Inhibition of calcium-activated, phospholipid-dependent protein kinase (protein kinase C) activity in sphingolipidoses
Author:
Publisher
Wiley
Subject
Genetics(clinical),Genetics
Link
http://www.springerlink.com/index/pdf/10.1007/BF01811712
Reference8 articles.
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3. Downes, P., Mussat, M. C. and Michell, R. H. The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane.Biochem. J. 203 (1982) 169–177
4. Eto, Y., Weismann, U. and Hershkowitz, N. Sulfagalactosylsphingosine sulfatase. Characteristics of the enzyme and its deficiency in metachromatic leukodystrophy in human cultured skin fibroblasts.J. Biol. Chem. 249 (1974) 4955–4960
5. Hannun, Y. and Bell, R. M. Lysosphingolipids inhibit protein kinase C: Implications for the sphingolipidoses.Science 235 (1987) 670–674
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1. Possible role for protein kinase C in the pathogenesis of inborn errors of metabolism;Journal of Cellular Biochemistry;1995-09
2. Effect of fatty acids and their acyl-CoA esters on protein kinase C activity in fibroblasts: Possible implications in fatty acid oxidation defects;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1994-03
3. Sphingolipid breakdown products: anti-proliferative and tumor-suppressor lipids;Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes;1993-12
4. Bilirubin inhibits protein kinase C activity and protein kinase C-mediated phosphorylation of endogenous substrates in human skin fibroblasts;Clinica Chimica Acta;1993-12
5. Inhibition of protein kinase C activity in mucolipidosis type-4: a model for a new pathogenetic mechanism in inborn errors of metabolism;Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease;1993-08
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