Cited by 307HIV Research and TreatmentHIV/AIDS drug development and treatmentT-cell and Retrovirus Studies

The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.

Assembly Properties of the Human Immunodeficiency Virus Type 1 CA Protein

Open access

Ganser-Pornillos, Barbie K., von Schwedler, Uta K., Stray, Kirsten M., Aiken, Christopher, Sundquist, Wesley I.·2004·Journal of Virology

DOI 10.1128/jvi.78.5.2545-2552.2004PMC PMC369201

Open this paper in CoChat — free account

Abstract

During retroviral maturation, the CA protein oligomerizes to form a closed capsid that surrounds the viral genome. We have previously identified a series of deleterious surface mutations within human immunodeficiency virus type 1 (HIV-1) CA that alter infectivity, replication, and assembly in vivo. For this study, 27 recombinant CA proteins harboring 34 different mutations were tested for the ability to assemble into helical cylinders in vitro. These cylinders are composed of CA hexamers and are structural models for the mature viral capsid. Mutations that diminished CA assembly clustered within helices 1 and 2 in the N-terminal domain of CA and within the crystallographically defined dimer interface in the CA C-terminal domain. These mutations demonstrate the importance of these regions for CA cylinder production and, by analogy, mature capsid assembly. One CA mutant (R18A) assembled into cylinders, cones, and spheres. We suggest that these capsid shapes occur because the R18A mutation alters the frequency at which pentamers are incorporated into the hexagonal lattice. The fact that a single CA protein can simultaneously form all three known retroviral capsid morphologies supports the idea that these structures are organized on similar lattices and differ only in the distribution of 12 pentamers that allow them to close. In further support of this model, we demonstrate that the considerable morphological variation seen for conical HIV-1 capsids can be recapitulated in idealized capsid models by altering the distribution of pentamers.

Integrity signals

Registry

Crossref · 10.1128/jvi.78.5.2545-2552.2004

Cites

59 of 59 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Database resources of the National Center for Biotechnology Information: update
Wheeler, D. L. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh073 · Cited by 10,695
Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
Luban, J., Bossolt, K. L., Franke, E. K., Kalpana, G. V., & Goff, S. P. (1993) · Cell · doi:10.1016/0092-8674(93)90637-6 · Cited by 792
HIV-1 Gag proteins: diverse functions in the virus life cycle
Freed, E. O. (1998) · Virology · doi:10.1006/viro.1998.9398 · Cited by 717
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 1×
“important for infectivity and assembly (18, 52, 53, 56).”
BackgroundSelf-citation
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
Self-citation
Functional association of cyclophilin A with HIV-1 virions
Thali, M., Bukovsky, A., Kondo, E., Rosenwlrth, B., Walsh, C. T., Sodroski, J., & Göttlinger, H. G. (1994) · Nature · doi:10.1038/372363a0 · Cited by 629
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 2×
“The HIV type 1 (HIV-1) CA CTD dimerizes in solution and is also crystallized as a dimer ( 19 , 44, 56).”
BackgroundSelf-citation
Database resources of the National Center for Biotechnology Information
Wheeler, D. L. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.10 · Cited by 583
Image reconstructions of helical assemblies of the HIV-1 CA protein
Li, S., Hill, C. P., Sundquist, W. I., & Finch, J. T. (2000) · Nature · doi:10.1038/35030177 · Cited by 500
Self-citation
Structural organization of authentic, mature HIV‐1 virions and cores
Briggs, J. A. G., Wilk, T., Welker, R., Kräusslich, H., & Fuller, S. D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg143 · Cited by 496

