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  • Articles: DFG German National Licenses  (3)
  • Life and Medical Sciences  (2)
  • Autoradiography  (1)
  • Substantia gelatinosa
  • 1
    Electronic Resource
    Electronic Resource
    1,25(OH)2 vitamin D3 sites of action in spinal cord and sensory ganglion (1988)
    Springer
    Anatomy and embryology 177 (1988), S. 307-310 
    Details
    ISSN: 1432-0568
    Keywords: Vitamin D ; Receptor ; Spinal cord ; Autoradiography ; Motor neuron ; Substantia gelatinosa ; Spinal ganglion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Autoradiographic studies revealed concentration of 3H 1,25(OH)2 vitamin D3 in nuclei of certain neurons in the spinal cord of adult and neonatal mice, fed a normal or a vitamin D deficient diet. Nuclear uptake and retention was strongest in motor neurons in lamina IX. Nuclear concentration also existed in neurons of lamina II, lamina VIII, lamina X and intermediate nucleus of the lateral column. The results indicate that these neurons are target neurons which contain nuclear receptors for 1,25(OH)2 vitamin D3. this suggests that 1,25(OH)2 vitamin D3 has direct genomic actions on the innervation of skeletal muscle by exerting related trophic, secretory, and electrophysiological effects. In addition, these data point to direct genomic actions of 1,25(OH)2 vitamin D3 on spinal sensory perception, and on certain autonomic functions. Nuclear binding in certain neurons in the peripheral ganglion of the trigeminal nerve further suggests that sensory perception is influenced by 1,25(OH)2 vitamin D3 not only at the level of the substantia gelatinosa, but also at the level of spinal ganglia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315837
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Stabilization of C5a receptor-G-protein interactions through ligand binding (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 55 (1994), S. 380-388 
    Details
    ISSN: 0730-2312
    Keywords: C5a ; ligand binding ; G-protein ; second messenger systems ; neutrophils ; signal transduction ; receptor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Binding of biotin-C5a to the C5a receptor in membrane fragments followed by detergent solubilization and purification with streptavidin-agarose affinity chromatography resulted in the isolation of a receptor complex with associated G-proteins. In contrast, when receptor was detergent-solubilized in the absence of C5a and purified by affinity chromatography with Affigel-C5a, G-proteins did not copurify. Since the results indicate that receptor ligation stabilized the receptor-G-protein interaction to allow purification of the complex, the findings emphasize the dynamic nature of the C5a receptor-effector interactions. When biotin-C5a-ligated receptor was purified from a mouse cell line overexpressing recombinant human receptor, both Gialpha2 and Gialpha3 subunits copurified, confirming that multiple transducing systems are linked to the C5a receptor. The method of stabilization of receptor-transducer complexes offers the opportunity to further elaborate the interactions of the C5a receptor with diverse transducing elements and second messenger systems. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240550316
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Binding of glucocorticoid receptors to model DNA response elements (1991)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 47 (1991), S. 330-336 
    Details
    ISSN: 0730-2312
    Keywords: glucocorticoids ; steroid-receptor family ; steroid-hormone ; gene regulation ; transacting-factors ; mouse mammary tumor virus ; DNA-binding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: DNA sequences were synthesized that contained the consensus 15-base pair glucocorticoid receptor binding site linked to flanking sequences of various lengths. Binding of these synthetic oligomers to glucocorticoid receptor, employing a reconstituted binding system with purified components, indicated that a minimal size of approximately 45 base pairs was necessary to bind the receptor optimally. Sequences containing multiple receptor binding sites competed more effectively for binding. These findings are consistent with recent demonstrations that multiple control elements act synergistically to affect transcriptional control by glucocorticoids and confirm that regions flanking the consensus GRE binding site are instrumental in optimizing binding interactions.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240470407
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    Paper (German National Licenses)
    Fulltext
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