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  • Kinetics  (66)
  • American Association for the Advancement of Science (AAAS)  (59)
  • Springer  (7)
  • American Institute of Physics (AIP)
  • National Academy of Sciences
  • 1990-1994  (66)
  • 1975-1979
  • 1960-1964
  • 1992  (66)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (59)
  • Springer  (7)
  • American Institute of Physics (AIP)
  • National Academy of Sciences
  • Wiley-Blackwell  (3)
Years
  • 1990-1994  (66)
  • 1975-1979
  • 1960-1964
Year
  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of the solvolysis of chloropentacyanocobaltate(III) ions in water + 2-propanol mixtures (1992)
    Springer
    Journal of solution chemistry 21 (1992), S. 93-103 
    Details
    ISSN: 1572-8927
    Keywords: Kinetics ; solvolysis ; complex ions ; solvent mixtures
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Rates of solvolysis of [Co(CN) 5 Cl] 3− have been determined in a range of water-rich water + 2-propanol mixtures over a range of temperatures and they show no simple correlation with dielectric constant. The variation of the enthalpy and entropy of activation with solvent composition show broad extrema and these are discussed in relation to the physical properties of the media. The application of a free energy cycle to the dissociative loss of the chloride ion in the transition state shows that the effect of changes in solvent structure as the alcohol content increases is to stabilize the emergent pentacyanocobaltate(III) ion Co(CN) 5 2− relative to the chloropentacyanocobaltate(III) anion in the initial state.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00648982
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  • 2
    Electronic Resource
    Electronic Resource
    Zur Kinetik der Reaktion von Aluminium(III) mit Chromotropsäure in wäßrigem Chloressigsäure-Medium (1992)
    Springer
    Monatshefte für Chemie 123 (1992), S. 291-299 
    Details
    ISSN: 1434-4475
    Keywords: Aluminium(III) ; Chloroacetate buffer ; Chromotropic acid ; Kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The kinetics of the reaction of aluminium(III) with chromotropic acid (H4 L) by formation of the complex AlL − was studied in the range ofpH=(2.34...3.23) and by variation of the buffer addition to the Al(III) solution. The results leads to a reaction scheme with the species AlOH2+, Al(OH)2 + and H2 L 2− in Al(III) solutions “not prebuffered”, in Al(III) solutions “prebuffered” additionally the species AlClac 2−. The difference in the course of the functionsk exp =f[c 0(Al);c(H+)] in the Al(III) solutions not prebuffered respective prebuffered was explained: Chromotrophic acid as de facto neutral ligand does not react — contrary to the anionic ligands — with the dimeric Al(III) species present in the Al(III) solutions prebuffered. Water exchange rate constants for the contributing species according to the Eigen-Tamm-model were evaluated and correspond very well with the expected values.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00810939
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  • 3
    Electronic Resource
    Electronic Resource
    Enzyme formation by a yeast cell wall lytic Arthrobacter species: formation of amylase (1992)
    Springer
    Applied microbiology and biotechnology 38 (1992), S. 214-219 
    Details
    ISSN: 1432-0614
    Keywords: Amylase ; Arthrobacter sp. ; Kinetics ; Yeast glykogen ; Trehalose ; Maltose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The kinetics of amylolytic enzyme formation by a yeast cell wall lytic Arthrobacter species were studied. Cultivation on autoclaved cells of baker's yeast showed that amylase formation was closely related to trehalose and glycogen dissimilation. Growth on yeast glycogen (0.5%) proceeded quite rapidly (μ = 0.31 h−1) with extensive amylase formation during exponential cell multiplication and a further low increase in activity during the stationary phase. Beside amylolytic activity [450 units (U) l−1] the formation of a relatively high level of α-glucosidase (90 U l−1) was detected, the latter almost exclusively bound to bacterial cells. Growth on 0.5% trehalose occurred at a reduced rate (μ = 0.22 h−1) with post-logarithmic enzyme synthesis in the stationary phase. Amylase activity attained a level of 1200 U l−1, whereas α-glucosidase was very low at 7.7 U l−1. Continuous culture experiments in the chemostat showed maximal volumetric productivity of amylase (105 U l−1 h−1) at a dilution rate of 0.15 h−1. Growth on various carbohydrates revealed low levels of amylolytic activity (〈100 U l−1), which were increased by a α-1,4-glucans and oligosaccharides such as starch, dextrin, maltotriose and maltose. On 0.5% maltose, growth-associated enzyme synthesis (230 U l−1) was detected at a reduced growth rate (μ = 0.14 h−1). Amylolytic enzyme preparations from the culture fluid showed an unusual cleavage pattern; acting on starch, the polymer was almost completely hydrolysed to maltotriose and maltose in a molar ratio of 3:1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00174471
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  • 4
    Electronic Resource
    Electronic Resource
    Kinetics of hydroxyapatite dissolution in acetic, lactic, and phosphoric acid solutions (1992)
    Springer
    Calcified tissue international 50 (1992), S. 137-143 
    Details
    ISSN: 1432-0827
    Keywords: Hydroxyapatite ; Enamel ; Dissolution ; Kinetics ; Caries
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The present study was undertaken in an attempt to relate the kinetics of hydroxyapatite dissolution to solution parameters, under experimental conditions relevant to the dental caries process. Thus, the dissolution of hydroxyapatite was studied in acetic, lactic, and dilute phosphoric acid solutions having initial pH values from 4 to 6. Rates of dissolution and the corresponding degree of saturation with respect to hydroxyapatite were determined at various times throughout the dissolution process. Rates of dissolution of all solutions were found to decrease with increasing degree of solution saturation and were greater in solutions with lower initial values of pH. However, rates of dissolution in partially saturated phosphoric acid solutions (without added organic acid) were at least one order of magnitude lower than those observed in the organic acid buffers with the same initial pH, over the same range of saturation values. The data obtained are consistent with a surface-controlled dissolution model in which the rate of dissolution is dependent upon the degree of saturation and the sum of the activities of the acidic species in solution, i.e., phosphoric and organic acids. These results suggest that in order to assess the cariogenic potential of a given medium (e.g., plaque fluid), one must determine both the degree of saturation with respect to the dissolving mineral and the activities of acidic species in solution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00298791
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  • 5
    Electronic Resource
    Electronic Resource
    Kinetics and hydrodynamics of Agapanthus umbellatus pollen-tube growth: A structural and stereological study (1992)
    Springer
    Sexual plant reproduction 5 (1992), S. 163-168 
    Details
    ISSN: 1432-2145
    Keywords: Pollen tube ; Kinetics ; Hydrodynamics ; Agapanthus sp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In vitro pollen germination of Agapanthus umbellatus follows a logistic-type curve. It has a lag phase, which corresponds to pollen grain (PG) hydration, followed by an exponential phase — initial pollentube (PT) growth. The lag phase is characterized by an increase of about 40% in the volume of the PG as a result of the hydration process. During the exponential phase the PT emerges, and 40 min later it possesses an ultrastructural organization with a typical two-layer wall and four well-defined zones: the apical, sub-apical, nuclear and vacuolar zones. In this period the material transported by the Golgi vesicles seems to be mostly incorporated into the pollen-tube wall (PTW). Stereological analysis showed that the increase in tube volume is correlated with the increase in the vacuolar compartment at the PG level. The decrease in the relative volume occupied by the mitochondria, generative cell and vegetative nucleus in the PG suggests that these organelles move to the PT. A correlation between the disappearance of lipid droplets in the lag phase and the metabolic reactions that take place during hydration is suggested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00189807
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  • 6
    Electronic Resource
    Electronic Resource
    Theoretical NMR study of the chemical exchange of amide protons of proteins (1992)
    Springer
    Journal of biomolecular NMR 2 (1992), S. 173-181 
    Details
    ISSN: 1573-5001
    Keywords: Amide proton ; Exchange rate ; Kinetics ; NOE ; Cross-relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A model is proposed to evaluate the rate of exchange between the amide protons of proteins and the solvent water molecules. Using this model we determined the extent of the error for the chemical exchange rate constant when cross relaxation was neglected; both selective inversion and saturation-transfer techniques were evaluated. Furthermore, the fluctuations in the NOE intensities were determined when the exchange rate was varied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01875528
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  • 7
    Electronic Resource
    Electronic Resource
    A model of ion channel kinetics based on deterministic, chaotic motion in a potential with two local minima (1992)
    Springer
    Annals of biomedical engineering 20 (1992), S. 517-531 
    Details
    ISSN: 1573-9686
    Keywords: Ion channel ; Kinetics ; Nonlinear dynamics ; Chaos ; Mathematical model
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Abstract Models of the gating of ion channels have usually assumed that the switching between the open and closed states is a random process without a mechanistic basis. We explored the properties of a deterministic model of channel gating based on a chaotic dynamic system. The channel is modeled as a nonlinear oscillator, that has a potential function with two minima, which correspond to the stable open and closed states, and is driven by a periodic driving force. The properties of the model are like some properties of single channel data and unlike other properties. The model is like the data in that: the current switches between two well-defined states, this switching is nonperiodic, and there are subconductance states. These subconductance states are subharmonic resonances, due to the nonlinearities in the equation of the model, rather than stable conformational states due to local minima in the potential energy. The model is not like the data in that the current fluctuates too much within in each state and there are sometimes periodic fluctuations within a state. At the present time, the selection of the most appropriate channel model (Markov, chaotic, or other) is not possible, and in addition to chaotic models, other nonlinear models may be suitable.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02368171
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  • 8
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    Diverse migratory pathways in the developing cerebral cortex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: During early development of the mammalian cerebral cortex, young neurons migrate outward from the site of their final mitosis in the ventricular zone into the cortical plate, where they form the adult cortex. Time-lapse confocal microscopy was used to observe directly the dynamic behaviors of migrating cells in living slices of developing cortex. The majority of cells migrated along a radial pathway, consistent with the view that cortical neurons migrate along radial glial fibers. A fraction of cells, however, turned within the intermediate zone and migrated orthogonal to the radial fibers. This orthogonal migration may contribute to the tangential dispersion of clonally related cortical neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Rourke, N A -- Dailey, M E -- Smith, S J -- McConnell, S K -- EY06314/EY/NEI NIH HHS/ -- NS09027/NS/NINDS NIH HHS/ -- NS28587/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):299-302.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411527" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Carbocyanines ; Cell Movement ; Cerebral Cortex/cytology/*growth & development ; Culture Techniques ; Ferrets ; Fluorescent Dyes ; Immunohistochemistry ; Kinetics ; Lasers ; Microscopy ; Neurons/*physiology ; Vimentin/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
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    Cooperativity induced by a single mutation at the subunit interface of a dimeric enzyme: glutathione reductase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-13
