Assembly Properties of the Human Immunodeficiency Virus Type 1 CA Protein

Ganser-Pornillos, Barbie K.; von Schwedler, Uta K.; Stray, Kirsten M.; Aiken, Christopher; Sundquist, Wesley I.

doi:10.1128/jvi.78.5.2545-2552.2004

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

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?

The cores are typically conical in HIV (5 pentamers at the tip and 7 at the base), tubular in M-PMV (6 pentamers at each end), and polyhedral in RSV and MLV (12 pentamers homogenously distributed).
“The cores are typically conical in HIV (5 pentamers at the tip and 7 at the base), tubular in M-PMV (6 pentamers at each end), and polyhedral in RSV and MLV (12 pentamers homogenously distributed).”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [60]

Database resources of the National Center for Biotechnology Information: update
Wheeler, D. L. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh073 · Cited by 10,691 · see citing works
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 · see citing works
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 · see citing works
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× · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
Self-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 · see citing works
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 · see citing works
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 · see citing works
Structure of the Amino-Terminal Core Domain of the HIV-1 Capsid Protein
Gitti, R. K., Lee, B. M., Walker, J., Summers, M. F., Yoo, S., & Sundquist, W. I. (1996) · Science · doi:10.1126/science.273.5272.231 · Cited by 459 · see citing works
Self-citation
GenBank
Benson, D. A. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.17 · Cited by 456 · see citing works
Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein
von Schwedler, U. K., Stray, K. M., Garrus, J. E., & Sundquist, W. I. (2003) · Journal of Virology · doi:10.1128/jvi.77.9.5439-5450.2003 · Cited by 421 · see citing works
Self-citation
Cyclophilin A modulates the sensitivity of HIV-1 to host restriction factors
Towers, G. J., Hatziioannou, T., Cowan, S., Goff, S. P., Luban, J., & Bieniasz, P. D. (2003) · Nature Medicine · doi:10.1038/nm910 · Cited by 377 · see citing works
Proteolytic refolding of the HIV‐1 capsid protein amino‐terminus facilitates viral core assembly
von Schwedler, U. K., Stemmler, T. L., Klishko, V. Y., Li, S., Albertine, K. H., Davis, D. R., & Sundquist, W. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1555 · Cited by 337 · see citing works
Self-citation
Crystal structure of dimeric HIV-1 capsid protein
Momany, C., Kovari, L. C., Prongay, A., Keller, W., Gitti, R. K., Lee, B. M., Gorbalenya, A. E., Tong, L., McClure, J., Ehrlich, L. S., et al. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0996-763 · Cited by 313 · see citing works
Efficient particle production by minimal gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
Accola, M. A., Strack, B., & Göttlinger, H. G. (2000) · Journal of Virology · doi:10.1128/jvi.74.12.5395-5402.2000 · Cited by 288 · see citing works
Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
Worthylake, D. K., Wang, H., Yoo, S., Sundquist, W. I., & Hill, C. P. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998007689 · Cited by 235 · see citing works
Self-citation
Retroviral Virions and Genomes
Vogt, V. (1997) · Europe PMC (PubMed Central) · Cited by 222 · see citing works
Functional domains of the capsid protein of human immunodeficiency virus type 1
Dorfman, T., Bukovský, A., Öhagen, Å., Höglund, S., & Göttlinger, H. G. (1994) · Journal of Virology · doi:10.1128/jvi.68.12.8180-8187.1994 · Cited by 218 · see citing works
Antiviral Inhibition of the HIV-1 Capsid Protein
Tang, C., Loeliger, E., Kinde, I., Kyere, S., Mayo, K., Barklis, E., Sun, Y., Huang, M., & Summers, M. F. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00289-4 · Cited by 218 · see citing works
Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
Ehrlich, L. S., Agresta, B. E., & Carter, C. A. (1992) · Journal of Virology · doi:10.1128/jvi.66.8.4874-4883.1992 · Cited by 218 · see citing works
A rapid and efficient one-tube PCR-based mutagenesis technique usingPfuDNA polymerase
Picard, V., Ersdal-Badju, E., Lu, A., & Bock, S. C. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.13.2587 · Cited by 215 · see citing works
Polymorphism in the assembly of polyomavirus capsid protein VP1
Salunke, D. M., Caspar, D. L. D., & Garcea, R. L. (1989) · Biophysical Journal · doi:10.1016/s0006-3495(89)82735-3 · Cited by 212 · see citing works
Biochemical and Structural Analysis of Isolated Mature Cores of Human Immunodeficiency Virus Type 1
Welker, R., Hohenberg, H., Tessmer, U., Huckhagel, C., & Kräusslich, H. (2000) · Journal of Virology · doi:10.1128/jvi.74.3.1168-1177.2000 · Cited by 207 · see citing works
Identification of Novel Interactions in HIV-1 Capsid Protein Assembly by High-resolution Mass Spectrometry
