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  • ASTROPHYSICS
  • Analytical Chemistry and Spectroscopy
  • Chemistry
  • Inorganic Chemistry
  • Life and Medical Sciences
  • Organic Chemistry
  • American Association for the Advancement of Science (AAAS)  (30)
  • 1995-1999
  • 1990-1994  (3)
  • 1985-1989  (27)
  • 1950-1954
  • 1993
  • 1991  (3)
  • 1988  (12)
  • 1985  (15)
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  • 1995-1999
  • 1990-1994  (3)
  • 1985-1989  (27)
  • 1950-1954
Year
  • 1
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    Clathrate hydrate formation in amorphous cometary ice analogs in vacuo (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: The presence of clathrate hydrates in cometary ice has been suggested to account for anomalous gas release at large radial distances from the sun as well as the retention of volatiles in comets to elevated temperatures. However, how clathrate hydrates can form in low-pressure environments, such as in cold interstellar molecular clouds, in the outer reaches of the early solar nebula, or in cometary ices, has been poorly understood. Experiments performed with the use of a modified electron microscope demonstrate that during the warming of vapor-deposited amorphous ices in vacuo, clathrate hydrates can form by rearrangements in the solid state. Phase separations and microporous textures that are the result of these rearrangements may account for a variety of anomalous cometary phenomena.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blake, D -- Allamandola, L -- Sandford, S -- Hudgins, D -- Freund, F -- New York, N.Y. -- Science. 1991 Oct 25;254:548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Planetary Biology Branch, Ames Research Center, Moffett Field, CA 94035, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11538372" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Crystallography ; Earth (Planet) ; Hydrocarbons/chemistry ; Ice/*analysis ; *Meteoroids ; Microscopy, Electron ; *Solar System
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  • 2
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    Manifest destiny at the Scripps Research Institute (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baskin, Y -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):140-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853198" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes ; Biology ; California ; Chemical Phenomena ; Chemistry ; Research Support as Topic
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  • 3
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    At the crossroads of chemistry and immunology: catalytic antibodies (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: Immunochemistry has historically focused on the nature of antigenicity and antibody-antigen recognition. However, in the last 5 years, the field of immunochemistry has taken a new direction. With the aid of mechanistic and synthetic chemistry, the vast network of molecules and cells of the immune system has been tapped to produce antibodies with a new function--catalytic antibodies. Because antibodies can be generated that selectively bind almost any molecule of interest, this new technology offers the potential to tailor-make highly selective catalysts for applications in biology, chemistry, and medicine. In addition, catalytic antibodies provide fundamental insight into important aspects of biological catalysis, including the importance of transition-state stabilization, proximity effects, general acid and base catalysts, electrophilic and nucleophilic catalysis, and strain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerner, R A -- Benkovic, S J -- Schultz, P G -- New York, N.Y. -- Science. 1991 May 3;252(5006):659-67.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024118" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies/chemistry/immunology/metabolism ; Antibodies, Monoclonal/immunology/metabolism ; Antibody Specificity ; Antigens/chemistry/immunology/metabolism ; Binding Sites, Antibody ; *Catalysis ; Chemical Phenomena ; Chemistry ; Haptens ; Hydrogen-Ion Concentration ; Hydrolysis ; Metals ; Molecular Conformation ; Recombinant Proteins ; Thermodynamics ; Zinc
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  • 4
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    Characterization of a helical protein designed from first principles (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structures. A systematic approach was aimed at the design of a four-helix bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomeric, highly helical, and very stable to denaturation by guanidine hydrochloride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regan, L -- DeGrado, W F -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):976-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. I. du Pont de Nemours & Company, Central Research & Development Department, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3043666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; Chromatography, Gel ; Escherichia coli/genetics ; Molecular Sequence Data ; Plasmids ; *Protein Conformation ; *Proteins/genetics
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  • 5
