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Molecular Immunology|August 9, 2006
Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopesStephanie Carmicle, N Kalaya Steede, Samuel J LandryThe Journal of Biological Chemistry|October 17, 2001
Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10. Role of disordered loopsGuixiang Dai, Stephanie Carmicle, N Kalaya Steede, et al.The Journal of Biological Chemistry|October 24, 2001
Proteolytic sensitivity and helper T-cell epitope immunodominance associated with the mobile loop in Hsp10sStephanie Carmicle, Guixiang Dai, N Kalaya Steede, et al.Journal of Virology|January 22, 2010
Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120Denise Mirano-Bascos, N Kalaya Steede, James E Robinson, et al.Vaccine|May 7, 2015
Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120Hong-Nam P Nguyen, N Kalaya Steede, James E Robinson, et al.Plos One|June 19, 2013
Shaping T cell - B cell collaboration in the response to human immunodeficiency virus type 1 envelope glycoprotein gp120 by peptide primingN Kalaya Steede, Blake J Rust, Mohammad M Hossain, et al.Journal of Virology|June 13, 2014
Comprehensive analysis of contributions from protein conformational stability and major histocompatibility complex class II-peptide binding affinity to CD4+ epitope immunogenicity in HIV-1 envelope glycoproteinTingfeng Li, N Kalaya Steede, Hong-Nam P Nguyen, et al.Frontiers in Immunology|August 4, 2026
Conformational bias in SARS-CoV-2 Spike CD4+ T-cell epitope dominanceSamuel J Landry, N Kalaya Steede, Yali Tiomkin, et al.Pageof 1