Lanman, J., Lam, T. T., Barnes, S., Sakalian, M., Emmett, M. R., Marshall, A. G., & Prevelige, P. E. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01245-7 · Cited by 206 · see citing works
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
Tang, C., Ndassa, Y., & Summers, M. F. (2002) · Nature Structural Biology · doi:10.1038/nsb806 · Cited by 205 · see citing works
In Vitro Assembly Properties of Purified Bacterially Expressed Capsid Proteins of Human Immunodeficiency Virus
Gross, I., Hohenberg, H., & Kräusslich, H. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00592.x · Cited by 198 · see citing works
Head‐to‐tail dimers and interdomain flexibility revealed by the crystal structure of HIV‐1 capsid protein (p24) complexed with a monoclonal antibody Fab
Berthet-Colominas, C., Monaco, S., Novelli, A., Sibaı̈, G., Mallet, F., & Cusack, S. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1124 · Cited by 191 · see citing works
Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity
Reicin, A., Paik, S., Berkowitz, R., Luban, J., Lowy, I., & Goff, S. (1995) · Journal of Virology · doi:10.1128/jvi.69.2.642-650.1995 · Cited by 155 · see citing works
The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly
Borsetti, A., Öhagen, Å., & Göttlinger, H. G. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.9313-9317.1998 · Cited by 126 · see citing works
Association of Nef with the Human Immunodeficiency Virus Type 1 Core
Kotov, A., Zhou, J., Flicker, P. F., & Aiken, C. (1999) · Journal of Virology · doi:10.1128/jvi.73.10.8824-8830.1999 · Cited by 124 · see citing works
Self-citation
The HIV-1 assembly machine
Göttlinger, H. G. (2001) · AIDS · doi:10.1097/00002030-200100005-00003 · Cited by 124 · see citing works
Kinetic Analysis of the Role of Intersubunit Interactions in Human Immunodeficiency Virus Type 1 Capsid Protein Assembly In Vitro
Lanman, J. K., Sexton, J., Sakalian, M., & Prevelige, P. E. (2002) · Journal of Virology · doi:10.1128/jvi.76.14.6900-6908.2002 · Cited by 123 · see citing works
Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein
Earnshaw, W. C., & King, J. W. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90017-7 · Cited by 121 · see citing works
Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses 1 1Edited by P. E. Wright
Campos-Olivas, R., Newman, J. L., & Summers, M. F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3475 · Cited by 119 · see citing works
Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26
Jin, Z., Jin, L., Peterson, D. L., & Lawson, C. L. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2443 · Cited by 113 · see citing works
Structure and self-association of the Rous sarcoma virus capsid protein
Kingston, R. L., Fitzon-Ostendorp, T., Eisenmesser, E. Z., Schatz, G. W., Vogt, V. M., Post, C. B., & Rossmann, M. G. (2000) · Structure · doi:10.1016/s0969-2126(00)00148-9 · Cited by 112 · see citing works
Spontaneous mutations in the human immunodeficiency virus type 1 gag gene that affect viral replication in the presence of cyclosporins
Aberham, C., Weber, S., & Phares, W. (1996) · Journal of Virology · doi:10.1128/jvi.70.6.3536-3544.1996 · Cited by 106 · see citing works
Solution Structure of the Capsid Protein from the Human T-cell Leukemia Virus Type-I
Khorasanizadeh, S., Campos‐Olivas, R., & Summers, M. F. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2986 · Cited by 101 · see citing works
Human Immunodeficiency Virus Type 1 Replication Is Modulated by Host Cyclophilin A Expression Levels
Yin, L., Braaten, D. C., & Luban, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.8.6430-6436.1998 · Cited by 96 · see citing works
Electron microscope studies of mutants of lambda bacteriophage
Kemp, C. L., Howatson, A. F., & Siminovitch, L. (1968) · Virology · doi:10.1016/0042-6822(68)90174-8 · Cited by 90 · see citing works
Isolation of Human Immunodeficiency Virus Type 1 Cores: Retention of Vpr in the Absence of p6 gag
Accola, M. A., Öhagen, Å., & Göttlinger, H. G. (2000) · Journal of Virology · doi:10.1128/jvi.74.13.6198-6202.2000 · Cited by 80 · see citing works
Cones and Tubes: Geometry in the Chemistry of Carbon
Ebbesen, T. W. (1998) · Accounts of Chemical Research · doi:10.1021/ar960168i · Cited by 79 · see citing works
Retrovirus Capsid Protein Assembly Arrangements
Mayo, K., Huseby, D. L., McDermott, J., Arvidson, B., Finlay, L. A., & Barklis, E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01176-2 · Cited by 75 · see citing works
HIV surveillance among injecting drug users
Jarlais, D. C. D., Dehne, K. L., & Casabona, J. (2001) · AIDS · doi:10.1097/00002030-200104003-00003 · Cited by 71 · see citing works
In VitroAssembly Properties of Wild-Type and Cyclophilin-Binding Defective Human Immunodeficiency Virus Capsid Proteins in the Presence and Absence of Cyclophilin A
Grättinger, M., Hohenberg, H., Thomas, D. R., Wilk, T., Müller, B., & Kräusslich, H. (1999) · Virology · doi:10.1006/viro.1999.9668 · Cited by 70 · see citing works