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    DNA binding by proteins (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Study of proteins that recognize specific DNA sequences has yielded much information, but the field is still in its infancy. Already two major structural motifs have been discovered, the helix-turn-helix and zinc finger, and numerous examples of DNA-binding proteins containing either of them are known. The restriction enzyme Eco RI uses yet a different motif. Additional motifs are likely to be found as well. There is a growing understanding of some of the physical chemistry involved in protein-DNA binding, but much remains to be learned before it becomes possible to engineer a protein that binds to a specific DNA sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schleif, R -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1182-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842864" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/metabolism ; Binding Sites ; Chemical Phenomena ; Chemistry ; DNA/metabolism ; DNA Restriction Enzymes/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease EcoRI ; Electrochemistry ; Nucleic Acids/metabolism ; Protein Conformation ; Zinc
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  • 6
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    Introduction of nucleophiles and spectroscopic probes into antibody combining sites (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: A general chemical strategy has been developed whereby antibody combining sites can be selectively derivatized with natural or synthetic molecules, such as catalytic groups, drugs, metals, or reporter molecules. Cleavable affinity labels were used to selectively introduce a thiol into the combining site of the immunoglobulin A MOPC 315. This thiol acted both as a nucleophile to accelerate ester thiolysis 60,000-fold and as a handle for selectively derivatizing the antibody with additional functional groups. For example, derivatization of the antibody with a fluorophore made possible a direct spectroscopic assay of antibody-ligand complexation. This chemistry should not only extend our ability to exploit antibody specificity in chemical catalysis, diagnostics, and therapeutics, but may also prove generally applicable to the functional modification of other proteins for which detailed structural information is unavailable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pollack, S J -- Nakayama, G R -- Schultz, P G -- AI24695-02/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1038-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194752" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Animals ; *Antigen-Antibody Reactions ; *Binding Sites, Antibody ; Chemical Phenomena ; Chemistry ; Dinitrobenzenes ; Immunoglobulin Fab Fragments ; Mice ; Spectrometry, Fluorescence ; Sulfhydryl Compounds
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  • 7
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    Insights into enzyme function from studies on mutants of dihydrofolate reductase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-03-04
    Description: Kinetic analysis and protein mutagenesis allow the importance of individual amino acids in ligand binding and catalysis to be assessed. A kinetic analysis has shown that the reaction catalyzed by dihydrofolate reductase is optimized with respect to product flux, which in turn is predetermined by the active-site hydrophobic surface. Protein mutagenesis has revealed that specific hydrophobic residues contribute 2 to 5 kilocalories per mole to ligand binding and catalysis. The extent to which perturbations within this active-site ensemble may affect catalysis is discussed in terms of the constraints imposed by the energy surface for the reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benkovic, S J -- Fierke, C A -- Naylor, A M -- GM24129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1105-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park 16802.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3125607" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Chemical Phenomena ; Chemistry ; Escherichia coli/enzymology ; Kinetics ; Lactobacillus casei/enzymology ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/genetics/*metabolism ; Thermodynamics
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  • 8
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    Induction of an antibody that catalyzes the hydrolysis of an amide bond (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Catalysis of amide bond hydrolysis is of singular importance in enzymology. An antibody was induced to an analog of a high-energy intermediate anticipated along the reaction coordinate of amide hydrolysis. This antibody is an amidase with high specificity and a large rate enhancement (250,000) relative to the uncatalyzed reaction. This reaction represents the kinetically most difficult hydrolysis reaction yet catalyzed by an antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, K D -- Schloeder, D -- Benkovic, S J -- Lerner, R A -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1188-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413482" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/metabolism ; Animals ; Antibodies, Monoclonal/biosynthesis/*physiology ; Antibody Specificity ; Antigens/immunology ; *Catalysis ; Chemical Phenomena ; Chemistry ; Hemocyanin/analogs & derivatives/immunology ; Hydrolysis ; Immunization ; Kinetics ; Mice ; Organophosphorus Compounds/immunology ; Substrate Specificity
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  • 9
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    The S1-sensitive form of d(C-T)n.d(A-G)n: chemical evidence for a three-stranded structure in plasmids (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-30
