The DOI matches its Crossref record; 53 of the 54 references it cites were found in a registry or an index.
Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
Open accessAbstract
The capsids of mature retroviruses perform the essential function of organizing the viral genome for efficient replication. These capsids are modeled as fullerene structures composed of closed hexameric arrays of the viral CA protein, but a high-resolution structure of the lattice has remained elusive. A three-dimensional map of two-dimensional crystals of the R18L mutant of HIV-1 CA was derived by electron cryocrystallography. The docking of high-resolution domain structures into the map yielded the first unambiguous model for full-length HIV-1 CA. Three important protein-protein assembly interfaces are required for capsid formation. Each CA hexamer is composed of an inner ring of six N-terminal domains and an outer ring of C-terminal domains that form dimeric linkers connecting neighboring hexamers. Interactions between the two domains of CA further stabilize the hexamer and provide a structural explanation for the mechanism of action of known HIV-1 assembly inhibitors.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In HIV six CA-NTDs form a hexameric ring with a central 18 helix bundle formed by helices 1, 2, and 3, providing the main intrahexamer stability”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [52]
Citations
Cites
Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
Henderson, R. A., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E., & Downing, K. H. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80271-2 · Cited by 2,982
Automated molecular microscopy: The new Leginon system
Suloway, C. J. M., Pulokas, J., Fellmann, D., Cheng, A., Guerra, F., Quispe, J. D., Stagg, S. M., Potter, C. S., & Carragher, B. O. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.03.010 · Cited by 1,695
Self-citationCrowther, R. A., Henderson, R. A., & Smith, J. M. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0003 · Cited by 716
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706 · cited 2×
“…the HIV-1 CA NTD is shaped as an arrowhead, with seven a helices (numbered 1–7) and an amino-terminal b-hairpin (Berthet-Colominas et al., 1999; Gamble et al., 1996; Gitti et al., 1996), while the CTD is more globular, with a single-turn 3 10 -helix and four short a helices (numbered 8–11)…”
Henderson, R. A., Baldwin, J. M., Downing, K. H., Lepault, J., & Zemlin, F. (1986) · Ultramicroscopy · doi:10.1016/0304-3991(86)90203-2 · Cited by 677
Assembly and Analysis of Conical Models for the HIV-1 Core
Ganser, B. K., Li, S., Klishko, V. Y., Finch, J. T., & Sundquist, W. I. (1999) · Science · doi:10.1126/science.283.5398.80 · Cited by 671
Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H., McCutcheon, J. P., Sundquist, W. I., & Hill, C. P. (1997) · Science · doi:10.1126/science.278.5339.849 · Cited by 598 · cited 11×
“…CA proteins have revealed an atomic resolution model for the hexamer formed by the NTD of N-tropic murine leukemia virus (Mortuza et al., 2004) and several possible models for the CTD dimer (Gamble et al., 1997; Ivanov et al., 2007; Jin et al., 1999; Ternois et al., 2005; Worthylake et al., 1999).”
InfluentialThe stoichiometry of Gag protein in HIV-1
Briggs, J. A. G., Simon, M. N., Gross, I., Kräusslich, H.-G., Fuller, S. D., Vogt, V. M., & Johnson, M. C. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb785 · Cited by 539
Situs: A Package for Docking Crystal Structures into Low-Resolution Maps from Electron Microscopy
Wriggers, W. R., Milligan, R. A., & McCammon, J. A. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1998.4080 · Cited by 521
Three-dimensional structure determination by electron microscopy of two-dimensional crystals
Amos, L., Henderson, R. A., & Unwin, P. N. T. (1982) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(83)90017-2 · Cited by 509
Flagged first, then by citations
1 of the 54 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 301–327 of 327
Biswas, N., Ghosh, S., & Bag, A. (2019) · ChemRxiv · doi:10.26434/chemrxiv.9992081.v1
Faculty Opinions recommendation of Atomic-level modelling of the HIV capsid.
Columbus, L. M., & Dewald, A. H. (2011) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.8136959.10321054
Faculty Opinions recommendation of Visualization of a missing link in retrovirus capsid assembly.