Show all 59 references

Sorted by citations

Items 101–200 of 307

In vitro protease cleavage and computer simulations reveal the HIV-1 capsid maturation pathway
Ning, J., Erdemci-Tandogan, G., Yufenyuy, E. L., Wagner, J., Himes, B. A., Zhao, G., Aiken, C., Zandi, R., & Zhang, P. (2016) · Nature Communications · doi:10.1038/ncomms13689 · Cited by 55
Self-citation
Site-Specific Structural Variations Accompanying Tubular Assembly of the HIV-1 Capsid Protein
Bayro, M. J., Chen, B., Yau, W., & Tycko, R. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.12.021 · Cited by 54
Characterization of the In Vitro HIV-1 Capsid Assembly Pathway
Barklis, E., Alfadhli, A., McQuaw, C. M., Yalamuri, S. M., Still, A., Barklis, R. L., Kukull, B., & López, C. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.058 · Cited by 54
The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability
Jiang, J., Ablan, S. D., Derebail, S. S., Hercík, K., Soheilian, F., Thomas, J. A., Tang, S., HEWLETT, I. K., Nagashima, K., Gorelick, R. J., et al. (2011) · Virology · doi:10.1016/j.virol.2011.09.012 · Cited by 57
Simulated Self-Assembly of the HIV-1 Capsid: Protein Shape and Native Contacts Are Sufficient for Two-Dimensional Lattice Formation
Chen, B., & Tycko, R. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.05.025 · Cited by 51
Live cell visualization of the interactions between HIV-1 Gag and the cellular RNA-binding protein Staufen1
Milev, M. P., Brown, C. M., & Mouland, A. J. (2010) · Retrovirology · doi:10.1186/1742-4690-7-41 · Cited by 52
Structural and dynamical characterization of tubular HIV‐1 capsid protein assemblies by solid state nuclear magnetic resonance and electron microscopy
Chen, B., & Tycko, R. (2010) · Protein Science · doi:10.1002/pro.348 · Cited by 54
HIV Capsid Assembly, Mechanism, and Structure
Chen, B. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00159 · Cited by 57
Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5α identified by magic-angle spinning NMR and molecular dynamics simulations
Quinn, C. M., Wang, M., Fritz, M. P., Runge, B., Ahn, J., Xu, C., Perilla, J. R., Gronenborn, A. M., & Polenova, T. E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800796115 · Cited by 53
Investigation of N-Terminal Domain Charged Residues on the Assembly and Stability of HIV-1 CA
Douglas, C. C., Thomas, D. R., Lanman, J. K., & Prevelige, P. E. (2004) · Biochemistry · doi:10.1021/bi049359g · Cited by 51
The thermodynamics of Pr55Gag-RNA interaction regulate the assembly of HIV
Tanwar, H. S., Khoo, K. K., Garvey, M., Waddington, L., Leis, A., Hijnen, M., Velkov, T., Dumsday, G. J., McKinstry, W. J., & Mak, J. (2017) · PLOS Pathogens · doi:10.1371/journal.ppat.1006221 · Cited by 51
Critical Role of Conserved Hydrophobic Residues within the Major Homology Region in Mature Retroviral Capsid Assembly
Purdy, J. G., Flanagan, J. M., Ropson, I. J., Rennoll-Bankert, K. E., & Craven, R. C. (2008) · Journal of Virology · doi:10.1128/jvi.00214-08 · Cited by 50
Virus Particle Core Defects Caused by Mutations in the Human Immunodeficiency Virus Capsid N-Terminal Domain
Scholz, I., Arvidson, B., Huseby, D. L., & Barklis, E. (2005) · Journal of Virology · doi:10.1128/jvi.79.3.1470-1479.2005 · Cited by 49
In Vitro Assembly of Retroviruses
Bush, D. L., & Vogt, V. M. (2014) · Annual Review of Virology · doi:10.1146/annurev-virology-031413-085427 · Cited by 49
Dual-acting stapled peptides target both HIV-1 entry and assembly
Zhang, H., Curreli, F., Waheed, A. A., Mercredi, P. Y., Mehta, M., Bhargava, P., Scacalossi, D., Tong, X., Lee, S., Cooper, A., et al. (2013) · Retrovirology · doi:10.1186/1742-4690-10-136 · Cited by 48
HIV-1 requires capsid remodelling at the nuclear pore for nuclear entry and integration
Guedán, A., Donaldson, C. D., Caroe, E. R., Cosnefroy, O., Taylor, I. A., & Bishop, K. N. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009484 · Cited by 47
Novel Inhibitor Binding Site Discovery on HIV-1 Capsid N-Terminal Domain by NMR and X-ray Crystallography
Goudreau, N., Lemke, C. T., Faucher, A., Grand‐Maître, C., Goulet, S., Lacoste, J., Rancourt, J., Malenfant, É., Mercier, J.-F., Titolo, S., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb400075f · Cited by 46
