; *Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Tetrahydrofolate Dehydrogenase/*chemistry/metabolism
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    Mediation of Sonic hedgehog-induced expression of COUP-TFII by a protein phosphatase (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: A Sonic hedgehog (Shh) response element was identified in the chicken ovalbumin upstream promoter-transcription factor II (COUP-TFII) promoter that binds to a factor distinct from Gli, a gene known to mediate Shh signaling. Although this binding activity is specifically stimulated by Shh-N (amino-terminal signaling domain), it can also be unmasked with protein phosphatase treatment in the mouse cell line P19, and induction by Shh-N can be blocked by phosphatase inhibitors. Thus, Shh-N signaling may result in dephosphorylation of a target factor that is required for activation of COUP-TFII-, Islet1-, and Gli response element-dependent gene expression. This finding identifies another step in the Shh-N signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krishnan, V -- Pereira, F A -- Qiu, Y -- Chen, C H -- Beachy, P A -- Tsai, S Y -- Tsai, M J -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1947-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395397" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COUP Transcription Factor II ; COUP Transcription Factors ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/*genetics/metabolism ; Enzyme Inhibitors/pharmacology ; *Gene Expression Regulation ; Hedgehog Proteins ; Mice ; Okadaic Acid/pharmacology ; Oxazoles/pharmacology ; Phosphoprotein Phosphatases/antagonists & inhibitors/*metabolism ; Phosphorylation ; Promoter Regions, Genetic ; Proteins/*genetics/*metabolism ; *Receptors, Steroid ; Signal Transduction ; *Trans-Activators ; Transcription Factors/*genetics/metabolism
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    Life at the freezing point (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Psenner, R -- Sattler, B -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2073-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Zoology and Limnology, Innsbruck University, Austria. roland.psenner@uibk.ac.at〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669962" target="_blank"〉PubMed〈/a〉
    Keywords: Antarctic Regions ; Bacteria/*growth & development/metabolism ; Cyanobacteria/growth & development/metabolism ; *Ecosystem ; Exobiology ; Freezing ; Geologic Sediments/*microbiology ; *Ice ; Jupiter ; Mars ; Origin of Life ; *Water Microbiology
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    Progression to AIDS (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donfield, S M -- Lynn, H S -- Hilgartner, M W -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1819-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669928" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/genetics/*immunology ; CD4 Lymphocyte Count ; Cell Line ; Cohort Studies ; Disease Progression ; Genotype ; HIV Infections/genetics/*immunology ; HIV Seropositivity ; Humans ; Mutation ; Receptors, CCR2 ; Receptors, Chemokine/*genetics
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  • 258
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    Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-16
    Description: alpha-Dystroglycan (alpha-DG) is a component of the dystroglycan complex, which is involved in early development and morphogenesis and in the pathogenesis of muscular dystrophies. Here, alpha-DG was shown to serve as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy. Mycobacterium leprae specifically bound to alpha-DG only in the presence of the G domain of the alpha2 chain of laminin-2. Native alpha-DG competitively inhibited the laminin-2-mediated M. leprae binding to primary Schwann cells. Thus, M. leprae may use linkage between the extracellular matrix and cytoskeleton through laminin-2 and alpha-DG for its interaction with Schwann cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rambukkana, A -- Yamada, H -- Zanazzi, G -- Mathus, T -- Salzer, J L -- Yurchenco, P D -- Campbell, K P -- Fischetti, V A -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2076-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, NY 10021, USA. rambuka@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851927" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bacterial Adhesion ; Binding Sites ; Calcium/physiology ; Cell Line, Transformed ; Cells, Cultured ; Cytoskeletal Proteins/*metabolism/pharmacology ; Dystroglycans ; Edetic Acid/pharmacology ; Glycosylation ; Humans ; Laminin/chemistry/*metabolism ; Membrane Glycoproteins/*metabolism/pharmacology ; Mycobacterium leprae/*metabolism ; Peripheral Nerves/chemistry ; Rats ; Receptors, Laminin/metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/chemistry/metabolism ; Schwann Cells/metabolism/*microbiology
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    Botanical gardens cope with bioprospecting loophole (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dove, A -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1273.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735039" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Products ; *Drug Industry ; *Ecosystem ; Guidelines as Topic ; International Cooperation ; Ownership ; *Plants ; Plants, Medicinal
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    Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: Topoisomerases I promote the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. The crystal structures at 2.1 and 2.5 angstrom resolution of reconstituted human topoisomerase I comprising the core and carboxyl-terminal domains in covalent and noncovalent complexes with 22-base pair DNA duplexes reveal an enzyme that "clamps" around essentially B-form DNA. The core domain and the first eight residues of the carboxyl-terminal domain of the enzyme, including the active-site nucleophile tyrosine-723, share significant structural similarity with the bacteriophage family of DNA integrases. A binding mode for the anticancer drug camptothecin is proposed on the basis of chemical and biochemical information combined with these three-dimensional structures of topoisomerase I-DNA complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Redinbo, M R -- Stewart, L -- Kuhn, P -- Champoux, J J -- Hol, W G -- CA65656/CA/NCI NIH HHS/ -- GM49156/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1504-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomolecular Structure Center and Department of Biological Structure, Box 357742, School of Medicine, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9488644" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents, Phytogenic/metabolism/pharmacology ; Binding Sites ; Camptothecin/analogs & derivatives/metabolism/pharmacology ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Topoisomerases, Type I/*chemistry/genetics/metabolism ; *DNA-Binding Proteins ; Homeodomain Proteins/chemistry ; Host Cell Factor C1 ; Humans ; Hydrogen Bonding ; Integrases/chemistry ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Octamer Transcription Factor-1 ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Transcription Factors/chemistry ; Tyrosine/chemistry/metabolism
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    The structure of the potassium channel: molecular basis of K+ conduction and selectivity (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-29
    Description: The potassium channel from Streptomyces lividans is an integral membrane protein with sequence similarity to all known K+ channels, particularly in the pore region. X-ray analysis with data to 3.2 angstroms reveals that four identical subunits create an inverted teepee, or cone, cradling the selectivity filter of the pore in its outer end. The narrow selectivity filter is only 12 angstroms long, whereas the remainder of the pore is wider and lined with hydrophobic amino acids. A large water-filled cavity and helix dipoles are positioned so as to overcome electrostatic destabilization of an ion in the pore at the center of the bilayer. Main chain carbonyl oxygen atoms from the K+ channel signature sequence line the selectivity filter, which is held open by structural constraints to coordinate K+ ions but not smaller Na+ ions. The selectivity filter contains two K+ ions about 7.5 angstroms apart. This configuration promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter. The architecture of the pore establishes the physical principles underlying selective K+ conduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doyle, D A -- Morais Cabral, J -- Pfuetzner, R A -- Kuo, A -- Gulbis, J M -- Cohen, S L -- Chait, B T -- MacKinnon, R -- New York, N.Y. -- Science. 1998 Apr 3;280(5360):69-77.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology and Biophysics and the 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/9525859" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; Binding Sites ; Cesium/metabolism ; Crystallization ; Crystallography, X-Ray ; Fourier Analysis ; Hydrogen Bonding ; Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Potassium/*metabolism ; Potassium Channel Blockers ; Potassium Channels/*chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Rubidium/metabolism ; Scorpion Venoms/metabolism/pharmacology ; Sodium/metabolism ; Static Electricity ; Streptomyces/chemistry ; Tetraethylammonium/metabolism/pharmacology ; Water
