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  • 1990-1994  (9)
  • 1955-1959  (1)
  • 1920-1924
  • Life and Medical Sciences  (5)
  • Analytical Chemistry and Spectroscopy  (3)
  • Memory  (2)
  • 1
    ISSN: 1432-2072
    Keywords: Benzodiazepines ; Diazepam ; Human ; Lorazepam ; Memory ; Repetition priming
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effects of two benzodiazepines, diazepam (15 or 20 mg orally) and lorazepam (1.75 or 2.5 mg orally), and a placebo on explicit memory, lexical priming and perceptual priming were assessed using a freerecall, a word-completion and a picture-completion test. The picture-completion test included two different study conditions intended to manipulate the magnitude of the priming effect. Sixty healthy volunteers took part in this double-blind study. Free-recall performances were altered by both drugs. Lorazepam impaired word-completion and picture-completion performance, whereas diazepam only exhibited a deleterious effect on the more sensitive of the two measures of the picture-completion test. These results indicate that the two benzodiazepines have differential amnestic effects. It is suggested that these differential effects could be accounted for by a different cortical distribution of the two benzodiazepines.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2072
    Keywords: Benzodiazepine ; Diazepam ; Human ; Lorazepam ; Memory ; Perceptual priming
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Unlike diazepam, lorazepam has repeatedly been shown to impair perceptual priming as well as explicit memory. To determine whether this deleterious effect was due to an impairment in acquisition of information, 60 healthy volunteers were randomly assigned to five treatment groups (placebo, lorazepam 0.026 or 0.038 mg/kg, diazepam 0.2 or 0.3 mg/kg) and successively performed perceptual priming tasks and a free-recall task. Priming performance on information learned before or 2 h after drug administration, i.e. at the peak concentration of lorazepam, was assessed under the influence of the drugs, using a picture-fragment and a word-stem completion task. Free-recall performance was altered by both drugs. Lorazepam decreased priming performance when information was acquired after, but not before, drug administration, indicating that the drug alters the acquisition of information. Lorazepam also impaired the ability to identify fragmented pictures, but there was no evidence that this perceptual effect accounts for the priming impairment. Surprisingly, diazepam also decreased priming when information was acquired after drug administration, suggesting that, at least in certain circumstances, the two benzodiazepines may exert similar effects on priming measures.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 133 (1959), S. 219-239 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0730-2312
    Keywords: DNA/protein interaction ; simple repetitive DNA ; binding domain ; conformation changes ; intron 2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Electrophoretic mobility shift assays reveal that HeLa neuclear proteins bind fast and with measurable affinity to target DNAs containing mixed simple repetitive (gt)n(ga)m stretches. Preincubation of the proteins at elevated temperature prevents the formation of the major DNA/protein complex in favour of several distinct assemblies. A similar pattern of retarded bands was observed employing higher salt concentrations in binding reaction. Thus conformational changes of different proteins appear to influence the complex rather than alternating DNA structures. Separation of the total nuclear extract into a water soluble and an insoluble protein fraction leads to a complete loss of target DNA bindinlg capability of the fractions. The binding capacity is restored by combining the two fractions suggesting that at least two protein components are necessary to form a complex with the target sequence. The proteins can be differentiated into head sensitive, water soluble and temporary stable, water insoluble, respectively. Furthermore, specifically binding polypeptides are not detectable by Southwestern analyses, probably because the essential components are separated during electrophoresis. DNase 1 footpoint analyses yield four different protein binding regions only on the (gt)n(ga)m harbouring strand. The footprints cover larger portions of the mixed simple repeat in addition to a portion 5′ of the (gt)n part. Hence at lealst two nuclear protein components of unknown biological function have to be present simultaneously to protect preferentially the (gt)n(ga)m-containing strand intron 2 in HLA-DRB genes
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 8 (1994), S. 692-694 
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Electrospray mass spectrometry has been applied to ionic inorganic systems such as heteropolyacids in methanol + water (1/1) or acetonitrile + water (1/1) solutions. Negative-ion mass spectra were obtained on four different heteropolyacids. Heteropolymolybdates H3PMo12O40 and H4PMo11VO40 and heteropolytungstates H3PW12O40 and H4SiW12O40 gave ions with different charges. H3PMo12O40 gave ions of m/z 1822, 912 and 608 which correspond respectively to [PMo12O403- + 2H+], [PMo12O403- + H+]2- and [PMo12O40]3- ions. Resolution of 1:2200 has demonstrated the charge of each ion acquired. Furthermore, the isotope distribution of the observed ions was in good agreement with theory. Thus, electrospray mass spectrometry has become a powerful soft ionization technique for the analysis of such ionic compounds, provided they are soluble and stable in the solvent system used.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 38 (1994), S. 440-452 