    Description: Homopurine-homopyrimidine sequences that flank certain actively transcribed genes are hypersensitive to single strand-specific nucleases such as S1. This has raised the possibility that an unusual structure exists in these regions that might be involved in recognition or regulation. Several of these sequences, including d(C-T)n.d(A-G)n, are known to undergo a transition in plasmids to an underwound state that is hypersensitive to single strand-specific nucleases; this transition occurs under conditions of moderately acid pH and negative supercoiling. Chemical probes were used to examine the reactivity of a restriction fragment from a human U1 gene containing the sequence d(C-T)18.d(A-G)18 as a function of supercoiling and pH, and thus analyze the structure in this region. Hyperreactivity was seen in the center and at one end of the (C-T)n tract, and continuously from the center to the same end of the (A-G)n tract, in the presence of supercoiling and pH less than or equal to 6.0. These results provide strong support for a triple-helical model recently proposed for these sequences and are inconsistent with other proposed structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnston, B H -- New York, N.Y. -- Science. 1988 Sep 30;241(4874):1800-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845572" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chemical Phenomena ; Chemistry ; *Dna ; DNA, Superhelical ; Endonucleases/*metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Plasmids ; Single-Strand Specific DNA and RNA Endonucleases
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  • 10
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    Structural and functional roles of glycosyl-phosphatidylinositol in membranes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-15
    Description: Glycosylated forms of phosphatidylinositol, which have only recently been described in eukaryotic organisms, are now known to play important roles in biological membrane function. These molecules can serve as the sole means by which particular cell-surface proteins are anchored to the membrane. Lipids with similar structures may also be involved in signal transduction mechanisms for the hormone insulin. The utilization of this novel class of lipid molecules for these two distinct functions suggests new mechanisms for the regulation of proteins in biological membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Low, M G -- Saltiel, A R -- DK33804/DK/NIDDK NIH HHS/ -- GM35873/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 15;239(4837):268-75.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Cellular Biophysics, College of Physicians and Surgeons of Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3276003" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*physiology ; Chemical Phenomena ; Chemistry ; Glycolipids/biosynthesis/*physiology ; Glycosylation ; Humans ; Hydrolysis ; Insulin/physiology ; Membrane Lipids/physiology ; Membrane Proteins/physiology ; Phosphatidylinositols/biosynthesis/*physiology ; Phospholipases/metabolism ; Phospholipid Ethers/biosynthesis/physiology ; Trypanosoma brucei brucei/metabolism
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  • 11
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    The design of molecular hosts, guests, and their complexes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-06
    Description: The origins, definitions, tools, and guiding principles of host-guest chemistry are developed. Perching, nesting, and capsular complexes are exemplified through molecular model and crystal structure comparisons. The degree of preorganization of a host for binding is a central determinant of its binding power. Complementarity of binding site placement in host and guest is a central determinant of structural recognition in complexation. Examples are given of chiral recognition in complexation, of partial transacylase mimics, of caviplexes, and of a synthetic molecular cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cram, D J -- New York, N.Y. -- Science. 1988 May 6;240(4853):760-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283937" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Binding Sites ; Chemical Phenomena ; Chemistry ; Crystallization ; Enzymes ; *Models, Chemical ; Models, Molecular ; Nucleic Acids ; Thermodynamics
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  • 12
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    Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-29
    Description: Exposure of Escherichia coli to low concentrations of hydrogen peroxide results in DNA damage that causes mutagenesis and kills the bacteria, whereas higher concentrations of peroxide reduce the amount of such damage. Earlier studies indicated that the direct DNA oxidant is a derivative of hydrogen peroxide whose formation is dependent on cell metabolism. The generation of this oxidant depends on the availability of both reducing equivalents and an iron species, which together mediate a Fenton reaction in which ferrous iron reduces hydrogen peroxide to a reactive radical. An in vitro Fenton system was established that generates DNA strand breaks and inactivates bacteriophage and that also reproduces the suppression of DNA damage by high concentrations of peroxide. The direct DNA oxidant both in vivo and in this in vitro system exhibits reactivity unlike that of a free hydroxyl radical and may instead be a ferryl radical.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imlay, J A -- Chin, S M -- Linn, S -- GM19020/GM/NIGMS NIH HHS/ -- P30ES01896/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):640-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2834821" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda ; Chemical Phenomena ; Chemistry ; *DNA Damage ; DNA Repair ; DNA, Bacterial/*drug effects ; Escherichia coli/drug effects/*genetics ; Ferrous Compounds ; Free Radicals ; Hydrogen Peroxide/administration & dosage/*pharmacology ; Hydrogen-Ion Concentration ; Hydroxides ; Hydroxyl Radical ; Oxidation-Reduction
