Structure-guided stabilization improves the ability of the HIV-1 gp41 hydrophobic pocket to elicit neutralizing antibodies-Reference-Cited by-同舟云学术

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Structure-guided stabilization improves the ability of the HIV-1 gp41 hydrophobic pocket to elicit neutralizing antibodies

Published:2023-04 Issue:4 Volume:299 Page:103062
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bruun Theodora U.J.^ORCID,Tang Shaogeng^ORCID,Erwin Graham^ORCID,Deis Lindsay,Fernandez Daniel^ORCID,Kim Peter S.

Funder

NIH

Publisher

Elsevier BV

Reference70 articles.

1. Core structure of Gp41 from the HIV envelope glycoprotein;Chan;Cell,1997

2. HIV entry and its inhibition;Chan;Cell,1998

3. Atomic structure of the ectodomain from HIV-1 Gp41;Weissenhorn;Nature,1997

4. Viral membrane fusion;Harrison;Virology,2015

5. Electron tomography visualization of HIV-1 fusion with target cells using fusion inhibitors to trap the pre-hairpin intermediate;Ladinsky;eLife,2020

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1. A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning;Nature Communications;2025-05-18

2. Allosteric inhibition of the IZUMO1–JUNO fertilization complex by the naturally occurring antisperm antibody OBF13;Proceedings of the National Academy of Sciences;2025-03-05

3. Stabilized trimeric peptide immunogens of the complete HIV-1 gp41 N-heptad repeat and their use as HIV-1 vaccine candidates;Proceedings of the National Academy of Sciences;2024-05-20

4. Bringing immunofocusing into focus;npj Vaccines;2024-01-09

5. Alpaca-derived nanobody targeting the hydrophobic pocket of the HIV-1 gp41 NHR broadly neutralizes HIV-1 by blocking six-helix bundle formation;Current Research in Microbial Sciences;2024

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