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Issue 1, 2017
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Exploring inhibitor structural features required to engage the 216-loop of human parainfluenza virus type-3 hemagglutinin-neuraminidase

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Abstract

Human parainfluenza virus type-3 is a leading cause of acute respiratory infection in infants and children. There is currently neither vaccine nor clinically effective treatment for parainfluenza virus infection. Hemagglutinin-neuraminidase glycoprotein is a key protein in viral infection, and its inhibition has been a target for inhibitor development. In this study, we explore the structural features required for Neu2en derivatives to efficiently lock-open the 216-loop of the human parainfluenza virus type-3 hemagglutinin-neuraminidase protein.

Graphical abstract: Exploring inhibitor structural features required to engage the 216-loop of human parainfluenza virus type-3 hemagglutinin-neuraminidase

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Publication details

The article was received on 12 Sep 2016, accepted on 04 Oct 2016 and first published on 05 Oct 2016


Article type: Research Article
DOI: 10.1039/C6MD00519E
Citation: Med. Chem. Commun., 2017,8, 130-134
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    Exploring inhibitor structural features required to engage the 216-loop of human parainfluenza virus type-3 hemagglutinin-neuraminidase

    I. M. El-Deeb, P. Guillon, L. Dirr and M. von Itzstein, Med. Chem. Commun., 2017, 8, 130
    DOI: 10.1039/C6MD00519E

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