Identification, Biochemical and Structural Evaluation of Species-Specific Inhibitors against Type I Methionine Aminopeptidases-Reference-Cited by-同舟云学术

Identification, Biochemical and Structural Evaluation of Species-Specific Inhibitors against Type I Methionine Aminopeptidases

Published:2013-06-27 Issue:13 Volume:56 Page:5295-5305
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Kishor Chandan¹,Arya Tarun¹,Reddi Ravikumar¹,Chen Xiaochun²,Saddanapu Venkateshwarlu¹,Marapaka Anil Kumar¹,Gumpena Rajesh¹,Ma Dawei³,Liu Jun O.⁴,Addlagatta Anthony¹

Affiliation:

1. Center for Chemical Biology, CSIR-Indian Institute of Chemical Technology, Tarnaka, Hyderabad AP-500 007, India

2. Department of Pediatrics, University of Maryland School of Medicine, 655 West Baltimore, Street, Baltimore, Maryland 21201, United States

3. State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 354 Fenglin Road, Shanghai 200032, China

4. Departments of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, United States

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm400395p

Reference39 articles.

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

2. Metalloaminopeptidases: Common Functional Themes in Disparate Structural Surroundings

3. Identification of an SH3-Binding Motif in a New Class of Methionine Aminopeptidases from Mycobacterium tuberculosis Suggests a Mode of Interaction with the Ribosome,

4. Methionine Aminopeptidases as Potential Targets for Treatment of Gastrointestinal Cancers and other Tumors

5. Kinetic and Mutational Studies of the Number of Interacting Divalent Cations Required by Bacterial and Human Methionine Aminopeptidases

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