    Description: When glycine418 of Escherichia coli glutathione reductase, which is in a closely packed region of the dimer interface, is replaced with a bulky tryptophan residue, the enzyme becomes highly cooperative (Hill coefficient 1.76) for glutathione binding. The cooperativity is lost when the mutant subunit is hybridized with a wild-type subunit to create a heterodimer. The mutation appears to disrupt atomic packing at the dimer interface, which induces a change of kinetic mechanism. A single mutation in a region of the protein remote from the active site can thus act as a molecular switch to confer cooperativity on an enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scrutton, N S -- Deonarain, M P -- Berry, A -- Perham, R N -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439821" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Escherichia coli/*enzymology/genetics ; Genes, Bacterial ; Glutathione/metabolism ; Glutathione Reductase/*chemistry/genetics/metabolism ; Glycine/chemistry ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; *Mutagenesis, Site-Directed ; NADP/metabolism ; Plasmids ; Protein Multimerization ; Tryptophan/chemistry
    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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  • 10
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    Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: Diacylglycerols, which are generated during phospholipase-catalyzed hydrolysis of phospholipids, stimulated actin polymerization in the presence of highly purified plasma membranes from the cellular slime mold Dictyostelium discoideum. The increased rate of actin polymerization apparently resulted from de novo formation of actin nucleation sites rather than uncapping of existing filament ends, because the membranes lacked detectable endogenous actin. The increased actin nucleation was mediated by a peripheral membrane component other than protein kinase C, the classical target of diacylglycerol action. These results indicate that diacylglycerols increase actin nucleation at plasma membranes and suggest a mechanism whereby signal transduction pathways may control cytoskeletal assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shariff, A -- Luna, E J -- GM-33048/GM/NIGMS NIH HHS/ -- R01 GM033048/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):245-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology Group, Worcester Foundation for Experimental Biology, Shresbury, MA 01545.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373523" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Alkaloids/pharmacology ; Animals ; Calcium/pharmacology ; Cell Membrane/drug effects/*metabolism ; Dictyostelium/*metabolism ; Diglycerides/*pharmacology ; Kinetics ; Macromolecular Substances ; *Naphthalenes ; Polycyclic Compounds/pharmacology ; Protein Kinase C/antagonists & inhibitors ; Staurosporine ; Tetradecanoylphorbol Acetate/pharmacology ; Time Factors
    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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  • 11
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    DNA hydrolyzing autoantibodies (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-01
    Description: A DNA-nicking activity was detected in the sera of patients with various autoimmune pathologies and was shown to be a property of autoantibodies. The DNA hydrolyzing activity, which was purified by affinity and high-performance liquid chromatography, corresponded in size to immunoglobulin M (IgM) and IgG and had a positive response to antibodies to human IgG. The DNA hydrolyzing autoantibodies were stable to acid shock and yielded a DNA degradation pattern that was different from that of deoxyribonuclease (DNase) I and blood DNase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuster, A M -- Gololobov, G V -- Kvashuk, O A -- Bogomolova, A E -- Smirnov, I V -- Gabibov, A G -- New York, N.Y. -- Science. 1992 May 1;256(5057):665-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉V.A. Engelhardt Institute of Molecular Biology, Academy of Sciences of Russia, Moscow.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585181" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/pharmacology ; Acetic Acid ; Autoantibodies/isolation & purification/*metabolism ; Autoimmune Diseases/*metabolism ; Chromatography, High Pressure Liquid ; DNA/*metabolism ; DNA Polymerase I/metabolism ; Deoxyribonuclease I/metabolism ; Electrophoresis, Agar Gel ; Humans ; Immunoglobulin G/isolation & purification/metabolism ; Immunoglobulin M/isolation & purification/metabolism ; Kinetics ; Lupus Erythematosus, Systemic/immunology ; Plasmids
    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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  • 12
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    Cloning and expression in yeast of a plant potassium ion transport system (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-01
    Description: A membrane polypeptide involved in K+ transport in a higher plant was cloned by complementation of a yeast mutant defective in K+ uptake with a complementary DNA library from Arabidopsis thaliana. A 2.65-kilobase complementary DNA conferred ability to grow on media with K+ concentration in the micromolar range and to absorb K+ (or 86Rb+) at rates similar to those in wild-type yeast. The predicted amino acid sequence (838 amino acids) has three domains: a channel-forming region homologous to animal K+ channels, a cyclic nucleotide-binding site, and an ankyrin-like region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sentenac, H -- Bonneaud, N -- Minet, M -- Lacroute, F -- Salmon, J M -- Gaymard, F -- Grignon, C -- New York, N.Y. -- Science. 1992 May 1;256(5057):663-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochimie et Physiologie Vegetales, ENSA-M/INRA/CNRS URA 573, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Arabidopsis Proteins ; Biological Transport ; Blotting, Southern ; Carrier Proteins/chemistry/genetics ; *Cloning, Molecular ; DNA/genetics ; Deoxyribonuclease EcoRI ; Gene Expression ; Kinetics ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics ; Plants/*genetics ; Potassium/*metabolism ; Potassium Channels/chemistry/*genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Homology, Nucleic Acid
    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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  • 13
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    Pseudo--half-knot formation with RNA (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: A pseudo--half-knot can be formed by binding an oligonucleotide asymmetrically to an RNA hairpin loop. This binding motif was used to target the human immunodeficiency virus TAR element, an important viral RNA structure that is the receptor for Tat, the major viral transactivator protein. Oligonucleotides complementary to different halves of the TAR structure bound with greater affinity than molecules designed to bind symmetrically around the hairpin. The pseudo--half-knot--forming oligonucleotides altered the TAR structure so that specific recognition and binding of a Tat-derived peptide was disrupted. This general binding motif may be used to disrupt the structure of regulatory RNA hairpins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ecker, D J -- Vickers, T A -- Bruice, T W -- Freier, S M -- Jenison, R D -- Manoharan, M -- Zounes, M -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):958-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ISIS Pharmaceuticals, Carlsbad, CA 92008.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502560" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA, Viral/metabolism ; Gene Products, tat/metabolism ; HIV/*genetics ; Kinetics ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/*chemistry ; RNA, Viral/*chemistry/genetics/metabolism ; tat Gene Products, Human Immunodeficiency Virus
    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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  • 14
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    G protein activation of a hormone-stimulated phosphatase in human tumor cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The growth-inhibiting peptide hormone somatostatin stimulates phosphotyrosine phosphatase activity in the human pancreatic cell line MIA PaCa-2. This hormonal activation was mediated by a pertussis toxin-sensitive guanosine 5'-triphosphate-binding protein (G protein) in the membranes of these cells. Activation of this G protein by somatostatin stimulated the dephosphorylation of exogenous epidermal growth factor receptor prepared from A-431 cells in vitro. This pathway may mediate the antineoplastic action of somatostatin in these cells and in human tumors and could represent a general mechanism of G protein coupling that is utilized by normal cells in the hormonal control of cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pan, M G -- Florio, T -- Stork, P J -- New York, N.Y. -- Science. 1992 May 22;256(5060):1215-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350382" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Carcinoma, Squamous Cell ; Cell Line ; Cell Membrane/metabolism ; Dose-Response Relationship, Drug ; Enzyme Activation ; GTP-Binding Proteins/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/analogs & derivatives/pharmacology ; Humans ; Kinetics ; Pancreatic Neoplasms ; Peptides/metabolism ; Pertussis Toxin ; Phosphorylation ; Protein Kinases/metabolism ; Protein Tyrosine Phosphatases/*metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Somatostatin/*pharmacology ; Thionucleotides/pharmacology ; Virulence Factors, Bordetella/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Dimerization of a specific DNA-binding protein on the DNA (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-10
    Description: Many specific DNA-binding proteins bind to sites with dyad symmetry, and the bound form of the protein is a dimer. For some proteins, dimers form in solution and bind to DNA. LexA repressor of Escherichia coli has been used to test an alternative binding model in which two monomers bind sequentially. This model predicts that a repressor monomer should bind with high specificity to an isolated operator half-site. Monomer binding to a half-site was observed. A second monomer bound to an intact operator far more tightly than the first monomer; this cooperativity arose from protein-protein contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, B -- Little, J W -- GM24178/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):203-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Arizona, Tucson 85721.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553548" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; Base Sequence ; Binding Sites ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonucleases ; Escherichia coli/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Structural ; Molecular Sequence Data ; Oligodeoxyribonucleotides/metabolism ; Operon ; Rec A Recombinases/genetics ; Repressor Proteins/metabolism ; *Serine Endopeptidases
    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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  • 16
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    Converting trypsin to chymotrypsin: the role of surface loops (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-06
    Description: Trypsin (Tr) and chymotrypsin (Ch) have similar tertiary structures, yet Tr cleaves peptides at arginine and lysine residues and Ch prefers large hydrophobic residues. Although replacement of the S1 binding site of Tr with the analogous residues of Ch is sufficient to transfer Ch specificity for ester hydrolysis, specificity for amide hydrolysis is not transferred. Trypsin is converted to a Ch-like protease when the binding pocket alterations are further modified by exchange of the Ch surface loops 185 through 188 and 221 through 225 for the analogous Tr loops. These loops are not structural components of either the S1 binding site or the extended substrate binding sites. This mutant enzyme is equivalent to Ch in its catalytic rate, but its substrate binding is impaired. Like Ch, this mutant utilizes extended substrate binding to accelerate catalysis, and substrate discrimination occurs during the acylation step rather than in substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedstrom, L -- Szilagyi, L -- Rutter, W J -- DK21344/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1249-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Research Institute, University of California, San Francisco 94143-0534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546324" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chymotrypsin/*chemistry/metabolism ; Hydrolysis ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Protein Conformation ; Substrate Specificity ; Trypsin/*chemistry/genetics/metabolism
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  • 17
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    Removal of nonhomologous DNA ends in double-strand break recombination: the role of the yeast ultraviolet repair gene RAD1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-16
    Description: Double-strand breaks (DSBs) in Saccharomyces cerevisiae can be repaired by gene conversions or by deletions resulting from single-strand annealing between direct repeats of homologous sequences. Although rad1 mutants are resistant to x-rays and can complete DSB-mediated mating-type switching, they could not complete recombination when the ends of the break contained approximately 60 base pairs of nonhomology. Recombination was restored when the ends of the break were made homologous to donor sequences. Additionally, the absence of RAD1 led to the frequent appearance of a previously unobserved type of recombination product. These data suggest RAD1 is required to remove nonhomologous DNA from the 3' ends of recombining DNA, a process analogous to the excision of photodimers during repair of ultraviolet-damaged DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fishman-Lobell, J -- Haber, J E -- GM01722/GM/NIGMS NIH HHS/ -- GM20056/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 16;258(5081):480-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411547" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Repair ; DNA, Fungal/genetics ; Deoxyribonucleases, Type II Site-Specific/*metabolism ; Gene Conversion ; Kinetics ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Ultraviolet Rays
