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Quantitative Correlation between Infectivity and Gp120 Density on HIV-1 Virions Revealed by Optical Trapping Virometry

DeSantis, M. C., Kim, J. H., Song, H., Klasse, P. J., & Cheng, W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.729210 · Cited by 36 · see citing works

Subtle alteration of residues including N-linked glycans in V2 loop modulate HIV-1 neutralization by PG9 and PG16 monoclonal antibodies

Ringe, R. P., Phogat, S. K., & Bhattacharya, J. (2012) · Virology · doi:10.1016/j.virol.2012.01.011 · Cited by 35 · see citing works

Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection

Raška, M., Czerneková, L., Moldoveanu, Z., Zachová, K., Elliott, M. C., Novák, Z., Hall, S. D., Höelscher, M., Maboko, L., Brown, R., et al. (2014) · AIDS Research and Therapy · doi:10.1186/1742-6405-11-23 · Cited by 35 · see citing works

Outer Domain of HIV-1 gp120: Antigenic Optimization, Structural Malleability, and Crystal Structure with Antibody VRC-PG04

Joyce, M. G., Kanekiyo, M., Xu, L., Biertümpfel, C., Boyington, J. C., Moquin, S. A., Shi, W., Wu, X., Yang, Y., Yang, Z., et al. (2012) · Journal of Virology · doi:10.1128/jvi.02717-12 · Cited by 35 · see citing works

Surfactant Protein D Inhibits HIV-1 Infection of Target Cells via Interference with gp120-CD4 Interaction and Modulates Pro-Inflammatory Cytokine Production

Pandit, H., Gopal, S., Sonawani, A., Yadav, A. K., Qaseem, A. S., Warke, H. S., Patil, A. D., Gajbhiye, R., Kulkarni, V., Al-Mozaini, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102395 · Cited by 34 · see citing works

The Current Landscape of mRNA Vaccines Against Viruses and Cancer–A Mini Review

Ladak, R. J., He, A. J., Huang, Y.-H., & Ding, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.885371 · Cited by 33 · see citing works

Single-Molecule FRET Imaging of Virus Spike–Host Interactions

Lu, M. (2021) · Viruses · doi:10.3390/v13020332 · Cited by 35 · see citing works

A Single Residue within the V5 Region of HIV-1 Envelope Facilitates Viral Escape from the Broadly Neutralizing Monoclonal Antibody VRC01

Guo, D., Shi, X., Arledge, K. C., Song, D., Jiang, L., Fu, L., Gong, X., Zhang, S., Wang, X., & Zhang, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.399402 · Cited by 31 · see citing works

Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site

Wibmer, C. K., Gorman, J., Anthony, C. S., Mkhize, N. N., Druz, A., York, T., Schmidt, S. D., Labuschagne, J. P. L., Louder, M. K., Bailer, R. T., et al. (2016) · Journal of Virology · doi:10.1128/jvi.01357-16 · Cited by 31 · see citing works

HIV-1 Envelope Glycoprotein Variable Loops Are Indispensable for Envelope Structural Integrity and Virus Entry

Yuan, T., Li, J., & Zhang, M.-Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069789 · Cited by 30 · see citing works

Susceptibility to Neutralization by Broadly Neutralizing Antibodies Generally Correlates with Infected Cell Binding for a Panel of Clade B HIV Reactivated from Latent Reservoirs

Ren, Y., Korom, M., Truong, R., Chan, D., Huang, S.-H., Kovacs, C. C., Benko, E., Safrit, J. T., Lee, J., Garbán, H., et al. (2018) · Journal of Virology · doi:10.1128/jvi.00895-18 · Cited by 30 · see citing works

Isolate-Specific Differences in the Conformational Dynamics and Antigenicity of HIV-1 gp120

Davenport, T. M., Guttman, M., Guo, W., Cleveland, B., Kahn, M., Hu, S.-L., & Lee, K. K. (2013) · Journal of Virology · doi:10.1128/jvi.01535-13 · Cited by 29 · see citing works

Broadly resistant HIV-1 against CD4-binding site neutralizing antibodies

Zhou, P.-P., Wang, H., Fang, M., Li, Y., Wang, H., Shi, S., Li, Z., Wu, J., Han, X., Shi, X., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007819 · Cited by 29 · see citing works

Neutralization Properties of Simian Immunodeficiency Viruses Infecting Chimpanzees and Gorillas

Barbian, H. J., Decker, J. M., Bibollet‐Ruche, F., Galimidi, R. P., West, A. P., Learn, G. H., Parrish, N. F., Iyer, S. S., Li, Y., Pace, C. S., et al. (2015) · mBio · doi:10.1128/mbio.00296-15 · Cited by 29 · see citing works

High-Resolution Longitudinal Study of HIV-1 Env Vaccine–Elicited B Cell Responses to the Virus Primary Receptor Binding Site Reveals Affinity Maturation and Clonal Persistence

Wang, Y., Sundling, C., Wilson, R., O'Dell, S. J., Chen, Y., Dai, K., Phad, G. E., Zhu, J., Xiao, Y., Mascola, J. R., et al. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1502543 · Cited by 28 · see citing works

Phage-DMS: A Comprehensive Method for Fine Mapping of Antibody Epitopes

Garrett, M. E., Itell, H. L., Crawford, K. H. D., Basom, R., Bloom, J. D., & Overbaugh, J. M. (2020) · iScience · doi:10.1016/j.isci.2020.101622 · Cited by 28 · see citing works