VSV-G pseudotyping rescues HIV-1 CA mutations that impair core assembly or stability
Brun, S., Solignat, M., Gay, B., Bernard, É., Chaloin, L., Fenard, D., Devaux, C. A., Chazal, N., & Briant, L. (2008) · Retrovirology · doi:10.1186/1742-4690-5-57 · Cited by 46
Complex Interplay between HIV-1 Capsid and MX2-Independent Alpha Interferon-Induced Antiviral Factors
Bulli, L., Apolonia, L., Kutzner, J., Pollpeter, D., Goujon, C., Herold, N., Schwarz, S.-M., Giernat, Y., Keppler, O. T., Malim, M. H., et al. (2016) · Journal of Virology · doi:10.1128/jvi.00458-16 · Cited by 46
Solution Structure of a Double Mutant of the Carboxy-Terminal Dimerization Domain of the HIV-1 Capsid Protein,
Wong, H. C., Shin, R., & Krishna, N. R. (2008) · Biochemistry · doi:10.1021/bi7022128 · Cited by 46
Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy
Deshmukh, L., Ghirlando, R., & Clore, G. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501985112 · Cited by 47
Elastic properties and mechanical stability of chiral and filled viral capsids
Buenemann, M., & Lenz, P. (2008) · Physical Review E · doi:10.1103/physreve.78.051924 · Cited by 44
Molecular recognition in the human immunodeficiency virus capsid and antiviral design
Bocanegra, R., Rodríguez‐Huete, A., Fuertes, M. A., del Álamo, M., & Mateu, M. G. (2012) · Virus Research · doi:10.1016/j.virusres.2012.06.016 · Cited by 43
Discovery of dual inhibitors targeting both HIV-1 capsid and human cyclophilin A to inhibit the assembly and uncoating of the viral capsid
Li, J., Tan, Z., Tang, S., HEWLETT, I. K., Pang, R., He, M., He, S., Tian, B., Chen, K., & Yang, M. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.02.051 · Cited by 43
Protease Cleavage Leads to Formation of Mature Trimer Interface in HIV-1 Capsid
Meng, X., Zhao, G., Yufenyuy, E. L., Ke, D., Ning, J., DeLucia, M., Ahn, J., Gronenborn, A. M., Aiken, C., & Zhang, P. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002886 · Cited by 44
Self-citation
Atomic-scale characterization of mature HIV-1 capsid stabilization by inositol hexakisphosphate (IP 6 )
Yu, A., Lee, E., Jin, J., & Voth, G. A. (2020) · Science Advances · doi:10.1126/sciadv.abc6465 · Cited by 42
Role of Protein Interactions in Defining HIV-1 Viral Capsid Shape and Stability: A Coarse-Grained Analysis
Krishna, V., Ayton, G. S., & Voth, G. A. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.09.049 · Cited by 42
Discovery and Structural Characterization of a New Inhibitor Series of HIV-1 Nucleocapsid Function: NMR Solution Structure Determination of a Ternary Complex Involving a 2:1 Inhibitor/NC Stoichiometry
Goudreau, N., Hucke, O., Faucher, A., Grand‐Maître, C., Lepage, O., Bonneau, P. R., Mason, S. W., & Titolo, S. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.022 · Cited by 48
Second-Site Compensatory Mutations of HIV-1 Capsid Mutations
Noviello, C., López, C., Kukull, B., McNett, H., Still, A., Eccles, J., Sloan, R., & Barklis, E. (2011) · Journal of Virology · doi:10.1128/jvi.00099-11 · Cited by 40
Mutations in the Spacer Peptide and Adjoining Sequences in Rous Sarcoma Virus Gag Lead to Tubular Budding
Keller, P. W., Johnson, M. C., & Vogt, V. M. (2008) · Journal of Virology · doi:10.1128/jvi.00213-08 · Cited by 40
Hierarchical assembly governs TRIM5α recognition of HIV-1 and retroviral capsids
Skorupka, K. A., Roganowicz, M., Christensen, D. E., Wan, Y., Pornillos, O., & Ganser‐Pornillos, B. K. (2019) · Science Advances · doi:10.1126/sciadv.aaw3631 · Cited by 38
Self-citation
HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules
Saito, A., & Yamashita, M. (2021) · Retrovirology · doi:10.1186/s12977-021-00577-x · Cited by 41
Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography
Obal, G., Trajtenberg, F., Carrión, F., Tomé, L., Larrieux, N., Zhang, X., Pritsch, O., & Buschiazzo, A. (2015) · Science · doi:10.1126/science.aaa5182 · Cited by 39
Antiviral activity of recombinant ankyrin targeted to the capsid domain of HIV-1 Gag polyprotein
