Refolding Dynamics of gp41 from Pre-fusion to Pre-hairpin States during HIV-1 Entry-Reference-Cited by-同舟云学术

Refolding Dynamics of gp41 from Pre-fusion to Pre-hairpin States during HIV-1 Entry

Published:2019-12-17 Issue:1 Volume:60 Page:162-174
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Lin Mengna¹,Da Lin-Tai¹^ORCID

Affiliation:

1. Key Laboratory of System Biomedicine (Ministry of Education), Shanghai Center for Systems Biomedicine, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai 200240, China

Funder

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.9b00746

Reference81 articles.

1. Molecular architecture of native HIV-1 gp120 trimers

2. Partially Open HIV-1 Envelope Structures Exhibit Conformational Changes Relevant for Coreceptor Binding and Fusion

3. Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor

4. Structural basis of coreceptor recognition by HIV-1 envelope spike

5. A dynamic three-step mechanism drives the HIV-1 pre-fusion reaction

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