Specificity for inhibitors of metal-substituted methionine aminopeptidase
- 24 June 2003
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 307 (1) , 172-179
- https://doi.org/10.1016/s0006-291x(03)01144-6
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Methionine In and Out of Proteins: Targets for Drug DesignCurrent Medicinal Chemistry, 2002
- Genome sequence of enterohaemorrhagic Escherichia coli O157:H7Nature, 2001
- Structure and function of the methionine aminopeptidasesPublished by Elsevier ,2000
- Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2Proceedings of the National Academy of Sciences, 1998
- Structure of Human Methionine Aminopeptidase-2 Complexed with FumagillinScience, 1998
- N-Terminal processing: the methionine aminopeptidase and Nα-acetyl transferase familiesTrends in Biochemical Sciences, 1998
- The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2Proceedings of the National Academy of Sciences, 1997
- Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.Proceedings of the National Academy of Sciences, 1995
- pepM is an essential gene in Salmonella typhimuriumJournal of Bacteriology, 1989
- Methionine aminopeptidase gene of Escherichia coli is essential for cell growthJournal of Bacteriology, 1989