@misc{d'angelo_astro_de luise_kurelac_umesh-ganesh_ding_fearnley_zeviani_gasparre_porcelli_et al._2020, 
  title={Biogenesis of NDUFS3-less complex I indicates TMEM126A/OPA7 as an assembly factor of the ND4-module}, 
  DOI={10.1101/2020.10.22.350587}, 
  abstractNote={<jats:p>Complex I (CI) is the largest enzyme of the mitochondrial respiratory chain and its defects constitute the principal cause of mitochondrial disease. To understand the mechanisms regulating the extremely intricate biogenesis of this fundamental bioenergetic machine, we dissected the structural and functional consequences of the depletion of NDUFS3, a non-catalytic core subunit. We prove that in diverse cell contexts a small, but still detectable, proportion of functional CI can still be found in the absence of NDUFS3. In addition, we have determined the dynamics of disassembly of CI when the amounts of NDUFS3 are gradually decreased. The process of degradation of the complex occurs in a hierarchical and modular fashion where the ND4-module remains stable and bound to TMEM126A. We have thus, uncovered the function of TMEM126A, the product of a disease gene causing optic atrophy, as a factor necessary for the correct assembly and function of CI.</jats:p>}, 
  publisher={Cold Spring Harbor Laboratory}, 
  author={D'Angelo, Luigi and Astro, Elisa and De Luise, Monica and Kurelac, Ivana and Umesh-Ganesh, Nikkitha and Ding, Shujing and Fearnley, Ian M. and Zeviani, Massimo and Gasparre, Giuseppe and Porcelli, Anna Maria and et al.}, 
  year={2020}, 
  month={Oct}
  }