High-resolution structure of a retroviral capsid hexameric amino-terminal domain

Automated MAD and MIR structure solution

Terwilliger, T. C., & Berendzen, J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999000839 · Cited by 3,032

The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys

Stremlau, M. H., Owens, C. M., Perron, M. J., Kießling, M. K., Autissier, P., & Sodroski, J. (2004) · Nature · doi:10.1038/nature02343 · Cited by 1,810

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×

The stoichiometry of Gag protein in HIV-1

Briggs, J. A. G., Simon, M. N., Gross, I., Kräusslich, H.-G., Fuller, S. D., Vogt, V. M., & Johnson, M. C. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb785 · Cited by 539

Synthesis, Assembly, and Processing of Viral Proteins

Swanstrom, R. I., & Wills, J. (1997) · Europe PMC (PubMed Central) · Cited by 518

Formation of a Human Immunodeficiency Virus Type 1 Core of Optimal Stability Is Crucial for Viral Replication

Forshey, B. M., von Schwedler, U. K., Sundquist, W. I., & Aiken, C. (2002) · Journal of Virology · doi:10.1128/jvi.76.11.5667-5677.2002 · Cited by 514

ARP⧸wARP and Automatic Interpretation of Protein Electron Density Maps

Morris, R. J., Anastassis Perrakis, A., & Lamzin, V. S. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)74011-7 · Cited by 508

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

Positional cloning of the mouse retrovirus restriction gene Fvl

Best, S., Tissier, P. L., Towers, G. J., & Stoye, J. P. (1996) · Nature · doi:10.1038/382826a0 · Cited by 499

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

Retroviral Env Glycoprotein Trafficking and Incorporation into Virions

Murakami, T. (2012) · Molecular Biology International · doi:10.1155/2012/682850 · Cited by 30

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

Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles

Hyun, J., Radjainia, M., Kingston, R. L., & MITRA, A. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.108209 · Cited by 25

Characterization of the invariable residue 51 mutations of human immunodeficiency virus type 1 capsid protein on in vitro CA assembly and infectivity

Abdurahman, S., Youssefi, M., Höglund, S., & Vahlne, A. G. (2007) · Retrovirology · doi:10.1186/1742-4690-4-69 · Cited by 25

Oligomeric viral proteins: small in size, large in presence

Jayaraman, B., Smith, A. M., Fernandes, J. D., & Frankel, A. D. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2016.1215406 · Cited by 26

An RNA-binding compound that stabilizes the HIV-1 gRNA packaging signal structure and specifically blocks HIV-1 RNA encapsidation

Ingemarsdotter, C. K., Zeng, J., Long, Z., Lever, A. M. L., & Kenyon, J. C. (2018) · Retrovirology · doi:10.1186/s12977-018-0407-4 · Cited by 24

Complex determinants within the Moloney murine leukemia virus capsid modulate susceptibility of the virus to Fv1 and Ref1-mediated restriction

Ulm, J. W., Perron, M. J., Sodroski, J., & Mulligan, R. C. (2007) · Virology · doi:10.1016/j.virol.2006.09.048 · Cited by 25

Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control

Cottee, M. A., Beckwith, S. L., Letham, S. C., Kim, S. J., Young, G. R., Stoye, J. P., Garfinkel, D. J., & Taylor, I. A. (2021) · Nature Communications · doi:10.1038/s41467-021-25849-0 · Cited by 24

Transcriptional Regulation of Endogenous Retroviruses and Their Misregulation in Human Diseases

Zhang, Q., Pan, J., Cong, Y., & Mao, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710112 · Cited by 25

Structural basis for Fullerene geometry in a human endogenous retrovirus capsid

Acton, O. J., Grant, T., Nicastro, G., Ball, N. J., Goldstone, D. C., Robertson, L. E., Sader, K., Nans, A., Ramos, A., Stoye, J. P., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13786-y · Cited by 22

Impact of TRIM5α in vivo

Nakayama, E. E., & Shioda, T. (2015) · AIDS · doi:10.1097/qad.0000000000000812 · Cited by 24

Role of Human TRIM5α in Intrinsic Immunity

Nakayama, E. E., & Shioda, T. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00097 · Cited by 22

Effect of Dimerizing Domains and Basic Residues on In Vitro and In Vivo Assembly of Mason-Pfizer Monkey Virus and Human Immunodeficiency Virus