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  • 18
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    Antibody-catalyzed rearrangement of the peptide bond (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-30
    Description: The generation of antibodies from a bifunctional cyclic phosphinate transition-state analog provided agents capable of efficiently catalyzing both steps of the overall conversion of a substrate containing an asparaginyl-glycyl sequence through a succinimide intermediate to the products aspartyl-glycyl and the rearranged isoaspartyl-glycyl sequence. This reaction provides a potential means in addition to amide cleavage for the deactivation of protein or peptide biological functions in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbs, R A -- Taylor, S -- Benkovic, S J -- New York, N.Y. -- Science. 1992 Oct 30;258(5083):803-5.〈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/1439788" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/*metabolism ; Asparagine/metabolism ; Aspartic Acid/metabolism ; Chromatography, High Pressure Liquid ; Dipeptides/metabolism ; Glycine/metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Peptides/chemistry/*metabolism ; Stereoisomerism ; Succinimides/metabolism
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  • 19
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    Tertiary structure around the guanosine-binding site of the Tetrahymena ribozyme (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-24
    Description: A cleavage reagent directed to the active site of the Tetrahymena catalytic RNA was synthesized by derivatization of the guanosine substrate with a metal chelator. When complexed with iron(II), this reagent cleaved the RNA in five regions. Cleavage at adenosine 207, which is far from the guanosine-binding site in the primary and secondary structure, provides a constraint for the higher order folding of the RNA. This cleavage site constitutes physical evidence for a key feature of the Michel-Westhof model. Targeting a reactive entity to a specific site should be generally useful for determining proximity within folded RNA molecules or ribonucleoprotein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J F -- Cech, T R -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):526-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1315076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Edetic Acid/metabolism ; Free Radicals ; Guanosine/*metabolism ; Guanosine Monophosphate/metabolism ; Iron/metabolism ; Iron Chelating Agents/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; Pentetic Acid/metabolism ; RNA, Catalytic/*chemistry/metabolism ; Tetrahymena/*chemistry
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  • 20
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    Calcium-dependent transmitter secretion reconstituted in Xenopus oocytes: requirement for synaptophysin (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-31
    Description: Calcium-dependent glutamate secretion was reconstituted in Xenopus oocytes by injecting the oocyte with total rat cerebellar messenger RNA (mRNA). Co-injection of total mRNA with antisense oligonucleotides to synaptophysin message decreased the expression of synaptophysin in the oocyte and reduced the calcium-dependent secretion. A similar effect on secretion was observed for oocytes injected with total mRNA together with an antibody to rat synaptophysin. These results indicate that synaptophysin is necessary for transmitter secretion and that the oocyte expression system may be useful for dissecting the molecular events associated with the secretory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alder, J -- Lu, B -- Valtorta, F -- Greengard, P -- Poo, M M -- MH 39327/MH/NIMH NIH HHS/ -- NS 22764/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1353905" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Western ; Calcimycin/pharmacology ; Calcium/*pharmacology ; Cerebellum/chemistry ; Fluorescent Antibody Technique ; Gene Expression ; Glutamates/*secretion ; Glutamic Acid ; Kinetics ; Liver/chemistry ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Oocytes/*physiology ; RNA, Messenger/genetics ; Rats ; Synaptophysin/genetics/*physiology ; Transfection ; Xenopus
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  • 21
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    Regulation of dynein-driven microtubule sliding by the radial spokes in flagella (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-11
    Description: The regulation of microtubule sliding in flagellar axonemes was studied with the use of Chlamydomonas mutants and in vitro assays. Microtubule sliding velocities were diminished in axonemes from mutant cells missing radial spoke structures but could be restored upon reconstitution with dynein from axonemes with wild-type radial spokes. These experiments demonstrate that the radial spokes activate dynein's microtubule sliding activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, E F -- Sale, W S -- GM 08367/GM/NIGMS NIH HHS/ -- HD 20497/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1557-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1387971" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Movement ; Chlamydomonas/genetics/*physiology/ultrastructure ; Dyneins/genetics/*metabolism ; Flagella/*physiology/ultrastructure ; Kinetics ; Microscopy, Electron ; Microtubules/*physiology/ultrastructure
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  • 22
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    Participation of non-zinc finger residues in DNA binding by two nuclear orphan receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Steroid-thyroid hormone receptors typically bind as dimers to DNA sequences that contain repeated elements termed half-sites. NGFI-B, an early response protein and orphan member of this receptor superfamily, binds to a DNA sequence that contains only one half-site (5'-AAAGGTCA-3'). A domain separate from the NGFI-B zinc fingers, termed the A box, was identified and is required for recognition of the two adenine-thymidine (A-T) base pairs at the 5' end of the NGFI-B DNA binding element. In addition, a domain downstream of the zinc fingers of the orphan receptor H-2 region II binding protein, termed the T box, determined binding to tandem repeats of the estrogen receptor half-site (5'-AGGTCA-3').〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Paulsen, R E -- Padgett, K A -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314418" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; CHO Cells ; Cell Nucleus/*physiology ; Cricetinae ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligodeoxyribonucleotides/metabolism ; Polymerase Chain Reaction ; Receptors, Cell Surface/*metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Transcription Factors/genetics/*metabolism ; Transfection ; Zinc Fingers/genetics
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  • 23
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    Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-13
    Description: Two DNA strand transfer reactions occur during retroviral reverse transcription. The mechanism of the first, minus strand strong-stop DNA, transfer has been studied in vitro with human immunodeficiency virus 1 reverse transcriptase (HIV-1 RT) and a model template-primer system derived from the HIV-1 genome. The results reveal that HIV-1 RT alone can catalyze DNA strand transfer reactions. Two kinetically distinct ribonuclease (RNase) H activities associated with HIV-1 RT are required for removal of RNA fragments annealed to the nascent DNA strand. Examination of the binding of DNA.RNA duplex and single-stranded RNA to HIV-1 RT during strand transfer supports a model where the enzyme accommodates both the acceptor RNA template and the nascent DNA strand before the transfer event is completed. The polymerase activity incorporated additional bases beyond the 5' end of the RNA template, resulting in a base misincorporation upon DNA strand transfer. Such a process occurring in vivo during retroviral homologous recombination could contribute to the hypermutability of the HIV-1 genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peliska, J A -- Benkovic, S J -- AI08275/AI/NIAID NIH HHS/ -- GM13306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1112-8.〈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/1279806" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; DNA, Viral/biosynthesis/chemistry/*metabolism ; Deoxyribonucleotides ; HIV Reverse Transcriptase ; HIV-1/*enzymology/genetics ; Kinetics ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; RNA, Transfer/metabolism ; RNA, Viral/chemistry/metabolism ; RNA-Directed DNA Polymerase/genetics/*metabolism ; Ribonuclease H/metabolism ; Templates, Genetic
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  • 24
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    High-efficiency expression and solubilization of functional T cell antigen receptor heterodimers (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-29
    Description: The T cell receptor (TCR) zeta chain was attached to the TCR alpha and beta extracellular domains to induce efficient expression of alpha beta heterodimers that can recognize complexes of antigen with major histocompatibility complex (MHC) molecules. Chimeric constructs expressed in RBL-2H3 cells were efficiently transported to the cell surface uniquely as disulfide-linked heterodimers. Transfectants were activated by specific antigen-MHC complexes, which demonstrated that the expressed alpha beta was functional and that CD3 was not required for antigen-MHC binding. Constructs with thrombin cleavage sites were efficiently cleaved to soluble disulfide-linked heterodimers. Thus, attachment of TCR zeta domains and protease cleavage sites to TCR alpha and beta induces expression of demonstrably functional heterodimers that can be solubilized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engel, I -- Ottenhoff, T H -- Klausner, R D -- New York, N.Y. -- Science. 1992 May 29;256(5061):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598575" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/immunology ; Disulfides ; Flow Cytometry ; Histocompatibility Antigens/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Receptors, Antigen, T-Cell/genetics/isolation & purification/*metabolism ; Solubility ; Transfection
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  • 25
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    A surface protease and the invasive character of plague (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-11-06
    Description: A 9.5-kilobase plasmid of Yersinia pestis, the causative agent of plague, is required for high virulence when mice are inoculated with the bacterium by subcutaneous injection. Inactivation of the plasmid gene pla, which encodes a surface protease, increased the median lethal dose of the bacteria for mice by a millionfold. Moreover, cloned pla was sufficient to restore segregants lacking the entire pla-bearing plasmid to full virulence. Both pla+ strains injected subcutaneously and pla- mutants injected intravenously reached high titers in liver and spleen of infected mice, whereas pla- mutants injected subcutaneously failed to do so even though they establish a sustained local infection at the injection site. More inflammatory cells accumulated in lesions caused by the pla- mutants than in lesions produced by the pla+ parent. The Pla protease was shown to be a plasminogen activator with unusual kinetic properties. It can also cleave complement C3 at a specific site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodeinde, O A -- Subrahmanyam, Y V -- Stark, K -- Quan, T -- Bao, Y -- Goguen, J D -- AI22176/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):1004-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439793" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Bacterial Proteins ; Colony Count, Microbial ; Escherichia coli/enzymology ; Fibrinolysin/chemistry/metabolism ; Injections, Intravenous ; Kinetics ; Liver/microbiology ; Mice ; Molecular Sequence Data ; Mutation ; Plague/microbiology ; Plasmids ; Plasminogen Activators/genetics/*physiology ; Recombinant Proteins/metabolism ; Spleen/microbiology ; Tissue Plasminogen Activator/metabolism ; Urokinase-Type Plasminogen Activator/metabolism ; Yersinia pestis/*enzymology/isolation & purification/*pathogenicity
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  • 26
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    Aminoacyl esterase activity of the Tetrahymena ribozyme (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-05
