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Vercellino, I., &; Sazanov, L. A. (2022). The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. Springer Nature.https://doi.org/10.1038/s41580-021-00415-0 

Kampjut, D., &; Sazanov, L. A. (2022). Structure of respiratory complex I – An emerging blueprint for the mechanism. Current Opinion in Structural Biology. Elsevier.https://doi.org/10.1016/j.sbi.2022.102350 

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Kravchuk, V., Petrova, O., Kampjut, D., Wojciechowska-Bason, A., Breese, Z., &; Sazanov, L. A. (2022). A universal coupling mechanism of respiratory complex I. Nature. Springer Nature.https://doi.org/10.1038/s41586-022-05199-7 

Abas, L., Kolb, M., Stadlmann, J., Janacek, D. P., Lukic, K., Schwechheimer, C.,https://doi.org/10.1073/pnas.2020857118__Hammes, U. Z. (2021). Naphthylphthalamic acid associates with and inhibits PIN auxin transporters. PNAS. National Academy of Sciences.https://doi.org/10.1073/pnas.2020857118 

Kampjut, D., Steiner, J., &; Sazanov, L. A. (2021). Cryo-EM grid optimization for membrane proteins. IScience. Elsevier.https://doi.org/10.1016/j.isci.2021.102139 

Vercellino, I., &; Sazanov, L. A. (2021). Structure and assembly of the mammalian mitochondrial supercomplex CIII<sub>2</sub>CIV. Nature. Springer Nature.https://doi.org/10.1038/s41586-021-03927-z 

Adjobo-Hermans, M. J. W., De Haas, R., Willems, P. H. G. M., Wojtala, A., Van Emst-De Vries, S. E., Wagenaars, J. A.,https://doi.org/10.1016/j.bbabio.2020.148213__Koopman, W. J. H. (2020). NDUF deletion triggers loss of NDUF in Nduf/ mice and Leigh syndrome patients: A stabilizing role for NDUFA. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/j.bbabio.2020.148213 

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Gutierrez-Fernandez, J., Kaszuba, K., Minhas, G. S., Baradaran, R., Tambalo, M., Gallagher, D. T., &; Sazanov, L. A. (2020). Key role of quinone in the mechanism of respiratory complex I. Nature Communications. Springer Nature.https://doi.org/10.1038/s41467-020-17957-0 

Pinke, G., Zhou, L., &; Sazanov, L. A. (2020). Cryo-EM structure of the entire mammalian F-type ATP synthase. Nature Structural and Molecular Biology. Springer Nature.https://doi.org/10.1038/s41594-020-0503-8 

Kampjut, D., &; Sazanov, L. A. (2020). The coupling mechanism of mammalian respiratory complex I. Science. American Association for the Advancement of Science.https://doi.org/10.1126/science.abc4209 

Steiner, J., &; Sazanov, L. A. (2020). Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter. ELife. eLife Sciences Publications.https://doi.org/10.7554/eLife.59407 

Zhou, L., &; Sazanov, L. A. (2019). Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science. AAAS.https://doi.org/10.1126/science.aaw9144 

Letts, J. A., Fiedorczuk, K., Degliesposti, G., Skehel, M., &; Sazanov, L. A. (2019). Structures of respiratory supercomplex I+II reveal functional and conformational crosstalk. Molecular Cell. Cell Press.https://doi.org/10.1016/j.molcel.2019.07.022 

Kampjut, D., &; Sazanov, L. A. (2019). Structure and mechanism of mitochondrial proton-translocating transhydrogenase. Nature. Springer Nature.https://doi.org/10.1038/s41586-019-1519-2 

Fiedorczuk, K., &; Sazanov, L. A. (2018). Mammalian mitochondrial complex I structure and disease causing mutations. Trends in Cell Biology. Elsevier.https://doi.org/10.1016/j.tcb.2018.06.006 

Hardie, R., Van Dam, E., Cowley, M., Han, T., Balaban, S., Pajic, M.,https://doi.org/10.1186/s40170-017-0164-1__Saunders, D. (2017). Mitochondrial mutations and metabolic adaptation in pancreatic cancer. Cancer &; Metabolism. BioMed Central.https://doi.org/10.1186/s40170-017-0164-1 

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Letts, J. A., &; Sazanov, L. A. (2017). Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain. Nature Structural and Molecular Biology. Nature Publishing Group.https://doi.org/10.1038/nsmb.3460 

Letts, J. A., Degliesposti, G., Fiedorczuk, K., Skehel, M., &; Sazanov, L. A. (2016). Purification of ovine respiratory complex i results in a highly active and stable preparation. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology.https://doi.org/10.1074/jbc.M116.735142 

Fiedorczuk, K., Letts, J. A., Degliesposti, G., Kaszuba, K., Skehel, M., &; Sazanov, L. A. (2016). Atomic structure of the entire mammalian mitochondrial complex i. Nature. Nature Publishing Group.https://doi.org/10.1038/nature19794 

Letts, J. A., Fiedorczuk, K., &; Sazanov, L. A. (2016). The architecture of respiratory supercomplexes. Nature. Nature Publishing Group.https://doi.org/10.1038/nature19774 

