Increased formation of N1-acetylspermidine in human breast cancer.

[1]  A. Pegg,et al.  Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. , 1988, Cancer research.

[2]  N. Seiler Functions of polyamine acetylation. , 1987, Canadian journal of physiology and pharmacology.

[3]  H. Wallace,et al.  Elevation of monoacetylated polyamines in human breast cancers. , 1985, European journal of cancer & clinical oncology.

[4]  N. Seiler,et al.  Polyamine metabolism and polyamine excretion in normal and tumor bearing rodents. , 1985, Anticancer research.

[5]  N. Seiler,et al.  The influence of catabolic reactions on polyamine excretion. , 1985, The Biochemical journal.

[6]  A. Pegg,et al.  Studies of the induction of spermidine/spermine N1-acetyltransferase using a specific antiserum. , 1984, The Journal of biological chemistry.

[7]  A. Pegg,et al.  Differential inhibition of histone and polyamine acetylases by multisubstrate analogues. , 1984, Biochemistry.

[8]  S. Takenoshita,et al.  Selective elevation of the N1-acetylspermidine level in human colorectal adenocarcinomas. , 1984, Cancer research.

[9]  D. Russell,et al.  Clinical relevance of polyamines. , 1983, Critical reviews in clinical laboratory sciences.

[10]  O. Rennert,et al.  Interconversion, catabolism and elimination of the polyamines. , 1981, Medical biology.

[11]  A. Pegg,et al.  Properties of spermidine N-acetyltransferase from livers of rats treated with carbon tetrachloride and its role in the conversion of spermidine into putrescine. , 1981, The Journal of biological chemistry.

[12]  P. Libby Rat liver nuclear N-acetyltransferases: separation of two enzymes with both histone and spermidine acetyltransferase activity. , 1980, Archives of biochemistry and biophysics.

[13]  M. Abdel-monem,et al.  Polyamine metabolism III: urinary acetyl polyamines in human cancer. , 1978, Journal of pharmaceutical sciences.

[14]  P. Libby Calf liver nuclear N-acetyltransferases. Purification and properties of two enzymes with both spermidine acetyltransferase and histone acetyltransferase activities. , 1978, The Journal of biological chemistry.