    ISSN: 1040-452X
    Keywords: Spermiogenesis ; Nuclear condensation ; Chromatin ; Protamines ; Protein-precursors ; Neogastropod mollusc ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During the process of chromatin cndensation in the spermiogenesis of the neogastropod mollusc Murex brandaris, the nuclear protein complement undergoes a complex series of changes. These changes lead to the appearance of three small protamines in the ripe sperm nuclei. We have characterized this system electrophoretically and at the compositions with antibodies elicited against a specific spermatozoan protamine. Our results indicate that the complex pattern of chromatin condensation during spermiogenesis in this species (M. brandaris) may be modulated by a series of post-translational (and intranuclear) modifications of DNA-interacting proteins, such as precursors to the sperm protamines. The amino acid composition of each sperm protamine is remarkably simple (lys + arg + gly ≥96 mol%). This system of spermiogenic/spermatozoal proteins in the neogastropod M. brandaris clearly differs from that in patellogastropods and archaeogastropods, and it may be helpful in understanding evolutionary changes in the chromatin condensation pattern during the spermiogenesis of gastropod molluscs. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1059-910X
    Keywords: Ultrastructure ; Immunocytochemistry ; Chromatin structure ; Nuclear proteins ; Testis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: We have followed the fine structural distribution of two nucleosomal core histones, H2B and H3, and of protamines in the course of mouse spermiogenesis by means of specific antibodies and ultrastructural immunocytochemistry.Our results demonstrate that the nuclear labeling density of histone H2B decreases during steps 6-8 and then increases again in step 9-10 spermatids, while the labeling for histone H3 is constant throughout this period. In step 12 spermatids, the anti-H2B antibody labels mainly the central area of the nucleus. The first signs of protamine labeling are present in step 12 spermatids, where the gold grains can be found over the periphery of the nucleus. Later on, protamine labeling constantly increases and, by the end of spermiogenesis, the whole nucleus is labeled.We suggest that the morphological and structural differences between the central area and the periphery of mouse spermatids are, at least partly, due to a difference in the protein moiety associated with DNA. The central area, which is peculiar to the mouse and has been previously considered as a focus of chromatin condensation, represents, however, the last nuclear region containing histones and consequently the last area where the substitution of histones by protamines takes place.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Until the present, analysis of aqueous solutions of atrazine has been conducted using a combination of liquid chromatography or gas chromatography with mass spectrometry, after a preconcentration step. We explore herein a new approach for studying support-phase-extracted atrazine and hydroxyatrazine samples. Solid-phase extraction membranes are inserted directly into the cell of a Fourier-transform mass spectrometer for analysis after laser ionization. It appears that atrazine and its metabolite have very different ionization processes. In the case of hydroxyatrazine, the [M + H]+ ion signal can be correlated to the concentration of the extracted solution. These encouraging results might open the route to a quantification method.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 0749-1581
    Keywords: 27 Al MAS NMR ; Quadruopolar interaction parameters ; Isotropic chemical shfits ; Spectral simulation ; Al2Ge2O7 ; LaAlGe2O7 ; Pentacoordinated aluminium environment ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Characterization by 27Al MAS NMR of two pentacoordinated environments of aluminium has been carried out in different fields and at different spinning speeds for Al2Ge2O7 and LaAlGe2O7. Complete simulations of the spectra have been performed, including computation of the individual shape and intensity of each spinning side band, which lead to the determination of both the quadrupolar interaction parameters and isotropic chemical shifts, and enable the detection of impurities in the material. The parameters determined are: .
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 117-120 
    ISSN: 0749-503X
    Keywords: Thioredoxin ; TRX1 ; TRX2 ; genetic map location ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The two genes encoding thioredoxims in Saccharomyces cerevisiae, TRX1 and TRX2, map to chromosome XII and VII, respectively. From the DNA sequence of the intragenic region TRX1 is 500 bp downstream of PDC1. Tetrad analysis places TRX21·1 cM from ADE3, while a physical map of this region positions TRX2 4·5 kb downstreams of ADE3. The mapping of TRX1 adjacent to PDC1 clarifies previous results (Muller, E. G. D. J. Biol. Chem. 266, 9194-9202, 1991) that suggested a third thioredoxims gene.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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