Holt, P., Efremov, R., Nakamaru Ogiso, E., &; Sazanov, L. A. (2016). Reversible FMN dissociation from Escherichia coli respiratory complex I. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/j.bbabio.2016.08.008 

Berrisford, J., Baradaran, R., &; Sazanov, L. A. (2016). Structure of bacterial respiratory complex I. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/j.bbabio.2016.01.012 

Sazanov, L. A. (2015). A giant molecular proton pump: structure and mechanism of respiratory complex I. Nature Reviews Molecular Cell Biology. Nature Publishing Group.https://doi.org/10.1038/nrm3997 

Letts, J. A., &; Sazanov, L. A. (2015). Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions. Current Opinion in Structural Biology. Elsevier.https://doi.org/10.1016/j.sbi.2015.08.008 

Garvin, M., Bielawski, J., Sazanov, L. A., &; Gharrett, A. (2014). Review and meta-analysis of natural selection in mitochondrial complex I in metazoans. Journal of Zoological Systematics and Evolutionary Research. Wiley-Blackwell.https://doi.org/10.1111/jzs.12079 

Heikal, A., Nakatani, Y., Dunn, E., Weimar, M., Day, C., Baker, E.,https://doi.org/10.1111/mmi.12507__Cook, G. (2014). Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation. Molecular Microbiology. Wiley-Blackwell.https://doi.org/10.1111/mmi.12507 

Sazanov, L. A. (2014). The mechanism of coupling between electron transfer and proton translocation in respiratory complex I. Journal of Bioenergetics and Biomembranes. Springer.https://doi.org/10.1007/s10863-014-9554-z 

Sazanov, L. A., Baradaran, R., Efremov, R., Berrisford, J., &; Minhas, G. (2013). A long road towards the structure of respiratory complex I, a giant molecular proton pump. Biochemical Society Transactions. Portland Press.https://doi.org/10.1042/BST20130193 

Baradaran, R., Berrisford, J., Minhas, G., &; Sazanov, L. A. (2013). Crystal structure of the entire respiratory complex i. Nature. Nature Publishing Group.https://doi.org/10.1038/nature11871 

Efremov, R., &; Sazanov, L. A. (2012). The coupling mechanism of respiratory complex i - A structural and evolutionary perspective. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/j.bbabio.2012.02.015 

Efremov, R., &; Sazanov, L. A. (2012). Structure of Escherichia coli OmpF porin from lipidic mesophase. Journal of Structural Biology. Academic Press.https://doi.org/10.1016/j.jsb.2012.03.005 

Yip, C., Harbour, M., Jayawardena, K., Fearnley, I., &; Sazanov, L. A. (2011). Evolution of respiratory complex I &;quot;Supernumerary&;quot; subunits are present in the ;1-proteobacterial enzyme. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology.https://doi.org/10.1074/jbc.M110.194993 

Efremov, R., &; Sazanov, L. A. (2011). Structure of the membrane domain of respiratory complex i. Nature. Nature Publishing Group.https://doi.org/10.1038/nature10330 

Efremov, R., &; Sazanov, L. A. (2011). Respiratory complex I: “steam engine”https://doi.org/10.1016/j.sbi.2011.07.002__of the cell? Current Opinion in Structural Biology. Elsevier.https://doi.org/10.1016/j.sbi.2011.07.002 

Efremov, R., Baradaran, R., &; Sazanov, L. A. (2010). The architecture of respiratory complex I. Nature. Nature Publishing Group.https://doi.org/10.1038/nature09066 

Berrisford, J., &; Sazanov, L. A. (2009). Structural basis for the mechanism of respiratory complex I. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology.https://doi.org/10.1074/jbc.M109.032144 

Berrisford, J., Thompson, C., &; Sazanov, L. A. (2008). Chemical and NADH-induced, ROS-dependent, cross-linking between sublimits of complex I from Escherichia coli and Thermus thermophilus. Biochemistry. ACS.https://doi.org/10.1021/bi801160u 

Morgan, D., &; Sazanov, L. A. (2008). Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/j.bbabio.2008.03.023 

Baranova, E., Holt, P., &; Sazanov, L. A. (2007). Projection structure of the membrane domain of Escherichia coli respiratory Complex I at 8 Å resolution. Journal of Molecular Biology. Elsevier.https://doi.org/10.1016/j.jmb.2006.11.026 

Baranova, E., Morgan, D., &; Sazanov, L. A. (2007). Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I. Journal of Structural Biology. Academic Press.https://doi.org/10.1016/j.jsb.2007.01.009 

Sazanov, L. A. (2007). Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry. ACS.https://doi.org/10.1021/bi602508x 

Sazanov, L. A., &; Hinchliffe, P. (2006). Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science. American Association for the Advancement of Science.https://doi.org/10.1126/science.1123809 

Hinchliffe, P., Carroll, J., &; Sazanov, L. A. (2006). Identification of a novel subunit of respiratory complex I from Thermus thermophilus. Biochemistry. ACS.https://doi.org/10.1021/bi0600998 

Hinchliffe, P., &; Sazanov, L. A. (2005). Biochemistry: Organization of iron-sulfur clusters in respiratory complex I. Science. American Association for the Advancement of Science.https://doi.org/10.1126/science.1113988 