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    Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-25
    Description: The proapoptotic Bax protein induces cell death by acting on mitochondria. Bax binds to the permeability transition pore complex (PTPC), a composite proteaceous channel that is involved in the regulation of mitochondrial membrane permeability. Immunodepletion of Bax from PTPC or purification of PTPC from Bax-deficient mice yielded a PTPC that could not permeabilize membranes in response to atractyloside, a proapoptotic ligand of the adenine nucleotide translocator (ANT). Bax and ANT coimmunoprecipitated and interacted in the yeast two-hybrid system. Ectopic expression of Bax induced cell death in wild-type but not in ANT-deficient yeast. Recombinant Bax and purified ANT, but neither of them alone, efficiently formed atractyloside-responsive channels in artificial membranes. Hence, the proapoptotic molecule Bax and the constitutive mitochondrial protein ANT cooperate within the PTPC to increase mitochondrial membrane permeability and to trigger cell death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marzo, I -- Brenner, C -- Zamzami, N -- Jurgensmeier, J M -- Susin, S A -- Vieira, H L -- Prevost, M C -- Xie, Z -- Matsuyama, S -- Reed, J C -- Kroemer, G -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):2027-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS, UPR 420, 19 rue Guy Moquet, F-94801 Villejuif, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748162" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Atractyloside/metabolism/pharmacology ; Binding Sites ; Bongkrekic Acid/metabolism/pharmacology ; Cyclosporine/pharmacology ; Dimerization ; HT29 Cells ; Humans ; Intracellular Membranes/physiology ; Liposomes ; Mice ; Mice, Inbred C57BL ; Mitochondria/*physiology ; Mitochondrial ADP, ATP Translocases/chemistry/*metabolism ; Permeability ; Proto-Oncogene Proteins/chemistry/genetics/*metabolism/pharmacology ; Proto-Oncogene Proteins c-bcl-2/pharmacology ; Rats ; Rats, Wistar ; Recombinant Proteins/pharmacology ; Saccharomyces cerevisiae/cytology/genetics ; Transfection ; bcl-2-Associated X Protein
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    Decoupled temporal patterns of evolution and ecology in two post-Paleozoic clades (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-07
    Description: Counts of taxonomic diversity are the prevailing standards for documenting large-scale patterns of evolution in the fossil record. However, the secular pattern of relative ecological importance between the bryozoan clades Cyclostomata and Cheilostomata is not reflected fully in compilations of generic diversity or within-fauna species richness, and the delayed ecological recovery of the Cheilostomata after the mass extinction at the Cretaceous-Tertiary boundary is missed entirely. These observations demonstrate that evolutionary success and ecological dominance can be decoupled and profoundly different, even over tens of millions of years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKinney, F K -- Lidgard, S -- Sepkoski, J J Jr -- Taylor, P D -- DEB 9306729/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):807-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology, Appalachian State University, Boone, NC 28608-2067, USA. mckinneyfk@appstate.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694648" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bryozoa/*classification/physiology ; Earth (Planet) ; *Ecosystem ; *Fossils ; Marine Biology ; *Paleontology
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    Inactivation of a serotonin-gated ion channel by a polypeptide toxin from marine snails (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-24
    Description: The venom of predatory marine snails is a rich source of natural products that act on specific receptors and ion channels within the mammalian nervous system. A 41-amino acid peptide, final sigma-conotoxin GVIIIA, was purified on the basis of its ability to inactivate the 5-HT3 receptor, an excitatory serotonin-gated ion channel. final sigma-Conotoxin contains a brominated tryptophan residue, which may be important for peptide activity because the endogenous ligand for the 5-HT3 receptor is a hydroxylated derivative of tryptophan. final sigma-Conotoxin inactivates the 5-HT3 receptor through competitive antagonism and is a highly selective inhibitor of this receptor. Serotonin receptors can now be included among the molecular targets of natural polypeptide neurotoxins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉England, L J -- Imperial, J -- Jacobsen, R -- Craig, A G -- Gulyas, J -- Akhtar, M -- Rivier, J -- Julius, D -- Olivera, B M -- GM44298/GM/NIGMS NIH HHS/ -- GM48677/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 24;281(5376):575-8.〈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/9677203" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; Benzamides/pharmacology ; Bicyclo Compounds, Heterocyclic/pharmacology ; Binding Sites ; Cell Line ; Cloning, Molecular ; *Conotoxins ; DNA, Complementary ; Ion Channel Gating ; Ion Channels/*antagonists & inhibitors ; Molecular Sequence Data ; Mollusk Venoms/chemistry/genetics/isolation & purification/*pharmacology ; Peptides, Cyclic/pharmacology ; Receptors, Serotonin/*metabolism ; Receptors, Serotonin, 5-HT3 ; Receptors, Serotonin, 5-HT4 ; Recombinant Fusion Proteins/antagonists & inhibitors/metabolism ; Recombinant Proteins/antagonists & inhibitors ; Serotonin/metabolism/pharmacology ; Serotonin Antagonists/chemistry/isolation & purification/*pharmacology ; Snails/*chemistry ; Tryptophan/analysis/metabolism
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    Catalytic galactose oxidase models: biomimetic Cu(II)-phenoxyl-radical reactivity (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: Biomimetic functional models of the mononuclear copper enzyme galactose oxidase are presented that catalytically oxidize benzylic and allylic alcohols to aldehydes with O2 under mild conditions. The mechanistic fidelity between the models and the natural system is pronounced. Modest structural mimicry proves sufficient to transfer an unusual ligand-based radical mechanism, previously unprecedented outside the protein matrix, to a simple chemical system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Y -- DuBois, J L -- Hedman, B -- Hodgson, K O -- Stack, T D -- GM50730/GM/NIGMS NIH HHS/ -- RR-01209/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):537-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438841" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohols/*metabolism ; Aldehydes/metabolism ; Binding Sites ; Catalysis ; Copper/metabolism ; Electron Spin Resonance Spectroscopy ; Free Radicals ; Galactose Oxidase/*chemistry/*metabolism ; Hydrogen Peroxide/metabolism ; *Models, Chemical ; Oxidation-Reduction ; Oxygen/metabolism ; Phenols/chemistry/*metabolism ; Spectrum Analysis
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  • 266
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    Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin was determined to a resolution of 2.3 angstroms. When P-site inhibitors were soaked into native crystals of the complex, the active site of adenylyl cyclase was located and structural elements important for substrate recognition and catalysis were identified. On the basis of these and other structures, a molecular mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tesmer, J J -- Sunahara, R K -- Gilman, A G -- Sprang, S R -- DK38828/DK/NIDDK NIH HHS/ -- DK46371/DK/NIDDK NIH HHS/ -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1907-16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235-9050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417641" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases/*chemistry/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalysis ; Colforsin/metabolism ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Enzyme Activation ; GTP-Binding Protein alpha Subunits, Gs/*chemistry/metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/*chemistry/metabolism ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    'Playing chicken' over gene markers (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 Dec 19;278(5346):2046-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9432713" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Chromosome Mapping ; Confidentiality ; *Databases, Factual ; *Databases, Nucleic Acid ; Federal Government ; Genetic Privacy ; *Genetic Research ; Genetic Techniques ; Genetic Variation ; Genome, Human ; *Human Genome Project/economics ; Humans ; *Information Dissemination ; Informed Consent ; National Institutes of Health (U.S.) ; Patents as Topic ; *Polymorphism, Genetic ; Research Support as Topic ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 268