    Description: Several classes of ribozymes (catalytic RNA's) catalyze reactions at phosphorus centers, but apparently no reaction at a carbon center has been demonstrated. The active site of the Tetrahymena ribozyme was engineered to bind an oligonucleotide derived from the 3' end of N-formyl-methionyl-tRNA(fMet). This ribozyme catalyzes the hydrolysis of the aminoacyl ester bond to a modest extent, 5 to 15 times greater than the uncatalyzed rate. Catalysis involves binding of the oligonucleotide to the internal guide sequence of the ribozyme and requires Mg2+ and sequence elements of the catalytic core. The ability of RNA to catalyze reactions with aminoacyl esters expands the catalytic versatility of RNA and suggests that the first aminoacyl tRNA synthetase could have been an RNA molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Piccirilli, J A -- McConnell, T S -- Zaug, A J -- Noller, H F -- Cech, T R -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1420-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Carboxylic Ester Hydrolases/*metabolism ; Kinetics ; Models, Structural ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides ; RNA, Catalytic/genetics/*metabolism ; RNA, Transfer, Amino Acyl/metabolism ; *RNA, Transfer, Met ; Substrate Specificity ; Tetrahymena/*enzymology
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  • 27
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    Cloning of a delta opioid receptor by functional expression (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-28
    Description: Opiate drugs have potent analgesic and addictive properties. These drugs interact with receptors that also mediate the response to endogenous opioid peptide ligands. However, the receptors for opioids have eluded definitive molecular characterization. By transient expression in COS cells and screening with an iodinated analog of the opioid peptide enkephalin, a complementary DNA clone encoding a functional delta opioid receptor has been identified. The sequence shows homology to G protein-coupled receptors, in particular the receptors for somatostatin, angiotensin, and interleukin-8.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, C J -- Keith, D E Jr -- Morrison, H -- Magendzo, K -- Edwards, R H -- DA05010/DA/NIDA NIH HHS/ -- P50 DA005010/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of California, School of Medicine, Los Angeles 90024-1759.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1335167" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Blotting, Northern ; Blotting, Southern ; Cell Line ; Cyclic AMP/metabolism ; Diprenorphine/metabolism ; Enkephalin, D-Penicillamine (2,5)- ; Enkephalins/pharmacology ; Etorphine/pharmacology ; Gene Expression ; Humans ; Kinetics ; Models, Structural ; Molecular Sequence Data ; Naloxone/pharmacology ; Narcotics/pharmacology ; Protein Structure, Secondary ; Receptors, Opioid, delta/chemistry/*genetics/*metabolism ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
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  • 28
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    Cloning and characterization of inducible nitric oxide synthase from mouse macrophages (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: Nitric oxide (NO) conveys a variety of messages between cells, including signals for vasorelaxation, neurotransmission, and cytotoxicity. In some endothelial cells and neurons, a constitutive NO synthase is activated transiently by agonists that elevate intracellular calcium concentrations and promote the binding of calmodulin. In contrast, in macrophages, NO synthase activity appears slowly after exposure of the cells to cytokines and bacterial products, is sustained, and functions independently of calcium and calmodulin. A monospecific antibody was used to clone complementary DNA that encoded two isoforms of NO synthase from immunologically activated mouse macrophages. Liquid chromatography-mass spectrometry was used to confirm most of the amino acid sequence. Macrophage NO synthase differs extensively from cerebellar NO synthase. The macrophage enzyme is immunologically induced at the transcriptional level and closely resembles the enzyme in cytokine-treated tumor cells and inflammatory neutrophils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xie, Q W -- Cho, H J -- Calaycay, J -- Mumford, R A -- Swiderek, K M -- Lee, T D -- Ding, A -- Troso, T -- Nathan, C -- AI30165/AI/NIAID NIH HHS/ -- CA43610/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):225-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beatrice and Samuel A. Seaver Laboratory, Department of Medicine, Cornell University Medical College, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373522" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/biosynthesis/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Codon ; Enzyme Induction ; Interferon-gamma/pharmacology ; Isoenzymes/biosynthesis/*genetics ; Kinetics ; Lipopolysaccharides ; Macrophages/drug effects/*enzymology ; Mammary Neoplasms, Experimental ; Mice ; Molecular Sequence Data ; Molecular Weight ; Neutrophils/drug effects/enzymology ; Nitric Oxide Synthase ; Oligodeoxyribonucleotides ; Poly A/genetics ; RNA/genetics ; RNA, Messenger ; Rats ; Sequence Homology, Nucleic Acid ; Transcription, Genetic
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  • 29
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    Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: Activation of B lymphocytes by engagement of their immunoglobulin M antigen receptors results in phosphorylation of a number of proteins on tyrosine residues. One such protein is p95vav, the product of the vav proto-oncogene. Tyrosine phosphorylation of p95vav occurred within seconds of immunoglobulin M cross-linking and was independent of other events induced during stimulation of B cells, such as protein kinase C activation, guanosine triphosphate-binding protein signaling, and calcium mobilization. Moreover, engagement of antigen receptors induced the rapid (approximately 5 seconds) and transient (approximately 60 seconds) association of p95vav with a 70-kilodalton tyrosine-phosphorylated protein, Vap-1, an interaction mediated by the Src homology 2 domain of p95vav. These results suggest that the vav proto-oncogene participates in the signaling processes that mediate the antigen-induced activation of B lymphocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bustelo, X R -- Barbacid, M -- New York, N.Y. -- Science. 1992 May 22;256(5060):1196-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543-4000.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375396" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/analysis ; Animals ; B-Lymphocytes/immunology/*physiology ; *Cell Cycle Proteins ; Cell Line ; Kinetics ; *Lymphocyte Activation ; Mice ; Phosphorylation ; Phosphotyrosine ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-vav ; *Proto-Oncogenes ; Tyrosine/analogs & derivatives/analysis
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  • 30
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    Lithium-sensitive production of inositol phosphates during amphibian embryonic mesoderm induction (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: Mesoderm induction and body axis determination in frog (Xenopus) embryos are thought to involve growth factor-mediated cell-cell signaling, but the signal transduction pathways are unknown. Li+, which inhibits the polyphosphoinositide (PI) cycle signal transduction pathway in many cells, also disrupts axis determination and mesoderm induction. Amounts of the PI cycle-derived second messenger, inositol 1,4,5-trisphosphate, increased during mesoderm induction in normal embryos; addition of Li+ inhibited the embryonic inositol monophosphatase and reversed this increase. Embryonic PI cycle activity thus shows characteristics that indicate it may function in mesoderm induction and axis determination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maslanski, J A -- Leshko, L -- Busa, W B -- HD22879/HD/NICHD NIH HHS/ -- HD27546/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):243-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Johns Hopkins University, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314424" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chlorides/*pharmacology ; Choline/pharmacology ; Embryo, Nonmammalian/physiology ; Female ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol Phosphates/*metabolism ; Kinetics ; Lithium/*pharmacology ; Lithium Chloride ; Mesoderm/drug effects/*physiology ; Signal Transduction/drug effects ; Teratogens/*pharmacology ; Xenopus/*embryology
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  • 31
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    Fast perceptual learning in visual hyperacuity (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-15
    Description: In many different spatial discrimination tasks, such as in determining the sign of the offset in a vernier stimulus, the human visual system exhibits hyperacuity by evaluating spatial relations with the precision of a fraction of a photoreceptor's diameter. It is proposed that this impressive performance depends in part on a fast learning process that uses relatively few examples and that occurs at an early processing stage in the visual pathway. This hypothesis is given support by the demonstration that it is possible to synthesize, from a small number of examples of a given task, a simple network that attains the required performance level. Psychophysical experiments agree with some of the key predictions of the model. In particular, fast stimulus-specific learning is found to take place in the human visual system, and this learning does not transfer between two slightly different hyperacuity tasks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poggio, T -- Fahle, M -- Edelman, S -- New York, N.Y. -- Science. 1992 May 15;256(5059):1018-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Artificial Intelligence Laboratory, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589770" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Computer Simulation ; Humans ; Kinetics ; Learning/*physiology ; Models, Biological ; Photoreceptor Cells/physiology ; Visual Acuity/*physiology ; Visual Pathways/physiology ; Visual Perception/*physiology
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  • 32
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    Range of messenger action of calcium ion and inositol 1,4,5-trisphosphate (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: The range of messenger action of a point source of Ca2+ or inositol 1,4,5-trisphosphate (IP3) was determined from measurements of their diffusion coefficients in a cytosolic extract from Xenopus laevis oocytes. The diffusion coefficient (D) of [3H]IP3 injected into an extract was 283 microns 2/s. D for Ca2+ increased from 13 to 65 microns 2/s when the free calcium concentration was raised from about 90 nM to 1 microM. The slow diffusion of Ca2+ in the physiologic concentration range results from its binding to slowly mobile or immobile buffers. The calculated effective ranges of free Ca2+ before it is buffered, buffered Ca2+, and IP3 determined from their diffusion coefficients and lifetimes were 0.1 micron, 5 microns, and 24 microns, respectively. Thus, for a transient point source of messenger in cells smaller than 20 microns, IP3 is a global messenger, whereas Ca2+ acts in restricted domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allbritton, N L -- Meyer, T -- Stryer, L -- 5F32AI0814203/AI/NIAID NIH HHS/ -- MH45324/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1812-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465619" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Calcium-Transporting ATPases/antagonists & inhibitors ; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone/pharmacology ; Chromatography, High Pressure Liquid ; Cytosol/metabolism ; Diffusion ; Inositol 1,4,5-Trisphosphate/*metabolism ; Kinetics ; Oocytes/drug effects/*metabolism ; *Second Messenger Systems ; *Signal Transduction ; Terpenes/pharmacology ; Thapsigargin ; Time Factors ; Xenopus laevis
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    IP3 receptor: localization to plasma membrane of T cells and cocapping with the T cell receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: Immune responses in lymphocytes require cellular accumulation of large amounts of calcium (Ca2+) from extracellular sources. In the T cell tumor line Jurkat, receptors for the Ca(2+)-releasing messenger inositol 1,4,5-trisphosphate (IP3) were localized to the plasma membrane (PM). Capping of the T cell receptor-CD3 complex, which is associated with signal transduction, was accompanied by capping of IP3 receptors. The IP3 receptor on T cells appears to be responsible for the entry of Ca2+ that initiates proliferative responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khan, A A -- Steiner, J P -- Klein, M G -- Schneider, M F -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- MH-18501/MH/NIMH NIH HHS/ -- P01-HL27867/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):815-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins University School of Medicine, Department of Neuroscience, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323146" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/metabolism ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/analysis/*metabolism ; Burkitt Lymphoma ; Calcium/*metabolism ; *Calcium Channels ; Cell Line ; Cell Membrane/*metabolism ; Cells, Cultured ; Concanavalin A/pharmacology ; Fluorescent Antibody Technique ; Humans ; Inositol 1,4,5-Trisphosphate/*metabolism ; Inositol 1,4,5-Trisphosphate Receptors ; Kinetics ; Receptors, Antigen, T-Cell/analysis/*metabolism ; Receptors, Cell Surface/analysis/*metabolism ; *Receptors, Cytoplasmic and Nuclear ; Second Messenger Systems ; T-Lymphocytes/*immunology
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  • 34