The Capsid Size-determining Protein Sid Forms an External Scaffold on Phage P4 Procapsids
Marvik, O. J., Dokland, T., Nøkling, R. H., Jacobsen, E., Larsen, T., & Lindqvist, B. H. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0416 · Cited by 67 · see citing works
Three‐dimensional structure of the M‐MuLV CA protein on a lipid monolayer: a general model for retroviral capsid assembly
Ganser, B. K., Cheng, A., Sundquist, W. I., & Yeager, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg276 · Cited by 65 · see citing works
Self-citation
Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein
Cornilescu, C. C., Bouamr, F., Yao, X., Carter, C., & Tjandra, N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4395 · Cited by 64 · see citing works
Geometry of phage head construction
Moody, M. F. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3011 · Cited by 59 · see citing works
Second-Site Suppressors of Rous Sarcoma Virus CA Mutations: Evidence for Interdomain Interactions
Bowzard, J. B., Wills, J. W., & Craven, R. C. (2001) · Journal of Virology · doi:10.1128/jvi.75.15.6850-6856.2001 · Cited by 58 · see citing works
Characterization of HIV‐1 p24 self‐association using analytical affinity chromatography
Rosé, S. D., Hensley, P., O'Shannessy, D. J., Culp, J. S., Debouck, C. M., & CHAIKEN, I. M. (1992) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340130204 · Cited by 54 · see citing works
Morphogenesis and Maturation of Retroviruses
Kräusslich, H. (1996) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-642-80145-7 · Cited by 54 · see citing works
Tricornaviridae – a Proposed Family of Plant Viruses with Tripartite, Single-Stranded RNA Genomes
Vloten-Doting, L. V., Francki, R. I. B., Fulton, R. W., Kaper, J. M., & Lane, L. C. (1981) · Intervirology · doi:10.1159/000149232 · Cited by 49 · see citing works
Analysis of rous sarcoma virus capsid protein variants assembled on lipid monolayers
Mayo, K., Vana, M. L., McDermott, J., Huseby, D. L., Leis, J. P., & Barklis, E. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5354 · Cited by 42 · see citing works
Backbone Dynamics of the N-Terminal Domain of the HIV-1 Capsid Protein and Comparison with the G94D Mutant Conferring Cyclosporin Resistance/Dependence
Campos‐Olivas, R., & Summers, M. F. (1999) · Biochemistry · doi:10.1021/bi990991x · Cited by 29 · see citing works
Effect of C-Terminal Mutations of Alfalfa Mosaic Virus Coat Protein on Dimer Formation and Assembly in Vitro
Choi, J., & Loesch‐Fries, L. S. (1999) · Virology · doi:10.1006/viro.1999.9805 · Cited by 23 · see citing works
In Vitro Phosphorylation of the Polyomavirus Major Capsid Protein VP1 on Serine 66 by Casein Kinase II
Li, M., Lyon, M. K., & Garcea, R. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.26006 · Cited by 17 · see citing works

Flagged first, then by citations

Sorted by citations

Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677 · see citing works
HIV-1 assembly, budding, and maturation
Sundquist, W. I., & Krausslich, H.-G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006924 · Cited by 814 · see citing works
Self-citation
X-Ray Structures of the Hexameric Building Block of the HIV Capsid
Pornillos, O., Ganser-Pornillos, B. K., Kelly, B. N., Hua, Y., Whitby, F. G., Stout, C. D., Sundquist, W. I., Hill, C. P., & Yeager, M. (2009) · Cell · doi:10.1016/j.cell.2009.04.063 · Cited by 523 · see citing works
Self-citation
The structural biology of HIV assembly
Ganser‐Pornillos, B. K., Yeager, M. J., & Sundquist, W. I. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.02.001 · Cited by 500 · see citing works
Self-citation
Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4
Huang, C.-C., Lam, S. N., Acharya, P., Tang, M., Xiang, S.-H., Shahzad‐ul‐Hussan, S., Stanfield, R. L., Robinson, J. E., Sodroski, J., Wilson, I. A., et al. (2007) · Science · doi:10.1126/science.1145373 · Cited by 416 · see citing works
Higher-Order Oligomerization Targets Plasma Membrane Proteins and HIV Gag to Exosomes
Fang, Y., Wu, N., Gan, X., Yan, W., Morrell, J. C., & Gould, S. J. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050158 · Cited by 382 · see citing works
Origin of icosahedral symmetry in viruses
Zandi, R., Reguera, D., Bruinsma, R., Gelbart, W. M., & Rudnick, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405844101 · Cited by 375 · see citing works
Atomic-level modelling of the HIV capsid
Pornillos, O., Ganser-Pornillos, B. K., & Yeager, M. (2011) · Nature · doi:10.1038/nature09640 · Cited by 372 · see citing works
Self-citation
Structure and assembly of immature HIV
Briggs, J. A. G., Riches, J. D., Glass, B., Bartonova, V., Zanetti, G., & Kräusslich, H.-G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903535106 · Cited by 368 · see citing works
Electron cryotomography of immature HIV‐1 virions reveals the structure of the CA and SP1 Gag shells
Wright, E. R., Schooler, J. B., Ding, H. J., Kieffer, C., Fillmore, C., Sundquist, W. I., & Jensen, G. J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601664 · Cited by 325 · see citing works
