By George Klein (ed.), Sidney Weinhouse (ed.)

ISBN-10: 0120066491

ISBN-13: 9780120066490

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J. Levine, G. F. Wande Woude, W. C. Topp, and J. D. ),Vol. 1, pp. 191-200. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York. , and Holtzer, H. (1977). Cell 11, 891-899. Palmieri, S. J . Virol. 58, 134-141. , and Graf, T. (1982). Virology 123, 296-311. , and Graf, T. (1983). EMBO J . 2,2385-2389. , Bartholomew, J. , and Bissell, M. J. (1980). Nature (London)288,720-722. Paterson, B. , and Eldridge, J. D. (1984). Science 224, 1436-1438. Pearson, M. , and Epstein, H. , eds. (1982). ” Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.

1985). Thus, the gag moiety of FBR-MSV can be removed without affecting its transforming potential. 15. The transformingfos proteins vary in size from 268 amino acids (FBJ/R) to 381 amino acids (FBJ), but they all have nuclear location. Additionally, all fos proteins coimmunoprecipitate a 39K cellular protein whose identify remains obscure. 16. , 1985). 17. , 1984). , 1984). The extent and precise nature of the fos protein modifications remain unknown, but part of the modifications is due to phosphorylation (J.

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Advances in Cancer Research, Vol. 49 by George Klein (ed.), Sidney Weinhouse (ed.)

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