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    Calmodulin trapping by calcium-calmodulin-dependent protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: Multifunctional calcium-calmodulin-dependent protein kinase (CaM kinase) transduces transient elevations in intracellular calcium into changes in the phosphorylation state and activity of target proteins. By fluorescence emission anisotropy, the affinity of CaM kinase for dansylated calmodulin was measured and found to increase 1000 times after autophosphorylation of the threonine at position 286 of the protein. Autophosphorylation markedly slowed the release of bound calcium-calmodulin; the release time increased from less than a second to several hundred seconds. In essence, calmodulin is trapped by autophosphorylation. The shift in affinity does not occur in a site-directed mutant in which threonine at position 286 has been replaced by a non-phosphorylatable amino acid. These experiments demonstrate the existence of a new state in which calmodulin is bound to CaM kinase even though the concentration of calcium is basal. Calmodulin trapping provides for molecular potentiation of calcium transients and may enable detection of their frequency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, T -- Hanson, P I -- Stryer, L -- Schulman, H -- GM 40600/GM/NIGMS NIH HHS/ -- GM24032/GM/NIGMS NIH HHS/ -- MH45324/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 May 22;256(5060):1199-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317063" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Calcium/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases ; Calmodulin/*metabolism ; Cell Line ; Egtazic Acid/pharmacology ; Kinetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Protein Binding ; Protein Kinases/genetics/*metabolism ; Recombinant Proteins/metabolism ; Spectrometry, Fluorescence ; Threonine ; Time Factors ; Transfection
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  • 35
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    Selective role of N-type calcium channels in neuronal migration (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: Analysis of neuronal migration in mouse cerebellar slice preparations by a laser scanning confocal microscope revealed that postmitotic granule cells initiate their migration only after the expression of N-type calcium channels on their plasmalemmal surface. Furthermore, selective blockade of these channels by addition of omega-conotoxin to the incubation medium curtailed cell movement. In contrast, inhibitors of L- and T-type calcium channels, as well as those of sodium and potassium channels, had no effect on the rate of granule cell migration. These results suggest that N-type calcium channels, which have been predominantly associated with neurotransmitter release in adult brain, also play a transient but specific developmental role in directed migration of immature neurons before the establishment of their synaptic circuits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Komuro, H -- Rakic, P -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):806-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neurobiology, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323145" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/pharmacology ; Calcium Channels/drug effects/*physiology ; Cell Movement/drug effects ; Cells, Cultured ; Cerebellum/cytology/*physiology ; In Vitro Techniques ; Kinetics ; Mice ; Mollusk Venoms/pharmacology ; Neurons/cytology/drug effects/*physiology ; Peptides, Cyclic/pharmacology ; Time Factors ; *omega-Conotoxins
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  • 36
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    Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-08
    Description: Voltage-sensitive sodium channels are responsible for the initiation and propagation of the action potential and therefore are important for neuronal excitability. Complementary DNA clones encoding the beta 1 subunit of the rat brain sodium channel were isolated by a combination of polymerase chain reaction and library screening techniques. The deduced primary structure indicates that the beta 1 subunit is a 22,851-dalton protein that contains a single putative transmembrane domain and four potential extracellular N-linked glycosylation sites, consistent with biochemical data. Northern blot analysis reveals a 1,400-nucleotide messenger RNA in rat brain, heart, skeletal muscle, and spinal cord. Coexpression of beta 1 subunits with alpha subunits increases the size of the peak sodium current, accelerates its inactivation, and shifts the voltage dependence of inactivation to more negative membrane potentials. These results indicate that the beta 1 subunit is crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the rat brain sodium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Isom, L L -- De Jongh, K S -- Patton, D E -- Reber, B F -- Offord, J -- Charbonneau, H -- Walsh, K -- Goldin, A L -- Catterall, W A -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- NS26729/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 8;256(5058):839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Brain/*physiology ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Female ; Kinetics ; Macromolecular Substances ; Membrane Potentials ; Molecular Sequence Data ; Oocytes/physiology ; Polymerase Chain Reaction/methods ; Protein Conformation ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Rats ; Sodium Channels/*genetics/*physiology ; Voltage-Gated Sodium Channel beta-1 Subunit ; Xenopus
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    An efficient antibody-catalyzed aminoacylation reaction (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-04-17
    Description: An antibody generated against a neutral phosphonate diester transition-state analog was found to catalyze the aminoacylation of the 3'-hydroxyl group of thymidine with an alanyl ester. A comparison of the apparent second-order rate constant of the antibody-catalyzed reaction [5.4 x 10(4) molar-1 minute-1 (M-1 min-1)] with that of the uncatalyzed reaction (2.6 x 10(-4) M-1 min-1) revealed this to be a remarkably efficient catalyst. Moreover, although the concentration of water (55 M) greatly exceeds that of the secondary alcohol, the antibody selectively catalyzes acyl transfer to thymidine. The antibody exhibits sequential binding, with Michaelis constants of 770 microM and 260 microM for acyl acceptor and donor, respectively, and a dissociation constant of 240 pM for hapten. This antibody-catalyzed reaction provides increased insight into the requirements for efficient aminoacylation catalysts and may represent a first step toward the generation of "aminoacyl transfer RNA synthetases" with novel specificities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobsen, J R -- Prudent, J R -- Kochersperger, L -- Yonkovich, S -- Schultz, P G -- AI24695/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):365-7.〈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/1566082" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Alanine/*metabolism ; Amino Acyl-tRNA Synthetases/metabolism ; Antibodies, Monoclonal/*metabolism ; *Catalysis ; Chromatography, High Pressure Liquid ; Esterification ; Haptens/immunology ; Hemocyanin/immunology ; Kinetics ; Organophosphonates/*immunology ; Serum Albumin, Bovine/immunology ; Thymidine/*metabolism
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    Dynamics of ribozyme binding of substrate revealed by fluorescence-detected stopped-flow methods (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-11-20
    Description: Fluorescence-detected stopped-flow and equilibrium methods have been used to study the mechanism for binding of pyrene (pyr)-labeled RNA oligomer substrates to the ribozyme (catalytic RNA) from Tetrahymena thermophila. The fluorescence of these substrates increases up to 25-fold on binding to the ribozyme. Stopped-flow experiments provide evidence that pyr experiences at least three different microenvironments during the binding process. A minimal mechanism is presented in which substrate initially base pairs to ribozyme and subsequently forms tertiary contacts in an RNA folding step. All four microscopic rate constants are measured for ribozyme binding of pyrCCUCU.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bevilacqua, P C -- Kierzek, R -- Johnson, K A -- Turner, D H -- GM 22939/GM/NIGMS NIH HHS/ -- GM44613/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Rochester, NY 14627.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455230" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Hydrogen Bonding ; Kinetics ; *RNA Splicing ; RNA, Catalytic/*metabolism ; RNA, Guide/*metabolism ; RNA, Protozoan/*metabolism ; RNA, Ribosomal/*metabolism ; Substrate Specificity ; Tetrahymena thermophila ; Thermodynamics
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  • 39
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    Activation of transcription factors by interferon-alpha in a cell-free system (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-08-07
    Description: The signal transduction mechanisms of interferons (IFNs) remain unclear partly because no effect of IFN has been reproducible in a cell-free system. IFN-alpha rapidly induces the transcription of a set of early response genes, and a multicomponent transcriptional activator, interferon stimulated gene factor 3 (ISGF3), is activated within minutes after binding of IFN-alpha to its receptor. A system was developed in which IFN-alpha activated ISGF3 in homogenates of HeLa cells. Subcellular fractionation revealed that incubation of a plasma membrane-enriched fraction with IFN-alpha was sufficient to activate the regulatory subcomponent of ISGF3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉David, M -- Larner, A C -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):813-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cytokine Biology, Center for Biologics Evaluation and Research, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496402" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell-Free System ; DNA-Binding Proteins/biosynthesis/isolation & purification/*metabolism ; HeLa Cells ; Humans ; Interferon-Stimulated Gene Factor 3 ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; Interferon-alpha/*pharmacology ; Interferon-gamma/pharmacology ; Kinetics ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Transcription Factors/biosynthesis/isolation & purification/*metabolism ; Transcription, Genetic/*drug effects
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  • 40
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    Molecular code for cooperativity in hemoglobin (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-03
    Description: Although tetrameric hemoglobin has been studied extensively as a prototype for understanding mechanisms of allosteric regulation, the functional and structural properties of its eight intermediate ligation forms have remained elusive. Recent experiments on the energetics of cooperativity of these intermediates, along with assignments of their quaternary structures, have revealed that the allosteric mechanism is controlled by a previously unrecognized symmetry feature: quaternary switching from form T to form R occurs whenever heme-site binding creates a tetramer with at least one ligated subunit on each dimeric half-molecule. This "symmetry rule" translates the configurational isomers of heme-site ligation into six observed switchpoints of quaternary transition. Cooperativity arises from both "concerted" quaternary switching and "sequential" modulation of binding within each quaternary form, T and R. Binding affinity is regulated through a hierarchical code of tertiary-quaternary coupling that includes the classical allosteric models as limiting cases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ackers, G K -- Doyle, M L -- Myers, D -- Daugherty, M A -- P01-HL40453/HL/NHLBI NIH HHS/ -- R37-GM24486/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):54-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553532" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Calorimetry ; Circular Dichroism ; Hemoglobins/*chemistry/genetics/metabolism ; Kinetics ; Ligands ; Macromolecular Substances ; Models, Molecular ; Mutation ; Oxyhemoglobins/chemistry/metabolism ; Protein Conformation ; Thermodynamics
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  • 41
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    Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected] (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: The D and L forms of the enzyme HIV-1 protease have been prepared by total chemical synthesis. The two proteins had identical covalent structures. However, the folded protein-enzyme enantiomers showed reciprocal chiral specificity on peptide substrates. That is, each enzyme enantiomer cut only the corresponding substrate enantiomer. Reciprocal chiral specificity was also evident in the effect of enantiomeric inhibitors. These data imply that the folded forms of the chemically synthesized D- and L-enzyme molecules are mirror images of one another in all elements of the three-dimensional structure. Enantiomeric proteins are expected to display reciprocal chiral specificity in all aspects of their biochemical interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milton, R C -- Milton, S C -- Kent, S B -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1445-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604320" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acids ; HIV Protease/chemical synthesis/*chemistry/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Oligopeptides/pharmacology ; Protein Conformation ; Stereoisomerism ; Substrate Specificity ; X-Ray Diffraction
