Features of the spermidine-binding site of deoxyhypusine synthase as derived from inhibition studies. Effective inhibition by bis- and mono-guanylated diamines and polyamines
Open Access
- 1 June 1993
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (18), 13151-13159
- https://doi.org/10.1016/s0021-9258(19)38631-4
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Protein interactions with urea and guanidinium chlorideJournal of Molecular Biology, 1992
- Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptideBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- Fluorinated analogues of spermidine as substrates of spermine synthaseEuropean Journal of Biochemistry, 1988
- Chemistry of naturally occurring polyamines. 9. Synthesis of spermidine and spermine photoaffinity labeling reagentsThe Journal of Organic Chemistry, 1985
- Cellular proliferation and hypusine synthesisExperimental Cell Research, 1984
- An 18 000-dalton protein metabolically labeled by polyamines in various mammalian cell linesBiochimica et Biophysica Acta (BBA) - General Subjects, 1983
- Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growthCell, 1982
- Reagents for the Selective SecondaryN-Acylation of Linear TriaminesSynthesis, 1982
- Anion Coordination Chemistry: Polyguanidinium Salts as Anion ComplexonesHelvetica Chimica Acta, 1979
- Selective reductions. XVIII. Fast reaction of primary, secondary, and tertiary amides with diborane. Simple, convenient procedure for the conversion of amides to the corresponding aminesThe Journal of Organic Chemistry, 1973