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  • Chemistry
  • American Association for the Advancement of Science (AAAS)  (23)
  • Springer  (3)
  • American Chemical Society
  • Elsevier
  • International Union of Crystallography
  • 2000-2004  (2)
  • 1985-1989  (24)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (23)
  • Springer  (3)
  • American Chemical Society
  • Elsevier
  • International Union of Crystallography
    • +
Years
Year
  • 1
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    The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-09-19
    Description: WIN 51711 and WIN 52084 are structurally related, antiviral compounds that inhibit the replication of rhino (common cold) viruses and related picornaviruses. They prevent the pH-mediated uncoating of the viral RNA. The compounds consist of a 3-methylisoxazole group that inserts itself into the hydrophobic interior of the VP1 beta-barrel, a connecting seven-membered aliphatic chain, and a 4-oxazolinylphenoxy group (OP) that covers the entrance to an ion channel in the floor of the "canyon." Viral disassembly may be inhibited by preventing the collapse of the VP1 hydrophobic pocket or by blocking the flow of ions into the virus interior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, T J -- Kremer, M J -- Luo, M -- Vriend, G -- Arnold, E -- Kamer, G -- Rossmann, M G -- McKinlay, M A -- Diana, G D -- Otto, M J -- New York, N.Y. -- Science. 1986 Sep 19;233(4770):1286-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3018924" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/metabolism/*pharmacology ; Binding Sites ; Chemical Phenomena ; Chemistry ; Humans ; Isoxazoles/metabolism/pharmacology ; Poliovirus/drug effects/metabolism ; Rhinovirus/*drug effects/metabolism ; X-Ray Diffraction
    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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  • 2
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    Aromatic cross-links in insect cuticle: detection by solid-state 13C and 15N NMR (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-06
    Description: Cross-polarization magic-angle-spinning nuclear magnetic resonance spectroscopy has been used to determine insect cuticle composition and cross-link structure during sclerotization or tanning. Unsclerotized cuticle from newly ecdysed pupae of the tobacco hornworm, Manduca sexta L., had a high protein content with lesser amounts of lipid and chitin. Concentrations of chitin, protein, and catechol increased substantially as dehydration and sclerotization progressed. Analysis of intact cuticle specifically labeled with carbon-13 and nitrogen-15 revealed direct covalent linkages between ring nitrogens of protein histidyl residues and ring carbons derived from the catecholamine dopamine. This carbon-nitrogen adduct was present in chitin isolated from cuticle by alkaline extraction and is probably bound covalently to chitin. These data support the hypothesis that the stiffening of insect cuticle during sclerotization results primarily from the deposition of protein and chitin polymers and their crosslinking by quinonoid derivatives of catecholamines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaefer, J -- Kramer, K J -- Garbow, J R -- Jacob, G S -- Stejskal, E O -- Hopkins, T L -- Speirs, R D -- New York, N.Y. -- Science. 1987 Mar 6;235(4793):1200-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823880" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbon Isotopes ; Chemical Phenomena ; Chemistry ; Cross-Linking Reagents/*metabolism ; Insects/*metabolism ; Magnetic Resonance Spectroscopy ; Nitrogen Isotopes ; Skin/*metabolism
    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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  • 3
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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
    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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  • 4
    Electronic Resource
    Electronic Resource
    Etoposide and teniposide (1988)
    Springer
    Pharmacy world & science 10 (1988), S. 101-116 
    Details
    ISSN: 1573-739X
    Keywords: Chemistry ; Chromatography ; Etoposide ; Immunoassay ; Metabolism ; Podophyllotoxin ; Pharmacokinetics ; Teniposide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Etoposide (VP 16-213) and teniposide (VM 26) are semisynthetic epipodophyllotoxin derivatives active against a variety of tumours. The clinical efficacy has led to an increasing interest in these compounds. This review presents information on the mechanism of action, biochemical pharmacology, bioanalysis, metabolism and pharmacokinetics of etoposide and teniposide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01959294
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  • 5
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    Three-dimensional structure of poliovirus at 2.9 A resolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 6
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    Dynamics and conformational energetics of a peptide hormone: vasopressin (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 7
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    Single-carbon chemistry of acetogenic and methanogenic bacteria (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 8
    Electronic Resource
    Electronic Resource
    Eupatorium cannabinum L. (1986)
    Springer
    Pharmacy world & science 8 (1986), S. 245-251 
    Details
    ISSN: 1573-739X
    Keywords: Analysis ; Antineoplastic agents ; Biosynthesis ; Botany ; Chemistry ; Cytotoxins ; Eupatorium cannabium ; Sesquiterpenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A review onEupatorium cannabinum L. is given, including botany, history and constituents. The sesquiterpene lactones are discussed in more detail, covering their biosynthesis, isolation, analysis and biological activity. Special attention is paid to the cytotoxic and antitumour activities of the sesquiterpene lactones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01960068
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  • 9
    Electronic Resource
    Electronic Resource
    Shower Meteoroids: Constraints From Interplanetary Dust Particles And Leonid Meteors (2000)
    Springer
    Earth, moon and planets 88 (2000), S. 35-58 
    Details
    ISSN: 1573-0794
    Keywords: Chemistry ; interplanetary dust particles (IDPs) ; Leonids ; meteor trails ; meteoroids ; meteors ; structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The cometary Leonid meteoroids represent a size range in between largest carbon-richIDPs and the smallest CI meteorites. Their dustball structure and chemistry offer anopportunity to constrain hierarchical dust accretion inferred from petrologic studies ofaggregate and cluster IDPs. The Leonid shower meteoroids of known ``comet ejection''ages provide an opportunity to study space weathering of cometary dust over periodsof up to several hundred years. The meteors and aggregate and cluster IDPs displaycontinuous thermal modification of organics and volatile element (Na, K-bearing phases), that occur as discrete minerals and amorphous solids each different response during kinetically controlled ablation. Leonid meteoroids are not excessively Na-rich. The occurrences of Leonid meteors can now be accurate predicted and combined withknowledge better models for the settling rates, collections of surviving dust becomea comet nucleus-sampling mission.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1013862627781
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  • 10
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    Patent law. Natural substances and patentable inventions (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Demaine, Linda J -- Fellmeth, Aaron X -- New York, N.Y. -- Science. 2003 May 30;300(5624):1375-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉RAND, Santa Monica, CA 90401, USA. demaine@rand.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12775825" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Oxide ; Chemical Phenomena ; Chemistry ; Natural Science Disciplines ; Patents as Topic/*legislation & jurisprudence ; Plant Extracts ; Plant Roots ; Titanium ; United States
    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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