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The Role of Capsid in the Early Steps of HIV-1 Infection: New Insights into the Core of the Matter

AlBurtamani, N., Paul, A., & Fassati, A. (2021) · Viruses · doi:10.3390/v13061161 · Cited by 20 · see citing works

Design and exploration of C-3 benzoic acid bioisosteres and alkyl replacements in the context of GSK3532795 (BMS-955176) that exhibit broad spectrum HIV-1 maturation inhibition

Swidorski, J. J., Jenkins, S., Hanumegowda, U., Parker, D. D., Beno, B. R., Protack, T., Ng, A., Gupta, A., Shanmugam, Y., Dicker, I. B., et al. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.127823 · Cited by 19 · see citing works

Multidomain Assembler (MDA) Generates Models of Large Multidomain Proteins

Hertig, S., Goddard, T. D., Johnson, G. T., & Ferrin, T. E. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.03.051 · Cited by 19 · see citing works

The Role of Peripheral Amide Groups as Hydrogen‐Bonding Directors in the Tubular Self‐Assembly of Dinucleobase Monomers

Vázquez‐González, V., Mayoral, M. J., Aparicio, F., Martinez-Arjona, P., & González‐Rodríguez, D. (2021) · ChemPlusChem · doi:10.1002/cplu.202100255 · Cited by 18 · see citing works

Allosteric Regulation of HIV-1 Capsid Structure for Gag Assembly, Virion Production, and Viral Infectivity by a Disordered Interdomain Linker

Koma, T., Kotani, O., Miyakawa, K., Ryo, A., Yokoyama, M., Doi, N., Adachi, A., Sato, H., & Nomaguchi, M. (2019) · Journal of Virology · doi:10.1128/jvi.00381-19 · Cited by 17 · see citing works

Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging

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Role of Mason-Pfizer Monkey Virus CA-NC Spacer Peptide-Like Domain in Assembly of Immature Particles

Strohalmová, K., Spiwok, V., Lepšı́k, M., Hadravová, R., Křížová, I., Ulbrich, P., Pichová, I., Bednářová, L., Ruml, T., & Rumlová, M. (2014) · Journal of Virology · doi:10.1128/jvi.02286-14 · Cited by 17 · see citing works

FAITH – Fast Assembly Inhibitor Test for HIV

Hadravová, R., Rumlová, M., & Ruml, T. (2015) · Virology · doi:10.1016/j.virol.2015.08.029 · Cited by 17 · see citing works

Poxvirus under the eyes of electron microscope

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The Effect of Inositol Hexakisphosphate on HIV-1 Particle Production and Infectivity can be Modulated by Mutations that Affect the Stability of the Immature Gag Lattice

Kleinpeter, A. B., Zhu, Y., Mallery, D. L., Ablan, S. D., Chen, L., Hardenbrook, N. J., Saiardi, A., James, L. C., Zhang, P., & Freed, E. O. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168037 · Cited by 15 · see citing works

Cryo-electron tomography to study viral infection

Graham, M., & Zhang, P. (2023) · Biochemical Society Transactions · doi:10.1042/bst20230103 · Cited by 15 · see citing works

Cryo-electron microscopy and single molecule fluorescent microscopy detect CD4 receptor induced HIV size expansion prior to cell entry

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Modeling the dynamics and kinetics of HIV-1 Gag during viral assembly

Tomasini, M. D., Johnson, D. S., Mincer, J. S., & Simon, S. M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0196133 · Cited by 14 · see citing works

Dynamics of upstream ESCRT organization at the HIV-1 budding site

Hudait, A., Hurley, J. H., & Voth, G. A. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.05.020 · Cited by 13 · see citing works

Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline

Folio, C., Sierra, N., Dujardin, M., Álvarez, G., & Guillon, C. (2017) · Viruses · doi:10.3390/v9110335 · Cited by 13 · see citing works

Antiviral Properties of HIV-1 Capsid Inhibitor GSK878

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A simple, high-throughput stabilization assay to test HIV-1 uncoating inhibitors

Dostálková, A., Hadravová, R., Kaufman, F., Křížová, I., Škach, K., Flegel, M., Hrabal, R., Ruml, T., & Rumlová, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-53483-w · Cited by 12 · see citing works

The HIV-1 gag p6: a promising target for therapeutic intervention

Chen, X., & Wang, X. (2024) · Retrovirology · doi:10.1186/s12977-024-00633-2 · Cited by 12 · see citing works

Cryo-electron microscopy in the study of virus entry and infection

Dutta, M., & Acharya, P. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1429180 · Cited by 11 · see citing works

HIV-1 Gag release from yeast reveals ESCRT interaction with the Gag N-terminal protein region

Meusser, B., Purfürst, B., & Luft, F. C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014710 · Cited by 10 · see citing works

Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice

Obr, M., Percipalle, M., Chernikova, D., Yang, H., Thader, A., Pinke, G., Porley, D., Mansky, L. M., Dick, R. A., & Schur, F. K. M. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01390-8 · Cited by 9 · see citing works

Structure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396

Murgatroyd, C., Pirrie, L., Tran, F., Smith, T., Westwood, N. J., & Adamson, C. S. (2016) · Journal of Virology · doi:10.1128/jvi.01075-16 · Cited by 9 · see citing works

Composite Sequence–Structure Stability Models as Screening Tools for Identifying Vulnerable Targets for HIV Drug and Vaccine Development

Manocheewa, S., Mittler, J. E., Samudrala, R., & Mullins, J. I. (2015) · Viruses · doi:10.3390/v7112901 · Cited by 9 · see citing works

Virus Matryoshka: A Bacteriophage Particle—Guided Molecular Assembly Approach to a Monodisperse Model of the Immature Human Immunodeficiency Virus

Saxena, P., He, L., Malyutin, A. G., Datta, S. A. K., Rein, A. R., Bond, K. M., Jarrold, M. F., Spilotros, A., Svergun, D. I., Douglas, T., et al. (2016) · Small · doi:10.1002/smll.201601712 · Cited by 9 · see citing works

Functional and Structural Characterization of Novel Type of Linker Connecting Capsid and Nucleocapsid Protein Domains in Murine Leukemia Virus

Doležal, M., Hadravová, R., Kožíšek, M., Bednářová, L., Langerová, H., Ruml, T., & Rumlová, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.746461 · Cited by 8 · see citing works

Recent advances in retroviruses via cryo-electron microscopy

Mak, J., & de Marco, A. (2018) · Retrovirology · doi:10.1186/s12977-018-0405-6 · Cited by 8 · see citing works

LIFE: International Journal of Health and Life-Sciences

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The HIV-1 maturation inhibitor, EP39, interferes with the dynamic helix-coil equilibrium of the CA-SP1 junction of Gag

Chen, X., Coric, P., Larue, V., Turcaud, S., Wang, X., Nonin‐Lecomte, S., & Bouaziz, S. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112634 · Cited by 7 · see citing works

The capsid revolution

Taylor, I. A., & Fassati, A. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad076 · Cited by 8 · see citing works

The Conserved Tyr176/Leu177 Motif in the α-Helix 9 of the Feline Immunodeficiency Virus Capsid Protein Is Critical for Gag Particle Assembly

Ovejero, C. A., González, S. A., & Affranchino, J. L. (2019) · Viruses · doi:10.3390/v11090816 · Cited by 7 · see citing works

Mathematical determination of the HIV-1 matrix shell structure and its impact on the biology of HIV-1

Sun, W., Reyes-Serratos, E., Barilla, D., Santos, J. R. L., Bujold, M., Graves, S., & Marcet-Palacios, M. (2019) · PLOS ONE · doi:10.1371/journal.pone.0224965 · Cited by 6 · see citing works

Effect of Small Polyanions on In Vitro Assembly of Selected Members of Alpha-, Beta- and Gammaretroviruses

Dostálková, A., Vokatá, B., Kaufman, F., Ulbrich, P., Ruml, T., & Rumlová, M. (2021) · Viruses · doi:10.3390/v13010129 · Cited by 6 · see citing works

Intrinsic resistance of HIV-2 and SIV to the maturation inhibitor GSK2838232

Smith, R. A., Raugi, D. N., Nixon, R. S., Song, J. K., Seydi, M., & Gottlieb, G. S. (2023) · PLoS ONE · doi:10.1371/journal.pone.0280568 · Cited by 5 · see citing works

Human immunodeficiency virus

Spearman, P. W. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00047-2 · Cited by 9 · see citing works

Inositol Phosphates and Retroviral Assembly: A Cellular Perspective

Ricana, C. L., & Dick, R. A. (2021) · Viruses · doi:10.3390/v13122516 · Cited by 5 · see citing works

Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition

Fu, L., Cheng, S., Riedel, D., Kopecny, L., Schuh, M., & Görlich, D. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01684-5 · Cited by 6 · see citing works

New windows into retroviral RNA structures

Jayaraman, D., & Kenyon, J. C. (2018) · Retrovirology · doi:10.1186/s12977-018-0393-6 · Cited by 4 · see citing works

Role for Gag-CA Interdomain Linker in Primate Lentiviral Replication

Doi, N., Koma, T., Adachi, A., & Nomaguchi, M. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01831 · Cited by 3 · see citing works

A single G10T polymorphism in HIV-1 subtype C Gag-SP1 regulates sensitivity to maturation inhibitors

