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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

Narthesterol     (3S,8S,9S,10R,13S,14S,17R)- 17-[(2S,3R)-3...

Synonyms: CHEMBL422904, SureCN103516, AG-K-44746, CHEBI:67237, H9384_SIGMA, ...
 
 
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Disease relevance of C05502

 

Psychiatry related information on C05502

 

High impact information on C05502

 

Biological context of C05502

 

Anatomical context of C05502

 

Associations of C05502 with other chemical compounds

 

Gene context of C05502

  • However, this stimulation was observed in cells when acutely (3 h) stimulated with hCG (0.01-1 ng/ml) but not when incubated with 22R-hydroxycholesterol (0.01-10 micrograms/ml) [17].
  • TAT-STPHSTP behaved as a competitive PBR antagonist, which did not affect 22R-hydroxycholesterol-supported steroidogenesis [18].
  • LH- or 22R -hydroxycholesterol-stimulated steroidogenesis in Leydig cells from immature rats did not decrease during the 24-h culture period, whereas ATP levels increased [19].
  • The neuroprotective property of these compounds was coupled to their ability to displace radiolabeled 22R-hydroxycholesterol from Abeta, suggesting that the Abeta-22R-hydroxycholesterol physicochemical interaction contributes to their beneficial effect [20].
  • Computational docking simulations of 22R-hydroxycholesterol and its derivatives on Abeta identified two binding sites [20].
 