Conway, J. F. (2009) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1148048.605159
Informatically-informed biochemical characterization of aptamer-protein complexes
Gruenke, P. R. (2022) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/91663
Nakamura, T., Takamune, N., Okumura, M., Yasunaga, J., Sugiura, M., & Amano, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.19.649630
Transient Occupancy and Pore Dynamics: IP6 Behavior in HIV-1 T = 4 Capsids
Macke, A. C., Xu, C., Sudhakar, S., & Perilla, J. R. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c05351 · Cited by 1
Cabrera-Rodríguez, R., Pons-Grífols, A., Pernas, M., Casado, C., Trujillo‐González, R., Lorenzo-Sánchez, I., Reyes-Castañeda, I., Trinité, B., Blanco, J., & Valenzuela-Fernández, A. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02762-x
Lysova, I., Didier, P., Messaddeq, N., Bouthenet, J., Mély, Y., & Anton, H. (2026) · Methods and Applications in Fluorescence · doi:10.1088/2050-6120/ae5504
Giroud, C. (2012) · theses.fr (ABES) · doi:10.70675/dcb13f1azfc90z47d6zb978z456e9b4d70d5
Implication de la machinerie des microRNA dans la réplication rétrovirale
Bouttier, M. (2011) · theses.fr (ABES) · doi:10.70675/7705ed5cz61a8z4e90z8edfz5de46a1563ed
Interactions between primate lentiviral capsids and heterologous cellular host factors
Mamede, J. I. (2012) · theses.fr (ABES) · doi:10.70675/e3f4366bzb31fz4382z8f0cz19483f12bfe7
Caractérisation et conservation des mécanismes antiviraux des protéines IFITMs
Appourchaux, R. (2017) · theses.fr (ABES) · doi:10.70675/d001d208z7f71z40f3za8abzbf3a6cd40964
Identification of specific phylogenetic properties of HIV-1 M and O integrases
Toccafondi, E. (2022) · theses.fr (ABES) · doi:10.70675/2facab6ezc20az472dz8350z9fb6e718e1d4 · Cited by 1
Mechanisms of HIV-1 assembly, release and maturation
Kleinpeter, A. B., & Freed, E. O. (2026) · Nature Reviews Microbiology · doi:10.1038/s41579-026-01327-6 · Cited by 2
HIV capsid inhibitors: Mechanisms, resistance, and therapeutic advances
Mahdi, M., Lakatos, B., Mótyán, J. A., Hoffka, G., & Tőzsér, J. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014361
Jiang, X., Yu, R., Foley, N., Xue, X., Dai, J., Wang, M., Nie, Z., Chen, C., Clercq, E. D., Pannecouque, C. C., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c01058
Knelissen, Y. K., Escrig, J., Macke, A. C., Sudhakar, S., Domínguez‐Zotes, S., Maity, S., Mateu, M. G., Perilla, J. R., Roos, W. H., & Valbuena, A. (2026) · ACS Nano · doi:10.1021/acsnano.6c07706 · Cited by 1
Capillary physics links HIV capsid geometry to nuclear pore translocation
Brown, A. W., Al-Izzi, S. C., Parker, J. L., Hertel, S., Jacques, D. A., Kusumaatmaja, H., & Morris, R. G. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2605059123
BindingDB Entry 50015611: An insight on medicinal aspects of novel HIV-1 capsid protein inhibitors.
BindingDB (2023) · UC San Diego · doi:10.7270/q21z48bw
HIV-1 and the Nucleolus: A Role for Nucleophosmin/NPM1 in Viral Replication: A Dissertation
Schmidt, T. E. (2013) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/m2mk6v
Metadata
- Authors
- Ganser-Pornillos, B. K., Cheng, A., & Yeager, M.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Yeager, Mark
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-10
- Volume
- 131
- Issue
- 1
- Pages
- 70-79
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2034606779
- Cited by
- 321
- References
- 54
- Citations by year
- 2026: 8 · 2025: 4 · 2024: 8 · 2023: 3 · 2022: 7 · 2021: 16 · 2020: 18 · 2019: 15 · 2018: 6 · 2017: 19 · 2016: 11 · 2015: 23 · 2014: 16 · 2013: 28 · 2012: 26
- FWCI
- 10.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2116 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM066087)
- National Institute of Allergy and Infectious Diseases (T32AI07244, T32AI007244)
- National Center for Research Resources (P41 RR17573, P41RR017573)
- 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 capsid protein, capsid lattice, hexamer assembly, protein-protein interaction, N-terminal domain, C-terminal domain, viral capsid structure
- MeSH terms
- Capsid, Humans, Models, Molecular, HIV-1, Crystallography, X-Ray, Cryoelectron Microscopy, Protein Structure, Quaternary, Capsid Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