Nangola, S., Urvoas, A., Valerio‐Lepiniec, M., Khamaikawin, W., Sakkhachornphop, S., Hong, S. S., Boulanger, P. A., Minard, P., & Tayapiwatana, C. (2012) · Retrovirology · doi:10.1186/1742-4690-9-17 · Cited by 39
HIV-1 capsid exploitation of the host microtubule cytoskeleton during early infection
Naghavi, M. H. (2021) · Retrovirology · doi:10.1186/s12977-021-00563-3 · Cited by 41
Designing a Nanotube Using Naturally Occurring Protein Building Blocks
Tsai, C., Zheng, J., & Nussinov, R. (2006) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020042 · Cited by 39
Proton-Linked Dimerization of a Retroviral Capsid Protein Initiates Capsid Assembly
Bailey, G. D., Hyun, J., MITRA, A. K., & Kingston, R. L. (2009) · Structure · doi:10.1016/j.str.2009.03.010 · Cited by 38
A Trimer of Dimers Is the Basic Building Block for Human Immunodeficiency Virus-1 Capsid Assembly
Tsiang, M., Niedziela‐Majka, A., Hung, M., Jin, D., Hu, E. Y., Yant, S. R., Samuel, D., Liu, X., & Sakowicz, R. (2012) · Biochemistry · doi:10.1021/bi300052h · Cited by 39
High-throughput profiling of point mutations across the HIV-1 genome
Al‐Mawsawi, L. Q., Wu, N. C., Olson, C. A., Shi, V. C., Qi, H., Zheng, X., Wu, T.-T., & Sun, R. X. (2014) · Retrovirology · doi:10.1186/s12977-014-0124-6 · Cited by 37
New insights in the role of nucleoporins: A bridge leading to concerted steps from HIV-1 nuclear entry until integration
Nunzio, F. D. (2013) · Virus Research · doi:10.1016/j.virusres.2013.09.003 · Cited by 43
Structure by design: from single proteins and their building blocks to nanostructures
Tsai, C., Zheng, J., Alemán, C., & Nussinov, R. (2006) · Trends in biotechnology · doi:10.1016/j.tibtech.2006.08.004 · Cited by 37
Irregular and Semi‐Regular Polyhedral Models for Rous Sarcoma Virus Cores
Heymann, J. B., Butan, C., Winkler, D. C., Craven, R. C., & Steven, A. C. (2008) · Computational and Mathematical Methods in Medicine · doi:10.1080/17486700802168106 · Cited by 36
Inhibition of HIV-1 capsid assembly: Optimization of the antiviral potency by site selective modifications at N1, C2 and C16 of a 5-(5-furan-2-yl-pyrazol-1-yl)-1H-benzimidazole scaffold
Tremblay, M., Bonneau, P. R., Bousquet, Y., DeRoy, P., Duan, J., Duplessis, M., Gagnon, A., Garneau, M., Goudreau, N., Guse, I., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.10.034 · Cited by 35
Distinct Roles for Nucleic Acid in In Vitro Assembly of Purified Mason-Pfizer Monkey Virus CANC Proteins
Ulbrich, P., Haubova, S., Nermut, M. V., Hunter, E., Rumlová, M., & Ruml, T. (2006) · Journal of Virology · doi:10.1128/jvi.02694-05 · Cited by 35
Mechanisms of PI(4,5)P2 Enrichment in HIV-1 Viral Membranes
Wen, Y., Feigenson, G. W., Vogt, V. M., & Dick, R. A. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.07.018 · Cited by 37
Compensatory Substitutions Restore Normal Core Assembly in Simian Immunodeficiency Virus Isolates with Gag Epitope Cytotoxic T-Lymphocyte Escape Mutations
Yeh, W. W., Cale, E. M., Jaru-ampornpan, P., Lord, C. I., Peyerl, F. W., & Letvin, N. L. (2006) · Journal of Virology · doi:10.1128/jvi.00068-06 · Cited by 34
Cyclic peptide inhibitors of HIV-1 capsid-human lysyl-tRNA synthetase interaction
Dewan, V., Liu, T., Chen, K.-M., Qian, Z., Xiao, Y., Kleiman, L., Mahasenan, K. V., Li, C., Matsuo, H., Pei, D., et al. (2012) · ACS Chemical Biology · doi:10.1021/cb200450w · Cited by 33
HIV-1 Capsid Core: A Bullet to the Heart of the Target Cell
Toccafondi, E., Lener, D., & Negroni, M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.652486 · Cited by 33
Expression and purification of soluble recombinant full length HIV-1 Pr55Gag protein in Escherichia coli
McKinstry, W. J., Hijnen, M., Tanwar, H. S., Sparrow, L. G., Nagarajan, S., Pham, S. T., & Mak, J. (2014) · Protein Expression and Purification · doi:10.1016/j.pep.2014.04.013 · Cited by 41
Mechanism of polymorphism and curvature of HIV capsid assemblies probed by 3D simulations with a novel coarse grain model
Qiao, X., Jeon, J., Weber, J., Zhu, F., & Chen, B. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.08.017 · Cited by 33
A Retroviral Chimeric Capsid Protein Reveals the Role of the N-Terminal β-Hairpin in Mature Core Assembly
