@article{17884,
  abstract     = {Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron tomography studies of HTLV-1 virus-like particles assembled in vitro, as well as derived from cells. This work shows that HTLV-1 uses a distinct mechanism of Gag–Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature capsid (CA) tubular arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal domain of CA. Mutagenesis analysis supports this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the C-terminal domain of CA. These results provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain why HTLV-1 particles are morphologically distinct.},
  author       = {Obr, Martin and Percipalle, Mathias and Chernikova, Darya and Yang, Huixin and Thader, Andreas and Pinke, Gergely and Porley, Dario J and Mansky, Louis M. and Dick, Robert A. and Schur, Florian KM},
  issn         = {1545-9985},
  journal      = {Nature Structural & Molecular Biology},
  pages        = {268--276},
  publisher    = {Springer Nature},
  title        = {{Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice}},
  doi          = {10.1038/s41594-024-01390-8},
  volume       = {32},
  year         = {2025},
}

@article{8581,
  abstract     = {The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the ‘proton translocation cluster’ attached to the c-ring and a more distant ‘hook apparatus’ holding subunit e. Unexpectedly, this subunit is anchored to a lipid ‘plug’ capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine.},
  author       = {Pinke, Gergely and Zhou, Long and Sazanov, Leonid A},
  issn         = {1545-9985},
  journal      = {Nature Structural and Molecular Biology},
  number       = {11},
  pages        = {1077--1085},
  publisher    = {Springer Nature},
  title        = {{Cryo-EM structure of the entire mammalian F-type ATP synthase}},
  doi          = {10.1038/s41594-020-0503-8},
  volume       = {27},
  year         = {2020},
}