Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475

Tissue sulfhydryl groups

Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824

PROCHECK: a program to check the stereochemical quality of protein structures

Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

Schägger, H., & von Jagow, G. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90587-2 · Cited by 11,420

Solvent content of protein crystals

Matthews, B. W. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90205-2 · Cited by 7,970

[6] Use of T7 RNA polymerase to direct expression of cloned genes

Studier, F. W., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562

Calculation of protein extinction coefficients from amino acid sequence data.

Gill, S., & von Hippel, P. H. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90602-7 · Cited by 5,382

AMoRe: an automated package for molecular replacement

Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877

Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc

Hallin, E. I., Markússon, S., Böttger, L., Torda, A. E., Bramham, C. R., & Kursula, P. (2021) · PLoS ONE · doi:10.1371/journal.pone.0251459 · Cited by 6

Lethal mutations in the major homology region and their suppressors act by modulating the dimerization of the rous sarcoma virus capsid protein C‐terminal domain

Dalessio, P. M., Craven, R. C., Lokhandwala, P. M., & Ropson, I. J. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24188 · Cited by 5

The isolated major homology region of the HIV capsid protein is mainly unfolded in solution and binds to the intact protein

Doménech, R., Bocanegra, R., Velázquez‐Campoy, A., & Neira, J. L. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.011 · Cited by 4

Escherichia coli LysU is a potential surrogate for human lysyl tRNA synthetase in interactions with the C-terminal domain of HIV-1 capsid protein

Boonyalai, N., Pullen, J., Abdul‐Wahab, M. F., Wright, M., & Miller, A. D. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob26499d · Cited by 4

Application of Nuclear Magnetic Resonance and Hybrid Methods to Structure Determination of Complex Systems

Prischi, F., & Pastore, A. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-27216-0_22 · Cited by 5

Larger Helical Populations in Peptides Derived from the Dimerization Helix of the Capsid Protein of HIV-1 Results in Peptide Binding toward Regions Other than the “Hotspot” Interface

Doménech, R., Bocanegra, R., González‐Muñiz, R., Gómez, J., Mateu, M. G., & Neira, J. L. (2011) · Biomacromolecules · doi:10.1021/bm2007168 · Cited by 4

3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins

Liu, L., & Gronenborn, A. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374920-8.00309-x · Cited by 3

Crowding, molecular volume and plasticity: An assessment involving crystallography, NMR and simulations

Selvaraj, M., Ahmad, R., Varshney, U., & Vijayan, M. (2012) · Journal of Biosciences · doi:10.1007/s12038-012-9276-5 · Cited by 3

CryoEM Analysis of Capsid Assembly and Structural Changes Upon Interactions with a Host Restriction Factor, TRIM5α

Zhao, G., & Zhang, P. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-670-2_2 · Cited by 4

Parameter Optimization for Interaction between C-Terminal Domains of HIV-1 Capsid Protein

Sha, H., & Zhu, F. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00011 · Cited by 4

Maturation inhibitors facilitate virus assembly and release of HIV-1 capsid P224 mutant

Timilsina, U., Ghimire, D., Adhikari, L. P., Bhattarai, A., Mishra, N., Rai, M., Dubey, R. C., & Gaur, R. (2018) · Virology · doi:10.1016/j.virol.2018.05.024 · Cited by 2

Magic angle spinning NMR spectroscopy guided atomistic characterization of structure and dynamics in HIV-1 protein assemblies

Gupta, R., & Polenova, T. E. (2017) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2017.12.005 · Cited by 1

Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila ArcPreprint

Hallin, E. I., Markússon, S., Böttger, L., Torda, A. E., Bramham, C. R., & Kursula, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.18.388496 · Cited by 2

Discovery and Development of New HIV Medicines

Garvey, E. P., Romines, K. R., & Boone, L. R. (2004) · Elsevier eBooks · doi:10.1016/b978-012764051-8/50034-2 · Cited by 1