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  • 13
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    DNA damage and oxygen radical toxicity (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-03
    Description: A major portion of the toxicity of hydrogen peroxide in Escherichia coli is attributed to DNA damage mediated by a Fenton reaction that generates active forms of hydroxyl radicals from hydrogen peroxide, DNA-bound iron, and a constant source of reducing equivalents. Kinetic peculiarities of DNA damage production by hydrogen peroxide in vivo can be reproduced by including DNA in an in vitro Fenton reaction system in which iron catalyzes the univalent reduction of hydrogen peroxide by the reduced form of nicotinamide adenine dinucleotide (NADH). To minimize the toxicity of oxygen radicals, the cell utilizes scavengers of these radicals and DNA repair enzymes. On the basis of observations with the model system, it is proposed that the cell may also decrease such toxicity by diminishing available NAD(P)H and by utilizing oxygen itself to scavenge active free radicals into superoxide, which is then destroyed by superoxide dismutase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imlay, J A -- Linn, S -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1302-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, Berkeley.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3287616" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *DNA Damage ; DNA, Bacterial/*drug effects ; Escherichia coli/drug effects/*genetics ; Free Radicals ; Hydrogen Peroxide/*pharmacology ; Iron ; NAD/metabolism ; Oxidation-Reduction ; Oxygen/*metabolism
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  • 14
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    Escherichia coli aspartate transcarbamylase: the relation between structure and function (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-05
    Description: The x-ray structures of the allosteric enzyme aspartate transcarbamylase from Escherichia coli have been solved and refined for both allosteric forms. The T form was determined in the presence of the heterotropic inhibitor cytidine triphosphate, CTP, while the R form was determined in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate. These two x-ray structures provide the starting point for an understanding of how allosteric enzymes are able to control the rates of metabolic pathways. Insights into the mechanisms of both catalysis and homotropic cooperativity have been obtained by using site-directed mutagenesis to probe residues thought to be critical to the function of the enzyme based on these x-ray structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kantrowitz, E R -- Lipscomb, W N -- GM 06920/GM/NIGMS NIH HHS/ -- GM26237/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):669-74.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Boston College, MA 02167.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3041592" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Allosteric Site ; Aspartate Carbamoyltransferase/*physiology ; Binding Sites ; Chemical Phenomena ; Chemistry ; Escherichia coli/*enzymology ; Macromolecular Substances ; Protein Conformation ; Structure-Activity Relationship
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  • 15
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    Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: The crystal structure of a complex containing the DNA-binding domain of lambda repressor and a lambda operator site was determined at 2.5 A resolution and refined to a crystallographic R factor of 24.2 percent. The complex is stabilized by an extensive network of hydrogen bonds between the protein and the sugar-phosphate backbone. Several side chains form hydrogen bonds with sites in the major groove, and hydrophobic contacts also contribute to the specificity of binding. The overall arrangement of the complex is quite similar to that predicted from earlier modeling studies, which fit the protein dimer against linear B-form DNA. However, the cocrystal structure reveals important side chain-side chain interactions that were not predicted from the modeling or from previous genetic and biochemical studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jordan, S R -- Pabo, C O -- GM-31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):893-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187530" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; Chemical Phenomena ; Chemistry ; Crystallization ; DNA/*metabolism ; *DNA-Binding Proteins ; Glutamine/metabolism ; Hydrogen Bonding ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; *Operator Regions, Genetic ; Protein Binding ; Protein Conformation ; Repressor Proteins/genetics/*metabolism ; Sugar Phosphates/metabolism ; Transcription Factors/*metabolism ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 16
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    Bond order and charge localization in nucleoside phosphorothioates (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-03
