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  1. Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly
  2. Potential Role for CA-SP in Nucleating Retroviral Capsid Maturation
  3. A Two-Pronged Structural Analysis of Retroviral Maturation Indicates that Core Formation Proceeds by a Disassembly-Reassembly Pathway Rather than a Displacive Transition
  4. Lethal mutations in the major homology region and their suppressors act by modulating the dimerization of the rous sarcoma virus capsid protein C‐terminal domain
  5. Retrovirus Capsid Assembly and Polymorphism Studied by Cryo-EM and Cryo-ET
  6. Suppression of a Morphogenic Mutant in Rous Sarcoma Virus Capsid Protein by a Second-Site Mutation: a Cryoelectron Tomography Study
  7. Retroviral Capsid Assembly: A Role for the CA Dimer in Initiation
  8. Visualization of a missing link in retrovirus capsid assembly
  9. Cooperative role of the MHR and the CA dimerization helix in the maturation of the functional retrovirus capsid
  10. Critical Role of Conserved Hydrophobic Residues within the Major Homology Region in Mature Retroviral Capsid Assembly
  11. RSV Capsid Polymorphism Correlates with Polymerization Efficiency and Envelope Glycoprotein Content: Implications that Nucleation Controls Morphogenesis
  12. Second-Site Suppressors of Rous Sarcoma Virus CA Mutations: Evidence for Interdomain Interactions
  13. Form, function, and use of retroviral Gag proteins