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    Protein disulfide isomerase as a regulator of chloroplast translational activation (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: Light-regulated translation of chloroplast messenger RNAs (mRNAs) requires trans-acting factors that interact with the 5' untranslated region (UTR) of these mRNAs. Chloroplast polyadenylate-binding protein (cPABP) specifically binds to the 5'-UTR of the psbA mRNA and is essential for translation of this mRNA. A protein disulfide isomerase that is localized to the chloroplast and copurifies with cPABP was shown to modulate the binding of cPABP to the 5'-UTR of the psbA mRNA by reversibly changing the redox status of cPABP through redox potential or adenosine 5'-diphosphate-dependent phosphorylation. This mechanism allows for a simple reversible switch regulating gene expression in the chloroplast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, J -- Mayfield, S P -- GM54659/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1954-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and The Skaggs Institute for Chemical 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/9395399" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Catalysis ; Chlamydomonas reinhardtii/enzymology/*genetics/metabolism ; Chloroplasts/*genetics/metabolism ; Cloning, Molecular ; Dithiothreitol/pharmacology ; *Gene Expression Regulation ; Glutathione Disulfide/pharmacology ; Molecular Sequence Data ; Oxidation-Reduction ; Phosphorylation ; Photosynthetic Reaction Center Complex Proteins/genetics ; Photosystem II Protein Complex ; *Protein Biosynthesis ; Protein Disulfide-Isomerases/chemistry/genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid
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    Chemistry prize taps the energy of life (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):579.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381166" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Chemistry/history ; Denmark ; Great Britain ; History, 20th Century ; *Nobel Prize ; Protein Conformation ; *Proton-Translocating ATPases/chemistry/history/metabolism ; *Sodium-Potassium-Exchanging ATPase/history/metabolism ; United States
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    Biodiversity in a vial of sugar water (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):390.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381141" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; *Biological Evolution ; Carbohydrate Metabolism ; Culture Media ; *Ecosystem ; Escherichia coli/*physiology ; Glucose/metabolism ; Pseudomonas fluorescens/*physiology ; *Selection, Genetic
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    Pieces of the true grail: a G protein finds its target (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bourne, H R -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1898-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California Medical Center, San Francisco, CA 94143, USA. h_bourne@quickmail.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417637" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Adenylyl Cyclases/*chemistry/metabolism ; Binding Sites ; Catalysis ; Cell Membrane/chemistry ; Colforsin/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/biosynthesis/metabolism ; Cytoplasm/metabolism ; Dimerization ; GTP-Binding Protein alpha Subunits, Gi-Go/metabolism ; GTP-Binding Protein alpha Subunits, Gs/*chemistry/metabolism ; Guanosine Triphosphate/chemistry/metabolism ; Models, Molecular ; Protein Structure, Secondary
    Print ISSN: 0036-8075
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  • 272
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    Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: Nucleosomes, the nucleohistone subunits of chromatin, are present on transcribed eukaryotic genes but do not prevent transcription. It is shown here that the large yeast RNA polymerase III transcribes through a single nucleosome. This takes place through a direct internal nucleosome transfer in which histones never leave the DNA template. During this process, the polymerase pauses with a pronounced periodicity of 10 to 11 base pairs, which is consistent with restricted rotation in the DNA loop formed during transfer. Transcription through nucleosomes by the eukaryotic enzyme and by much smaller prokaryotic RNA polymerases thus shares many features, reflecting an important property of nucleosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Studitsky, V M -- Kassavetis, G A -- Geiduschek, E P -- Felsenfeld, G -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1960-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395401" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA/chemistry/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Histones/metabolism ; Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleosomes/genetics/*metabolism ; Promoter Regions, Genetic ; RNA Polymerase III/*metabolism ; Templates, Genetic ; *Transcription, Genetic
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    Perennial Antarctic lake ice: an oasis for life in a polar desert (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-26
    Description: The permanent ice covers of Antarctic lakes in the McMurdo Dry Valleys develop liquid water inclusions in response to solar heating of internal aeolian-derived sediments. The ice sediment particles serve as nutrient (inorganic and organic)-enriched microzones for the establishment of a physiologically and ecologically complex microbial consortium capable of contemporaneous photosynthesis, nitrogen fixation, and decomposition. The consortium is capable of physically and chemically establishing and modifying a relatively nutrient- and organic matter-enriched microbial "oasis" embedded in the lake ice cover.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Priscu, J C -- Fritsen, C H -- Adams, E E -- Giovannoni, S J -- Paerl, H W -- McKay, C P -- Doran, P T -- Gordon, D A -- Lanoil, B D -- Pinckney, J L -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2095-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Montana State University, Bozeman, MT 59717, USA. 59717, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9641910" target="_blank"〉PubMed〈/a〉
    Keywords: Antarctic Regions ; Bacteria/*growth & development/metabolism ; Carbon/metabolism ; Carbon Dioxide/metabolism ; Cyanobacteria/genetics/growth & development/metabolism ; *Ecosystem ; Exobiology ; Geologic Sediments/*microbiology ; *Ice ; Jupiter ; Mars ; Nitrogen Fixation ; Photosynthesis ; Phylogeny ; RNA, Bacterial/genetics ; RNA, Ribosomal, 16S/genetics ; *Water Microbiology
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  • 274
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    Crystal structure of the adenylyl cyclase activator Gsalpha (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: The crystal structure of Gsalpha, the heterotrimeric G protein alpha subunit that stimulates adenylyl cyclase, was determined at 2.5 A in a complex with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is the prototypic member of a family of GTP-binding proteins that regulate the activities of effectors in a hormone-dependent manner. Comparison of the structure of Gsalpha.GTPgammaS with that of Gialpha.GTPgammaS suggests that their effector specificity is primarily dictated by the shape of the binding surface formed by the switch II helix and the alpha3-beta5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein signaling to stimulate the GTPase activity of Gsalpha. The betagamma binding surface of Gsalpha is largely conserved in sequence and structure to that of Gialpha, whereas differences in the surface formed by the carboxyl-terminal helix and the alpha4-beta6 loop may mediate receptor specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sunahara, R K -- Tesmer, J J -- Gilman, A G -- Sprang, S R -- DK46371/DK/NIDDK NIH HHS/ -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1943-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235-9041, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395396" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/chemistry/*metabolism ; Amino Acid Sequence ; Binding Sites ; Conserved Sequence ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Enzyme Activation ; GTP Phosphohydrolases/metabolism ; GTP-Binding Protein alpha Subunits, Gi-Go/chemistry/metabolism ; GTP-Binding Protein alpha Subunits, Gs/*chemistry/metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/*chemistry/metabolism ; Guanosine Triphosphate/metabolism ; Hydrolysis ; Magnesium/metabolism ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Structure, Secondary ; Signal Transduction