    Description: In the recent literature on nucleoside phosphorothioate anions the structural formulas show a double bond between phosphorus and sulfur and a single bond between phosphorus and oxygen with a negative charge localized on oxygen. However, a review of physical data on these compounds shows the reverse to be the case; that is, in phosphorothioate anions the P-S bond is a single bond with a negative charge localized on sulfur, while the P-O bond order for exocyclic and nonbridging oxygens is greater than 1, approaching 2 in O-alkyl phosphorothioate monoanions and O,O-dialkyl phosphorothioates. The P-O bond orders in phosphorothioate dianions and trianions approach 1 1/2 and 1 1/3, respectively, owing to delocalization of negative charge among two or three oxygens. These conclusions are based on bond lengths obtained from x-ray crystallographic data and electron diffraction, the magnitudes of the effects of 18O on the 31P-nuclear magnetic resonance chemical shifts of phosphorus in nucleoside [18O]phosphorothioates, the pH-dependence of 17O-NMR chemical shifts in [17O]phosphate and [17O]thiophosphate, the vibrational spectra of thiophosphate di- and trianions, and the pKa (dissociation constant) values for phosphoric and thiophosphoric acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frey, P A -- Sammons, R D -- GM30480/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 May 3;228(4699):541-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2984773" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Chemistry, Physical ; Cyclic AMP/metabolism ; Magnetic Resonance Spectroscopy ; Phosphates/metabolism ; Phosphoric Acids/metabolism ; Physicochemical Phenomena ; *Thionucleotides/metabolism
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    Dissociation of antitumor potency from anthracycline cardiotoxicity in a doxorubicin analog (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: The search for new congeners of the leading anticancer drug doxorubicin has led to an analog that is approximately 1000 times more potent, noncardiotoxic at therapeutic dose levels, and non-cross-resistant with doxorubicin. The new anthracycline, 3'-deamino-3'-(3-cyano-4-morpholinyl)doxorubicin (MRA-CN), is produced by incorporation of the 3' amino group of doxorubicin in a new cyanomorpholinyl ring. The marked increase in potency was observed against human ovarian and breast carcinomas in vitro; it was not accompanied by an increase in cardiotoxicity in fetal mouse heart cultures. Doxorubicin and MRA-CN both produced typical cardiac ultrastructural and biochemical changes, but at equimolar concentrations. In addition, MRA-CN was not cross-resistant with doxorubicin in a variant of the human sarcoma cell line MES-SA selected for resistance to doxorubicin. Thus antitumor efficacy was dissociated from both cardiotoxicity and cross-resistance by this modification of anthracycline structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikic, B I -- Ehsan, M N -- Harker, W G -- Friend, N F -- Brown, B W -- Newman, R A -- Hacker, M P -- Acton, E M -- CA 24543/CA/NCI NIH HHS/ -- CA 32250/CA/NCI NIH HHS/ -- CA 33303/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1544-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012308" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antineoplastic Agents ; Breast Neoplasms/drug therapy ; Cell Line ; Chemical Phenomena ; Chemistry ; Dose-Response Relationship, Drug ; Doxorubicin/adverse effects/*analogs & derivatives/therapeutic use ; Female ; Heart/drug effects ; Humans ; Isoenzymes ; L-Lactate Dehydrogenase/analysis ; Mice ; Myocardium/enzymology ; Ovarian Neoplasms/drug therapy ; Pregnancy
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  • 18
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    A potent nonpeptide cholecystokinin antagonist selective for peripheral tissues isolated from Aspergillus alliaceus (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-11
    Description: A new, competitive, nonpeptide cholecystokinin (CCK) antagonist, asperlicin, was isolated from the fungus Aspergillus alliaceus. The compound has 300 to 400 times the affinity for pancreatic, ileal, and gallbladder CCK receptors than proglumide, a standard agent of this class. Moreover, asperlicin is highly selective for peripheral CCK receptors relative to brain CCK and gastrin receptors. Since asperlicin also exhibits long-lasting CCK antagonist activity in vivo, it should provide a valuable tool for investigating the physiological and pharmacological actions of CCK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, R S -- Lotti, V J -- Monaghan, R L -- Birnbaum, J -- Stapley, E O -- Goetz, M A -- Albers-Schonberg, G -- Patchett, A A -- Liesch, J M -- Hensens, O D -- New York, N.Y. -- Science. 1985 Oct 11;230(4722):177-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994227" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspergillus/*metabolism ; Benzodiazepinones/*isolation & purification/pharmacology ; Chemical Phenomena ; Chemistry ; Cholecystokinin/*antagonists & inhibitors/pharmacology/physiology ; Dose-Response Relationship, Drug ; Gallbladder/drug effects ; Guinea Pigs ; Ileum/drug effects ; Pancreas/drug effects ; Rats ; Receptors, Cell Surface/drug effects ; Receptors, Cholecystokinin
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  • 19
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    Three-dimensional structure of poliovirus at 2.9 A resolution (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-09-27
    Description: The three-dimensional structure of poliovirus has been determined at 2.9 A resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a "core" consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the "connecting loops" and NH2- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit "cores" to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH2- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the "connecting loops" and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogle, J M -- Chow, M -- Filman, D J -- AI-20566/AI/NIAID NIH HHS/ -- AI-22346/AI/NIAID NIH HHS/ -- NS-07078/NS/NINDS NIH HHS/ -- R01 AI020566/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1358-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/immunology ; Capsid/physiology ; Chemical Phenomena ; Chemistry ; HeLa Cells/microbiology ; Mutation ; Poliovirus/physiology/*ultrastructure ; Protein Conformation ; Virus Replication ; X-Ray Diffraction
