The antigenic structure of the HIV gp120 envelope glycoprotein
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DOI: 10.1038/31514
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Cited by:
- Durgadevi Parthasarathy & Karunakar Reddy Pothula & Sneha Ratnapriya & Héctor Cervera Benet & Ruth Parsons & Xiao Huang & Salam Sammour & Katarzyna Janowska & Miranda Harris & Joseph Sodroski & Priyam, 2024. "Conformational flexibility of HIV-1 envelope glycoproteins modulates transmitted/founder sensitivity to broadly neutralizing antibodies," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
- Swetha Garimalla & Thomas Kieber-Emmons & Anastas D Pashov, 2015. "The Patterns of Coevolution in Clade B HIV Envelope's N-Glycosylation Sites," PLOS ONE, Public Library of Science, vol. 10(6), pages 1-18, June.
- Dongxiao Han & Liuquan Sun & Yanqing Sun & Li Qi, 2017. "Mark-specific additive hazards regression with continuous marks," Lifetime Data Analysis: An International Journal Devoted to Statistical Methods and Applications for Time-to-Event Data, Springer, vol. 23(3), pages 467-494, July.
- Shixia Wang & Kun-Wei Chan & Danlan Wei & Xiuwen Ma & Shuying Liu & Guangnan Hu & Saeyoung Park & Ruimin Pan & Ying Gu & Alexandra F. Nazzari & Adam S. Olia & Kai Xu & Bob C. Lin & Mark K. Louder & Kr, 2024. "Human CD4-binding site antibody elicited by polyvalent DNA prime-protein boost vaccine neutralizes cross-clade tier-2-HIV strains," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
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