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    Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: Anthrax lethal toxin, produced by the bacterium Bacillus anthracis, is the major cause of death in animals infected with anthrax. One component of this toxin, lethal factor (LF), is suspected to be a metalloprotease, but no physiological substrates have been identified. Here it is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 (MAPKK1 and MAPKK2) and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway. The identification of a cleavage site for LF may facilitate the development of LF inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duesbery, N S -- Webb, C P -- Leppla, S H -- Gordon, V M -- Klimpel, K R -- Copeland, T D -- Ahn, N G -- Oskarsson, M K -- Fukasawa, K -- Paull, K D -- Vande Woude, G F -- New York, N.Y. -- Science. 1998 May 1;280(5364):734-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Advanced BioScience Laboratories-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, Post Office Box B, Frederick, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563949" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Bacterial ; *Bacillus anthracis/enzymology ; Bacterial Toxins/metabolism/*toxicity ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Cell Line, Transformed ; Enzyme Activation ; Enzyme Inhibitors/toxicity ; Humans ; MAP Kinase Kinase 1 ; MAP Kinase Kinase 2 ; Metalloendopeptidases/metabolism/toxicity ; Mice ; *Mitogen-Activated Protein Kinase Kinases ; Myelin Basic Protein/metabolism ; Oocytes/physiology ; Phosphorylation ; Protein-Serine-Threonine Kinases/*antagonists & ; inhibitors/chemistry/genetics/metabolism ; Protein-Tyrosine Kinases/*antagonists & inhibitors/chemistry/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Deletion ; Signal Transduction ; Xenopus laevis
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    Linkage of ATM to cell cycle regulation by the Chk2 protein kinase (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-04
    Description: In response to DNA damage and replication blocks, cells prevent cell cycle progression through the control of critical cell cycle regulators. We identified Chk2, the mammalian homolog of the Saccharomyces cerevisiae Rad53 and Schizosaccharomyces pombe Cds1 protein kinases required for the DNA damage and replication checkpoints. Chk2 was rapidly phosphorylated and activated in response to replication blocks and DNA damage; the response to DNA damage occurred in an ataxia telangiectasia mutated (ATM)-dependent manner. In vitro, Chk2 phosphorylated Cdc25C on serine-216, a site known to be involved in negative regulation of Cdc25C. This is the same site phosphorylated by the protein kinase Chk1, which suggests that, in response to DNA damage and DNA replicational stress, Chk1 and Chk2 may phosphorylate Cdc25C to prevent entry into mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsuoka, S -- Huang, M -- Elledge, S J -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 4;282(5395):1893-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, 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/9836640" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ataxia Telangiectasia Mutated Proteins ; *Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Line ; Checkpoint Kinase 2 ; *DNA Damage ; *DNA Replication ; DNA-Binding Proteins ; Enzyme Activation ; Gamma Rays ; HeLa Cells ; Humans ; Models, Biological ; Molecular Sequence Data ; Phosphorylation ; *Protein Kinases ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/cytology/genetics/growth & development ; Tumor Suppressor Proteins ; Ultraviolet Rays ; *cdc25 Phosphatases
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    Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3beta (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: Control of stability of beta-catenin is central in the wnt signaling pathway. Here, the protein conductin was found to form a complex with both beta-catenin and the tumor suppressor gene product adenomatous polyposis coli (APC). Conductin induced beta-catenin degradation, whereas mutants of conductin that were deficient in complex formation stabilized beta-catenin. Fragments of APC that contained a conductin-binding domain also blocked beta-catenin degradation. Thus, conductin is a component of the multiprotein complex that directs beta-catenin to degradation and is located downstream of APC. In Xenopus embryos, conductin interfered with wnt-induced axis formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Behrens, J -- Jerchow, B A -- Wurtele, M -- Grimm, J -- Asbrand, C -- Wirtz, R -- Kuhl, M -- Wedlich, D -- Birchmeier, W -- New York, N.Y. -- Science. 1998 Apr 24;280(5363):596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Delbruck Center for Molecular Medicine, Robert-Rossle-Strasse 10, 13122 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9554852" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Amino Acid Sequence ; Animals ; Axin Protein ; Binding Sites ; Body Patterning ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cytoskeletal Proteins/chemistry/genetics/*metabolism ; Glycogen Synthase Kinase 3 ; Humans ; Mice ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Proteins/chemistry ; Proto-Oncogene Proteins/metabolism ; *Repressor Proteins ; Signal Transduction ; *Trans-Activators ; Tumor Cells, Cultured ; Xenopus/embryology ; Xenopus Proteins ; beta Catenin
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    Rapid identification of subtype-selective agonists of the somatostatin receptor through combinatorial chemistry (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: Nonpeptide agonists of each of the five somatostatin receptors were identified in combinatorial libraries constructed on the basis of molecular modeling of known peptide agonists. In vitro experiments using these selective compounds demonstrated the role of the somatostatin subtype-2 receptor in inhibition of glucagon release from mouse pancreatic alpha cells and the somatostatin subtype-5 receptor as a mediator of insulin secretion from pancreatic beta cells. Both receptors regulated growth hormone release from the rat anterior pituitary gland. The availability of high-affinity, subtype-selective agonists for each of the somatostatin receptors provides a direct approach to defining their physiological functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rohrer, S P -- Birzin, E T -- Mosley, R T -- Berk, S C -- Hutchins, S M -- Shen, D M -- Xiong, Y -- Hayes, E C -- Parmar, R M -- Foor, F -- Mitra, S W -- Degrado, S J -- Shu, M -- Klopp, J M -- Cai, S J -- Blake, A -- Chan, W W -- Pasternak, A -- Yang, L -- Patchett, A A -- Smith, R G -- Chapman, K T -- Schaeffer, J M -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):737-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biochemistry and Physiology, Merck Research Laboratories, Post Office Box 2000, Rahway, NJ 07065, USA. susanvrohrer@merck.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784130" target="_blank"〉PubMed〈/a〉
    Keywords: Amides/metabolism/*pharmacology ; Amino Acid Sequence ; Animals ; Cell Line ; Cells, Cultured ; Cricetinae ; Drug Design ; Glucagon/secretion ; Growth Hormone/secretion ; Insulin/secretion ; Islets of Langerhans/drug effects/secretion ; Ligands ; Membrane Proteins ; Mice ; Models, Chemical ; Molecular Sequence Data ; Pituitary Gland, Anterior/drug effects/metabolism ; Rats ; Receptors, Somatostatin/*agonists/physiology
