Neutralizing antibody responses to an HIV envelope glycan hole are not easily broadened
暂无分享,去创建一个
D. Burton | I. Wilson | H. Turner | A. Ward | R. Sanders | M. V. van Gils | C. Cottrell | M. Yuan | G. Ozorowski | M. Pauthner | Y. Yang | R. Andrabi | L. McCoy | Terrence Messmer | J. Voss | T. M. Polveroni | T. Polveroni
[1] R. Wyatt,et al. The HIV-1 Envelope Glycoprotein C3/V4 Region Defines a Prevalent Neutralization Epitope following Immunization , 2019, Cell reports.
[2] D. Burton. Advancing an HIV vaccine; advancing vaccinology , 2018, Nature Reviews Immunology.
[3] Bette Korber,et al. Completeness of HIV-1 Envelope Glycan Shield at Transmission Determines Neutralization Breadth , 2018, Cell reports.
[4] D. Burton,et al. Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited during HIV-1 BG505 Envelope Trimer Immunization , 2018, Immunity.
[5] B. Pulendran,et al. Epitopes for neutralizing antibodies induced by HIV-1 envelope glycoprotein BG505 SOSIP trimers in rabbits and macaques , 2018, PLoS pathogens.
[6] D. Agard,et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.
[7] David J. Fleet,et al. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.
[8] Mehran Kardar,et al. Optimal immunization cocktails can promote induction of broadly neutralizing Abs against highly mutable pathogens , 2016, Proceedings of the National Academy of Sciences.
[9] John P. Moore,et al. Sequential and Simultaneous Immunization of Rabbits with HIV-1 Envelope Glycoprotein SOSIP.664 Trimers from Clades A, B and C , 2016, PLoS pathogens.
[10] Bryan Briney,et al. Holes in the Glycan Shield of the Native HIV Envelope Are a Target of Trimer-Elicited Neutralizing Antibodies. , 2016, Cell reports.
[11] Dennis R Burton,et al. Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design. , 2016, Annual review of immunology.
[12] Frank DiMaio,et al. Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta , 2016, bioRxiv.
[13] Kai Zhang,et al. Gctf: Real-time CTF determination and correction , 2015, bioRxiv.
[14] John R Mascola,et al. Antibody responses to envelope glycoproteins in HIV-1 infection , 2015, Nature Immunology.
[15] Nathaniel Echols,et al. EMRinger: Side-chain-directed model and map validation for 3D Electron Cryomicroscopy , 2015, Nature Methods.
[16] John P. Moore,et al. A Native-Like SOSIP.664 Trimer Based on an HIV-1 Subtype B env Gene , 2015, Journal of Virology.
[17] John P. Moore,et al. Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex , 2014, Proceedings of the National Academy of Sciences.
[18] Anders Larsson,et al. AliView: a fast and lightweight alignment viewer and editor for large datasets , 2014, Bioinform..
[19] James C Paulson,et al. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. , 2014, Immunity.
[20] Wayne C Koff,et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. , 2014, Immunity.
[21] Adam Godzik,et al. bNAber: database of broadly neutralizing HIV antibodies , 2013, Nucleic Acids Res..
[22] Brian D. Weitzner,et al. Serverification of Molecular Modeling Applications: The Rosetta Online Server That Includes Everyone (ROSIE) , 2013, PloS one.
[23] Vincent B. Chen,et al. Correspondence e-mail: , 2000 .
[24] Christopher Irving,et al. Appion: an integrated, database-driven pipeline to facilitate EM image processing. , 2009, Journal of structural biology.
[25] J. Binley,et al. Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1 , 2006, Journal of Virology.
[26] Xiping Wei,et al. Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies , 2005, Journal of Virology.
[27] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[28] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[29] D. Burton,et al. Heterogeneity of Envelope Molecules Expressed on Primary Human Immunodeficiency Virus Type 1 Particles as Probed by the Binding of Neutralizing and Nonneutralizing Antibodies , 2003, Journal of Virology.
[30] John P. Moore,et al. Stabilization of the Soluble, Cleaved, Trimeric Form of the Envelope Glycoprotein Complex of Human Immunodeficiency Virus Type 1 , 2002, Journal of Virology.
[31] Min Lu,et al. Oligomeric and Conformational Properties of a Proteolytically Mature, Disulfide-Stabilized Human Immunodeficiency Virus Type 1 gp140 Envelope Glycoprotein , 2002, Journal of Virology.
[32] J Pulokas,et al. Leginon: an automated system for acquisition of images from vitreous ice specimens. , 2000, Journal of structural biology.