Analytical, diagnostic and therapeutic context of C05502

References

  1. 22R-Hydroxycholesterol protects neuronal cells from beta-amyloid-induced cytotoxicity by binding to beta-amyloid peptide. Yao, Z.X., Brown, R.C., Teper, G., Greeson, J., Papadopoulos, V. J. Neurochem. (2002) [Pubmed]
  2. Effect of 22R-hydroxycholesterol on the action of sphingomyelinase from Bacillus cereus toward bovine erythrocytes. Tomita, M., Togami, J., Fujimoto, Y., Ikekawa, N., Taguchi, R., Ikezawa, H. Toxicon (1992) [Pubmed]
  3. Peripheral-type benzodiazepine receptor in neurosteroid biosynthesis, neuropathology and neurological disorders. Papadopoulos, V., Lecanu, L., Brown, R.C., Han, Z., Yao, Z.X. Neuroscience (2006) [Pubmed]
  4. 22R-hydroxycholesterol and 9-cis-retinoic acid induce ATP-binding cassette transporter A1 expression and cholesterol efflux in brain cells and decrease amyloid beta secretion. Koldamova, R.P., Lefterov, I.M., Ikonomovic, M.D., Skoko, J., Lefterov, P.I., Isanski, B.A., DeKosky, S.T., Lazo, J.S. J. Biol. Chem. (2003) [Pubmed]
  5. Targeted disruption of the peripheral-type benzodiazepine receptor gene inhibits steroidogenesis in the R2C Leydig tumor cell line. Papadopoulos, V., Amri, H., Li, H., Boujrad, N., Vidic, B., Garnier, M. J. Biol. Chem. (1997) [Pubmed]
  6. Cytochrome P450 17alpha hydroxylase/17,20 lyase (CYP17) function in cholesterol biosynthesis: identification of squalene monooxygenase (epoxidase) activity associated with CYP17 in Leydig cells. Liu, Y., Yao, Z.X., Papadopoulos, V. Mol. Endocrinol. (2005) [Pubmed]
  7. Leukemia inhibitory factor antagonizes gonadotropin induced-testosterone synthesis in cultured porcine leydig cells: sites of action. Mauduit, C., Goddard, I., Besset, V., Tabone, E., Rey, C., Gasnier, F., Dacheux, F., Benahmed, M. Endocrinology (2001) [Pubmed]
  8. Side-chain specificities of human and bovine cytochromes P-450scc. Tuckey, R.C., Cameron, K.J. Eur. J. Biochem. (1993) [Pubmed]
  9. Cholesterol side-chain cleavage by mitochondria from the human placenta. Studies using hydroxycholesterols as substrates. Tuckey, R.C. J. Steroid Biochem. Mol. Biol. (1992) [Pubmed]
  10. Tumor necrosis factor alpha inhibits gonadotropin action in cultured porcine Leydig cells: site(s) of action. Mauduit, C., Hartmann, D.J., Chauvin, M.A., Revol, A., Morera, A.M., Benahmed, M. Endocrinology (1991) [Pubmed]
  11. Tumor necrosis factor-alpha inhibits leydig cell steroidogenesis through a decrease in steroidogenic acute regulatory protein expression. Mauduit, C., Gasnier, F., Rey, C., Chauvin, M.A., Stocco, D.M., Louisot, P., Benahmed, M. Endocrinology (1998) [Pubmed]
  12. Fetal epidermal differentiation and barrier development In vivo is accelerated by nuclear hormone receptor activators. Hanley, K., Kömüves, L.G., Bass, N.M., He, S.S., Jiang, Y., Crumrine, D., Appel, R., Friedman, M., Bettencourt, J., Min, K., Elias, P.M., Williams, M.L., Feingold, K.R. J. Invest. Dermatol. (1999) [Pubmed]
  13. Pharmacological regulation of cholesterol efflux in human monocyte-derived macrophages in the absence of exogenous cholesterol acceptors. Cignarella, A., Engel, T., von Eckardstein, A., Kratz, M., Lorkowski, S., Lueken, A., Assmann, G., Cullen, P. Atherosclerosis (2005) [Pubmed]
  14. Differences in the control of sterol metabolism between mouse and rat Leydig cells. Quinn, P.G., Georgiou, M., Payne, A.H. Endocrinology (1985) [Pubmed]
  15. Differential effects of dimethylsulfoxide on steroidogenesis in mouse MA-10 and rat R2C Leydig tumor cells. Stocco, D.M., King, S., Clark, B.J. Endocrinology (1995) [Pubmed]
  16. A role for src tyrosine kinase in regulating adrenal aldosterone production. Sirianni, R., Sirianni, R., Carr, B.R., Pezzi, V., Rainey, W.E. J. Mol. Endocrinol. (2001) [Pubmed]
  17. Epidermal growth factor directly stimulates steroidogenesis in primary cultures of porcine Leydig cells: actions and sites of action. Sordoillet, C., Chauvin, M.A., de Peretti, E., Morera, A.M., Benahmed, M. Endocrinology (1991) [Pubmed]
  18. Identification of a peptide antagonist to the peripheral-type benzodiazepine receptor that inhibits hormone-stimulated leydig cell steroid formation. Gazouli, M., Han, Z., Papadopoulos, V. J. Pharmacol. Exp. Ther. (2002) [Pubmed]
  19. Development of adenosine responsiveness after isolation of Leydig cells. Rommerts, F.F., Molenaar, R., Hoogerbrugge, J.W., van der Molen, H.J. Biol. Reprod. (1984) [Pubmed]
  20. Identification of naturally occurring spirostenols preventing beta-amyloid-induced neurotoxicity. Lecanu, L., Yao, W., Teper, G.L., Yao, Z.X., Greeson, J., Papadopoulos, V. Steroids (2004) [Pubmed]
  21. Studies of distant members of the P450 superfamily (P450scc and P450c27) by random chimeragenesis. Pikuleva, I.A., Björkhem, I., Waterman, M.R. Arch. Biochem. Biophys. (1996) [Pubmed]
  22. Identification of intermediates in the conversion of cholesterol to pregnenolone with a reconstituted cytochrome p-450scc system: accumulation of the intermediate modulated by the adrenodoxin level. Sugano, S., Miura, R., Morishima, N. J. Biochem. (1996) [Pubmed]
 
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