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    Immunological origins of binding and catalysis in a Diels-Alderase antibody (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding interactions that control the relative geometries of the bound substrates and electronic distribution in the dienophile. A single somatic mutation, serine-91 of the light chain to valine, is largely responsible for the increase in affinity and catalytic activity of the affinity-matured antibody. Structural and functional studies of the germ-line precursor suggest that 39-A11 and related antibodies derive from a family of germ-line genes that have been selected throughout evolution for the ability of the encoded proteins to form a polyspecific combining site. Germ line-encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of structures, may help to expand the binding potential associated with the structural diversity of the primary antibody repertoire.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Romesberg, F E -- Spiller, B -- Schultz, P G -- Stevens, R C -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1929-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and the Department of Chemistry, University of California, Berkeley, CA 94720, USA. 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506942" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies/chemistry/genetics/immunology/metabolism ; Antibodies, Catalytic/*chemistry/genetics/immunology/*metabolism ; Antibody Affinity ; Antibody Specificity ; Binding Sites ; Binding Sites, Antibody ; Catalysis ; Chemistry, Organic ; Cloning, Molecular ; Crystallography, X-Ray ; Evolution, Molecular ; Germ-Line Mutation ; Haptens/immunology ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/immunology/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Organic Chemistry Phenomena ; Protein Conformation ; Recombinant Proteins/chemistry/metabolism
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    Auxin-dependent cell expansion mediated by overexpressed auxin-binding protein 1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-06
    Description: To test the hypothesis that auxin-binding protein 1 (ABP1) is a receptor controlling auxin-mediated plant cell expansion, ABP1 complementary DNAs were expressed in a controllable fashion in tobacco plants and constitutively in maize cell lines. Induction of Arabidopsis ABP1 expression in tobacco leaf strips resulted in an increased capacity for auxin-mediated cell expansion, whereas induction of ABP1 in intact plants resulted in leaves with a normal morphology, but larger cells. Similarly, constitutive expression of maize ABP1 in maize cell lines conferred on them the capacity to respond to auxin by increasing cell size. These results support a role of ABP1 as an auxin receptor controlling plant growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, A M -- Im, K H -- Savka, M A -- Wu, M J -- DeWitt, N G -- Shillito, R -- Binns, A N -- GM7369-06/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill, NC 27599-3280, USA. alan_jones@unc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9804548" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cell Size ; Gene Expression Regulation, Plant ; Genes, Plant ; Indoleacetic Acids/*metabolism/pharmacology ; Phenotype ; *Plant Growth Regulators ; Plant Leaves/*cytology/growth & development/metabolism ; *Plant Proteins ; Plants, Genetically Modified ; Plants, Toxic ; Receptors, Cell Surface/*genetics/*physiology ; Tetracyclines/pharmacology ; Tobacco/cytology/metabolism ; Transformation, Genetic ; Transgenes ; Zea mays/cytology/metabolism
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    Dependence of BSAP repressor and activator functions on BSAP concentration (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: During a B cell immune response, the transcription factor BSAP maintains its activator functions but is relieved of its repressor functions. This selective targeting of BSAP activities was shown to be regulated by a concentration-dependent mechanism whereby activator motifs for BSAP had a 20-fold higher binding affinity than repressor motifs. An exchange of activator and repressor motifs, however, showed that the context of the motif, rather than the affinity, determined whether BSAP operated as an activator or repressor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallin, J J -- Gackstetter, E R -- Koshland, M E -- CA09179/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1961-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunology Division, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506950" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD19/genetics ; B-Cell-Specific Activator Protein ; B-Lymphocytes/cytology/immunology/*metabolism ; Binding Sites ; Cell Line ; DNA-Binding Proteins/*genetics/*metabolism ; Gene Expression ; *Gene Expression Regulation ; Genes, Immunoglobulin ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin J-Chains/genetics ; Mice ; Nuclear Proteins/*genetics/*metabolism ; Phenotype ; Plasma Cells/immunology/metabolism ; Promoter Regions, Genetic ; *Regulatory Sequences, Nucleic Acid ; Repressor Proteins/genetics/metabolism ; Transcription Factors/*metabolism ; Transfection
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    Control of the supply line (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, J -- New York, N.Y. -- Science. 1997 Dec 19;278(5346):2073-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Cornell University, Ithaca, NY 14853, USA. jwr7@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9432720" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Bacterial Proteins/biosynthesis ; Binding Sites ; Cell Division ; Escherichia coli/*genetics/growth & development/metabolism ; Guanosine Tetraphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Models, Genetic ; RNA, Bacterial/biosynthesis/genetics ; RNA, Messenger/metabolism ; RNA, Ribosomal/*biosynthesis/genetics ; Ribosomal Proteins/biosynthesis/genetics/metabolism ; Ribosomes/*metabolism ; *Transcription, Genetic ; *rRNA Operon
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    Biologists catch their first detailed look at NO enzyme (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):389.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381140" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Enzyme Induction ; Enzyme Inhibitors/metabolism ; Heme/chemistry/metabolism ; Humans ; Isoenzymes/antagonists & inhibitors/*chemistry/metabolism ; Models, Molecular ; Nitric Oxide/biosynthesis/physiology ; Nitric Oxide Synthase/antagonists & inhibitors/*chemistry/metabolism ; *Protein Conformation ; Signal Transduction
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    Immune versus natural selection: antibody aldolases with enzymic rates but broader scope (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: Structural and mechanistic studies show that when the selection criteria of the immune system are changed, catalytic antibodies that have the efficiency of natural enzymes evolve, but the catalytic antibodies are much more accepting of a wide range of substrates. The catalytic antibodies were prepared by reactive immunization, a process whereby the selection criteria of the immune system are changed from simple binding to chemical reactivity. This process yielded aldolase catalytic antibodies that approximated the rate acceleration of the natural enzyme used in glycolysis. Unlike the natural enzyme, however, the antibody aldolases catalyzed a variety of aldol reactions and decarboxylations. The crystal structure of one of these antibodies identified the reactive lysine residue that was selected in the immunization process. This lysine is deeply buried in a hydrophobic pocket at the base of the binding site, thereby accounting for its perturbed pKa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barbas, C F 3rd -- Heine, A -- Zhong, G -- Hoffmann, T -- Gramatikova, S -- Bjornestedt, R -- List, B -- Anderson, J -- Stura, E A -- Wilson, I A -- Lerner, R A -- CA27489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 19;278(5346):2085-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Skaggs Institute for Chemical Biology and the Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9405338" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/chemistry/immunology/*metabolism ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Decarboxylation ; *Evolution, Molecular ; Fructose-Bisphosphate Aldolase/chemistry/immunology/*metabolism ; Glycolysis ; Hydrogen-Ion Concentration ; Immunization ; Immunoglobulin Fab Fragments/chemistry/immunology/*metabolism ; Kinetics ; Lysine/chemistry/metabolism ; Mice ; Models, Molecular ; Protein Conformation ; Pyridoxal/metabolism ; Selection, Genetic ; Substrate Specificity
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    From bench top to bedside (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1036-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381201" target="_blank"〉PubMed〈/a〉