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    Qinghaosu (artemisinin): an antimalarial drug from China (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-05-31
    Description: The herb Artemisia annua has been used for many centuries in Chinese traditional medicine as a treatment for fever and malaria. In 1971, Chinese chemists isolated from the leafy portions of the plant the substance responsible for its reputed medicinal action. This compound, called qinghaosu (QHS, artemisinin), is a sesquiterpene lactone that bears a peroxide grouping and, unlike most other antimalarials, lacks a nitrogen-containing heterocyclic ring system. The compound has been used successfully in several thousand malaria patients in China, including those with both chloroquine-sensitive and chloroquine-resistant strains of Plasmodium falciparum. Derivatives of QHS, such as dihydroqinghaosu, artemether, and the water-soluble sodium artesunate, appear to be more potent than QHS itself. Sodium artesunate acts rapidly in restoring to consciousness comatose patients with cerebral malaria. Thus QHS and its derivatives offer promise as a totally new class of antimalarials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klayman, D L -- New York, N.Y. -- Science. 1985 May 31;228(4703):1049-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3887571" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antimalarials ; *Artemisinins ; Brain Diseases/therapy ; Chemical Phenomena ; Chemistry ; Humans ; Liver/metabolism ; Malaria/*drug therapy ; Medicine, Chinese Traditional ; Metabolic Clearance Rate ; Plants, Medicinal/analysis ; Plasmodium berghei ; Plasmodium falciparum ; *Sesquiterpenes/isolation & purification/metabolism/therapeutic use/toxicity
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    Sculpting horizons in organic chemistry (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-02-22
    Description: Organic chemistry as a discipline derives from and impacts on the biological and abiological world in which we live. Its challenges lie in the areas of structure, reactivity, techniques, and concepts. Powerful structural tools reveal structures from biology that range from control of insect development and behavior to whole new metabolic pathways in humans. Unnatural products create beautiful new molecular shapes whose properties cannot be predicted as well as catalysts that function with enzyme-like control. From structure flows reactivity. Exploration of known reactions points to new directions, and development of new reactions offers the opportunity of streamlined synthetic design. Emerging new techniques offer new dimensions for performing and studying reactions as well as the hope for developing new ones. Merging disparate facts into unified concepts increases predictive capabilities. The extraordinary difficulty of finding the resultant of many small effects may obscure the presence of general theories, creates the art in the practice of the science, and challenges the practitioner. From these general themes derives the quest for selectivity--chemo-, regio-, diastereo-, and enantio-. An examination of the fundamental underpinnings of the applications of organic chemistry reveals that, while impressive strides have been made, the science is best described as being between infancy and childhood. The cross-fertilization between organic chemistry and molecular biology vividly illustrates a merging of chemistry and biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trost, B M -- New York, N.Y. -- Science. 1985 Feb 22;227(4689):908-16.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3969569" target="_blank"〉PubMed〈/a〉
    Keywords: Alkylation ; Animals ; Chemical Phenomena ; Chemistry ; *Chemistry, Organic ; Enzymes ; Humans ; Insects ; Mammals ; Organic Chemistry Phenomena ; Research ; Stereoisomerism
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    Hernandulcin: an intensely sweet compound discovered by review of ancient literature (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-01-25
    Description: Ancient Mexican botanical literature was systematically searched for new plant sources of intensely sweet substances. Lippia dulcis Trev., a sweet plant, emerged as a candidate for fractionation studies, and hernandulcin, a sesquiterpene, was isolated and judged by a human taste panel as more than 1000 times sweeter than sucrose. The structure of the sesquiterpene was determined spectroscopically and confirmed by chemical synthesis. Hernandulcin was nontoxic when administered orally to mice, and it did not induce bacterial mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Compadre, C M -- Pezzuto, J M -- Kinghorn, A D -- Kamath, S K -- N01-DE-02425/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):417-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3880922" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bibliography as Topic ; Botany/history ; Chemistry ; History, 16th Century ; Humans ; Magnetic Resonance Spectroscopy ; Mexico ; Mice ; Molecular Conformation ; Mutagenicity Tests ; *Plants/analysis ; *Sesquiterpenes/chemical synthesis/isolation & purification/toxicity ; *Sweetening Agents/chemical synthesis/history/isolation & purification/toxicity
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  • 23
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    Computer-assisted analysis in organic synthesis (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-04-26