Cortines, J. R., Monroe, E. B., Kang, S., & Prevelige, P. E. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.052 · Cited by 32
Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction
Yang, Y., Brandariz-Núñez, A., Fricke, T., Ivanov, D. N., Sarnak, Z., & Diaz‐Griffero, F. (2013) · Virology · doi:10.1016/j.virol.2013.10.012 · Cited by 32
Mechanical modeling of viral capsids
Gibbons, M. M., & Klug, W. S. (2007) · Journal of Materials Science · doi:10.1007/s10853-007-1741-4 · Cited by 32
Ty3 Capsid Mutations Reveal Early and Late Functions of the Amino-Terminal Domain
Larsen, L. S. Z., Zhang, M., Beliakova‐Bethell, N., Bilanchone, V., Lamsa, A., Nagashima, K., Najdi, R., Kosaka, K., Kovacevic, V., Cheng, J. J., et al. (2007) · Journal of Virology · doi:10.1128/jvi.02207-06 · Cited by 31
The Role of Capsid in HIV-1 Nuclear Entry
Guedán, A., Caroe, E. R., Barr, G. C. R., & Bishop, K. N. (2021) · Viruses · doi:10.3390/v13081425 · Cited by 29
Inhibition of Retroviral Replication by Members of the TRIM Protein Family
Fletcher, A. J., & Towers, G. J. (2013) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-37765-5_2 · Cited by 32
Molecular Biology and Diversification of Human Retroviruses
Meissner, M. E., Talledge, N., & Mansky, L. M. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.872599 · Cited by 36
A molecular switch required for retrovirus assembly participates in the hexagonal immature lattice
Phillips, J. M., Murray, P. S., Murray, D., & Vogt, V. M. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.71 · Cited by 29
A novel inhibitor-binding site on the HIV-1 capsid N-terminal domain leads to improved crystallizationviacompound-mediated dimerization
Lemke, C. T., Titolo, S., Goudreau, N., Faucher, A., Mason, S. W., & Bonneau, P. R. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913006409 · Cited by 30
The primary mechanism for highly potent inhibition of HIV-1 maturation by lenacapavir
Huang, S., Briganti, L., Annamalai, A. S., Greenwood, J., Shkriabai, N., Haney, R., Armstrong, M., Wempe, M. F., Singh, S. P., Francis, A. C., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012862 · Cited by 30
Inositol phosphates promote HIV-1 assembly and maturation to facilitate viral spread in human CD4+ T cells
Sowd, G. A., & Aiken, C. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009190 · Cited by 28
Self-citation
HIV‐1 capsids mimic a microtubule regulator to coordinate early stages of infection
da Silva, E. S., Shanmugapriya, S., Malikov, V., Gu, F., Delaney, M. K., & Naghavi, M. H. (2020) · The EMBO Journal · doi:10.15252/embj.2020104870 · Cited by 29
Large-Scale Functional Purification of Recombinant HIV-1 Capsid
Hung, M., Niedziela‐Majka, A., Jin, D., Wong, M. H. L., Leavitt, S. A., Brendza, K. M., Liu, X., & Sakowicz, R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058035 · Cited by 27
Retroviral Capsid Assembly: A Role for the CA Dimer in Initiation
Purdy, J. G., Flanagan, J. M., Ropson, I. J., & Craven, R. C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.006 · Cited by 27
Rationally Designed Interfacial Peptides Are Efficient In Vitro Inhibitors of HIV-1 Capsid Assembly with Antiviral Activity
Bocanegra, R., Nevot, M., Doménech, R., López‐Font, I., Abián, O., Rodríguez‐Huete, A., Cavasotto, C. N., Velázquez‐Campoy, A., Gómez, J., Martı́nez, M. Á., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023877 · Cited by 28
NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason–Pfizer Monkey Virus
Macek, P., Chmelík, J., Křížová, I., Kadeřávek, P., Padrta, P., Žı́dek, L., Wildová, M., Hadravová, R., Chaloupková, R., Pichová, I., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.029 · Cited by 27
Determinants of the HIV-1 core assembly pathway
López, C. S., Eccles, J. D., Still, A., Sloan, R., Barklis, R. L., Tsagli, S. M., & Barklis, E. (2011) · Virology · doi:10.1016/j.virol.2011.05.011 · Cited by 26
Higher-Order Structure of the Rous Sarcoma Virus SP Assembly Domain
Bush, D. L., Monroe, E. B., Bedwell, G. J., Prevelige, P. E., Phillips, J. M., & Vogt, V. M. (2014) · Journal of Virology · doi:10.1128/jvi.02659-13 · Cited by 25
