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  • Polymer and Materials Science  (5)
  • Amino Acid Sequence  (4)
  • 2005-2009
  • 1995-1999  (9)
  • 1990-1994
  • 1996  (9)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 62 (1996), S. 2237-2245 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Composition, tacticity, and processing history can affect the morphology of semicrystalline polymers. Although homopolyamides are a family of polymers well known for semicrystalline character, through copolymerization or multicomponent copolymerization significant changes in materials' crystalline and thermal properties can occur. Due to chain irregularities introduced by terpolymerization, differential scanning calorimetry shows RDG 114T, a commercial polyamide of nylon-6, -6/6, and 12, to have an atypically low Tm and exhibit interesting recrystallization behavior. Specifically, the polyamide is wholly amorphous upon cooling from the melt, and since its Tg is about 20°C (due to the presence of plasticizers), chain ordering is found to occur over time at room temperature. Since the polyamide's morphology is time-dependent, the tensile properties of the polymer are also found to vary with ambient aging. For instance, Young's moduli for an amorphous and 7-day room temperature-annealed sample are 1.3×102 and 2.8×102 MPa, respectively. © 1996 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Macromolecular Rapid Communications 17 (1996), S. 897-903 
    ISSN: 1022-1336
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Aromatic polyamides were prepared by an AlCl3 or HCl-catalyzed polymerization of toluene diisocyanate or methylenebis(phenyl isocyanate) with adipic acid at low temperatures (≤100°C) in a short reaction time (3-4 h). The intrinsic viscosity of the polymers was approximately 1.1 dL/g as determined at 25°C with m-cresol as solvent, indicating that the polyamides obtained by this method have relatively high molecular weights. The polymers exhibit high glass transition temperatures and good thermal stability.
    Additional Material: 3 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Macromolecular Chemistry and Physics 197 (1996), S. 3123-3133 
    ISSN: 1022-1352
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: A series of α-methylene-N-alkyl-2-pyrrolidone monomers with varying length of the alkyl chain from C1 to C8 were synthesised. The monomers were subjected to free radical polymerisation to yield a range of polymers each with a different balance in hydrophobic/hydrophilic properties originating from the pyrrolidone moiety and the N-alkyl chain. The equilibrium water content of polymers crosslinked with ethylene dimethacrylate were found to decrease with increasing alkyl chain length. The glass transition temperatures of the polymers are reported ranging from 98°C to -5°C on going from the methyl to the octyl derivative. The thermal degradation of the polymers was studied using thermogravimetric analysis and pyrolysis gas chromatography-mass spectroscopy. The polymers were found to degrade at ca. 400°C predominantly via an unzipping mechanism. Pyrolysis at 450°C results in five products.
    Additional Material: 2 Ill.
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  • 4
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The side chain of Tyr and Phe was fixed into the gauche (-) or gauche (+) conformation by using the Tic or Htc structures, and into the trans conformation by using an aminobenzazepine-type (Aba) structure. When incorporated into dermorphin or deltorphin II, the Tic and Htc analogues all showed a large decrease in both μ and δ affinities and activities. Fixation of Phe3 in the trans rotamer resulted in a large increase in δ affinity in the dermorphin analogue, whereas in the [Aba3-Gly4] deltorphin II analogue, good δ affinity is maintained despite the removal of the Glu side chain. Whereas several authors propose a gauche (-) preferred conformation for the Phe3 side chain, these results suggest a trans conformation at the δ receptor. The use of these conformationally constrained residues for evaluating the preferred solution conformation in the flexible N-terminal tripeptide Tyr-D-Ala-Phe is illustrated. The 1H-nmr parameters - chemical shift, temperature dependence, and nuclear Overhauser effects to the D-Ala2 methyl protons in the different analogues - provide direct evidence to confirm the proposed sandwich conformation in the native peptides. © 1996 John Wiley & Sons, Inc.
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  • 5
    ISSN: 0142-2421
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The photoionization efficiency of secondary neutral atoms from metal surfaces has been investigated by very intense (∽1014 W cm-2) and short-pulsed (∽200 fs) 248 nm laser radiation. Surface erosion of the samples was performed by Ar+ ion sputtering and by laser desorption (LD) from an N2 gas laser. Five polycrystalline samples (Al, Cu, Zr, In and Au) have been analyzed with respect to their ionization efficiency and LD yields. In order to estimate the desorption yield, we determined the useful yield of our time-of-flight (ToF) mass spectrometer by ion sputtering, followed by laser postionization with 193 nm radiation from an ArF excimer laser. The applied femtosecond pulse, high-intensity 248 nm laser radiation has been found to be an excellent source of non-selective photoionization. For each material in this study a large fraction of doubly ionized atoms was observed; the measurements on Au have also shown triply ionized atoms. For some spectra, the number of doubly ionized atoms was even higher than for singly ionized atoms. We have estimated that the useful yields for LD are significantly higher than the values observed in ion sputtering.
    Additional Material: 8 Ill.
