High-Speed AFM Reveals Molecular Dynamics of Human Influenza A Hemagglutinin and Its Interaction with Exosomes-Reference-Cited by-同舟云学术

High-Speed AFM Reveals Molecular Dynamics of Human Influenza A Hemagglutinin and Its Interaction with Exosomes

Published:2020-07-27 Issue:9 Volume:20 Page:6320-6328
ISSN:1530-6984
Container-title:Nano Letters
language:en
Short-container-title:Nano Lett.

Author:

Lim Keesiang¹,Kodera Noriyuki¹,Wang Hanbo²,Mohamed Mahmoud Shaaban²,Hazawa Masaharu¹²,Kobayashi Akiko²,Yoshida Takeshi¹³,Hanayama Rikinari¹³,Yano Seiji¹⁴,Ando Toshio¹^ORCID,Wong Richard W.¹²^ORCID

Affiliation:

1. WPI-Nano Life Science Institute, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan

2. Cell-Bionomics Research Unit, Institute for Frontier Science Initiative (INFINITI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan

3. Department of Immunology, Kanazawa University Graduate School of Medical Sciences, 13-1 Takara, Kanazawa, Ishikawa 920-8640, Japan

4. Division of Medical Oncology, Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan

Funder

Japan Society for the Promotion of Science

Kobayashi International Scholarship Foundation

Shimadzu Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Mechanical Engineering,Condensed Matter Physics,General Materials Science,General Chemistry,Bioengineering

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.nanolett.0c01755

Reference59 articles.

1. Influenza

2. Global and regional mortality from 235 causes of death for 20 age groups in 1990 and 2010: a systematic analysis for the Global Burden of Disease Study 2010

3. Receptor binding and pH stability — How influenza A virus hemagglutinin affects host-specific virus infection

4. THE STRUCTURE AND FUNCTION OF THE HEMAGGLUTININ MEMBRANE GLYCOPROTEIN OF INFLUENZA VIRUS

5. A spring-loaded mechanism for the conformational change of influenza hemagglutinin

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