Design of in Vitro Symmetric Complexes and Analysis by Hybrid Methods Reveal Mechanisms of HIV Capsid Assembly
Yeager, M. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.073 · Cited by 27
Structure–Activity Relationships of a Novel Capsid Targeted Inhibitor of HIV-1 Replication
Kortagere, S., Xu, J. P., Mankowski, M. K., Ptak, R. G., & Cocklin, S. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci500437r · Cited by 24
Structure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular Assemblies
Bayro, M. J., & Tycko, R. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03983 · Cited by 24
A domain directly C-terminal to the major homology region of human immunodeficiency type 1 capsid protein plays a crucial role in directing both virus assembly and incorporation of Gag–Pol
Chien, A.-I., Liao, W.-H., Yang, D., & Wang, C.-T. (2006) · Virology · doi:10.1016/j.virol.2005.12.009 · Cited by 21
Discovery of novel 1,2,4‐triazole phenylalanine derivatives targeting an unexplored region within the interprotomer pocket of the HIV capsid protein
Jiang, X., Sharma, P. P., Rathi, B., Ji, X., Hu, L., Gao, Z., Kang, D., Wang, Z., Xie, M., Xu, S., et al. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28064 · Cited by 22
INI1/hSNF5-interaction defective HIV-1 IN mutants exhibit impaired particle morphology, reverse transcription and integration in vivo
Mathew, S. I., Nguyen, M., Wu, X., Pal, A., Shah, V. B., Prasad, V. R., Aiken, C., & Kalpana, G. V. (2013) · Retrovirology · doi:10.1186/1742-4690-10-66 · Cited by 22
Self-citation
Initiation of HIV-1 Gag lattice assembly is required for recognition of the viral genome packaging signal
Lei, X., Gonçalves-Carneiro, D., Zang, T. M., & Bieniasz, P. D. (2023) · eLife · doi:10.7554/elife.83548 · Cited by 22
Multidisciplinary studies with mutated HIV-1 capsid proteins reveal structural mechanisms of lattice stabilization
Gres, A. T., Kirby, K. A., McFadden, W. M., Du, H., Liu, D., Xu, C., Bryer, A. J., Perilla, J. R., Shi, J., Aiken, C., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41197-7 · Cited by 20
Self-citation
Mutations in the α-helix Directly C-terminal to the Major Homology Region of Human Immunodeficiency Virus Type 1 Capsid Protein Disrupt Gag Multimerization and Markedly Impair Virus Particle Production
Chu, H.-H., Chang, Y.-F., & Wang, C.-T. (2006) · Journal of Biomedical Science · doi:10.1007/s11373-006-9094-6 · Cited by 21
Heat shock protein 90AB1 and hyperthermia rescue infectivity of HIV with defective cores
Joshi, P., Sloan, B. A., Torbett, B. E., & Stoddart, C. A. (2012) · Virology · doi:10.1016/j.virol.2012.11.005 · Cited by 21
Polymorphic Nature of Human T-Cell Leukemia Virus Type 1 Particle Cores as Revealed through Characterization of a Chronically Infected Cell Line
Meissner, M. E., Mendonça, L., Zhang, W., & Mansky, L. M. (2017) · Journal of Virology · doi:10.1128/jvi.00369-17 · Cited by 20
Dual role for motif 1 residues of human lysyl-tRNA synthetase in dimerization and packaging into HIV-1
Dewan, V., Wei, M., Kleiman, L., & Musier-Forsyth, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.421842 · Cited by 20
Discovery of Lenacapavir: First-in-Class Twice-Yearly Capsid Inhibitor for HIV-1 Treatment and Pre-exposure Prophylaxis
Canales, E., Tse, W. C., Schroeder, S. D., Chou, C., Liu, Q., Zhang, J., Lazerwith, S. E., Morganelli, P., Saito, R. D., Brizgys, G., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01625 · Cited by 19
The Effect of Chemical Chaperones on the Assembly and Stability of HIV-1 Capsid Protein
Lampel, A., Bram, Y., Levy‐Sakin, M., Bacharach, E., & Gazit, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060867 · Cited by 19
Novel In Vitro Screening System Based on Differential Scanning Fluorimetry to Search for Small Molecules against the Disassembly or Assembly of HIV-1 Capsid Protein
Miyazaki, Y., Doi, N., Koma, T., Adachi, A., & Nomaguchi, M. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01413 · Cited by 19
In Vitro Quantification of the Effects of IP6 and Other Small Polyanions on Immature HIV-1 Particle Assembly and Core Stability
