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CRISPR/Cas9 gene editing for the creation of an MGAT1-deficient CHO cell line to control HIV-1 vaccine glycosylation

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HIV-1-Specific IgA Monoclonal Antibodies from an HIV-1 Vaccinee Mediate Galactosylceramide Blocking and Phagocytosis

Wills, S., Hwang, K.-K., Liu, P., Dennison, S. M., Tay, M. Z., Shen, X., Pollara, J., Lucas, J. T., Parks, R., Rerks‐Ngarm, S., et al. (2018) · Journal of Virology · doi:10.1128/jvi.01552-17 · Cited by 41

Increased vaccine tolerability and protection via NF-κB modulation

Moser, B., Steinhardt, R. C., Escalante-Buendia, Y., Boltz, D. A., Barker, K., Cassaidy, B., Rosenberger, M. G., Yoo, S., McGonnigal, B., & Esser-Kahn, A. P. (2020) · Science Advances · doi:10.1126/sciadv.aaz8700 · Cited by 43

Human Ig knockin mice to study the development and regulation of HIV ‐1 broadly neutralizing antibodies

Verkoczy, L. K., Alt, F. W., & Tian, M. (2017) · Immunological Reviews · doi:10.1111/imr.12505 · Cited by 39

Prediction of VRC01 neutralization sensitivity by HIV-1 gp160 sequence features

Magaret, C. A., Benkeser, D. C., Williamson, B. D., Borate, B. R., Carpp, L. N., Georgiev, I. S., Setliff, I., Dingens, A. S., Simon, N., Carone, M., et al. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006952 · Cited by 39

Characterization of a Discontinuous Neutralizing Epitope on Glycoprotein B of Human Cytomegalovirus

Spindler, N., Rücker, P., Pötzsch, S., Diestel, U., Sticht, H., Martín-Parras, L., Winkler, T., & Mach, M. (2013) · Journal of Virology · doi:10.1128/jvi.00434-13 · Cited by 38

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 39

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

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

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

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

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 35

Single-Molecule FRET Imaging of Virus Spike–Host Interactions

Lu, M. (2021) · Viruses · doi:10.3390/v13020332 · Cited by 38

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

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

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

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

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 33

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

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 31

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

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

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., & Morris, L. (2013) · Virology · doi:10.1016/j.virol.2013.07.019 · Cited by 28

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

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 26

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 26

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

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

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

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

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 27

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

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 27

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 1,123

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

Wu, X., Yang, Z., Li, Y., Högerkorp, C., Schief, W. R., Seaman, M. S., Zhou, T., Schmidt, S. D., Wu, L., Xu, L., et al. (2010) · Science · doi:10.1126/science.1187659 · Cited by 1,724

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 94