The DOI matches its Crossref record; 43 of the 44 references it cites were found in a registry or an index.
Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly
Open accessAbstract
Significance: HIV-1 undergoes a two-step assembly process. First, an immature noninfectious particle is assembled, which leaves the infected cell. Second, the structural protein, Gag, is cleaved in the virus by the viral protease, and this leads to formation of the infectious virus. The immature virus particle therefore represents the key intermediate in HIV-1 assembly. There is currently no high-resolution information available on the arrangement of Gag within immature HIV-1. We have assembled part of HIV-1 Gag in vitro to form immature virus-like tubular protein arrays, and have solved a subnanometer-resolution structure of these arrays by using cryo-EM and tomography. This structure reveals interactions of the C-terminal capsid domain of Gag that are critical for HIV-1 assembly.
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“Secondly, a mutated HIV-1 CANC construct has been shown to assemble arrays in vitro in which the CA-CTD arrangement matches that seen in native immature HIV-1 virus particles, while the CA-NTD adopts an arrangement that would be unable to form a hexameric lattice in spherical virions”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [37]
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Self-citationX-Ray Structures of the Hexameric Building Block of the HIV Capsid
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An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation
Schur, F. K. M., Obr, M., Hagen, W. J. H., Wan, W., Jakobi, A. J., Kirkpatrick, J. M., Sachse, C., Kräusslich, H., & Briggs, J. A. G. (2016) · Science · doi:10.1126/science.aaf9620 · Cited by 423
Self-citationStructure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution
Schur, F. K. M., Hagen, W. J. H., Rumlová, M., Ruml, T., Müller, B., Kräusslich, H.-G., & Briggs, J. A. G. (2015) · Nature · doi:10.1038/nature13838 · Cited by 296
Self-citationStructural basis of HIV-1 capsid recognition by PF74 and CPSF6
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Bharat, T. A. M., & Scheres, S. H. W. (2016) · Nature Protocols · doi:10.1038/nprot.2016.124 · Cited by 254
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Metadata
- Authors
- Bharat, T. A. M., Castillo Menendez, L. R., Hagen, W. J. H., Lux, V., Igonet, S., Schorb, M., Schur, F. K. M., Kräusslich, H.-G., & Briggs, J. A. G.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Molecular Medicine Partnership Unit, European Molecular Biology Laboratory/Universitätsklinikum Heidelberg, Heidelberg, Germany;
- European Molecular Biology Laboratory (DE)
- University Hospital Heidelberg (DE)
- Unité de Virologie Structurale, Departement Virologie, Institut Pasteur, 75724 Paris, France; and
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-05-19
- Volume
- 111
- Issue
- 22
- Pages
- 8233-8238
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4050629
- OpenAlex
- W1994410560
- Cited by
- 107
- References
- 44
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 6 · 2023: 9 · 2022: 7 · 2021: 10 · 2020: 6 · 2019: 11 · 2018: 6 · 2017: 4 · 2016: 16 · 2015: 20 · 2014: 5
- FWCI
- 6.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Molecular Biology Laboratory
- Deutsche Forschungsgemeinschaft (KR 906/7-1, BR 3635/2-1)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- HIV-1 Gag, capsid protein, six-helix bundle, Mason-Pfizer monkey virus, retroviral assembly
- MeSH terms
- Virion, HIV-1, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Cryoelectron Microscopy, Capsid Proteins, Nanotubes, gag Gene Products, Human Immunodeficiency Virus
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