Dostálková, A., Kaufman, F., Křížová, I., Vokatá, B., Ruml, T., & Rumlová, M. (2020) · Journal of Virology · doi:10.1128/jvi.00991-20 · Cited by 21
Mutational Analysis of the N-Terminal Domain of Moloney Murine Leukemia Virus Capsid Protein
Auerbach, M. R., Brown, K. R., & Singh, I. R. (2007) · Journal of Virology · doi:10.1128/jvi.01286-07 · Cited by 19
Second site reversion of a mutation near the amino terminus of the HIV-1 capsid protein
López, C. S., Tsagli, S. M., Sloan, R., Eccles, J. D., & Barklis, E. (2013) · Virology · doi:10.1016/j.virol.2013.08.023 · Cited by 16
Biophysical Characterization of the Feline Immunodeficiency Virus p24 Capsid Protein Conformation and In Vitro Capsid Assembly
Serrière, J., Fenel, D., Schoehn, G., Gouet, P., & Guillon, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056424 · Cited by 19
Cell-free assays reveal that the HIV-1 capsid protects reverse transcripts from cGAS immune sensing
Scott, T. M., Arnold, L. M., Powers, J. A., McCann, D., Rowe, A. B., Christensen, D. E., Pereira, M. J. B., Zhou, W., Torrez, R. M., Iwasa, J., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012206 · Cited by 16
Self-citation
Insights into HIV uncoating from single-particle imaging techniques
Zhang, M. J., Stear, J. H., Jacques, D. A., & Böcking, T. (2022) · Biophysical Reviews · doi:10.1007/s12551-021-00922-6 · Cited by 16
HIV Assembly and Budding: Ca2+ Signaling and Non-ESCRT Proteins Set the Stage
Ehrlich, L. S., & Carter, C. A. (2012) · Molecular Biology International · doi:10.1155/2012/851670 · Cited by 16
The effect of point mutations within the N-terminal domain of Mason-Pfizer monkey virus capsid protein on virus core assembly and infectivity
Wildová, M., Hadravová, R., Štokrová, J., Křížová, I., Ruml, T., Hunter, E., Pichová, I., & Rumlová, M. (2008) · Virology · doi:10.1016/j.virol.2008.07.021 · Cited by 16
Mutational Analysis and Allosteric Effects in the HIV-1 Capsid Protein Carboxyl-Terminal Dimerization Domain
Yu, X., Wang, Q., Yang, J.-C., Buch, I., Tsai, C., Ma, B., Cheng, S. Z. D., Nussinov, R., & Zheng, J. (2009) · Biomacromolecules · doi:10.1021/bm801151r · Cited by 16
Novel Intersubunit Interaction Critical for HIV-1 Core Assembly Defines a Potentially Targetable Inhibitor Binding Pocket
Craveur, P., Gres, A. T., Kirby, K. A., Liu, D., Hammond, J. A., Deng, Y., Forli, S., Goodsell, D. S., Williamson, J. R., Sarafianos, S. G., et al. (2019) · mBio · doi:10.1128/mbio.02858-18 · Cited by 17
Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments
Lu, J., Bayro, M. J., & Tycko, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.720557 · Cited by 16
Molecular Determinants of Self-Association and Rearrangement of a Trimeric Intermediate during the Assembly of a Parvovirus Capsid
Pérez, R., Castellanos, M., Rodríguez‐Huete, A., & Mateu, M. G. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.08.020 · Cited by 15
Split trehalase as a versatile reporter for a wide range of biological analytes
Drikic, M., & Buck, J. D. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26556 · Cited by 15
Incorporation of Human Immunodeficiency Virus Type 1 Reverse Transcriptase into Virus-Like Particles
Liao, W.-H., Huang, K.-J., Chang, Y.-F., Wang, S.-M., Tseng, Y.-T., Chiang, C.-C., Wang, J.-J., & Wang, C.-T. (2007) · Journal of Virology · doi:10.1128/jvi.01796-06 · Cited by 15
HIV-1 adapts to lost IP6 coordination through second-site mutations that restore conical capsid assembly
Kleinpeter, A. B., Mallery, D. L., Renner, N., Albecka, A., Klarhof, J. O., Freed, E. O., & James, L. C. (2024) · Nature Communications · doi:10.1038/s41467-024-51971-w · Cited by 13
The Maturational Refolding of the β-Hairpin Motif of Equine Infectious Anemia Virus Capsid Protein Extends Its Helix α1 at Capsid Assembly Locus
Chen, K., Piszczek, G., Carter, C., & Tjandra, N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.425140 · Cited by 14
Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly
Heyrana, K. J., Goh, B. C., Perilla, J. R., Nguyen, T.-L. N., England, M. R., Bewley, M. C., Schulten, K. J., & Craven, R. C. (2016) · Journal of Virology · doi:10.1128/jvi.00378-16 · Cited by 13

