Binding of Influenza A Virus Hemagglutinin to the Sialoside Receptor Is Not Controlled by the Homotropic Allosteric Effect-Reference-Cited by-同舟云学术

Binding of Influenza A Virus Hemagglutinin to the Sialoside Receptor Is Not Controlled by the Homotropic Allosteric Effect

Published:2010-11-04 Issue:47 Volume:114 Page:15700-15705
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Sawada Toshihiko¹,Fedorov Dmitri G.¹,Kitaura Kazuo¹

Affiliation:

1. Nanosystem Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan, Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan, and Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp1068895

Reference73 articles.

1. Influenza: lessons from past pandemics, warnings from current incidents

2. Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin

3. Molecular Design of Artificial Molecular and Ion Recognition Systems with Allosteric Guest Responses

4. First Successful Molecular Design of an Artificial Lewis Oligosaccharide Binding System Utilizing Positive Homotropic Allosterism

5. Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study

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