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  • 1990-1994  (6)
  • 1955-1959  (1)
  • 1920-1924
  • 1915-1919  (1)
  • Life and Medical Sciences  (6)
  • Hippocampus  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 348 (1993), S. 1-6 
    ISSN: 1432-1912
    Keywords: Plasticity ; Rat ; Hippocampus ; LTP ; PKC ; Kinase antagonist
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have studied the effects of calphostin C, an antagonist of the regulatory subunit of protein kinase C, on the induction and expression of long-term potentiation (LTP) and on responses mediated by activation of N-methyl-d-aspartate (NMDA) receptors in rat hippocampal slices. No effect of calphostin C was observed on preestablished LTP, even at concentrations of 2–3 μmol/l. In contrast, the drug was found to prevent LTP induction. This effect was concentration-dependent, although high concentrations were needed (1–2 μmol/l), and, at the lower concentrations, it could be partially antagonized by using coactivation of two pathways instead of single input activation. While calphostin C did not alter synaptic transmission mediated by activation of α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptors, it considerably interfered with the function of NMDA receptors. The drug blocked the NMDA receptor-mediated component of burst responses, significantly antagonized the NMDA receptor-mediated synaptic responses recorded in the presence of an AMPA receptor antagonist, and blocked the effect of iontophoretic application of NMDA on regular synaptic transmission. These results are consistent with the idea that calphostin C prevents the induction of long-term potentiation by interfering with the function of NMDA receptors.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6792
    Keywords: 1H-NMR imaging ; (Rat) brain ; Fimbria fornix ; Hippocampus ; Ventricle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Mechanical lesions of the fimbria fornix (FF) have been widely used as a model to investigate the recovery of damaged brain tissue.1H-NMR imaging was employed to non-invasively measure changes in the brain after unilateral FF transection. Rats were subjected to NMR imaging at various times after the lesions were made. The experimental protocol included (multislice) T2-weighted and diffusion-weighted imaging thereby allowing the construction of two-dimensional maps of the relaxation time T2 (transverse or spin-spin relaxation time) and the apparent diffusion coefficient (ADC) of water. FF transection induced considerable changes in the status of the brain tissue at a number of different locations which were exclusively present in the affected hemisphere. At 1 day post-lesion the region of the lateral ventricle and hippocampus started to display pronounced changes in that T2- and diffusion-weighted images showed a hyperintensity and a hypointensity, respectively. These effects were maximal around day 2 to 4 whereafter a slow recovery towards the control situation was observed. Immediately after transection the FF lesion itself could be visualized. These early images pointed to an aspecific disruption of the tissue due to the mechanical intervention. Interestingly, however, from day 2 post-lesion a number of changes became evident in this region which seemed to be localized to specific structures, including the ventricle and hippocampus. After one month the presumably ventricular effect dominated and was predominantly localized to the anterior side of the FF lesion. These findings are indicative of pronounced changes in the status of water (e.g., in its distribution between extra- and intracellular compartments) at a number of locations distant from the site of FF transection. The mechanism by which these changes are brought about and the origin of their time-dependence remain to be elucidated.
    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 [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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 10 (1915), S. 53-65 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
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  • 8
    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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