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    Inhibition of neutrophil chemokinesis on vitronectin by inhibitors of calcineurin (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: Migration of human polymorphonuclear neutrophils on vitronectin is dependent on repeated transient increases in the concentration of intracellular free calcium ([Ca2+]i). A specific peptide inhibitor of the Ca(2+)-calmodulin-dependent phosphatase calcineurin was introduced into the cytoplasm of neutrophils. The peptide inhibited neutrophil migration on vitronectin by interfering with the release of the cells from sites of attachment. A similar reduction in motility on vitronectin occurred when cells were treated with the immunosuppressant FK506, which also inhibits calcineurin when bound to its binding protein, FKBP. These results indicate that a rise in [Ca2+]i reduces integrin-mediated adhesion to vitronectin by a mechanism that requires calcineurin activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hendey, B -- Klee, C B -- Maxfield, F R -- GM14150/GM/NIGMS NIH HHS/ -- GM34770/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):296-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1384129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aminoquinolines/pharmacology ; Calcineurin ; Calmodulin-Binding Proteins/*antagonists & inhibitors/physiology ; Carrier Proteins/metabolism ; Chemotaxis, Leukocyte/*drug effects ; Ethers, Cyclic/pharmacology ; *Glycoproteins ; Humans ; Kinetics ; Molecular Sequence Data ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/cytology/drug effects/*physiology ; Okadaic Acid ; Peptide Fragments/pharmacology ; Peptides/pharmacology ; Phosphoprotein Phosphatases/*antagonists & inhibitors/physiology ; Phosphorylation ; Tacrolimus/pharmacology ; Tacrolimus Binding Proteins ; Vitronectin
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Isolation and structure of a brain constituent that binds to the cannabinoid receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: Arachidonylethanolamide, an arachidonic acid derivative in porcine brain, was identified in a screen for endogenous ligands for the cannabinoid receptor. The structure of this compound, which has been named "anandamide," was determined by mass spectrometry and nuclear magnetic resonance spectroscopy and was confirmed by synthesis. Anandamide inhibited the specific binding of a radiolabeled cannabinoid probe to synaptosomal membranes in a manner typical of competitive ligands and produced a concentration-dependent inhibition of the electrically evoked twitch response to the mouse vas deferens, a characteristic effect of psychotropic cannabinoids. These properties suggest that anandamide may function as a natural ligand for the cannabinoid receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Devane, W A -- Hanus, L -- Breuer, A -- Pertwee, R G -- Stevenson, L A -- Griffin, G -- Gibson, D -- Mandelbaum, A -- Etinger, A -- Mechoulam, R -- DA 6481/DA/NIDA NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1946-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Natural Products, Medical Faculty, Hebrew University, Jerusalem, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470919" target="_blank"〉PubMed〈/a〉
    Keywords: Amides/chemistry/*isolation & purification/pharmacology ; Animals ; *Arachidonic Acids ; Binding, Competitive ; Brain/*metabolism ; Brain Chemistry ; Cannabinoids/metabolism ; Chromatography, Thin Layer ; Endocannabinoids ; Fatty Acids, Unsaturated/chemistry/*isolation & purification/pharmacology ; Gas Chromatography-Mass Spectrometry ; Kinetics ; Polyunsaturated Alkamides ; Receptors, Cannabinoid ; Receptors, Drug/*metabolism ; Swine
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    Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: Class II major histocompatibility complexes bind peptides in an endosome-like compartment. When the class II null cell line 721.174 was transfected with class II DR3 genes, DR molecules were produced in normal amounts. However, the DR molecules were abnormally conformed and unstable because deletion of an antigen-processing gene had impaired intracellular formation of most class II-peptide complexes. Yet, 70 percent of the DR molecules still bore peptides, 80 percent of which were 21- to 24-amino acid fragments of the class II-associated invariant chain. These peptides were rare on DR3 from control cells. Thus, a defect in the main antigen-processing pathway revealed a process in which DR molecules bind long peptides derived from proteins present in the same compartment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sette, A -- Ceman, S -- Kubo, R T -- Sakaguchi, K -- Appella, E -- Hunt, D F -- Davis, T A -- Michel, H -- Shabanowitz, J -- Rudersdorf, R -- AI15486/AI/NIAID NIH HHS/ -- AI18634/AI/NIAID NIH HHS/ -- GM37537/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1801-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465617" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Gene Deletion ; *Genes, MHC Class II ; HLA-DR Antigens/*genetics/*metabolism ; HLA-DR3 Antigen/*genetics/metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Peptides/*metabolism ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Components of sterol biosynthesis assembled on the oxygen-avid hemoglobin of Ascaris (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: The parasitic nematode Ascaris infests a billion people worldwide. Much of its proliferative success is due to prodigious egg production, up to 10(6) sterol-replete eggs per day. Sterol synthesis requires molecular oxygen for squalene epoxidation, yet oxygen is scarce in the intestinal folds the worms inhabit. Ascaris has an oxygen-avid hemoglobin in the perienteric fluid that bathes its reproductive organs. Purified hemoglobin contained tightly bound squalene and functioned as an NADPH-dependent, ferrihemoprotein reductase. All components of the squalene epoxidation reaction--squalene, oxygen, NADPH, and NADPH-dependent reductase--are assembled on the hemoglobin. This molecule may thus function in sterol biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherman, D R -- Guinn, B -- Perdok, M M -- Goldberg, D E -- AM-20579/AM/NIADDK NIH HHS/ -- RR-00954/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1930-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Washington University School of Medicine, St. Louis, MO.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470914" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ascaris/*metabolism ; Hemoglobins/*metabolism ; Kinetics ; Mass Spectrometry ; NADPH-Ferrihemoprotein Reductase/metabolism ; Oxyhemoglobins/*metabolism ; Squalene/metabolism ; Sterols/*biosynthesis/isolation & purification
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    Torsional rigidity of positively and negatively supercoiled DNA (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-03
    Description: Time-correlated single-photon counting of intercalated ethidium bromide was used to measure the torsion constants of positively supercoiled, relaxed, and negatively supercoiled pBR322 DNA, which range in superhelix density from +0.042 to -0.123. DNA behaves as coupled, nonlinear torsional pendulums under superhelical stress, and the anharmonic term in the Hamiltonian is approximately 15 percent for root-mean-square fluctuations in twist at room temperature. At the level of secondary structure, positively supercoiled DNA is significantly more flexible than negatively supercoiled DNA. These results exclude certain models that account for differential binding affinity of proteins to positively and negatively supercoiled DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selvin, P R -- Cook, D N -- Pon, N G -- Bauer, W R -- Klein, M P -- Hearst, J E -- FD 8R1 GM 41911A-03-NF-03/92/FD/FDA HHS/ -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):82-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of California, Berkeley.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553534" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Superhelical/*chemistry ; Ethidium ; Intercalating Agents ; Kinetics ; Mathematics ; Models, Theoretical ; Nucleic Acid Conformation ; *Plasmids ; Spectrometry, Fluorescence ; Stress, Mechanical ; Thermodynamics
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  • 47
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    CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Lymphocytes must proliferate and differentiate in response to low concentrations of a vast array of antigens. The requirements of broad specificity and sensitivity conflict because the former is met by low-affinity antigen receptors, which precludes achieving the latter with high-affinity receptors. Coligation of the membrane protein CD19 with the antigen receptor of B lymphocytes decreased the threshold for antigen receptor-dependent stimulation by two orders of magnitude. B lymphocytes proliferated when approximately 100 antigen receptors per cell, 0.03 percent of the total, were coligated with CD19. The B cell resolves its dilemma by having an accessory protein that enables activation when few antigen receptors are occupied.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, R H -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):105-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, 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/1373518" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD/genetics/*immunology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/genetics/*immunology ; B-Lymphocytes/*immunology ; Cell Line ; Cells, Cultured ; DNA Replication ; Humans ; Kinetics ; L Cells (Cell Line) ; *Lymphocyte Activation ; Mice ; Receptors, Antigen, B-Cell/*immunology ; Recombinant Proteins/immunology ; Thymidine/metabolism
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    Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: The immunosuppressant rapamycin inhibited proliferation of the H4IIEC hepatoma cell line. Rapamycin, but not its structural analog FK506, also inhibited the basal and insulin-stimulated activity of the p70 ribosomal protein S6 kinase. By contrast, insulin stimulation of the p85 Rsk S6 kinase and mitogen-activated protein (MAP) kinase activity were unaffected by drug. Rapamycin treatment of COS cells transfected with recombinant p70 S6 kinase completely inhibited the appearance of the hyperphosphorylated form of p70 S6 kinase concomitant with the inhibition of enzyme activity toward 40S subunits. Thus, rapamycin inhibits a signal transduction element that is necessary for the activation of p70 S6 kinase and mitogenesis but unnecessary for activation of p85 Rsk S6 kinase or MAP kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Price, D J -- Grove, J R -- Calvo, V -- Avruch, J -- Bierer, B E -- P01 CA39542/CA/NCI NIH HHS/ -- R01 DK17776/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Diabetes Unit, Massachusetts General Hospital, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1380182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases ; Cell Line ; Chromatography, Ion Exchange ; Cyclosporine/pharmacology ; Immunosuppressive Agents/*pharmacology ; Insulin/pharmacology ; Kinetics ; Liver Neoplasms, Experimental ; Polyenes/*pharmacology ; *Protein Kinase Inhibitors ; Protein Kinases/genetics/isolation & purification/*metabolism ; Recombinant Proteins/antagonists & inhibitors/isolation & purification ; Ribosomal Protein S6 Kinases ; Ribosomes/enzymology ; Sirolimus ; Tacrolimus/pharmacology ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
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    Ablation of transplanted HTLV-I Tax-transformed tumors in mice by antisense inhibition of NF-kappa B (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-12-11
    Description: Mice transgenic for the human T cell leukemia virus (HTLV-I) Tax gene develop fibroblastic tumors that express NF-kappa B-inducible early genes. In vitro inhibition of NF-kappa B expression by antisense oligodeoxynucleotides (ODNs) inhibited growth of these culture-adapted Tax-transformed fibroblasts as well as an HTLV-I-transformed human lymphocyte line. In contrast, antisense inhibition of Tax itself had no apparent effect on cell growth. Mice treated with antisense to NF-kappa B ODNs showed rapid regression of transplanted fibrosarcomas. This suggests that NF-kappa B expression may be necessary for the maintenance of the malignant phenotype and provides a therapeutic approach for HTLV-I-associated disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kitajima, I -- Shinohara, T -- Bilakovics, J -- Brown, D A -- Xu, X -- Nerenberg, M -- CA50234/CA/NCI NIH HHS/ -- MH47680/MH/NIMH NIH HHS/ -- NS01330/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1792-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuropharmacology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1299224" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; Cell Division/drug effects ; Cell Line ; Cell Transformation, Neoplastic ; Fibrosarcoma/*drug therapy/pathology ; *Genes, pX ; Human T-lymphotropic virus 1/*genetics ; Humans ; Kinetics ; Lymphocytes ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors/genetics ; Oligodeoxyribonucleotides ; Oligonucleotides, Antisense/*pharmacology/*therapeutic use
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    Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-31