    Description: The planning of alternative routes for the synthesis of complex organic molecules has been facilitated by the formulation of guiding strategies that can be applied to a broad range of problems. Analysis of organic synthesis can be carried out in the retrosynthetic direction, opposite to the actual process of chemical synthesis, or bidirectionally, that is, as a combined retrosynthetic and synthetic search. An interactive computer program is described which utilizes the general strategies of retrosynthetic analysis and an appropriate database to generate pathways of chemical intermediates for chemical synthesis of a particular target structure. Computer graphics and standard chemical structures are used for man-machine communication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, E J -- Long, A K -- Rubenstein, S D -- New York, N.Y. -- Science. 1985 Apr 26;228(4698):408-18.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838594" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Chemistry, Organic/*methods ; *Computers ; Forecasting ; Software
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    Dynamics and conformational energetics of a peptide hormone: vasopressin (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-03-15
    Description: A theoretical methodology for use in conjunction with experiment was applied to the neurohypophyseal hormone lysine vasopressin for elucidation of its accessible molecular conformations and associated flexibility, conformational transitions, and dynamics. Molecular dynamics and energy minimization techniques make possible a description of the conformational properties of a peptide in terms of the precise positions of atoms, their fluctuations in time, and the interatomic forces acting on them. Analysis of the dynamic trajectory of lysine vasopressin shows the ability of a flexible peptide hormone to undergo spontaneous conformational transitions. The excursions of an individual phenylalanine residue exemplify the dynamic flexibility and multiple conformational states available to small peptide hormones and their component residues, even within constraints imposed by a cyclic hexapeptide ring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagler, A T -- Osguthorpe, D J -- Dauber-Osguthorpe, P -- Hempel, J C -- New York, N.Y. -- Science. 1985 Mar 15;227(4692):1309-15.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3975616" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Chemistry, Physical ; Energy Metabolism ; Hydrogen Bonding ; Lypressin/*metabolism ; Phenylalanine/metabolism ; Physicochemical Phenomena ; Protein Conformation
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  • 25
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    Single-carbon chemistry of acetogenic and methanogenic bacteria (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-03-08
    Description: Methanogenic and acetogenic bacteria metabolize carbon monoxide, methanol, formate, hydrogen and carbon dioxide gases and, in the case of certain methanogens, acetate, by single-carbon (C1) biochemical mechanisms. Many of these reactions occur while the C1 compounds are linked to pteridine derivatives and tetrapyrrole coenzymes, including corrinoids, which are used to generate, reduce, or carbonylate methyl groups. Several metalloenzymes, including a nickel-containing carbon monoxide dehydrogenase, are used in both catabolic and anabolic oxidoreductase reactions. We propose biochemical models for coupling carbon and electron flow to energy conservation during growth on C1 compounds based on the carbon flow pathways inherent to acetogenic and methanogenic metabolism. Biological catalysts are therefore available which are comparable to those currently in use in the Monsanto process. The potentials and limitations of developing biotechnology based on these organisms or their enzymes and coenzymes are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zeikus, J G -- Kerby, R -- Krzycki, J A -- 144-T263/PHS HHS/ -- New York, N.Y. -- Science. 1985 Mar 8;227(4691):1167-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3919443" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/*metabolism ; Acetobacter/metabolism ; Bacteria/*metabolism ; Carbon Dioxide/metabolism ; Carbon Monoxide/metabolism ; Chemical Phenomena ; Chemistry ; Clostridium/metabolism ; Eubacterium/metabolism ; Euryarchaeota/*metabolism ; Formates/metabolism ; Methane/metabolism ; Methanol/metabolism
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  • 26
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    Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-03-22
    Description: Glutathione reductase from trypanosomes and leishmanias, unlike glutathione reductase from other organisms, requires an unusual low molecular weight cofactor for activity. The cofactor was purified from the insect trypanosomatid Crithidia fasciculata and identified as a novel glutathione-spermidine conjugate, N1,N8-bis(L-gamma-glutamyl-L-hemicystinyl-glycyl)spermidine, for which the trivial name trypanothione is proposed. This discovery may open a new chemotherapeutic approach to trypanosomiasis and leishmaniasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fairlamb, A H -- Blackburn, P -- Ulrich, P -- Chait, B T -- Cerami, A -- 1 R01 A127429/PHS HHS/ -- 1 R01 AI19428/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Mar 22;227(4693):1485-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3883489" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chemical Phenomena ; Chemistry ; Coenzymes/analysis/*isolation & purification/metabolism ; Crithidia/*enzymology ; Glutathione/*analogs & derivatives/analysis/isolation & purification/metabolism ; Glutathione Reductase/*metabolism ; Leishmania/*enzymology ; Oxidation-Reduction ; Spermidine/*analogs & derivatives/analysis/isolation & purification/metabolism ; Terminology as Topic ; Trypanosoma/*enzymology ; Trypanosoma brucei brucei/enzymology ; Trypanosoma cruzi/enzymology
