Peptidyl hydroxamic acids as methionine aminopeptidase inhibitors

Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.

P H Hirel, M J Schmitter, P Dessen et al. · Proceedings of the National Academy of Sciences · 1989 · 765 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +11

The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2

Ny Sin, Lihao Meng, Margaret Q. W. Wang et al. · Proceedings of the National Academy of Sciences · 1997 · 627 citations

Medicine, Oncology, Pharmacology +13

Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure

Arie Ben‐Bassat, K. L. Bauer, Sui‐Yuan Chang et al. · Journal of Bacteriology · 1987 · 511 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +8

Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin

Shenping Liu, Joanne Widom, Christopher W. Kemp et al. · Science · 1998 · 437 citations

Life Sciences, Biochemistry, Pharmacology +15

Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin

Eric C. Griffith, Zhuang Su, Benjamin E. Turk et al. · Chemistry & Biology · 1997 · 414 citations · Full text

Medicine, Oncology, Pharmacology +9