Self-citation
Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
Ganser-Pornillos, B. K., Cheng, A., & Yeager, M. (2007) · Cell · doi:10.1016/j.cell.2007.08.018 · Cited by 321 · see citing works
Self-citation
HIV Capsid is a Tractable Target for Small Molecule Therapeutic Intervention
Blair, W. S., Pickford, C., Irving, S. L., Brown, D. G., Anderson, M. D., Bazin, R., Cao, J. Q., Ciaramella, G., Isaacson, J., Jackson, L., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001220 · Cited by 294 · see citing works
The structure and flexibility of conical HIV-1 capsids determined within intact virions
Mattei, S., Glass, B., Hagen, W. J. H., Kräusslich, H., & Briggs, J. A. G. (2016) · Science · doi:10.1126/science.aah4972 · Cited by 280 · see citing works
Inositol phosphates are assembly co-factors for HIV-1
Dick, R. A., Zadrozny, K. K., Xu, C., Schur, F. K. M., Lyddon, T. D., Ricana, C. L., Wagner, J. M., Perilla, J. R., Ganser‐Pornillos, B. K., Johnson, M. C., et al. (2018) · Nature · doi:10.1038/s41586-018-0396-4 · Cited by 256 · see citing works
Self-citation
Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function
Byeon, I.-J. L., Meng, X., Jung, J., Zhao, G., Yang, R., Ahn, J., Shi, J., Concel, J., Aiken, C., Zhang, P., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.010 · Cited by 253 · see citing works
Self-citation
X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability
Gres, A. T., Kirby, K. A., KewalRamani, V. N., Tanner, J. J., Pornillos, O., & Sarafianos, S. G. (2015) · Science · doi:10.1126/science.aaa5936 · Cited by 248 · see citing works
Hexagonal assembly of a restricting TRIM5α protein
Ganser‐Pornillos, B. K., Chandrasekaran, V., Pornillos, O., Sodroski, J., Sundquist, W. I., & Yeager, M. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013426108 · Cited by 248 · see citing works
Self-citation
The Mechanism of HIV-1 Core Assembly: Insights from Three-Dimensional Reconstructions of Authentic Virions
Briggs, J. A. G., Grünewald, K., Glass, B., Förster, F., Kräusslich, H.-G., & Fuller, S. D. (2006) · Structure · doi:10.1016/j.str.2005.09.010 · Cited by 230 · see citing works
Viral capsids: Mechanical characteristics, genome packaging and delivery mechanisms
Roos, W. H., Ivanovska, I. L., Evilevitch, A., & Wuite, G. J. L. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6451-1 · Cited by 225 · see citing works
A peptide inhibitor of HIV-1 assembly in vitro
Sticht, J., Humbert, M., Findlow, S. C., Bodem, J., Müller, B., Dietrich, U., Werner, J. M., & Kräusslich, H. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb964 · Cited by 224 · see citing works
The Requirement for Nucleoporin NUP153 during Human Immunodeficiency Virus Type 1 Infection Is Determined by the Viral Capsid
Matreyek, K. A., & Engelman, A. (2011) · Journal of Virology · doi:10.1128/jvi.00325-11 · Cited by 224 · see citing works
A Cell-penetrating Helical Peptide as a Potential HIV-1 Inhibitor
Zhang, H., Zhao, Q., Bhattacharya, S., Waheed, A. A., Tong, X., Hong, A. L., Heck, S., Curreli, F., Goger, M. J., Cowburn, D., et al. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.02.066 · Cited by 215 · see citing works
Extreme Genetic Fragility of the HIV-1 Capsid
Rihn, S. J., Wilson, S. J., Loman, N. J., Alim, M., Bakker, S. E., Bhella, D., Gifford, R. J., Rixon, F. J., & Bieniasz, P. D. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003461 · Cited by 194 · see citing works
Human Nucleoporins Promote HIV-1 Docking at the Nuclear Pore, Nuclear Import and Integration
Nunzio, F. D., Danckaert, A., Fricke, T., Perez, P., Fernandez, J., Perret, E., Roux, P., Shorte, S., Charneau, P., Diaz-Griffero, F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046037 · Cited by 195 · see citing works
Three-dimensional Structure of HIV-1 Virus-like Particles by Electron Cryotomography
Benjamin, J., Ganser‐Pornillos, B. K., Tivol, W. F., Sundquist, W. I., & Jensen, G. J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.11.064 · Cited by 185 · see citing works
Self-citation
High-resolution structure of a retroviral capsid hexameric amino-terminal domain
Mortuza, G. B., Haire, L. F., Stevens, A., Smerdon, S. J., Stoye, J. P., & Taylor, I. A. (2004) · Nature · doi:10.1038/nature02915 · Cited by 185 · see citing works
Modeling Viral Capsid Assembly
Hagan, M. F. (2014) · Advances in chemical physics · doi:10.1002/9781118755815.ch01 · Cited by 181 · see citing works
Human immunodeficiency virus type 1 assembly, release, and maturation
Adamson, C. S., & Freed, E. O. (2007) · Advances in Pharmacology · doi:10.1016/s1054-3589(07)55010-6 · Cited by 179 · see citing works
The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor
Ternois, F., Sticht, J., Duquerroy, S., Kräusslich, H., & Rey, F. A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb967 · Cited by 176 · see citing works
Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication
