D. Kampjut and L. A. Sazanov, “Structure and mechanism of mitochondrial proton-translocating transhydrogenase,” Nature, vol. 573, no. 7773. Springer Nature, pp. 291–295, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/6848
DOI: 10.1038/s41586-019-1519-2
WoS: 000485415400061
PMID: 31462775

K. Fiedorczuk and L. A. Sazanov, “Mammalian mitochondrial complex I structure and disease causing mutations,” Trends in Cell Biology, vol. 28, no. 10. Elsevier, pp. 835–867, 2018.
LibreCat: https://research-explorer.ista.ac.at/record/152
DOI: 10.1016/j.tcb.2018.06.006
WoS: 000445118200007

L. A. Sazanov, “Structure of respiratory complex I: ‘Minimal’ bacterial and ‘de luxe’ mammalian versions,” in Mechanisms of primary energy transduction in biology , M. Wikström, Ed. Royal Society of Chemistry, 2017, pp. 25–59.
LibreCat: https://research-explorer.ista.ac.at/record/444
DOI: 10.1039/9781788010405-00025

J. A. Letts and L. A. Sazanov, “Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain,” Nature Structural and Molecular Biology, vol. 24, no. 10. Nature Publishing Group, pp. 800–808, 2017.
LibreCat: https://research-explorer.ista.ac.at/record/515
DOI: 10.1038/nsmb.3460

J. Gutierrez-Fernandez et al., “Modular architecture and unique teichoic acid recognition features of choline-binding protein L CbpL contributing to pneumococcal pathogenesis,” Scientific Reports, vol. 6. Nature Publishing Group, 2016.
LibreCat: https://research-explorer.ista.ac.at/record/1186
DOI: 10.1038/srep38094

J. A. Letts, G. Degliesposti, K. Fiedorczuk, M. Skehel, and L. A. Sazanov, “Purification of ovine respiratory complex i results in a highly active and stable preparation,” Journal of Biological Chemistry, vol. 291, no. 47. American Society for Biochemistry and Molecular Biology, pp. 24657–24675, 2016.
LibreCat: https://research-explorer.ista.ac.at/record/1209
DOI: 10.1074/jbc.M116.735142

K. Fiedorczuk, J. A. Letts, G. Degliesposti, K. Kaszuba, M. Skehel, and L. A. Sazanov, “Atomic structure of the entire mammalian mitochondrial complex i,” Nature, vol. 538, no. 7625. Nature Publishing Group, pp. 406–410, 2016.
LibreCat: https://research-explorer.ista.ac.at/record/1226
DOI: 10.1038/nature19794
PMID: 27595392

J. A. Letts, K. Fiedorczuk, and L. A. Sazanov, “The architecture of respiratory supercomplexes,” Nature, vol. 537, no. 7622. Nature Publishing Group, pp. 644–648, 2016.
LibreCat: https://research-explorer.ista.ac.at/record/1232
DOI: 10.1038/nature19774

P. Postila et al., “Atomistic determinants of co-enzyme Q reduction at the Qi-site of the cytochrome b complex,” Scientific Reports, vol. 6. Nature Publishing Group, 2016.
LibreCat: https://research-explorer.ista.ac.at/record/1276
DOI: 10.1038/srep33607

P. Holt, R. Efremov, E. Nakamaru Ogiso, and L. A. Sazanov, “Reversible FMN dissociation from Escherichia coli respiratory complex I,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1857, no. 11. Elsevier, pp. 1777–1785, 2016.
LibreCat: https://research-explorer.ista.ac.at/record/1288
DOI: 10.1016/j.bbabio.2016.08.008

J. Berrisford, R. Baradaran, and L. A. Sazanov, “Structure of bacterial respiratory complex I,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1857, no. 7. Elsevier, pp. 892–901, 2016.
LibreCat: https://research-explorer.ista.ac.at/record/1521
DOI: 10.1016/j.bbabio.2016.01.012

L. A. Sazanov, “A giant molecular proton pump: structure and mechanism of respiratory complex I,” Nature Reviews Molecular Cell Biology, vol. 16, no. 6. Nature Publishing Group, pp. 375–388, 2015.
LibreCat: https://research-explorer.ista.ac.at/record/1638
DOI: 10.1038/nrm3997

J. A. Letts and L. A. Sazanov, “Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions,” Current Opinion in Structural Biology, vol. 33, no. 8. Elsevier, pp. 135–145, 2015.
LibreCat: https://research-explorer.ista.ac.at/record/1683
DOI: 10.1016/j.sbi.2015.08.008