Bohmová, K., Hadravová, R., Štokrová, J., Tůma, R., Ruml, T., Pichová, I., & Rumlová, M. (2009) · Journal of Virology · doi:10.1128/jvi.02022-09 · Cited by 20

Structure of the Capsid Amino-Terminal Domain from the Betaretrovirus, Jaagsiekte Sheep Retrovirus

Mortuza, G. B., Goldstone, D. C., Pashley, C. L., Haire, L. F., Palmarini, M., Taylor, W. R., Stoye, J. P., & Taylor, I. A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.066 · Cited by 20

Intracellular immunity to HIV-1: newly defined retroviral battles inside infected cells

Zheng, Y., & Peterlin, B. M. (2005) · Retrovirology · doi:10.1186/1742-4690-2-25 · Cited by 20

Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid

Ball, N. J., Nicastro, G., Dutta, M., Pollard, D. J., Goldstone, D. C., Sanz-Ramos, M., Ramos, A., Müllers, E., Stirnnagel, K., Stanke, N., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005981 · Cited by 19

Characterization of an Amino-Terminal Dimerization Domain from Retroviral Restriction Factor Fv1

Bishop, K. N., Mortuza, G. B., Howell, S. A., Yap, M. W., Stoye, J. P., & Taylor, I. A. (2006) · Journal of Virology · doi:10.1128/jvi.00395-06 · Cited by 19

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

Control of the rate of evaporation in protein crystallization by the `microbatch under oil' method

Brumshtein, B., Greenblatt, H. M., Futerman, A. H., Silman, I., & Sussman, J. L. (2008) · Journal of Applied Crystallography · doi:10.1107/s0021889808024667 · Cited by 18

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

Obr, M., & Schur, F. K. M. (2019) · Advances in virus research · doi:10.1016/bs.aivir.2019.07.008 · Cited by 19

Coarse-grained protein-protein stiffnesses and dynamics from all-atom simulations

Hicks, S. D., & Henley, C. L. (2010) · Physical Review E · doi:10.1103/physreve.81.030903 · Cited by 18

Role of capsid sequence and immature nucleocapsid proteins p9 and p15 in Human Immunodeficiency Virus type 1 genomic RNA dimerization

Kafaie, J., Dolatshahi, M., Ajamian, L., Song, R., Mouland, A. J., Rouiller, I., & Laughrea, M. (2008) · Virology · doi:10.1016/j.virol.2008.11.028 · Cited by 18

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

Strohalmová, K., Spiwok, V., Lepšík, 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 16

Cooperative role of the MHR and the CA dimerization helix in the maturation of the functional retrovirus capsid

Lokhandwala, P. M., Nguyen, T.-L. N., Bowzard, J. B., & Craven, R. C. (2008) · Virology · doi:10.1016/j.virol.2008.03.001 · Cited by 17

Homology-based Identification of Capsid Determinants That Protect HIV1 from Human TRIM5α Restriction

Maillard, P. V., Zoete, V., Michielin, O. A., & Trono, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.187609 · 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

TRIM5α and TRIMCyp form apparent hexamers and their multimeric state is not affected by exposure to restriction-sensitive viruses or by treatment with pharmacological inhibitors

Nepveu-Traversy, M.-É., Bérubé, J., & Berthoux, L. (2009) · Retrovirology · doi:10.1186/1742-4690-6-100 · Cited by 16

Murine Leukemia Virus Gag Localizes to the Uropod of Migrating Primary Lymphocytes

Li, F., Sewald, X., Jin, J., Sherer, N. M., & Mothes, W. (2014) · Journal of Virology · doi:10.1128/jvi.01104-14 · Cited by 15

A comparative analysis of the foamy and ortho virus capsid structures reveals an ancient domain duplication

Taylor, W. R., Stoye, J. P., & Taylor, I. A. (2017) · BMC Structural Biology · doi:10.1186/s12900-017-0073-0 · Cited by 15

HIV-1 Protease Uses Bi-Specific S2/S2′ Subsites to Optimize Cleavage of Two Classes of Target Sites

Potempa, M., Lee, S.-K., Yılmaz, N. K., Nalivaika, E. A., Rogers, A., Spielvogel, E., Carter, C. W., Schiffer, C. A., & Swanstrom, R. I. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.10.022 · Cited by 16