Authors: Ganser-Pornillos, B. K., von Schwedler, U. K., Stray, K. M., Aiken, C., & Sundquist, W. I.
Affiliations: Department of Biochemistry, University of Utah, Salt Lake City, Utah 84132
University of Utah (US)
Vanderbilt University (US)
ORCID: Aiken, Christopher
Sundquist, Wesley I.
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 2004-03
Volume: 78
Issue: 5
Pages: 2545-2552
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.78.5.2545-2552.2004
PMC: PMC369201
OpenAlex: W2135035609
Cited by: 302
References: 59
Citations by year: 2026: 5 · 2025: 6 · 2024: 9 · 2023: 5 · 2022: 8 · 2021: 8 · 2020: 12 · 2019: 8 · 2018: 13 · 2017: 10 · 2016: 16 · 2015: 14 · 2014: 12 · 2013: 29 · 2012: 23
FWCI: 6.24
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Keywords: HIV-1, viral capsid assembly, capsid morphology, surface mutations, pentamer, dimer interface, N-terminal domain, capsid lattice
MeSH terms: Models, Molecular, Mutation, Phenotype, Protein Binding, Solubility, HIV-1, Protein Structure, Tertiary, Virus Assembly, Protein Structure, Quaternary, Cyclophilin A, 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

Assembly Properties of the Human Immunodeficiency Virus Type 1 CA Protein

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks