Discovery of potent, reversible MetAP2 inhibitors via fragment based drug discovery and structure based drug design

Discovery of potent, reversible MetAP2 inhibitors via fragment based drug discovery and structure based drug design—Part 1

Published:2016-06 Issue:12 Volume:26 Page:2774-2778
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Cheruvallath Zacharia,Tang Mingnam,McBride Christopher,Komandla Mallareddy,Miura Joanne,Ton-Nu Thu,Erikson Phil,Feng Jun,Farrell Pamela,Lawson J. David,Vanderpool Darin,Wu Yiqin,Dougan Douglas R.,Plonowski Artur,Holub Corine^ORCID,Larson Chris

Funder

U.S. Department of Energy

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference12 articles.

1. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.

2. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes.

3. An Unusual Peptide Deformylase Features in the Human Mitochondrial N-terminal Methionine Excision Pathway

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

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

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