Discovery and Structural Modification of Inhibitors of Methionine Aminopeptidases from Escherichia coli and Saccharomyces cerevisiae-Reference-Cited by-同舟云学术

Discovery and Structural Modification of Inhibitors of Methionine Aminopeptidases from Escherichia coli and Saccharomyces cerevisiae

Published:2003-05-22 Issue:13 Volume:46 Page:2631-2640
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Luo Qun-Li¹,Li Jing-Ya¹,Liu Zhi-Ying¹,Chen Ling-Ling¹,Li Jia¹,Qian Zhen¹,Shen Qiang¹,Li Yu¹,Lushington Gerald H.¹,Ye Qi-Zhuang¹,Nan Fa-Jun¹

Affiliation:

1. Chinese National Center for Drug Screening, Shanghai Institute of Materia Medica, Shanghai Institutes for Life Sciences, Chinese Academy of Sciences, 189 Guo Shou Jing Road, Zhangjiang Hi-Tech Park, Shanghai 201203, China, Department of Chemistry, Lanzhou University, 216 Tian Shui Road, Lanzhou, 730000, China, and High-Throughput Screening Laboratory and Molecular Graphics and Modeling Laboratory, University of Kansas, Lawrence, Kansas 66047

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm0300532

Reference16 articles.

1. The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation.

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

3. N-Terminal processing: the methionine aminopeptidase and Nα-acetyl transferase families

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