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

The p12 Domain Is Unstructured in a Murine Leukemia Virus p12-CAN Gag Construct

Kyere, S. K., Joseph, P. R. B., & Summers, M. F. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001902 · Cited by 13

Apparent effect of rabbit endogenous lentivirus type K acquisition on retrovirus restriction by lagomorph Trim5αs

Yap, M. W., & Stoye, J. P. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2012.0498 · Cited by 14

A Small Loop in the Capsid Protein of Moloney Murine Leukemia Virus Controls Assembly of Spherical Cores

Auerbach, M. R., Brown, K. R., Kaplan, A., Nueces, D. D. L., & Singh, I. R. (2006) · Journal of Virology · doi:10.1128/jvi.80.6.2884-2893.2006 · Cited by 13

The retroviral restriction factor TRIM5α

Sebastian, S., & Luban, J. (2007) · Current Infectious Disease Reports · doi:10.1007/s11908-007-0013-4 · Cited by 13

Suppression of a Morphogenic Mutant in Rous Sarcoma Virus Capsid Protein by a Second-Site Mutation: a Cryoelectron Tomography Study

Butan, C., Lokhandwala, P. M., Purdy, J. G., Giovanni Cardone, A., Craven, R. C., & Steven, A. C. (2010) · Journal of Virology · doi:10.1128/jvi.00207-10 · Cited by 12

T = 4 Icosahedral HIV-1 Capsid As an Immunogenic Vector for HIV-1 V3 Loop Epitope Display

Zhang, Z., He, M., Bai, S., Zhang, F., Jiang, J., Zheng, Q., Gao, S., Yan, X., Li, S., Gu, Y., et al. (2018) · Viruses · doi:10.3390/v10120667 · Cited by 11

A modified vapor-diffusion crystallization protocol that uses a common dehydrating agent

Dunlop, K. V., & Hazes, B. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905013806 · Cited by 11

Dynamic domain threading

Taylor, W. R., Lin, K., Klose, D., Fraternali, F., & Jonassen, I. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20915 · Cited by 11

Association Equilibrium of the HIV-1 Capsid Protein in a Crowded Medium Reveals that Hexamerization during Capsid Assembly Requires a Functional C-Domain Dimerization Interface

Bocanegra, R., Alfonso, C., Rodríguez‐Huete, A., Fuertes, M. A., Jiménez, M., Rivas, G., & Mateu, M. G. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.12.035 · Cited by 11

Functional Label-Free Assays for Characterizing the in Vitro Mechanism of Action of Small Molecule Modulators of Capsid Assembly

Lad, L., Clancy, S., Koditek, D., Wong, M. H. L., Jin, D., Niedziela‐Majka, A., Papalia, G. A., Hung, M., Yant, S. R., Somoza, J. R., et al. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00151 · Cited by 10

Isolation and characterization of a small antiretroviral molecule affecting HIV-1 capsid morphology

Abdurahman, S., Végvári, Á., Levi, M., Höglund, S., Högberg, M., Tong, W., Romero, I., Balzarini, J. M., & Vahlne, A. G. (2009) · Retrovirology · doi:10.1186/1742-4690-6-34 · Cited by 10

Structural Model of the Tubular Assembly of the Rous Sarcoma Virus Capsid Protein

Jeon, J., Qiao, X., Hung, I., MITRA, A. K., Desfosses, A., Huang, D. T., Gor’kov, P. L., Craven, R. C., Kingston, R. L., Gan, Z., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b11939 · Cited by 9

In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature

Jaballah, S. A., Bailey, G. D., Desfosses, A., Hyun, J., MITRA, A. K., & Kingston, R. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-02060-0 · Cited by 10

Capsid is an important determinant for functional complementation of murine leukemia virus and spleen necrosis virus Gag proteins.