Lego-Like Strategy for Assembling Multivalent Peptide-Based Vehicles Able to Deliver Molecular Cargoes into Cells

Langel, U. (2006) · CRC Press eBooks · doi:10.1201/9781420006087-27 · Cited by 1

Virus Assembly as a Target for Antiretroviral Therapy

Barklis, E. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7729-7_8 · Cited by 1

Conserved cysteines in Mason–Pfizer monkey virus capsid protein are essential for infectious mature particle formation

Píchalová, R., Füzik, T., Vokatá, B., Rumlová, M., Llano, M., Dostálková, A., Křížová, I., Ruml, T., & Ulbrich, P. (2018) · Virology · doi:10.1016/j.virol.2018.06.001 · Cited by 1

Conserved serines in simian immunodeficiency virus capsid are required for virus budding

Rue, S. M., Roos, J. W., Clements, J. E., & Barber, S. A. (2005) · Virology · doi:10.1016/j.virol.2005.03.006 · 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 on HIV-1 core assembly

Abdurahman, S. (2007) · Figshare

Noncanonical functions of lysyl-tRNA synthethase in HIV-1 packaging

Boonyalai, N. (2011) · NRCT Data Center · doi:10.14456/tjg.2011.9

Role of Mitochondria in HIV Infection

Lu, G. (2013)

The effect of alpha-HGA on HIV-1 replication

Youssefi, M. (2009) · Figshare

Predicting Bevirimat resistance of HIV-1 from

Heider, D., Verheyen, J., & Hoffmann, D. E. (2010)

Prediction of host-virus interaction networks

Doolittle‐Hall, J. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/mapt-1895

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

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

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

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

Informatically-informed biochemical characterization of aptamer-protein complexes

Gruenke, P. R. (2022) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/91663

Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding

Wapling, J., Srivastava, S., Shehu-Xhilaga, M., & Tachedjian, G. (2007) · Drug Target Insights · doi:10.33393/dti.2007.1318

Disulfide Crosslinking Induces Rapid Degradation of Arc/Arg3.1 via Hsp70‐Mediated Ubiquitin Ligase Pathway

So, D., Song, I.-K., Kim, Y. J., Lee, Y. P., Park, Y. S., Kim, H., Lee, K.-J., & Song, E. J. (2026) · The FASEB Journal · doi:10.1096/fj.202502555r · Cited by 1

Etude des mécanismes contrôlant la spécificité d'encapsidation des ARN dans le VIH-1

Didierlaurent, L. (2010) · theses.fr (ABES) · doi:10.70675/6af45cb6z95b9z414cz94fbzdcd9c17fde4a

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

Implication de la machinerie des microRNA dans la réplication rétrovirale

Bouttier, M. (2011) · theses.fr (ABES) · doi:10.70675/7705ed5cz61a8z4e90z8edfz5de46a1563ed

Etude de la nano-organisation dynamique de la protéine Gag du VIH-1 à la membrane plasmique des Lymphocytes T CD4+ au cours de l'assemblage viral

Floderer, C. (2016) · theses.fr (ABES) · doi:10.70675/e910410az165fz4e84z897ezb80869a4a592

Mechanisms of HIV-1 assembly, release and maturation

Kleinpeter, A. B., & Freed, E. O. (2026) · Nature Reviews Microbiology · doi:10.1038/s41579-026-01327-6 · Cited by 2

Mechanism of HIV-1 capsid rupture and uncoating by reverse transcription

Ghosh, K., Gupta, M., & Voth, G. A. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2617714123 · Cited by 2

BindingDB Entry 5770: Novel Inhibitor Binding Site Discovery on HIV-1 Capsid N-Terminal Domain by NMR and X-ray Crystallography.

BindingDB (2013) · UC San Diego · doi:10.7270/q2w094jx

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

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

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

A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface

Lampel, A., Yaniv, O., Berger, O., Bacharach, E., Gazit, E., & Frolow, F. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309113011871 · Cited by 9

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