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Stanley, B.A. S-adenosylmethionine decarboxylase regulation and processing. pp.
27-75 In Polyamines: Regulation and Molecular Interaction. Robert A. Casero, Jr.
(ed.) R.G. Landes Co., Georgetown, TX, 1995.
Xiong, H., Stanley, B.A., B. L. Tekwani, B.L., and Pegg, A.E. Processing of
mammalian and plant S-adenosylmethionine decarboxylase proenzymes. J. Biol.
Chem. 272(45): 28342-28348, 1997.
Xiong, H., Stanley, B.A., and Pegg, A.E. Role of Cysteine-82 in the Catalytic
Mechanism of Human S-Adenosylmethionine Decarboxylase. Biochemistry 38(8):
2462-2470, 1999
Ekstrom, J.E., Mathews, I.I., Stanley, B.A., Pegg, A.E., and Ealick, S.E. The
crystal structure of human S-adenosylmethionine decarboxylase at 2.25Å reveals
a novel fold. Structure, 7(5): 583-595, 1999
Han, X., Kazarinoff, M.N., Seiler, N., and Stanley, B.A. Rat Colon Ornithine and
Arginine Metabolism: Coordinated Effects after Proliferative Stimuli. Am J
Physiol Gastrointest Liver Physiol 280: G389–G399, 2001
Yerlikaya, A. and Stanley, B.A. S-adenosylmethionine decarboxylase degradation
by the 26S proteasome is accelerated by substrate-mediated transamination. J
Biol Chem. 279(13):12469-78, 2004
Shah, R., Coleman, C.S., Mir, K., Baldwin, J., Van Etten, J.L., Grishin, N.V.,
Pegg, A.E., Stanley, B.A., and Phillips, M.A. Paramecium bursaria Chlorella
Virus-1 Encodes an Unusual Arginine Decarboxylase That Is a Close Homolog of
Eukaryotic Ornithine Decarboxylases. J. Biol. Chem 279(34): 35760-35767,
2004
http://www.jbc.org/cgi/content/abstract/279/34/35760?ct
Coleman C.S., Stanley B.A., Jones A.D., Pegg A.E. Spermidine/spermine N
1-acetyltransferase-2 (SSAT2) acetylates thialysine and is not involved in
polyamine metabolism. Biochem J. 2004 Nov 15;384(Pt 1):139-48, 2004
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