Lee, S.-K., Boyko, V. P., & Hu, W.-S. (2007) · Virology · doi:10.1016/j.virol.2006.10.038 · Cited by 10

Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity

Obr, M., Hadravová, R., Doležal, M., Křžová, I., Papoušková, V., Žı́dek, L., Hrabal, R., Ruml, T., & Rumlová, M. (2014) · Retrovirology · doi:10.1186/s12977-014-0094-8 · Cited by 7

A Sensitive Assay Using a Native Protein Substrate for Screening HIV-1 Maturation Inhibitors Targeting the Protease Cleavage Site between the Matrix and Capsid

Lee, S.-K., Cheng, N., Hull-Ryde, E. A., Potempa, M., Schiffer, C. A., Janzen, W. P., & Swanstrom, R. I. (2013) · Biochemistry · doi:10.1021/bi4005232 · Cited by 8

Murine double minute 2 as a modulator of retroviral restrictions mediated by TRIM5α

Malbec, M., Pham, Q. T., Plourde, M. B., Létourneau-Hogan, A., Nepveu-Traversy, M.-É., & Berthoux, L. (2010) · Virology · doi:10.1016/j.virol.2010.06.021 · Cited by 8

Genetic Studies of the β-Hairpin Loop of Rous Sarcoma Virus Capsid Protein

Spidel, J. L., Wilson, C., Craven, R. C., & Wills, J. W. (2006) · Journal of Virology · doi:10.1128/jvi.01551-06 · Cited by 8

A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein

Tang, S., Ablan, S. D., Dueck, M. E., Ayala-López, W., Soto, B. L., Caplan, M. R., Nagashima, K., HEWLETT, I. K., Freed, E. O., & Levin, J. G. (2006) · Virology · doi:10.1016/j.virol.2006.09.027 · Cited by 8

Determining Interdomain Structure and Dynamics of a Retroviral Capsid Protein in the Presence of Oligomerization: Implication for Structural Transition in Capsid Assembly

Chen, K., & Tjandra, N. (2013) · Biochemistry · doi:10.1021/bi400592d · Cited by 7

The capsid revolution

Taylor, I. A., & Fassati, A. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad076 · Cited by 7

Two-hybrid analysis of Ty3 capsid subdomain interactions

Zhang, M., Larsen, L. S. Z., Irwin, B., Bilanchone, V., & Sandmeyer, S. B. (2010) · Mobile DNA · doi:10.1186/1759-8753-1-14 · Cited by 6

Natural-product-library-based screening for discovery of capsid C-terminal domain targeted HIV-1 inhibitors

Zhang, D., Luo, R., Xu, L., Yang, L., Xu, X., Zheng, Y., & Luo, H. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105926 · Cited by 6

Contribution of Glutamine Residues in the Helix 4-5 Loop to Capsid-Capsid Interactions in Simian Immunodeficiency Virus of Macaques

Tipper, C. H., & Sodroski, J. (2014) · Journal of Virology · doi:10.1128/jvi.01388-14 · Cited by 5

HIV-1 Maturation

Aiken, C., & Zhang, P. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7729-7_6 · Cited by 4

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 7

The Retrovirus Capsid Core

Zhang, W., Mendonça, L., & Mansky, L. M. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-10-8456-0_8 · Cited by 4

Restriction of Retroviruses by TRIM5α

Towers, G. J. (2005) · Future Virology · doi:10.2217/17460794.1.1.71 · Cited by 4

Consideration of the three-dimensional structure of core shells (capsids) in spherical retroviruses.

Nermut, M., & Mulloy, B. (2007) · Micron · doi:10.1016/j.micron.2006.11.007 · Cited by 3

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

Expression, purification, crystallization and preliminary X-ray diffraction analysis ofArabidopsis thalianacyclophilin 38 (AtCyp38)

Vasudevan, D., Gopalan, G., He, Z., Luan, S., & Swaminathan, K. (2005) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309105037681 · Cited by 2

1H, 13C, and 15N resonance assignment of the N-terminal domain of Mason-Pfizer monkey virus capsid protein, CA 1-140

Macek, P., Žı́dek, L., Rumlová, M., Pichová, I., & Sklenář, V. (2008) · Biomolecular NMR Assignments · doi:10.1007/s12104-008-9080-1 · Cited by 2

Erratum: 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/nature03065 · Cited by 2

Reduction of N-Tropic Mutant Porcine Endogenous Retrovirus Infectivity by Human Tripartite Motif-Containing 5-Isoform Alpha

Lee, J., Cho, Y. D., Heo, Y., Kwon, Y. C., Kim, D. G., Choi, B.-S., Kim, S. S., & Kim, Y. B. (2011) · Transplantation Proceedings · doi:10.1016/j.transproceed.2011.04.014 · Cited by 1

THE ROLE OF EARLY CYTOTOXIC LYMPHOCYTE (CTL) ESCAPE IN THE PATHOGENESIS OF HIV-1 SUBTYPE C INFECTION

Ntale, R. S. (2012) · Open University of Cape Town (University of Cape Town) · Cited by 1