    Keywords: Alkyl and Aryl Transferases/antagonists & inhibitors ; Animals ; Antibodies, Monoclonal/therapeutic use ; *Antineoplastic Agents/therapeutic use ; Apoptosis ; Binding Sites ; Clinical Trials as Topic ; Cyclin-Dependent Kinases/antagonists & inhibitors ; Drug Design ; Enzyme Inhibitors/therapeutic use ; Farnesyltranstransferase ; Genes, Tumor Suppressor ; Genes, p53 ; Genetic Therapy ; Humans ; Neoplasms/*drug therapy/genetics/therapy ; Oncogenes ; Protein-Tyrosine Kinases/antagonists & inhibitors ; Proto-Oncogene Proteins c-bcl-2/antagonists & inhibitors ; Receptor, ErbB-2/antagonists & inhibitors/immunology ; Receptors, Growth Factor/antagonists & inhibitors ; ras Proteins/antagonists & inhibitors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Phosphorylation and activation of p70s6k by PDK1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: Activation of the protein p70s6k by mitogens leads to increased translation of a family of messenger RNAs that encode essential components of the protein synthetic apparatus. Activation of the kinase requires hierarchical phosphorylation at multiple sites, culminating in the phosphorylation of the threonine in position 229 (Thr229), in the catalytic domain. The homologous site in protein kinase B (PKB), Thr308, has been shown to be phosphorylated by the phosphoinositide-dependent protein kinase PDK1. A regulatory link between p70s6k and PKB was demonstrated, as PDK1 was found to selectively phosphorylate p70s6k at Thr229. More importantly, PDK1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive PDK1 blocked insulin-induced activation of p70s6k.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pullen, N -- Dennis, P B -- Andjelkovic, M -- Dufner, A -- Kozma, S C -- Hemmings, B A -- Thomas, G -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):707-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445476" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Amino Acid Sequence ; Androstadienes/pharmacology ; Animals ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Catalysis ; Cell Line ; Enzyme Activation ; Insulin/pharmacology ; Insulin Antagonists/pharmacology ; Molecular Sequence Data ; Phosphorylation ; Phosphothreonine/metabolism ; Polyenes/pharmacology ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Recombinant Proteins/metabolism ; Ribosomal Protein S6 Kinases/*metabolism ; Sirolimus
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    Enhanced phosphorylation of p53 by ATM in response to DNA damage (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-11
    Description: The ATM protein, encoded by the gene responsible for the human genetic disorder ataxia telangiectasia (A-T), regulates several cellular responses to DNA breaks. ATM shares a phosphoinositide 3-kinase-related domain with several proteins, some of them protein kinases. A wortmannin-sensitive protein kinase activity was associated with endogenous or recombinant ATM and was abolished by structural ATM mutations. In vitro substrates included the translation repressor PHAS-I and the p53 protein. ATM phosphorylated p53 in vitro on a single residue, serine-15, which is phosphorylated in vivo in response to DNA damage. This activity was markedly enhanced within minutes after treatment of cells with a radiomimetic drug; the total amount of ATM remained unchanged. Various damage-induced responses may be activated by enhancement of the protein kinase activity of ATM.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Banin, S -- Moyal, L -- Shieh, S -- Taya, Y -- Anderson, C W -- Chessa, L -- Smorodinsky, N I -- Prives, C -- Reiss, Y -- Shiloh, Y -- Ziv, Y -- NS31763/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1674-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733514" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Androstadienes/pharmacology ; Ataxia Telangiectasia/metabolism ; Ataxia Telangiectasia Mutated Proteins ; *Carrier Proteins ; Cell Cycle Proteins ; Cell Line ; *DNA Damage ; DNA-Binding Proteins ; Enzyme Inhibitors/pharmacology ; Humans ; Mutation ; Phosphatidylinositol 3-Kinases/chemistry ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinase Inhibitors ; Protein Kinases/chemistry/*metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/antagonists & inhibitors/chemistry/genetics/*metabolism ; Recombinant Proteins/metabolism ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/*metabolism ; Tumor Suppressor Proteins ; Zinostatin/pharmacology
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    RasGRP, a Ras guanyl nucleotide- releasing protein with calcium- and diacylglycerol-binding motifs (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-06
    Description: RasGRP, a guanyl nucleotide-releasing protein for the small guanosine triphosphatase Ras, was characterized. Besides the catalytic domain, RasGRP has an atypical pair of "EF hands" that bind calcium and a diacylglycerol (DAG)-binding domain. RasGRP activated Ras and caused transformation in fibroblasts. A DAG analog caused sustained activation of Ras-Erk signaling and changes in cell morphology. Signaling was associated with partitioning of RasGRP protein into the membrane fraction. Sustained ligand-induced signaling and membrane partitioning were absent when the DAG-binding domain was deleted. RasGRP is expressed in the nervous system, where it may couple changes in DAG and possibly calcium concentrations to Ras activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebinu, J O -- Bottorff, D A -- Chan, E Y -- Stang, S L -- Dunn, R J -- Stone, J C -- New York, N.Y. -- Science. 1998 May 15;280(5366):1082-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9582122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*metabolism ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Catalysis ; Cell Cycle Proteins/genetics/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cell Size ; Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA, Complementary ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Diglycerides/metabolism ; Genes, ras ; *Guanine Nucleotide Exchange Factors ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Molecular Sequence Data ; Neurons/metabolism ; Phosphoprotein Phosphatases/genetics/metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; ras Proteins/*metabolism ; ras-GRF1
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    Conservation of T cell receptor conformation in epidermal gammadelta cells with disrupted primary Vgamma gene usage (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-28
    Description: A feature that distinguishes gammadelta T cell subsets from most alphabeta T cells and B cells is the association of expression of single T cell receptor (TCR) gamma and delta variable (V) region gene segments with specific anatomic sites. Mice lacking the TCR Vgamma5 chain normally expressed by most dendritic epidermal T cells were shown to retain a conformational determinant (idiotype) ordinarily expressed exclusively by such Vgamma5+ cells. Conservation by shuffled gammadelta TCR chains of an idiotype associated with a specific anatomic site indicates that for TCRgammadelta, as for immunoglobulin, conformation is associated to a greater extent with the function or development of lymphocyte repertoires than is the use of particular gene segments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mallick-Wood, C A -- Lewis, J M -- Richie, L I -- Owen, M J -- Tigelaar, R E -- Hayday, A C -- AI27404/AI/NIAID NIH HHS/ -- AI27855/AI/NIAID NIH HHS/ -- GM37759/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 13;279(5357):1729-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cell, and Developmental Biology and Section of Immunobiology, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9497293" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Dendritic Cells/*immunology ; Epidermis/cytology/*immunology ; Epitopes/analysis ; Female ; Gene Rearrangement ; Hybridomas ; Male ; Mice ; Mice, Inbred C57BL ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Protein Conformation ; Receptors, Antigen, T-Cell, gamma-delta/chemistry/*genetics/*immunology ; T-Lymphocyte Subsets/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Identification of c-MYC as a target of the APC pathway (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-04