    Description: Subdomain-size proteolytic fragments of Escherichia coli trp repressor have been produced that assemble in defined order to regenerate fully native dimers. By characterization of the secondary and tertiary structures of isolated and recombined fragments, the structure of assembly intermediates can be correlated with the kinetic folding pathway of the intact repressor deduced from spectroscopic measurement of folding rates. The nativelike structure of these intermediates provides further evidence that protein folding pathways reflect the stabilities of secondary structural units and assemblies found in the native state. The proteolytic method should be generally useful in adding structural detail to spectroscopically determined folding mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tasayco, M L -- Carey, J -- GM43558/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 31;255(5044):594-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemistry Department, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1736361" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry ; Circular Dichroism ; Escherichia coli/metabolism ; Kinetics ; Macromolecular Substances ; Magnetic Resonance Spectroscopy/methods ; Models, Structural ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Protein Conformation ; Repressor Proteins/*chemistry/metabolism
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    A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: The peptide binding cleft of the class I human histocompatibility antigen, HLA-A2, contains conserved amino acid residues clustered in the two ends of the cleft in pockets A and F as well as polymorphic residues. The function of two conserved tyrosines in the A pocket was investigated by mutating them to phenylalanines and of a conserved tyrosine and threonine in the F pocket by mutating them to phenylalanine and valine, respectively. Presentation of influenza virus peptides and of intact virus to cytolytic T lymphocytes (CTLs) was then examined. The magnitude of the reduction seen by the mutation of the two tyrosines in the A pocket suggests that hydrogen bonds involving them have a critical function in the binding of the NH2-terminal NH3+ of the peptide nonamer and possibly of all bound peptide nonamers. In contrast, the mutations in the F pocket had no effect on CTL recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Latron, F -- Pazmany, L -- Morrison, J -- Moots, R -- Saper, M A -- McMichael, A -- Strominger, J L -- AI 20182/AI/NIAID NIH HHS/ -- CA 47554/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):964-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1380181" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology ; Binding Sites ; Cell Line ; Cloning, Molecular ; Epitopes/immunology/metabolism ; HLA-A2 Antigen/chemistry/genetics/*metabolism ; Influenza A virus ; Kinetics ; Models, Molecular ; Mutagenesis, Site-Directed ; Oligopeptides/immunology/*metabolism ; Protein Conformation ; Recombinant Proteins/chemistry/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection ; Viral Proteins/metabolism
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  • 52
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    Functional modulation of GABAA receptors by cAMP-dependent protein phosphorylation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-31
    Description: gamma-Aminobutyric acidA (GABAA) receptors are ligand-gated ion channels that mediate inhibitory synaptic transmission in the central nervous system. The role of protein phosphorylation in the modulation of GABAA receptor function was examined with cells transiently transfected with GABAA receptor subunits. GABAA receptors consisting of the alpha 1 and beta 1 or the alpha 1, beta 1, and gamma 2 subunits were directly phosphorylated on the beta 1 subunit by adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA). The phosphorylation decreased the amplitude of the GABA response of both receptor types and the extent of rapid desensitization of the GABAA receptor that consisted of the alpha 1 and beta 1 subunits. Site-specific mutagenesis of the serine residue phosphorylated by PKA completely eliminated the PKA phosphorylation and modulation of the GABAA receptor. In primary embryonic rat neuronal cell cultures, a similar regulation of GABAA receptors by PKA was observed. These results demonstrate that the GABAA receptor is directly modulated by protein phosphorylation and suggest that neurotransmitters or neuropeptides that regulate intracellular cAMP levels may modulate the responses of neurons to GABA and consequently have profound effects on synaptic excitability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moss, S J -- Smart, T G -- Blackstone, C D -- Huganir, R L -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):661-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, 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/1323140" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Colforsin/pharmacology ; Cyclic AMP/*pharmacology ; Electric Conductivity ; Immunosorbent Techniques ; Kinetics ; Mice ; Mutagenesis, Site-Directed ; Neurons/drug effects/physiology ; Peptide Mapping ; Phosphorylation ; Protein Kinases/*metabolism ; Rats ; Receptors, GABA-A/genetics/*physiology ; Recombinant Proteins/physiology ; Transfection ; Zinc/pharmacology ; gamma-Aminobutyric Acid/pharmacology
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    Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-29
    Description: Immunophilins, a family of proteins that exhibit rotamase (peptidyl-prolyl cis-trans isomerase) activity in vitro, are expressed in many organisms and most tissues. Although some immunophilins can mediate the immunosuppressive actions of FK506, rapamycin, and cyclosporin A, the physiological role of the unligated proteins is not known. A 59-kilodalton member of the FK506- and rapamycin-binding class was found to associate in the absence of these drugs with two heat shock proteins (hsp90 and hsp70) and the glucocorticoid receptor (GR). Together, these proteins make up the inactive GR, thus biochemically linking two families of proteins proposed to be involved in protein folding and assembly as well as two potent immunosuppressive modalities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tai, P K -- Albers, M W -- Chang, H -- Faber, L E -- Schreiber, S L -- DK41881/DK/NIDDK NIH HHS/ -- GM-38627/GM/NIGMS NIH HHS/ -- HD28034/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 May 29;256(5061):1315-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Obstetrics and Gynecology, Medical College of Ohio, Toledo 43699.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1376003" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/isolation & purification/*metabolism ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Carrier Proteins/isolation & purification/*metabolism ; Cell Line ; Heat-Shock Proteins/isolation & purification/*metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Peptidylprolyl Isomerase ; Polyenes/metabolism ; Rats ; Receptors, Glucocorticoid/isolation & purification/*metabolism ; Sequence Homology, Nucleic Acid ; Sirolimus ; Tacrolimus/metabolism ; Tacrolimus Binding Proteins
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    Site-specific modification of pre-mRNA: the 2'-hydroxyl groups at the splice sites (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-15
    Description: A simple and efficient method for synthesizing long, site-specifically modified RNA molecules was developed whereby segments of RNA were joined with the use of bacteriophage T4 DNA ligase. A single hydrogen or O-methyl group was substituted for the 2'-hydroxyl group at either splice site of a nuclear pre-messenger RNA substrate. Splicing of the modified pre-messenger RNA's in vitro revealed that, although a 2'-hydroxyl is not absolutely required at either splice site, the 2'-hydroxyl at the 3' splice site is important for the second step of splicing. These results are compared to previous studies of analogous 2'-hydroxyl groups in the self-splicing Tetrahymena group I intron.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, M J -- Sharp, P A -- P30-CA14051/CA/NCI NIH HHS/ -- R01 GM34277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 15;256(5059):992-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589782" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; DNA Ligases/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Exons ; Introns ; Kinetics ; Molecular Sequence Data ; RNA Precursors/*chemistry/metabolism ; *RNA Splicing ; RNA, Messenger/*chemistry/metabolism ; Structure-Activity Relationship ; Tetrahymena/genetics ; Viral Proteins
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    Saltation and stasis: a model of human growth (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-30
    Description: Human growth has been viewed as a continuous process characterized by changing velocity with age. Serial length measurements of normal infants were assessed weekly (n = 10), semiweekly (n = 18), and daily (n = 3) (19 females and 12 males) during their first 21 months. Data show that growth in length occurs by discontinuous, aperiodic saltatory spurts. These bursts were 0.5 to 2.5 centimeters in amplitude during intervals separated by no measurable growth (2 to 63 days duration). These data suggest that 90 to 95 percent of normal development during infancy is growth-free and length accretion is a distinctly saltatory process of incremental bursts punctuating background stasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lampl, M -- Veldhuis, J D -- Johnson, M L -- DK 38942/DK/NIDDK NIH HHS/ -- KO4HD00634/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 30;258(5083):801-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439787" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Body Height ; Cephalometry ; Female ; *Growth ; Head/growth & development ; Humans ; Infant ; Infant, Newborn ; Kinetics ; Male ; *Models, Biological
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    Retinoids selective for retinoid X receptor response pathways (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-12-18
    Description: Retinoids have a broad spectrum of biological activities and are useful therapeutic agents. Their physiological activities are mediated by two types of receptors, the retinoic acid receptors (RARs) and the retinoid X receptors (RXRs). RARs, as well as several related receptors, require heterodimerization with RXRs for effective DNA binding and function. However, in the presence of 9-cis-retinoic acid, a ligand for both RARs and RXRs, RXRs can also form homodimers. A series of retinoids is reported that selectively activates RXR homodimers but does not affect RAR-RXR heterodimers and thus demonstrates that both retinoid response pathways can be independently activated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehmann, J M -- Jong, L -- Fanjul, A -- Cameron, J F -- Lu, X P -- Haefner, P -- Dawson, M I -- Pfahl, M -- CA50676/CA/NCI NIH HHS/ -- P01 CA51993/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1944-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Center, La Jolla Cancer Research Foundation, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1335166" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Structure ; Receptors, Cell Surface/drug effects/genetics/*metabolism ; *Receptors, Retinoic Acid ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; Retinoids/chemistry/*metabolism/pharmacology ; Structure-Activity Relationship ; *Transcription Factors ; Transcription, Genetic ; Transfection ; Tretinoin/metabolism/pharmacology
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    Identification of heregulin, a specific activator of p185erbB2 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The proto-oncogene designated erbB2 or HER2 encodes a 185-kilodalton transmembrane tyrosine kinase (p185erbB2), whose overexpression has been correlated with a poor prognosis in several human malignancies. A 45-kilodalton protein heregulin-alpha (HRG-alpha) that specifically induced phosphorylation of p185erbB2 was purified from the conditioned medium of a human breast tumor cell line. Several complementary DNA clones encoding related HRGs were identified, all of which are similar to proteins in the epidermal growth factor family. Scatchard analysis of the binding of recombinant HRG to a breast tumor cell line expressing p185erbB2 showed a single high affinity binding site [dissociation constant (Kd) = 105 +/- 15 picomolar]. Heregulin transcripts were identified in several normal tissues and cancer cell lines. The HRGs may represent the natural ligands for p185erbB2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Sliwkowski, M X -- Akita, R W -- Henzel, W J -- Lee, J -- Park, J W -- Yansura, D -- Abadi, N -- Raab, H -- Lewis, G D -- New York, N.Y. -- Science. 1992 May 22;256(5060):1205-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Chemistry, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350381" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Breast Neoplasms/genetics ; Cell Line ; Chromatography, High Pressure Liquid ; Codon ; Culture Media ; DNA-Binding Proteins/genetics/isolation & purification/*metabolism ; Epidermal Growth Factor/genetics ; Female ; Glycoproteins/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Neuregulins ; Oligonucleotide Probes ; Phosphorylation ; Protein Conformation ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; *Proto-Oncogenes ; Receptor, ErbB-2 ; Sequence Homology, Nucleic Acid ; Transfection
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    Activation of T cells by a tyrosine kinase activation domain in the cytoplasmic tail of CD3 epsilon (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-03