Statistical Mechanical Models Of Virus Capsid Assembly

Hicks, S. D. (2010) · eCommons (Cornell University) · Cited by 1

Identification, Optimization and Preliminary X-ray Diffraction of a New Crystal Form of the N-terminal Domain of the HIV-1 CA Protein

Woerkom, R. C. V., Dixon, A. S., Oslund, R., & Howard, B. (2007) · American Journal of Undergraduate Research · doi:10.33697/ajur.2007.008 · Cited by 1

In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes under physiological conditionsPreprint

Jaballah, S. A., Bailey, G. D., Desfosses, A., Hyun, J., MITRA, A. K., & Kingston, R. L. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/098400 · Cited by 1

Studies of Fv1 binding and restriction

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

Molecular Counting in Moloney Murine Leukemia Virus Assembly.

Johnson, S. F. (2012) · Deep Blue (University of Michigan)

Studies on HIV-1 core assembly

Abdurahman, S. (2007) · Figshare

ANALYSIS OF THE ROLES OF THE P10 DOMAIN OF GAG AND OF DIMERIZATION IN ROUS SARCOMA VIRUS ASSEMBLY

Phillips, J. M. (2008) · eCommons (Cornell University)

Characterisation of llama antibody fragments able to act as HIV-1 entry inhibitors

Quigley, A. F. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique)

Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR

Okazaki, H., Kaneko, C., Hirahara, M., Watanabe, S., Tochio, N., Kigawa, T., & Nishimura, C. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.06.009 · Cited by 1

STATISTICAL MECHANICAL MODELS OF VIRUS CAPSID

Hicks, S. D. (2010)

Open Access SHORT REPORT

Zhang, M., Larsen, L. S. Z., Irwin, B., Bilanchone, V., & Sandmeyer, S. B. (2010)

Identification of Novel Determinants of HIV-1 Uncoating in the Capsid Protein

Yang, R. (2009)

Faculty Opinions recommendation of Atomic-level modelling of the HIV capsid.

Columbus, L. M., & Dewald, A. H. (2011) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.8136959.10321054

Control of Viral Infectivity by Tripartite Motif Proteins

Towers, G. J. (2005) · Human Gene Therapy · doi:10.1089/hum.2005.16.ft-113

Faculty Opinions recommendation of Visualization of a missing link in retrovirus capsid assembly.

Conway, J. F. (2009) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1148048.605159

Monitor – biology

Spitzer, E. D., Collin, M., Noble, C. G., Zielinski, D., Henkel, T., Olivares-Reyes, J. A., Morquecho‐León, M. A., Barnes, M., & Miller, D. J. (2004) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03190-3

Rôle de la protéine kinase dépendante de l'AMPc (PKA) dans les étapes précoces du cycle réplicatif du VIH-1

Giroud, C. (2012) · theses.fr (ABES) · doi:10.70675/dcb13f1azfc90z47d6zb978z456e9b4d70d5

Interactions between primate lentiviral capsids and heterologous cellular host factors

Mamede, J. I. (2012) · theses.fr (ABES) · doi:10.70675/e3f4366bzb31fz4382z8f0cz19483f12bfe7

Etude du rétrotransposon SD' du rétrovirus leucémogène MLV

Akkawi, C. (2020) · theses.fr (ABES) · doi:10.70675/440d4c40zccb9z40b9z9038z0589be90e16d

Structure of B-MLV Capsid Amino-terminal Domain Reveals Key Features of Viral Tropism, Gag Assembly and Core Formation

Mortuza, G. B., Dodding, M. P., Goldstone, D. C., Haire, L. F., Stoye, J. P., & Taylor, I. A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.12.043 · Cited by 56

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

Structure and architecture of immature and mature murine leukemia virus capsids

Qu, K., Glass, B., Doležal, M., Schur, F. K. M., Murciano, B., Rein, A. R., Rumlová, M., Ruml, T., Kräusslich, H., & Briggs, J. A. G. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1811580115 · Cited by 98

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

Bharat, T. A. M., Davey, N. E., Ulbrich, P., Riches, J. D., de Marco, A., Rumlova, M., Sachse, C., Ruml, T., & Briggs, J. A. G. (2012) · Nature · doi:10.1038/nature11169 · Cited by 171

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