    Description: The adenomatous polyposis coli gene (APC) is a tumor suppressor gene that is inactivated in most colorectal cancers. Mutations of APC cause aberrant accumulation of beta-catenin, which then binds T cell factor-4 (Tcf-4), causing increased transcriptional activation of unknown genes. Here, the c-MYC oncogene is identified as a target gene in this signaling pathway. Expression of c-MYC was shown to be repressed by wild-type APC and activated by beta-catenin, and these effects were mediated through Tcf-4 binding sites in the c-MYC promoter. These results provide a molecular framework for understanding the previously enigmatic overexpression of c-MYC in colorectal cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, T C -- Sparks, A B -- Rago, C -- Hermeking, H -- Zawel, L -- da Costa, L T -- Morin, P J -- Vogelstein, B -- Kinzler, K W -- CA57345/CA/NCI NIH HHS/ -- CA62924/CA/NCI NIH HHS/ -- GM07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1509-12.〈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/9727977" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Binding Sites ; Cell Line ; Colorectal Neoplasms/*genetics ; Cytoskeletal Proteins/genetics/metabolism ; *Gene Expression Regulation, Neoplastic ; *Genes, APC ; Genes, Reporter ; *Genes, myc ; HT29 Cells ; Humans ; Mutation ; Promoter Regions, Genetic ; Proto-Oncogene Proteins c-myc/metabolism ; Signal Transduction ; TCF Transcription Factors ; *Trans-Activators ; Transcription Factor 7-Like 2 Protein ; Transcription Factors/metabolism ; Transcription, Genetic ; beta Catenin
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  • 291
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    Closing the circadian loop: CLOCK-induced transcription of its own inhibitors per and tim (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: The circadian oscillator generates a rhythmic output with a period of about 24 hours. Despite extensive studies in several model systems, the biochemical mode of action has not yet been demonstrated for any of its components. Here, the Drosophila CLOCK protein was shown to induce transcription of the circadian rhythm genes period and timeless. dCLOCK functioned as a heterodimer with a Drosophila homolog of BMAL1. These proteins acted through an E-box sequence in the period promoter. The timeless promoter contains an 18-base pair element encompassing an E-box, which was sufficient to confer dCLOCK responsiveness to a reporter gene. PERIOD and TIMELESS proteins blocked dCLOCK's ability to transactivate their promoters via the E-box. Thus, dCLOCK drives expression of period and timeless, which in turn inhibit dCLOCK's activity and close the circadian loop.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Darlington, T K -- Wager-Smith, K -- Ceriani, M F -- Staknis, D -- Gekakis, N -- Steeves, T D -- Weitz, C J -- Takahashi, J S -- Kay, S A -- MH-51573/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1599-603.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and NSF Center for Biological Timing, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616122" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Biological Clocks ; CLOCK Proteins ; Cell Line ; Cell Nucleus/metabolism ; Circadian Rhythm/genetics/*physiology ; Dimerization ; Drosophila ; *Drosophila Proteins ; Feedback ; Gene Expression ; Helix-Loop-Helix Motifs ; Insect Proteins/*genetics/metabolism ; Nuclear Proteins/*genetics/metabolism ; Period Circadian Proteins ; Promoter Regions, Genetic ; RNA, Messenger/genetics/metabolism ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/*metabolism ; *Transcriptional Activation ; Transfection
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  • 292
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    Crystal structure of the catalytic domain of human plasmin complexed with streptokinase (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-11
    Description: Streptokinase is a plasminogen activator widely used in treating blood-clotting disorders. Complexes of streptokinase with human plasminogen can hydrolytically activate other plasminogen molecules to plasmin, which then dissolves blood clots. A similar binding activation mechanism also occurs in some key steps of blood coagulation. The crystal structure of streptokinase complexed with the catalytic unit of human plasmin was solved at 2.9 angstroms. The amino-terminal domain of streptokinase in the complex is hypothesized to enhance the substrate recognition. The carboxyl-terminal domain of streptokinase, which binds near the activation loop of plasminogen, is likely responsible for the contact activation of plasminogen in the complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, X -- Lin, X -- Loy, J A -- Tang, J -- Zhang, X C -- HL 60626/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1662-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crystallography Program, Oklahoma Medical Research Foundation, 825 N.E. 13th Street, Oklahoma City, OK 73104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733510" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography, X-Ray ; Fibrinolysin/*chemistry/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Streptokinase/*chemistry/metabolism
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  • 293
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    Telomeres and senescence: ending the debate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Lange, T -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):334-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Biology and Genetics, The Rockefeller University, New York, NY 10021, USA. delange@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454329" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/pharmacology ; *Cell Aging ; *Cell Division ; Cell Line ; Cell Transformation, Neoplastic ; DNA-Binding Proteins ; Enzyme Activation ; Genes, Tumor Suppressor ; Humans ; Mice ; Neoplasms/drug therapy/enzymology/pathology ; Proteins/genetics/*metabolism ; *Rna ; RNA-Directed DNA Polymerase/genetics/metabolism ; Telomerase/antagonists & inhibitors/genetics/*metabolism ; Telomere/metabolism/*physiology/ultrastructure ; Transfection
    Print ISSN: 0036-8075
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  • 294
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    Patterning of cortical efferent projections by semaphorin-neuropilin interactions (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-04
    Description: Cortical neurons communicate with various cortical and subcortical targets by way of stereotyped axon projections through the white matter. Slice overlay experiments indicate that the initial growth of cortical axons toward the white matter is regulated by a diffusible chemorepulsive signal localized near the marginal zone. Semaphorin III is a major component of this diffusible signal, and cortical neurons transduce this signal by way of the neuropilin-1 receptor. These observations indicate that semaphorin-neuropilin interactions play a critical role in the initial patterning of projections in the developing cortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Polleux, F -- Giger, R J -- Ginty, D D -- Kolodkin, A L -- Ghosh, A -- NS35165/NS/NINDS NIH HHS/ -- NS36176/NS/NINDS NIH HHS/ -- NS534814/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 4;282(5395):1904-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9836643" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Cell Line ; Cerebral Cortex/*cytology/embryology ; Coculture Techniques ; Gene Targeting ; Glycoproteins/genetics/*physiology ; Humans ; Mice ; Nerve Growth Factors/*metabolism ; Nerve Tissue Proteins/*physiology ; Neurons, Efferent/cytology/*physiology ; Neuropilin-1 ; Rats ; Recombinant Proteins/metabolism ; Semaphorin-3A ; Signal Transduction
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  • 295
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    Revealing HIV's T cell passkey (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1833-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669932" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; Antigens, CD4/chemistry/metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; HIV Antibodies/immunology ; HIV Envelope Protein gp120/*chemistry/genetics/metabolism ; HIV-1/*chemistry/immunology ; Humans ; Mutation ; Peptide Fragments/chemistry/metabolism ; Protein Conformation ; Receptors, CCR5/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 296