    Description: The multichain T cell antigen receptor functions by interacting with and activating one or more nonreceptor tyrosine kinases. The cytoplasmic tail of the zeta chain can activate T cells independently of the rest of the receptor complex. The function of the remaining invariant CD3 chains remains unknown. A 22-amino acid region of the cytoplasmic tail of CD3 epsilon was also able to independently activate T cells. Stimulation of T cells by means of the cytoplasmic tails of either zeta or CD3 epsilon resulted in quantitatively distinct patterns of tyrosine phosphorylation, suggesting activation of different biochemical pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Letourneur, F -- Klausner, R D -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1532456" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/genetics/*metabolism ; Cell Line ; Cell Membrane/immunology/metabolism ; Chimera ; Clone Cells ; Humans ; Interleukin-2/biosynthesis ; Kinetics ; *Lymphocyte Activation ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Antigen, T-Cell/genetics/*metabolism ; Receptors, Interleukin-2/genetics/metabolism ; T-Lymphocytes/enzymology/*immunology ; Transfection
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    The disulfide folding pathway of BPTI (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Creighton, T E -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):111-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aprotinin/*chemistry ; Cattle ; *Cysteine ; *Disulfides ; Kinetics ; Models, Molecular ; Protein Conformation
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    Nondissociation of GAL4 and GAL80 in vivo after galactose induction (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-29
    Description: Transcription of galactose-inducible genes in yeast is regulated by interaction between the activator protein GAL4 and the negative regulatory protein GAL80. It has been suggested that GAL80 binds to and represses GAL4 under uninduced conditions and dissociates from GAL4 on induction. However, the possibility that GAL80 remains associated with GAL4 after induction has not been ruled out. Experiments to discriminate between these two models were performed and revealed that GAL80 stays bound after induction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leuther, K K -- Johnston, S A -- New York, N.Y. -- Science. 1992 May 29;256(5061):1333-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Texas-Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598579" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; DNA-Binding Proteins ; Fungal Proteins/biosynthesis/genetics/*metabolism ; Galactose/pharmacology ; *Genes, Fungal ; Kinetics ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/drug effects/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/metabolism ; Transcription, Genetic ; Transformation, Genetic ; beta-Galactosidase/genetics/metabolism
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    Nerve growth factor stimulation of the Ras-guanine nucleotide exchange factor and GAP activities (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: The biological activity of Ras proteins is thought to be controlled by the guanine nucleotide exchange factor and the guanosine triphosphatase activating protein (GAP). Treatment of rat pheochromocytoma PC-12 cells with nerve growth factor (NGF) increased the amount of active Ras guanosine triphosphate complex and stimulated the activities of both the guanine nucleotide exchange factor and GAP. In PC-12 cells that overexpressed the tyrosine kinase encoded by the trk proto-oncogene (a component of the high-affinity NGF receptor), the NGF-induced activation of the regulatory proteins was potentiated. These results suggest that the NGF receptor system enhances the activities of both the guanine nucleotide exchange factor and GAP and that the activation of Ras might be controlled by the balance in activity between these two regulatory proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, B Q -- Kaplan, D -- Kung, H F -- Kamata, T -- N01-CO-74101/CO/NCI NIH HHS/ -- N01-CO-74102/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1456-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Carcinogenesis and Development Program, Program Resources, Inc./DynCorp, Frederick, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604323" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatography, Ion Exchange ; GTPase-Activating Proteins ; Guanine Nucleotide Exchange Factors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Kinetics ; Molecular Weight ; Nerve Growth Factors/*pharmacology ; PC12 Cells ; Phosphates/metabolism ; Proteins/isolation & purification/*metabolism ; Subcellular Fractions/metabolism ; ras GTPase-Activating Proteins ; ras Guanine Nucleotide Exchange Factors
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    A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-22
    Description: The cardiac sodium channel alpha subunit (RHI) is less sensitive to tetrodotoxin (TTX) and saxitoxin (STX) and more sensitive to cadmium than brain and skeletal muscle (microliter) isoforms. An RHI mutant, with Tyr substituted for Cys at position 374 (as in microliter) confers three properties of TTX-sensitive channels: (i) greater sensitivity to TTX (730-fold); (ii) lower sensitivity to cadmium (28-fold); and (iii) altered additional block by toxin upon repetitive stimulation. Thus, the primary determinant of high-affinity TTX-STX binding is a critical aromatic residue at position 374, and the interaction may take place possibly through an ionized hydrogen bond. This finding requires revision of the sodium channel pore structure that has been previously suggested by homology with the potassium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Satin, J -- Kyle, J W -- Chen, M -- Bell, P -- Cribbs, L L -- Fozzard, H A -- Rogart, R B -- HL-20592/HL/NHLBI NIH HHS/ -- HL-37217/HL/NHLBI NIH HHS/ -- NS 23360/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 22;256(5060):1202-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375397" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/physiology ; Cadmium/pharmacology ; Cell Membrane/physiology ; Cloning, Molecular ; Drug Resistance/genetics ; Genetic Vectors ; Heart/*physiology ; Kinetics ; Molecular Sequence Data ; Muscles/physiology ; *Mutagenesis, Site-Directed ; Oocytes/drug effects/*physiology ; Polymerase Chain Reaction ; Protein Conformation ; RNA/genetics ; Rats ; Restriction Mapping ; Saxitoxin/pharmacology ; Sodium Channels/drug effects/genetics/*physiology ; Tetrodotoxin/*pharmacology ; Xenopus
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    Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-10-09
    Description: Altered processing of the amyloid precursor protein (APP) is a central event in the formation of amyloid deposits in the brains of individuals with Alzheimer's disease. To investigate whether cellular APP processing is controlled by cell-surface neurotransmitter receptors, human embryonic kidney (293) cell lines were transfected with the genes for human brain muscarinic acetylcholine receptors. Stimulation of m1 and m3 receptor subtypes with carbachol increased the basal release of APP derivatives within minutes of treatment, indicating that preexisting APP is released in response to receptor activation. Receptor-activated APP release was blocked by staurosporine, suggesting that protein kinases mediate neurotransmitter receptor-controlled APP processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nitsch, R M -- Slack, B E -- Wurtman, R J -- Growdon, J H -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):304-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411529" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/pharmacology ; Alzheimer Disease/*metabolism ; Amyloid beta-Protein Precursor/*secretion ; Atropine/pharmacology ; Blotting, Western ; Brain Chemistry ; Carbachol/pharmacology ; Cell Line ; Embryo, Mammalian ; Humans ; Kidney ; Kinetics ; Protein Kinase C/antagonists & inhibitors/metabolism ; Receptors, Muscarinic/drug effects/genetics/*physiology ; Staurosporine ; Transfection
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    Oxidized redox state of glutathione in the endoplasmic reticulum (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-09-11
    Description: The redox state of the endoplasmic reticulum (ER) was measured with the peptide N-Acetyl-Asn-Tyr-Thr-Cys-NH2. The peptide diffused across cellular membranes; some became glycosylated and thus trapped within the secretory pathway, and its cysteine residue underwent reversible thiol-disulfide exchanges with the surrounding redox buffer. Glycosylated peptides from cells were disulfide-linked to glutathione, indicating that glutathione is the major redox buffer in the secretory pathway. The redox state of the secretory pathway was more oxidative than that of the cytosol; the ratio of reduced glutathione to the disulfide form (GSH/GSSG) within the secretory pathway ranged from 1:1 to 3:1, whereas the overall cellular GSH/GSSG ratio ranged from 30:1 to 100:1. Cytosolic glutathione was also transported into the lumen of microsomes in a cell-free system. Although how the ER maintains an oxidative environment is not known, these results suggest that the demonstrated preferential transport of GSSG compared to GSH into the ER lumen may contribute to this redox compartmentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, C -- Sinskey, A J -- Lodish, H F -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1496-502.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1523409" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Chromatography, High Pressure Liquid ; Chromatography, Thin Layer ; Dogs ; Endoplasmic Reticulum/*metabolism ; Glutathione/analogs & derivatives/*metabolism ; Glutathione Disulfide ; Kinetics ; Microsomes/*metabolism ; Models, Biological ; Molecular Sequence Data ; Oligopeptides/isolation & purification/*metabolism ; Oxidation-Reduction ; Pancreas/metabolism
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    Identification of envelope V3 loop as the major determinant of CD4 neutralization sensitivity of HIV-1 (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-24
    Description: Laboratory isolates of human immunodeficiency virus type-1 (HIV-1) such as HTLV-IIIB are generally T cell line-tropic and highly sensitive to neutralization by soluble CD4 (sCD4), a potential antiviral agent that is undergoing clinical trial. However, many primary HIV-1 isolates are macrophage-tropic and sCD4-resistant. Envelope V3 loop sequences derived from primary HIV-1 isolates were sufficient to confer on HTLV-IIIB not only the tissue tropism but also the degree of sCD4 neutralization resistance characteristic of their HIV-1 strains of origin. Single amino acid changes in the V3 loop enhanced sCD4 resistance by up to tenfold. These observations suggest that the tissue tropism and sCD4 neutralization sensitivity of HIV-1 isolates are regulated by similar mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, S S -- Boyle, T J -- Lyerly, H K -- Cullen, B R -- AI28233/AI/NIAID NIH HHS/ -- AI28662/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 24;257(5069):535-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1636088" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*immunology ; Cell Line ; Cells, Cultured ; Gene Products, gag/*immunology ; HIV Envelope Protein gp120/*immunology ; HIV-1/*immunology/isolation & purification ; Humans ; Kinetics ; Molecular Sequence Data ; Neutralization Tests ; Proviruses/immunology ; T-Lymphocyte Subsets/*immunology ; Transfection ; Virion/immunology
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    Calcium channels coupled to glutamate release identified by omega-Aga-IVA (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-10-09
    Description: Presynaptic calcium channels are crucial elements of neuronal excitation-secretion coupling. In mammalian brain, they have been difficult to characterize because most presynaptic terminals are too small to probe with electrodes, and available pharmacological tools such as dihydropyridines and omega-conotoxin are largely ineffective. Subsecond measurements of synaptosomal glutamate release have now been used to assess presynaptic calcium channel activity in order to study the action of peptide toxins from the venom of the funnel web spider Agelenopsis aperta, which is known to inhibit dihydropyridine and omega-conotoxin-resistant neuronal calcium currents. A presynaptic calcium channel important in glutamate release is shown to be omega-Aga-IVA sensitive and omega-conotoxin resistant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turner, T J -- Adams, M E -- Dunlap, K -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):310-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Tufts University School of Medicine, Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1357749" target="_blank"〉PubMed〈/a〉
    Keywords: Agatoxins ; Animals ; Batrachotoxins/pharmacology ; Brain/physiology/ultrastructure ; Calcium/pharmacology ; Calcium Channels/*physiology ; Egtazic Acid/pharmacology ; Frontal Lobe/ultrastructure ; Glutamates/*secretion ; Glutamic Acid ; Kinetics ; Mollusk Venoms/pharmacology ; Potassium Chloride/pharmacology ; Rats ; Spider Venoms/*pharmacology ; Synaptosomes/physiology ; omega-Agatoxin IVA ; omega-Conotoxin GVIA
    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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