Nunzio, F. D., Fricke, T., Miccio, A., Valle‐Casuso, J. C., Perez, P., Souque, P., Rizzi, E., Severgnini, M., Mavilio, F., Charneau, P., et al. (2013) · Virology · doi:10.1016/j.virol.2013.02.008 · Cited by 171 · see citing works
Assembly and Architecture of HIV
Ganser‐Pornillos, B. K., Yeager, M. J., & Pornillos, O. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0980-9_20 · Cited by 161 · see citing works
Self-citation
Key interactions in HIV-1 maturation identified by hydrogen-deuterium exchange
Lanman, J., Lam, T. T., Emmett, M. R., Marshall, A. G., Sakalian, M., & Prevelige, P. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb790 · Cited by 164 · see citing works
A B-Box 2 Surface Patch Important for TRIM5α Self-Association, Capsid Binding Avidity, and Retrovirus Restriction
Diaz‐Griffero, F., Qin, X.-R., Hayashi, F., Kigawa, T., Finzi, A., Sarnak, Z., Lienlaf, M., Yokoyama, S., & Sodroski, J. (2009) · Journal of Virology · doi:10.1128/jvi.01307-09 · Cited by 159 · see citing works
Coarse-grained simulation reveals key features of HIV-1 capsid self-assembly
Grime, J. M. A., Dama, J. F., Ganser‐Pornillos, B. K., Woodward, C. L., Jensen, G. J., Yeager, M. J., & Voth, G. A. (2016) · Nature Communications · doi:10.1038/ncomms11568 · Cited by 156 · see citing works
Self-citation
A highly potent long-acting small-molecule HIV-1 capsid inhibitor with efficacy in a humanized mouse model
Yant, S. R., Mulato, A. S., Hansen, D., Tse, W. C., Niedziela‐Majka, A., Zhang, J. R., Stepan, G. J., Jin, D., Wong, M. H. L., Perreira, J. M., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0560-x · Cited by 156 · see citing works
Self-citation
Structure of the Antiviral Assembly Inhibitor CAP-1 Complex with the HIV-1 CA Protein
Kelly, B. N., Kyere, S. K., Kinde, I., Tang, C., Howard, B. R., Robinson, H. H., Sundquist, W. I., Summers, M. F., & Hill, C. P. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.07.070 · Cited by 152 · see citing works
Self-citation
Reconstitution and visualization of HIV-1 capsid-dependent replication and integration in vitro
Christensen, D. E., Ganser-Pornillos, B. K., Johnson, J. S., Pornillos, O., & Sundquist, W. I. (2020) · Science · doi:10.1126/science.abc8420 · Cited by 150 · see citing works
Self-citation
Conformation of the HIV-1 Gag Protein in Solution
Datta, S. A. K., Curtis, J. E., Ratcliff, W., Clark, P. K., Crist, R. M., Lebowitz, J., Krueger, S., & Rein, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.073 · Cited by 145 · see citing works
Novel approaches to inhibiting HIV-1 replication
Adamson, C. S., & Freed, E. O. (2009) · Antiviral Research · doi:10.1016/j.antiviral.2009.09.009 · Cited by 145 · see citing works
Elasticity theory and shape transitions of viral shells
Nguyen, T. T., Bruinsma, R., & Gelbart, W. M. (2005) · Physical Review E · doi:10.1103/physreve.72.051923 · Cited by 137 · see citing works
Chromatin organization at the nuclear pore favours HIV replication
Lelek, M., Casartelli, N., Pellin, D., Rizzi, E., Souque, P., Severgnini, M., Serio, C. D., Fricke, T., Diaz‐Griffero, F., Zimmer, C., et al. (2015) · Nature Communications · doi:10.1038/ncomms7483 · Cited by 133 · see citing works
Interactions between HIV-1 Gag Molecules in Solution: An Inositol Phosphate-mediated Switch
Datta, S. A. K., Zhao, Z., Clark, P. K., Tarasov, S. G., Alexandratos, J. N., Campbell, S. J., Kvaratskhelia, M., Lebowitz, J., & Rein, A. R. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.072 · Cited by 132 · see citing works
Disulfide Bond Stabilization of the Hexameric Capsomer of Human Immunodeficiency Virus
Pornillos, O., Ganser‐Pornillos, B. K., Sankaran, B., Hua, Y., & Yeager, M. J. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.06.042 · Cited by 132 · see citing works
Self-citation
Distinct Effects of Two HIV-1 Capsid Assembly Inhibitor Families That Bind the Same Site within the N-Terminal Domain of the Viral CA Protein
Lemke, C. T., Titolo, S., von Schwedler, U. K., Goudreau, N., Mercier, J.-F., Wardrop, E., Faucher, A., Coulombe, R., Banik, S. S. R., Fader, L. D., et al. (2012) · Journal of Virology · doi:10.1128/jvi.00493-12 · Cited by 125 · see citing works
Self-citation
Invariant Polymorphism in Virus Capsid Assembly
Nguyen, H. D., Reddy, V. S., & Brooks, C. L. (2009) · Journal of the American Chemical Society · doi:10.1021/ja807730x · Cited by 124 · see citing works
Discovery of Novel Small-Molecule HIV-1 Replication Inhibitors That Stabilize Capsid Complexes
Lamorte, L., Titolo, S., Lemke, C., Goudreau, N., Mercier, J., Wardrop, E., Shah, V. B., von Schwedler, U. V., Langelier, C., Banik, S., et al. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00985-13 · Cited by 108 · see citing works
Self-citation
Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution
Deshmukh, L., Schwieters, C. D., Grishaev, A., Ghirlando, R., Baber, J. L., & Clore, G. M. (2013) · Journal of the American Chemical Society · doi:10.1021/ja406246z · Cited by 114 · see citing works
Ebselen, a Small-Molecule Capsid Inhibitor of HIV-1 Replication