Mechanisms of HIV-1 subtype C resistance to GRFT, CV-N and SVN

Alexandre, K. B., Moore, P. L., Nonyane, M., Gray, E. S., Ranchobe, N., Chakauya, E., McMahon, J. B., O’Keefe, B. R., Chikwamba, R. K., & Morris, L. (2013) · Virology · doi:10.1016/j.virol.2013.07.019 · Cited by 28 · see citing works

Neutralizing Antibodies and Control of HIV: Moves and Countermoves

Hessell, A. J., & Haigwood, N. L. (2011) · Current HIV/AIDS Reports · doi:10.1007/s11904-011-0105-5 · Cited by 27 · see citing works

Broadly Neutralizing Antibodies against HIV: Back to Blood

Dashti, A., DeVico, A. L., Lewis, G. K., & Sajadi, M. M. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.01.007 · Cited by 27 · see citing works

Association of Enhanced HIV-1 Neutralization by a Single Y681H Substitution in gp41 with Increased gp120-CD4 Interaction and Macrophage Infectivity

Ringe, R. P., & Bhattacharya, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037157 · Cited by 27 · see citing works

Role of Human Immunodeficiency Virus Type 1 Envelope Structure in the Induction of Broadly Neutralizing Antibodies

Benjelloun, F., Lawrence, P., Verrier, B., Genin, C., & Paul, S. (2012) · Journal of Virology · doi:10.1128/jvi.01110-12 · Cited by 27 · see citing works

Sensitivity to Broadly Neutralizing Antibodies of Recently Transmitted HIV-1 Clade CRF02_AG Viruses with a Focus on Evolution over Time

Stéfic, K., Bouvin-Pley, M., Essat, A., Visdeloup, C., Moreau, A., Goujard, C., Chaix, M., Braibant, M., Meyer, L., & Barin, F. (2018) · Journal of Virology · doi:10.1128/jvi.01492-18 · Cited by 27 · see citing works

Characterization and Implementation of a Diverse Simian Immunodeficiency Virus SIVsm Envelope Panel in the Assessment of Neutralizing Antibody Breadth Elicited in Rhesus Macaques by Multimodal Vaccines Expressing the SIVmac239 Envelope

Kilgore, K. M., Murphy, M. K., Burton, S. L., Wetzel, K. S., Smith, S. A., Xiao, P., Reddy, S. M., Francella, N., Sodora, D. L., Silvestri, G., et al. (2015) · Journal of Virology · doi:10.1128/jvi.01221-14 · Cited by 26 · see citing works

Distinct HIV-1 entry phenotypes are associated with transmission, subtype specificity, and resistance to broadly neutralizing antibodies

Chikere, K., Webb, N. E., Chou, T., Borm, K., Sterjovski, J., Gorry, P. R., & Lee, B. (2014) · Retrovirology · doi:10.1186/1742-4690-11-48 · Cited by 26 · see citing works

Antigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers

Arnold, P., Himmels, P., Weiß, S., Decker, T.-M., Markl, J., Gatterdam, V., Tampé, R., Bartholomäus, P., Dietrich, U., & Duerr, R. (2014) · Retrovirology · doi:10.1186/1742-4690-11-42 · Cited by 26 · see citing works

Rectal tissue and vaginal tissue from intravenous VRC01 recipients show protection against ex vivo HIV-1 challenge

Astronomo, R. D., Lemos, M. P., Narpala, S., Czartoski, J., Ballweber-Fleming, L., Seaton, K. E., Prabhakaran, M. S., Huang, Y., Lu, Y., Westerberg, K., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci146975 · Cited by 25 · see citing works

Uses and Challenges of Antiviral Polyclonal and Monoclonal Antibody Therapies

Struble, E. B., Rawson, J. M. O., Stantchev, T. S., Scott, D., & Shapiro, M. A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15051538 · Cited by 25 · see citing works

SEE PROFILE

Zhou, T., Xu, L., Yang, Y., & Nussenzweig, M. C. (2016)

Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01

Zhou, T., Georgiev, I. S., Wu, X., Yang, Z., Dai, K., Finzi, A., Kwon, Y. D., Scheid, J. F., Shi, W., Xu, L., et al. (2010) · Science · doi:10.1126/science.1192819 · Cited by 1,132 · see citing works

Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1

Wu, X.-L., Yang, Z.-Y., Li, Y.-X., Hogerkorp, C.-M., Schief, W., Seaman, M., Zhou, T., Schmidt, S., Wu, L., Xu, L., et al. (2010) · Science · doi:10.1126/science.1187659 · Cited by 1,878 · see citing works

P09-05. Mechanism of HIV-1 resistance to a monoclonal antibody that effectively targets the site of CD4 attachment

Wu, X., Zhou, T., O'Dell, S. J., Wyatt, R. T., Kwong, P. D., & Mascola, J. (2009) · Retrovirology · doi:10.1186/1742-4690-6-s3-p118

Mechanism of Human Immunodeficiency Virus Type 1 Resistance to Monoclonal Antibody b12 That Effectively Targets the Site of CD4 Attachment

Wu, X., Zhou, T., O'Dell, S. J., Wyatt, R. T., Kwong, P. D., & Mascola, J. R. (2009) · Journal of Virology · doi:10.1128/jvi.01142-09 · Cited by 95 · see citing works