Mapping the Pathway and Dynamics of Bestatin Inhibition of the Plasmodium falciparum M1 Aminopeptidase Pf A‐M1-Reference-Cited by-同舟云学术

Mapping the Pathway and Dynamics of Bestatin Inhibition of the Plasmodium falciparum M1 Aminopeptidase Pf A‐M1

Published:2018-11-09 Issue:23 Volume:13 Page:2504-2513
ISSN:1860-7179
Container-title:ChemMedChem
language:en
Short-container-title:ChemMedChem

Author:

Yang Wei¹,Riley Blake T.²^ORCID,Lei Xiangyun³,Porebski Benjamin T.²⁴,Kass Itamar²⁵^ORCID,Buckle Ashley M.²^ORCID,McGowan Sheena¹^ORCID

Affiliation:

1. Infection and Immunity Program, Department of Microbiology, Biomedicine Discovery InstituteMonash University Clayton VIC 3800 Australia

2. Infection and Immunity Program, Department of Biochemistry and Molecular Biology, Biomedicine Discovery InstituteMonash University Clayton VIC 3800 Australia

3. School of Chemical and Biomolecular EngineeringGeorgia Institute of Technology Atlanta GA USA

4. Current address: Medical Research Council Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK

5. Victorian Life Sciences Computation CentreMonash University Clayton VIC 3800 Australia

Funder

National Health and Medical Research Council

Publisher

Wiley

Subject

Organic Chemistry,General Pharmacology, Toxicology and Pharmaceutics,Molecular Medicine,Drug Discovery,Biochemistry,Pharmacology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.201800563

Reference76 articles.

1. Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes.

2. Structural basis for multifunctional roles of mammalian aminopeptidase N

3. Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases

4. Structural basis for the inhibition of the essentialPlasmodium falciparumM1 neutral aminopeptidase

5. Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1

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