Thenin-Houssier, S., de Vera, I. M. S., Pedró-Rosa, L., Brady, A., Richard, A. S., Konnick, B., Opp, S., Buffone, C., Fuhrmann, J., Kota, S., et al. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02574-15 · Cited by 114 · see citing works
Design, synthesis and structure-activity relationships of 4-phenyl-1H-1,2,3-triazole phenylalanine derivatives as novel HIV-1 capsid inhibitors with promising antiviral activities
Sun, L., Huang, T., Dick, A., Meuser, M. E., Zalloum, W. A., Chen, C., Ding, X., Gao, P., Cocklin, S., Lee, K., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112085 · Cited by 113 · see citing works
Kinetics of HIV-1 capsid uncoating revealed by single-molecule analysis
Márquez, C. L., Lau, D., Walsh, J. C., Shah, V. B., McGuinness, C., Wong, A. K. H., Aggarwal, A., Parker, M. W., Jacques, D. A., Turville, S. G., et al. (2018) · eLife · doi:10.7554/elife.34772 · Cited by 111 · see citing works
Nup153 unlocks the nuclear pore complex for HIV-1 nuclear translocation in nondividing cells
Buffone, C., Martinez-Lopez, A., Fricke, T., Opp, S., Severgnini, M., Cifola, I., Petiti, L., Frabetti, S., Skorupka, K., Zadrozny, K. K., et al. (2018) · Journal of Virology · doi:10.1128/jvi.00648-18 · Cited by 109 · see citing works
Self-citation
Complementary Assays Reveal a Low Level of CA Associated with Viral Complexes in the Nuclei of HIV-1-Infected Cells
Hulme, A. E., Kelley, Z. L., Foley, D., & Hope, T. J. (2015) · Journal of Virology · doi:10.1128/jvi.00476-15 · Cited by 105 · see citing works
Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids
Li, Y.-L., Chandrasekaran, V., Carter, S. D., Woodward, C. L., Christensen, D. E., Dryden, K. A., Pornillos, O., Yeager, M. J., Ganser‐Pornillos, B. K., Jensen, G. J., et al. (2016) · eLife · doi:10.7554/elife.16269 · Cited by 105 · see citing works
Self-citation
Effect of Macromolecular Crowding Agents on Human Immunodeficiency Virus Type 1 Capsid Protein Assembly In Vitro
del Álamo, M., Rivas, G., & Mateu, M. G. (2005) · Journal of Virology · doi:10.1128/jvi.79.22.14271-14281.2005 · Cited by 100 · see citing works
HIV-1 Maturation: Lessons Learned from Inhibitors
Kleinpeter, A. B., & Freed, E. O. (2020) · Viruses · doi:10.3390/v12090940 · Cited by 95 · see citing works
Visualization of a missing link in retrovirus capsid assembly
Giovanni Cardone, A., Purdy, J. G., Cheng, N., Craven, R. C., & Steven, A. C. (2009) · Nature · doi:10.1038/nature07724 · Cited by 95 · see citing works
Requirements for capsid-binding and an effector function in TRIMCyp-mediated restriction of HIV-1
Diaz‐Griffero, F., Vandegraaff, N., Li, Y., Engelman, K. D., Stremlau, M. H., Welikala, S., Si, Z., Engelman, A., & Sodroski, J. (2006) · Virology · doi:10.1016/j.virol.2006.03.023 · Cited by 95 · see citing works
Direct Visualization of HIV-1 with Correlative Live-Cell Microscopy and Cryo-Electron Tomography
Jun, S., Ke, D., Debiec, K. T., Zhao, G., Meng, X., Ambrose, Z., Gibson, G. A., Watkins, S. C., & Zhang, P. (2011) · Structure · doi:10.1016/j.str.2011.09.006 · Cited by 93 · see citing works
Role of Transmitted Gag CTL Polymorphisms in Defining Replicative Capacity and Early HIV-1 Pathogenesis
Prince, J. L., Claiborne, D. T., Carlson, J., Schaefer, M., Yu, T.-W., Lahki, S., Prentice, H., Yue, L., Vishwanathan, S., Kilembe, W., et al. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1003041 · Cited by 100 · see citing works
Comparative requirements for the restriction of retrovirus infection by TRIM5α and TRIMCyp
Diaz‐Griffero, F., Kar, A. K., Lee, M. N., Stremlau, M. H., Poeschla, E. M., & Sodroski, J. (2007) · Virology · doi:10.1016/j.virol.2007.08.032 · Cited by 92 · see citing works
The Retroviral Capsid Domain Dictates Virion Size, Morphology, and Coassembly of Gag into Virus-Like Particles
Ako-adjei, D., Johnson, M. C., & Vogt, V. M. (2005) · Journal of Virology · doi:10.1128/jvi.79.21.13463-13472.2005 · Cited by 92 · see citing works
Myristoylation Is Required for Human Immunodeficiency Virus Type 1 Gag-Gag Multimerization in Mammalian Cells
Li, H., Dou, J., Ding, L., & Spearman, P. W. (2007) · Journal of Virology · doi:10.1128/jvi.01280-07 · Cited by 89 · see citing works
Unusual Arginine Formations in Protein Function and Assembly: Rings, Strings, and Stacks
Neves, M. A. C., Yeager, M. J., & Abagyan, R. A. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp3009699 · Cited by 87 · see citing works
Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly
Uetrecht, C., & Heck, A. J. R. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201008120 · Cited by 86 · see citing works
Contribution of E3-Ubiquitin Ligase Activity to HIV-1 Restriction by TRIM5α rh : Structure of the RING Domain of TRIM5α
Lienlaf, M., Hayashi, F., Nunzio, F. D., Tochio, N., Kigawa, T., Yokoyama, S., & Diaz‐Griffero, F. (2011) · Journal of Virology · doi:10.1128/jvi.00497-11 · Cited by 86 · see citing works
Mammalian SCAN Domain Dimer Is a Domain-Swapped Homolog of the HIV Capsid C-Terminal Domain
Ivanov, D., Stone, J. R., Maki, J. L., Collins, T., & Wagner, G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.015 · Cited by 86 · see citing works