Mamedova, A., Holt, P., Carroll, J., &; Sazanov, L. A. (2004). Substrate-induced conformational change in bacterial complex I. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology.https://doi.org/10.1074/jbc.M401539200 

Holt, P., Morgan, D., &; Sazanov, L. A. (2003). The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli Complex I: implications for the mechanism of proton pumping. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology.https://doi.org/10.1074/jbc.M308247200 

Sazanov, L. A., Carroll, J., Holt, P., Toime, L., &; Fearnley, I. (2003). A role for native lipids in the stabilization and two dimensional crystallization of the Escherichia coli NADH ubiquinone oxidoreductase (complex I). Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology.https://doi.org/10.1074/jbc.M208959200 

Sazanov, L. A., &; Walker, J. (2000). Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms. Journal of Molecular Biology. Elsevier.https://doi.org/10.1006/jmbi.2000.4079 

Sazanov, L. A., Peak Chew, S., Fearnley, I., &; Walker, J. (2000). Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme. Biochemistry. ACS.https://doi.org/10.1021/bi000335t 

Sazanov, L. A., Burrows, P., &; Nixon, P. (1998). The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes. PNAS. National Academy of Sciences.https://doi.org/10.1073/pnas.95.3.1319 

Burrows, P., Sazanov, L. A., Sváb, Z., Maliga, P., &; Nixon, P. (1998). Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO Journal. Wiley-Blackwell.https://doi.org/10.1093/emboj/17.4.868 

Sazanov, L. A., Burrows, P., &; Nixon, P. (1998). The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves. FEBS Letters. Elsevier.https://doi.org/10.1016/S0014-5793(98)00573-0 

Sazanov, L. A., Burrows, P., &; Nixon, P. J. (1996). Presence of a large protein complex containing the ndhK gene product and possessing NADH-specific dehydrogenase activity in thylakoid membranes of higher plant chloroplasts (Vol. 2, pp. 705–708). Presented at the IPC: International Photosynthesis Congress, Kluwer.

Bizouarn, T., Sazanov, L. A., Aubourg, S., &; Jackson, J. (1996). Estimation of the H+/H- ratio of the reaction catalysed by the nicotinamide nucleotide transhydrogenase in chromatophores from over-expressing strains of Rhodospirillum rubrum and in liposomes inlaid with the purified bovine enzyme. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/0005-2728(95)00125-5 

Sazanov, L. A., Burrows, P., &; Nixon, P. (1996). Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids. Biochemical Society Transactions. Portland Press.https://doi.org/10.1042/bst0240739 

Sazanov, L. A., &; Jackson, B. (1995). Cyclic reactions catalysed by detergent-dispersed and reconstituted transhydrogenase from beef heart mitochondria; implications for the mechanism of proton translocation. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/0005-2728(95)00096-2 

Sazanov, L. A., &; Jackson, J. (1994). Proton translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria. FEBS Letters. Elsevier.https://doi.org/10.1016/0014-5793(94)00370-X 

Efanov, A., Koshkin, A., Sazanov, L. A., Borodulina, O. I., Varfolomeev, S., &; Za0tsev, S. (1994). Inhibition of the respiratory burst in mouse macrophages by ultra-low doses of an opioid peptide is consistent with a possible adaptation mechanism. FEBS Letters. Elsevier.https://doi.org/10.1016/0014-5793(94)01109-5 

Sazanov, L. A., &; Jackson, J. (1993). Activation and inhibition of mitochondrial transhydrogenase by metal ions. Biochimica et Biophysica Acta - Bioenergetics. Elsevier.https://doi.org/10.1016/0005-2728(93)90177-H 

Sazanov, L. A., &; Jackson, J. (1993). Possible functions of the NADP-linked isocitrate dehydrogenase and H+ -transhydrogenase in heart mitochondria . Biochemical Society Transactions. Portland Press.https://doi.org/10.1042/bst021260s 

Jackson, J., Cotton, N. P. J., Williams, R., Bizouarn, T., Hutton, M., Sazanov, L. A., &; Thomas, C. (1993). Proton-translocating transhydrogenase in bacteria. Biochemical Society Transactions. Portland Press.https://doi.org/10.1042/bst0211010 

Sazanov, L. A., &; Za0tsev, S. (1992). Effect of superlow doses (10(-18)-10-(-14) M) of biologically active substances: general rules, features, and possible mechanisms. Biochemistry (Moscow). Izdatel’stvo Nauka.

Za0tsev, S., Sazanov, L. A., Koshkin, A., Sud’Ina, G., &; Varfolomeev, S. (1991). Respiratory burst inhibition in human neutrophils by ultra-low doses of [D-Al] methionine enkephalinamide. FEBS Letters. Elsevier.https://doi.org/10.1016/0014-5793(91)81109-L 

Sazanov, L. A., Karavaev, V. A., &; Kukushkin, A. K. (1988). Mathematical model of photosynthesis regulation accounts for the effects of changes in external conditions and observed oscillations. Russian Journal of Physical Chemistry B. Elsevier.