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  • 6
    Publication Date: 1996-06-21
    Description: ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR). Deletion analysis demonstrated that this binding interaction is mediated by the zinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase. Treatment of mammalian cells with EGF caused decreased binding of ZPR1 to the EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF to regulate ZPR1 binding is dependent on tyrosine phosphorylation of the EGFR. ZPR1 therefore represents a prototype for a class of molecule that binds to the EGFR and is released from the receptor after activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Konstantinov, K N -- Wu, I H -- Klier, F G -- Barrett, T -- Davis, R J -- R01-CA58396/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1797-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650580" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*metabolism/secretion ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytoplasm/metabolism ; Epidermal Growth Factor/pharmacology ; Humans ; Immunoblotting ; Male ; Mice ; Molecular Sequence Data ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Structure, Secondary ; RNA, Messenger/genetics/metabolism ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Testis/metabolism ; Type C Phospholipases/metabolism ; Vanadates/pharmacology ; *Zinc Fingers ; src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1996-03-29
    Description: Upon contacting its postsynaptic target, a neuronal growth cone transforms into a presynaptic terminal. A membrane component on the growth cone that facilitates synapse formation was identified by means of a complementary DNA-based screen followed by genetic analysis. The late bloomer (lbl) gene in Drosophila encodes a member of the tetraspanin family of cell surface proteins. LBL protein is transiently expressed on motor axons, growth cones, and terminal arbors. In lbl mutant embryos, the growth cone of the RP3 motoneuron contacts its target muscles, but synapse formation is delayed and neighboring motoneurons display an increase in ectopic sprouting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kopczynski, C C -- Davis, G W -- Goodman, C S -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1867-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596956" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/metabolism/ultrastructure ; Cloning, Molecular ; Drosophila/embryology/genetics/physiology ; *Drosophila Proteins ; *Genes, Insect ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Motor Neurons/cytology/metabolism/*physiology ; Muscles/innervation ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*physiology ; Neuromuscular Junction/*physiology ; Presynaptic Terminals/*physiology/ultrastructure ; Signal Transduction
    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
    Publication Date: 1996-10-04
    Description: Identification and characterization of antigen-specific T lymphocytes during the course of an immune response is tedious and indirect. To address this problem, the peptide-major histocompatability complex (MHC) ligand for a given population of T cells was multimerized to make soluble peptide-MHC tetramers. Tetramers of human lymphocyte antigen A2 that were complexed with two different human immunodeficiency virus (HIV)-derived peptides or with a peptide derived from influenza A matrix protein bound to peptide-specific cytotoxic T cells in vitro and to T cells from the blood of HIV-infected individuals. In general, tetramer binding correlated well with cytotoxicity assays. This approach should be useful in the analysis of T cells specific for infectious agents, tumors, and autoantigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, J D -- Moss, P A -- Goulder, P J -- Barouch, D H -- McHeyzer-Williams, M G -- Bell, J I -- McMichael, A J -- Davis, M M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305-5428, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810254" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*immunology ; Base Sequence ; CD8-Positive T-Lymphocytes/immunology ; Cell Line ; Coloring Agents ; Epitopes/immunology ; Flow Cytometry ; Gene Products, gag/immunology ; HIV Seropositivity/*immunology ; HLA-A2 Antigen/*immunology ; Humans ; Molecular Sequence Data ; Peptide Fragments/*immunology ; Phenotype ; RNA-Directed DNA Polymerase/immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Viral Matrix Proteins/immunology
    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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  • 9
    Publication Date: 1996-10-25
    Description: The genome of the yeast Saccharomyces cerevisiae has been completely sequenced through a worldwide collaboration. The sequence of 12,068 kilobases defines 5885 potential protein-encoding genes, approximately 140 genes specifying ribosomal RNA, 40 genes for small nuclear RNA molecules, and 275 transfer RNA genes. In addition, the complete sequence provides information about the higher order organization of yeast's 16 chromosomes and allows some insight into their evolutionary history. The genome shows a considerable amount of apparent genetic redundancy, and one of the major problems to be tackled during the next stage of the yeast genome project is to elucidate the biological functions of all of these genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goffeau, A -- Barrell, B G -- Bussey, H -- Davis, R W -- Dujon, B -- Feldmann, H -- Galibert, F -- Hoheisel, J D -- Jacq, C -- Johnston, M -- Louis, E J -- Mewes, H W -- Murakami, Y -- Philippsen, P -- Tettelin, H -- Oliver, S G -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):546, 563-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Universite Catholique de Louvain, Unite de Biochimie Physiologique, Place Croix du Sud, 2/20, 1348 Louvain-la-Neuve, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849441" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Fungal/genetics ; Computer Communication Networks ; DNA, Fungal/genetics ; Evolution, Molecular ; Fungal Proteins/chemistry/genetics/physiology ; Gene Library ; *Genes, Fungal ; *Genome, Fungal ; International Cooperation ; Multigene Family ; Open Reading Frames ; RNA, Fungal/genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Analysis, DNA
    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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