Maturation of retroviruses
Pornillos, O., & Ganser-Pornillos, B. K. (2019) · Current Opinion in Virology · doi:10.1016/j.coviro.2019.05.004 · Cited by 84 · see citing works
Self-citation
Generalized Structural Polymorphism in Self-Assembled Viral Particles
Nguyen, H. D., & Brooks, C. L. (2008) · Nano Letters · doi:10.1021/nl802828v · Cited by 83 · see citing works
HIV-1 capsid inhibitors as antiretroviral agents
Thenin-Houssier, S., & Valente, S. (2016) · Current HIV Research · doi:10.2174/1570162x14999160224103555 · Cited by 75 · see citing works
RING Domain Mutations Uncouple TRIM5α Restriction of HIV-1 from Inhibition of Reverse Transcription and Acceleration of Uncoating
Roa, A., Hayashi, F., Yang, Y., Lienlaf, M., Zhou, J., Shi, J., Watanabe, S., Kigawa, T., Yokoyama, S., Aiken, C., et al. (2011) · Journal of Virology · doi:10.1128/jvi.05811-11 · Cited by 79 · see citing works
Self-citation
The host protein Staufen1 interacts with the Pr55Gagzinc fingers and regulates HIV-1 assembly via its N-terminus
Chatel‐Chaix, L., Boulay, K., Mouland, A. J., & DesGroseillers, L. (2008) · Retrovirology · doi:10.1186/1742-4690-5-41 · Cited by 79 · see citing works
Virus-Like Particle Mediated CRISPR/Cas9 Delivery for Efficient and Safe Genome Editing
Lyu, P., Wang, L., & Lu, B. (2020) · Life · doi:10.3390/life10120366 · Cited by 79 · see citing works
Fabrication of Colloidal Crystals with Tubular-like Packings
Li, F., Badel, X., Linnros, J., & Wiley, J. B. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042928n · Cited by 78 · see citing works
Inhibiting Early-Stage Events in HIV-1 Replication by Small-Molecule Targeting of the HIV-1 Capsid
Kortagere, S., Madani, N., Mankowski, M. K., Schön, A., Zentner, I., Swaminathan, G., Princiotto, A. M., Anthony, K., Oza, A., Sierra, L., et al. (2012) · Journal of Virology · doi:10.1128/jvi.05006-11 · Cited by 77 · see citing works
19F Dynamic Nuclear Polarization at Fast Magic Angle Spinning for NMR of HIV-1 Capsid Protein Assemblies
Lu, M., Wang, M., Sergeyev, I. V., Quinn, C. M., Struppe, J. O., Rosay, M., Maas, W. E., Gronenborn, A. M., & Polenova, T. E. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09216 · Cited by 74 · see citing works
Retrovirus maturation-an extraordinary structural transformation
Mattei, S., Schur, F. K., & Briggs, J. A. (2016) · Current Opinion in Virology · doi:10.1016/j.coviro.2016.02.008 · Cited by 72 · see citing works
“Different core geometries are proposed to differ in the distribution of the pentamers within the hexameric lattice [41,60,61] (Figure 2c).”
Background
Virus maturation as a new HIV-1 therapeutic target
Adamson, C. S., Salzwedel, K., & Freed, E. O. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903039714 · Cited by 72 · see citing works
Modulation of Retroviral Restriction and Proteasome Inhibitor-Resistant Turnover by Changes in the TRIM5α B-Box 2 Domain
Diaz‐Griffero, F., Kar, A. K., Perron, M. J., Xiang, S.-H., Javanbakht, H., Li, X., & Sodroski, J. (2007) · Journal of Virology · doi:10.1128/jvi.00703-07 · Cited by 72 · see citing works
Irreversible growth model for virus capsid assembly
Hicks, S. D., & Henley, C. L. (2006) · Physical Review E · doi:10.1103/physreve.74.031912 · Cited by 71 · see citing works
IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating
Dick, R. A., Mallery, D. L., Vogt, V. M., & James, L. C. (2018) · Viruses · doi:10.3390/v10110640 · Cited by 71 · see citing works
Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity
Lu, C., Turley, S., Marionni, S. T., Park, Y., Lee, K. K., Patrick, M., Shah, R., Sandkvist, M., Bush, M. F., & Hol, W. G. J. (2013) · Structure · doi:10.1016/j.str.2013.06.027 · Cited by 69 · see citing works
A Two-Pronged Structural Analysis of Retroviral Maturation Indicates that Core Formation Proceeds by a Disassembly-Reassembly Pathway Rather than a Displacive Transition
Keller, P. W., Huang, R. K., England, M. R., Waki, K., Cheng, N., Heymann, J. B., Craven, R. C., Freed, E. O., & Steven, A. C. (2013) · Journal of Virology · doi:10.1128/jvi.01408-13 · Cited by 67 · see citing works
Rotten to the core: antivirals targeting the HIV-1 capsid core
McFadden, W. M., Snyder, A. A., Kirby, K. A., Tedbury, P. R., Raj, M., Wang, Z., & Sarafianos, S. G. (2021) · Retrovirology · doi:10.1186/s12977-021-00583-z · Cited by 65 · see citing works
Discovery of phenylalanine derivatives as potent HIV-1 capsid inhibitors from click chemistry-based compound library
Wu, G., Zalloum, W. A., Meuser, M. E., Jing, L., Kang, D., Chen, C., Tian, Y., Zhang, F., Cocklin, S., Lee, K., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.029 · Cited by 66 · see citing works
Permeability of the HIV-1 capsid to metabolites modulates viral DNA synthesis
Xu, C., Fischer, D. K., Rankovic, S., Li, W., Dick, R. A., Runge, B., Zadorozhnyi, R., Ahn, J., Aiken, C., Polenova, T. E., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3001015 · Cited by 65 · see citing works