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    Ultraviolet-induced cell death blocked by a selenoprotein from a human dermatotropic poxvirus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: Selenium, an essential trace element, is a component of prokaryotic and eukaryotic antioxidant proteins. A candidate selenoprotein homologous to glutathione peroxidase was deduced from the sequence of molluscum contagiosum, a poxvirus that causes persistent skin neoplasms in children and acquired immunodeficiency syndrome (AIDS) patients. Selenium was incorporated into this protein during biosynthesis, and a characteristic stem-loop structure near the end of the messenger RNA was required for alternative selenocysteine decoding of a potential UGA stop codon within the open reading frame. The selenoprotein protected human keratinocytes against cytotoxic effects of ultraviolet irradiation and hydrogen peroxide, providing a mechanism for a virus to defend itself against environmental stress.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shisler, J L -- Senkevich, T G -- Berry, M J -- Moss, B -- DK47320/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4 Center Drive, MSC 0445, Bethesda, MD 20892-0445, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417017" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Base Sequence ; Cell Line ; Codon ; Glutathione Peroxidase/genetics/*metabolism ; HeLa Cells ; Humans ; Hydrogen Peroxide/pharmacology ; Keratinocytes/*cytology/drug effects ; Molecular Sequence Data ; Molluscum contagiosum virus/genetics/*physiology ; Open Reading Frames ; Point Mutation ; Proteins/genetics/*metabolism ; Selenium/metabolism ; Selenocysteine/genetics ; Selenoproteins ; Transfection ; Ultraviolet Rays ; Viral Proteins/genetics/*metabolism
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    Binding of hepatitis C virus to CD81 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-30
    Description: Chronic hepatitis C virus (HCV) infection occurs in about 3 percent of the world's population and is a major cause of liver disease. HCV infection is also associated with cryoglobulinemia, a B lymphocyte proliferative disorder. Virus tropism is controversial, and the mechanisms of cell entry remain unknown. The HCV envelope protein E2 binds human CD81, a tetraspanin expressed on various cell types including hepatocytes and B lymphocytes. Binding of E2 was mapped to the major extracellular loop of CD81. Recombinant molecules containing this loop bound HCV and antibodies that neutralize HCV infection in vivo inhibited virus binding to CD81 in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pileri, P -- Uematsu, Y -- Campagnoli, S -- Galli, G -- Falugi, F -- Petracca, R -- Weiner, A J -- Houghton, M -- Rosa, D -- Grandi, G -- Abrignani, S -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):938-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉IRIS, Chiron, Siena 53100, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9794763" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/immunology ; Antibodies, Viral/immunology ; Antigens, CD/chemistry/genetics/immunology/*metabolism ; Antigens, CD81 ; Cell Line ; DNA, Complementary ; Gene Library ; Hepacivirus/immunology/*metabolism ; Hepatitis C/immunology ; Humans ; Liver/cytology/immunology/virology ; Lymphocytes/immunology/virology ; Membrane Proteins/chemistry/genetics/immunology/*metabolism ; Mice ; Molecular Sequence Data ; Pan troglodytes ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism/pharmacology ; Sequence Alignment ; Tumor Cells, Cultured ; Viral Envelope Proteins/genetics/immunology/*metabolism
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  • 298
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    A small, nonpeptidyl mimic of granulocyte-colony-stimulating factor [see commetns] (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-10
    Description: A nonpeptidyl small molecule SB 247464, capable of activating granulocyte-colony-stimulating factor (G-CSF) signal transduction pathways, was identified in a high-throughput assay in cultured cells. Like G-CSF, SB 247464 induced tyrosine phosphorylation of multiple signaling proteins and stimulated primary murine bone marrow cells to form granulocytic colonies in vitro. It also elevated peripheral blood neutrophil counts in mice. The extracellular domain of the murine G-CSF receptor was required for the activity of SB 247464, suggesting that the compound acts by oligomerizing receptor chains. The results indicate that a small molecule can activate a receptor that normally binds a relatively large protein ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tian, S S -- Lamb, P -- King, A G -- Miller, S G -- Kessler, L -- Luengo, J I -- Averill, L -- Johnson, R K -- Gleason, J G -- Pelus, L M -- Dillon, S B -- Rosen, J -- New York, N.Y. -- Science. 1998 Jul 10;281(5374):257-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Transcription Research, Ligand Pharmaceuticals, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9657720" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzimidazoles/chemistry/metabolism/*pharmacology ; Cell Line ; Colony-Forming Units Assay ; DNA-Binding Proteins/metabolism ; Dimerization ; Female ; Granulocyte Colony-Stimulating Factor/metabolism/pharmacology ; Granulocytes/cytology ; Guanidines/chemistry/metabolism/*pharmacology ; Humans ; Janus Kinase 1 ; Janus Kinase 2 ; Leukocyte Count ; Leukopoiesis ; Mice ; Mice, Inbred C57BL ; *Milk Proteins ; Neutrophils/cytology ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; Receptors, Granulocyte Colony-Stimulating Factor/chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; STAT3 Transcription Factor ; STAT5 Transcription Factor ; Signal Transduction/drug effects ; Species Specificity ; Trans-Activators/metabolism ; Transfection ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 299
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    Outsmarting HIV drug resistance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1623, 1625.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867659" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/*metabolism/pharmacology ; Binding Sites ; Crystallography, X-Ray ; DNA Primers/metabolism ; DNA, Viral/metabolism ; Deoxyribonucleotides/metabolism ; Drug Resistance, Microbial ; HIV Reverse Transcriptase/*chemistry/genetics/metabolism ; HIV-1/*drug effects/*enzymology ; Models, Molecular ; Mutation ; Protein Conformation ; Reverse Transcriptase Inhibitors/*metabolism/pharmacology ; Templates, Genetic
    Print ISSN: 0036-8075
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  • 300
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    Molecular basis for interactions of G protein betagamma subunits with effectors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Both the alpha and betagamma subunits of heterotrimeric guanine nucleotide-binding proteins (G proteins) communicate signals from receptors to effectors. Gbetagamma subunits can regulate a diverse array of effectors, including ion channels and enzymes. Galpha subunits bound to guanine diphosphate (Galpha-GDP) inhibit signal transduction through Gbetagamma subunits, suggesting a common interface on Gbetagamma subunits for Galpha binding and effector interaction. The molecular basis for interaction of Gbetagamma with effectors was characterized by mutational analysis of Gbeta residues that make contact with Galpha-GDP. Analysis of the ability of these mutants to regulate the activity of calcium and potassium channels, adenylyl cyclase 2, phospholipase C-beta2, and beta-adrenergic receptor kinase revealed the Gbeta residues required for activation of each effector and provides evidence for partially overlapping domains on Gbeta for regulation of these effectors. This organization of interaction regions on Gbeta for different effectors and Galpha explains why subunit dissociation is crucial for signal transmission through Gbetagamma subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ford, C E -- Skiba, N P -- Bae, H -- Daaka, Y -- Reuveny, E -- Shekter, L R -- Rosal, R -- Weng, G -- Yang, C S -- Iyengar, R -- Miller, R J -- Jan, L Y -- Lefkowitz, R J -- Hamm, H E -- DA02121/DA/NIDA NIH HHS/ -- DA02575/DA/NIDA NIH HHS/ -- MH40165/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 22;280(5367):1271-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Neuroscience and Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596582" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate Ribose/metabolism ; Adenylyl Cyclases/metabolism ; Binding Sites ; Calcium Channels/metabolism ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; G Protein-Coupled Inwardly-Rectifying Potassium Channels ; GTP-Binding Proteins/*chemistry/*metabolism ; Guanosine Diphosphate/metabolism ; *Heterotrimeric GTP-Binding Proteins ; Humans ; Isoenzymes/metabolism ; Models, Molecular ; Mutation ; Phospholipase C beta ; Potassium Channels/metabolism ; *Potassium Channels, Inwardly Rectifying ; Protein Conformation ; Rhodopsin/pharmacology ; *Signal Transduction ; Transducin/metabolism ; Type C Phospholipases/metabolism ; beta-Adrenergic Receptor Kinases
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