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  • 27
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    Mechanisms of coenzyme B12-dependent rearrangements (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-22
    Description: Coenzyme B12 serves as a cofactor in various enzymatic reactions in which a hydrogen atom is interchanged with a substituent on an adjacent carbon atom. Measurement of the dissociation energy of the coenzyme's cobalt-carbon bond and studies of the rearrangement of model free radicals related to those derived from methylmalonyl-coenzyme A suggest that these enzymatic reactions occur through homolytic dissociation of the coenzyme's cobalt-carbon bond, abstraction of a hydrogen atom from the substrate by the coenzyme-derived 5'-deoxyadenosyl radical, and rearrangement of the resulting substrate radical. The only role thus far identified for coenzyme B12 in these reactions--namely, that of a free radical precursor--reflects the weakness, and facile dissociation, of the cobalt-carbon bond.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halpern, J -- New York, N.Y. -- Science. 1985 Feb 22;227(4689):869-75.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857503" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon/metabolism ; Chemical Phenomena ; Chemistry ; Chemistry, Physical ; Cobalt/metabolism ; Cobamides/*metabolism ; Energy Metabolism ; Free Radicals ; Methylmalonyl-CoA Mutase/metabolism ; Physicochemical Phenomena
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    The structure of arthropod hemocyanins (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-08-09
    Description: Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly striking in the second domain of the subunit that contains the six histidines which ligate the two oxygen-binding copper atoms. The polypeptide architecture of spiny lobster hemocyanin appears to be the same in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, about 540 to 600 million years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linzen, B -- Soeter, N M -- Riggs, A F -- Schneider, H J -- Schartau, W -- Moore, M D -- Yokota, E -- Behrens, P Q -- Nakashima, H -- Takagi, T -- GM 21314/GM/NIGMS NIH HHS/ -- GM 28410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):519-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023698" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arachnida/genetics ; *Arthropods/genetics ; Binding Sites ; Biological Evolution ; Chemical Phenomena ; Chemistry ; Copper ; Crustacea/genetics ; *Hemocyanin/genetics ; Models, Molecular ; Protein Conformation ; Species Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 29
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    [2 + 2] photocycloadditions in the synthesis of chiral molecules (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-02-22
    Description: A strategy for the synthesis of chiral molecules that receives growing popularity among organic chemists employs the photochemically mediated [2 + 2] cycloaddition reaction. These reactions can be performed on a multigram scale and often proceed with high yield and with stereocontrol. These features, in combination with the useful properties of the four-membered ring photoproducts in subsequent chemical transformations, make them attractive options in the early stage of a synthesis design. Various combinations of unsaturated functional groups can participate in this reaction process. Accordingly, these chemical reactions can be economical solutions to problems relating to the synthesis of a variety of target molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schreiber, S L -- GM-32527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 22;227(4689):857-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4038558" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/chemical synthesis ; Antifungal Agents/chemical synthesis ; Chemical Phenomena ; Chemistry ; Cockroaches ; Female ; Furans/chemical synthesis ; Lactones/chemical synthesis ; Male ; Mycotoxins/chemical synthesis ; *Photochemistry ; Pyrones/chemical synthesis ; Sex Attractants/chemical synthesis/isolation & purification ; Stereoisomerism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 30
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    Computerized pattern recognition: a new technique for the analysis of chemical communication (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-12
    Description: Computerized pattern recognition techniques can be applied to the study of complex chemical communication systems. Analysis of high resolution gas chromatographic concentration patterns of the major volatile components of the scent marks of a South American primate, Saguinus fuscicollis, demonstrates that the concentration patterns can be used to predict the gender and subspecies of unknown donors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, A B 3rd -- Belcher, A M -- Epple, G -- Jurs, P C -- Lavine, B -- 5 T32 NSO7176-03/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 12;228(4696):175-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3975636" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chemical Phenomena ; Chemistry ; Chromatography, Gas ; *Computers ; Female ; Male ; *Pattern Recognition, Automated ; Pheromones/*physiology ; Saguinus/physiology ; Scent Glands/physiology ; Sex Attractants/*physiology ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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