Ghimire, D., Yuvraj, K. C., Timilsina, U., Goel, K., Nitz, T. J., Wild, C. T., & Gaur, R. (2021) · Retrovirology · doi:10.1186/s12977-021-00553-5 · Cited by 3 · see citing works

Understanding the co-evolutionary molecular mechanisms of resistance in the HIV-1 Gag and protease

Marie, V., & Gordon, M. L. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1950569 · Cited by 3 · see citing works

The life cycle of feline immunodeficiency virus

González, S. A., & Affranchino, J. L. (2024) · Virology · doi:10.1016/j.virol.2024.110304 · Cited by 3 · see citing works

Electron Microscopy of Viruses: Techniques to Prepare Viruses and Viral Proteins for Observation by Electron Microscopy☆

Fender, P., Moriscot, C., Ruigrok, R. W. H., & Schoehn, G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.02563-0 · Cited by 3 · see citing works

Advances in Molecular Simulation

Aldeghi, M., & Biggin, P. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12343-1 · Cited by 2 · see citing works

Governed by surface amino acid composition: HIV capsid passage through the NPC barrierPreprint

Fu, L., Cheng, S., Riedel, D., Kopecny, L., Schuh, M., & Görlich, D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.13.643050 · Cited by 3 · see citing works

Positive correlation between structural disorder of the HIV-1 Gag N-terminal segment and progeny virus particle formation

Koma, T., Kotani, O., Kamba, K., Miyakawa, K., Morita, T., Nakamura, H. K., Yokoyama, M., Doi, N., Kondo, T., Nagata, T., et al. (2025) · Journal of Virology · doi:10.1128/jvi.00887-25 · Cited by 2 · see citing works

Cryo-EM Structure of the Pol Polyprotein Provides Insights into HIV MaturationPreprint

Harrison, J. J. E. K., Passos, D. O., Bruhn, J. F., Bauman, J. D., Tuberty, L., DeStefano, J. J., Ruiz, F. X., Lyumkis, D., & Arnold, E. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.03.462959 · Cited by 2 · see citing works

The structure of a native orthobunyavirus ribonucleoprotein reveals a key role for viral RNA in maintaining its helical architecturePreprint

Hopkins, F. R., Álvarez‐Rodríguez, B., Heath, G. R., Panayi, K., Hover, S. E., Edwards, T. A., Barr, J. N., & Fontana, J. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.27.466080 · Cited by 2 · see citing works

Variability and Signatures of Capsid Amino Acid of HIV-1D Subtype from Drug-Naive and ARV-treated Individuals

Dimonte, S. (2015) · Journal of Virology & Antiviral Research · doi:10.4172/2324-8955.1000148 · Cited by 1 · see citing works

Mechanical response of polyprotein revealed by single-molecule optical tweezers

Li, S., Liu, H., Hu, C., He, C., & Hu, H. (2022) · Applied Physics Express · doi:10.35848/1882-0786/ac6a40 · Cited by 1 · see citing works

System scale

Li, G. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95917-9.00020-1 · Cited by 1 · see citing works

Identification and Characterization of Two Novel Syncytin-Like Retroviral Envelope Genes, Captured for a Possible role in the Atypical Structure of the Hyena Placenta and in the Emergence of the Non-Mammalian Mabuya Lizard Placenta a

Funk, M. (2018) · theses.fr (ABES) · doi:10.70675/0303ae66zace8z4f41zbc60zf747fb33a4aa · Cited by 1 · see citing works

Studies of Fv1 binding and restriction

Li, H. L. W. (2015) · UCL Discovery (University College London)

Biochemical and Genetic Investigation of Immature Murine Leukemia Virus Assembly

Tinaztepe, S. (2017) · doi:10.7916/d82v2tng

Characterization and epitope mapping of a panel of monoclonal antibodies against HIV‐1 matrix protein

Zhang, Z., Zhang, F., Bai, S., Qiao, J., Shen, H., Huang, F., Gao, S., Li, S., Gu, Y., & Xia, N. (2018) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1662

Organization of Upstream ESCRT Machinery at the HIV-1 Budding SitePreprint

Hudait, A., Hurley, J. H., & Voth, G. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.13.507863

Validation of HIV-1 MA Shell Structural Arrangements and Env Protein Interactions Predict a Role of the MA Shell in Viral Maturation

Mangukia, T. A., Santos, J. R. L., Sun, W., Cesarz, D., Ortiz, C. D., & Marcet‐Palacios, M. (2023) · Viruses · doi:10.3390/v15040893

Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution

Schur, F. K. M., Hagen, W. J. H., Rumlová, M., Ruml, T., Müller, B., Kräusslich, H.-G., & Briggs, J. A. G. (2015) · Nature · doi:10.1038/nature13838 · Cited by 296 · see citing works

Structure and assembly of immature HIV

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The stoichiometry of Gag protein in HIV-1

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Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy

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The Molecular Architecture of HIV

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