Self-citation
Molecular Studies of HTLV-1 Replication: An Update
Martin, J., Maldonado, J. O., Mueller, J. D., Zhang, W., & Mansky, L. M. (2016) · Viruses · doi:10.3390/v8020031 · Cited by 66 · see citing works
Virtual screening based identification of novel small-molecule inhibitors targeted to the HIV-1 capsid
Curreli, F., Zhang, H., Zhang, X., Pyatkin, I., Victor, Z., Altieri, A., & Debnath, A. K. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.11.045 · Cited by 63 · see citing works
Antiviral activity of α-helical stapled peptides designed from the HIV-1 capsid dimerization domain
Zhang, H., Curreli, F., Zhang, X., Bhattacharya, S., Waheed, A. A., Cooper, A., Cowburn, D., Freed, E. O., & Debnath, A. K. (2011) · Retrovirology · doi:10.1186/1742-4690-8-28 · Cited by 63 · see citing works
RSV Capsid Polymorphism Correlates with Polymerization Efficiency and Envelope Glycoprotein Content: Implications that Nucleation Controls Morphogenesis
Butan, C., Winkler, D. C., Heymann, J. B., Craven, R. C., & Steven, A. C. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.12.003 · Cited by 61 · see citing works
Electrostatic Repulsion, Compensatory Mutations, and Long-range Non-additive Effects at the Dimerization Interface of the HIV Capsid Protein
del Álamo, M., & Mateu, M. G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.086 · Cited by 60 · see citing works
Design, Synthesis, and Mechanism Study of Benzenesulfonamide-Containing Phenylalanine Derivatives as Novel HIV‑1 Capsid Inhibitors with Improved Antiviral Activities
Sun, L., Dick, A., Meuser, M. E., Huang, T., Zalloum, W. A., Chen, C., Cherukupalli, S., Xu, S., Ding, X., Gao, P., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00015 · Cited by 60 · see citing works
Mutation of Dileucine-Like Motifs in the Human Immunodeficiency Virus Type 1 Capsid Disrupts Virus Assembly, Gag-Gag Interactions, Gag-Membrane Binding, and Virion Maturation
Joshi, A., Nagashima, K., & Freed, E. O. (2006) · Journal of Virology · doi:10.1128/jvi.00355-06 · Cited by 60 · see citing works
Critical mechanistic features of HIV-1 viral capsid assembly
Gupta, M., Pak, A. J., & Voth, G. A. (2023) · Science Advances · doi:10.1126/sciadv.add7434 · Cited by 59 · see citing works
Interaction of the HIV-1 Intasome with Transportin 3 Protein (TNPO3 or TRN-SR2)
Larue, R. C., Gupta, K., Wuensch, C., Shkriabai, N., Kessl, J. J., Danhart, E., Feng, L., Taltynov, O., Christ, F., Duyne, G. D. V., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.384669 · Cited by 58 · see citing works
Continuum Theory of Retroviral Capsids
Nguyen, T. T., Bruinsma, R., & Gelbart, W. M. (2006) · Physical Review Letters · doi:10.1103/physrevlett.96.078102 · Cited by 59 · see citing works
The capsid protein of human immunodeficiency virus: intersubunit interactions during virus assembly
Mateu, M. G. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07313.x · Cited by 56 · see citing works
Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication
Nunzio, F. D., Fricke, T., Miccio, A., Valle-Casuso, J., Perez, P., Souque, P., Rizzi, E., Severgnini, M., Mavilio, F., Charneau, P., et al. (2013) · Retrovirology · doi:10.1186/1742-4690-10-s1-p111 · Cited by 171 · see citing works
Assembly of Human Immunodeficiency Virus Precursor Gag Proteins
Huseby, D. L., Barklis, R. L., Alfadhli, A., & Barklis, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412325200 · Cited by 56 · see citing works
A molecular switch modulates assembly and host factor binding of the HIV-1 capsid
Schirra, R. T., dos Santos, N. F. B., Zadrozny, K. K., Kucharska, I., Ganser‐Pornillos, B. K., & Pornillos, O. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00913-5 · Cited by 51 · see citing works
Self-citation
Direct and Dynamic Detection of HIV-1 in Living Cells
Helma, J., Schmidthals, K., Lux, V., Nüske, S., Scholz, A. M., Kräusslich, H., Rothbauer, U., & Leonhardt, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050026 · Cited by 55 · see citing works

Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
Ganser-Pornillos, B. K., Cheng, A., & Yeager, M. (2007) · Cell · doi:10.1016/j.cell.2007.08.018 · Cited by 321 · see citing works
Self-citation
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 · see citing works
Self-citation
Atomic-level modelling of the HIV capsid
Pornillos, O., Ganser-Pornillos, B. K., & Yeager, M. (2011) · Nature · doi:10.1038/nature09640 · Cited by 372 · see citing works
Self-citation
Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein
von Schwedler, U. K., Stray, K. M., Garrus, J. E., & Sundquist, W. I. (2003) · Journal of Virology · doi:10.1128/jvi.77.9.5439-5450.2003 · Cited by 421 · see citing works
Self-citation
AC. Visualization of a missing link in retrovirus capsid assembly. Nature. 2009; 457:694–698. [PubMed: 19194444
Giovanni Cardone, A., Purdy, J. G., Cheng, N., Craven, R. C., & Alasdair, C. (2016)

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

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks