Expression of a Major Surface Protein ofTrypanosoma bruceiInsect Forms Is Controlled by the Activity of Mitochondrial Enzymes
Author:
Affiliation:
1. Institute of Cell Biology, University of Bern, CH-3012 Bern, Switzerland
2. Institute of Zoology, University of Fribourg, CH-1700 Fribourg, Switzerland
3. Swiss Tropical Institute, CH-4002 Basel, Switzerland
Abstract
Publisher
American Society for Cell Biology (ASCB)
Subject
Cell Biology,Molecular Biology
Reference42 articles.
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2. Bayne, R.A., Kilbride, E.A., Lainson, F.A., Tetley, L., and Barry, J.D. (1993). A major surface antigen of procyclic stageTrypanosoma congolense.Mol. Biochem. Parasitol.61, 295-310.
3. Beecroft, R.P., Roditi, I., and Pearson, T.W. (1993). Identification and characterization of an acidic major surface glycoprotein from procyclic stageTrypanosoma congolense.Mol. Biochem. Parasitol.61, 285-294.
4. Bochud-Allemann, N., and Schneider, A. (2002). Mitochondrial substrate level phosphorylation is essential for growth of procyclicTrypanosoma brucei.J. Biol. Chem.277, 32849-32854.
5. Brun, R., and Schönenberger, M. (1979). Cultivation andin vitrocloning of procyclic culture forms ofTrypanosoma bruceiin a semi-defined medium.Acta Trop.36, 289-292.
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