Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus
By J. McLellan, Man Chen, M. Joyce, M. Sastry, Guillaume B. E. Stewart-Jones, Yongping Yang, Baoshan Zhang, Lei Chen, S. Srivatsan, A. Zheng and 18 more. 2013
989 citations recorded by the source corpus.
Subfields: Epidemiology, Immunology
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Citations in the corpus
- New Vaccine Design and Delivery Technologies (2019, background): “Common strategies include designing disulfide bonds to immobilize linked domains [28] [29] [30] [31] [32] , improved hydrophobic packing to stabilize a particular conformational state [22, 33] , proline mutations to constrain conformational flexibility, and proline/glycine mutations to discourage he”
- HIV-1 envelope trimer fusion proteins and their applications (2016, positive): “Experimental protein vaccines, some which are considered for clinical trials, also exploit IZ and/or Fd and include the spike proteins of human immunodeficiency virus (HIV-1) [11–20], respiratory syncytial virus [21,22] and influenza virus [4,23–28].”
- Influence of Respiratory Syncytial Virus F Glycoprotein Conformation on Induction of Protective Immune Responses (2016, background): “Since it is known that even stabilized prefusion F is less thermostable (30) in vitro than postfusion F (42), it is possible that the former is degraded more rapidly, once inoculated into mice, than other forms of the protein and favors the generation of nonneutralizing antibodies that can bind to p”