Stability of HA2 Prefusion Structure and pH-Induced Conformational Changes in the HA2 Domain of H3N2 Hemagglutinin-Reference-Cited by-同舟云学术

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Stability of HA2 Prefusion Structure and pH-Induced Conformational Changes in the HA2 Domain of H3N2 Hemagglutinin

Published:2021-08-26 Issue:35 Volume:60 Page:2623-2636
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Eller Micah W.¹,Siaw Hew Ming Helen¹,Dyer R. Brian¹^ORCID

Affiliation:

1. Department of Chemistry, Emory University, Atlanta, Georgia 30322, United States

Funder

National Center for Advancing Translational Sciences

Emory University School of Medicine

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00551

Reference50 articles.

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

2. A Sialylated Voltage-Dependent Ca2+ Channel Binds Hemagglutinin and Mediates Influenza A Virus Entry into Mammalian Cells

3. Hemagglutinin-Mediated Membrane Fusion: A Biophysical Perspective

4. Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

5. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Molecular dynamics investigation of the influenza hemagglutinin conformational changes in acidic pH;2024-07-10

2. A large HIV gp41 construct with trimer-of-hairpins structure exhibits V2E mutation-dominant attenuation of vesicle fusion and helicity very similar to V2E attenuation of HIV fusion and infection and supports: (1) hairpin stabilization of membrane apposition with larger distance for V2E; and (2) V2E dominance by an antiparallel β sheet with interleaved fusion peptide strands from two gp41 trimers;Biophysical Chemistry;2023-02

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