Structure-based optimisation of orally active & reversible MetAP-2 inhibitors maintaining a tight ‘molecular budget’-Reference-Cited by-同舟云学术

Structure-based optimisation of orally active & reversible MetAP-2 inhibitors maintaining a tight ‘molecular budget’

Published:2020-11 Issue:21 Volume:30 Page:127533
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Hirst David J.^ORCID,Brandt Martin,Bruton Gordon,Christodoulou Erica,Cutler Leanne,Deeks Nigel,Goodacre Jonathan D.,Jack Torquil,Lindon Matthew,Miah Afjal,Page Kevin,Parr Nigel,Shukla Lena,Sims Martin,Thomas Pamela,Thorpe James^ORCID,Holmes Duncan S.

Publisher

Elsevier BV

Subject

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

Reference24 articles.

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

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

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

4. High Expression of Methionine Aminopeptidase Type 2 in Germinal Center B Cells and Their Neoplastic Counterparts

5. Immunomodulatory activity of a methionine aminopeptidase-2 inhibitor on B cell differentiation

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