Gupta C, Khaniya U, Chan CK, Dehez F, Shekhar M, Gunner MR, Sazanov LA, Chipot C, Singharoy A. 2020. Charge transfer and chemo-mechanical coupling in respiratory complex I. Journal of the American Chemical Society. 142(20), 9220–9230.
LibreCat: https://research-explorer.ista.ac.at/record/8040
DOI: 10.1021/jacs.9b13450
WoS: 000537415600020
PMID: 32347721

Gutierrez-Fernandez J, Kaszuba K, Minhas GS, Baradaran R, Tambalo M, Gallagher DT, Sazanov LA. 2020. Key role of quinone in the mechanism of respiratory complex I. Nature Communications. 11(1), 4135.
LibreCat: https://research-explorer.ista.ac.at/record/8318
DOI: 10.1038/s41467-020-17957-0
WoS: 000607072900001
PMID: 32811817

Andrei A, Öztürk Y, Khalfaoui-Hassani B, Rauch J, Marckmann D, Trasnea PI, Daldal F, Koch H-G. 2020. Cu homeostasis in bacteria: The ins and outs. Membranes. 10(9), 242.
LibreCat: https://research-explorer.ista.ac.at/record/8579
DOI: 10.3390/membranes10090242
WoS: 000581446000001

Pinke G, Zhou L, Sazanov LA. 2020. Cryo-EM structure of the entire mammalian F-type ATP synthase. Nature Structural and Molecular Biology. 27(11), 1077–1085.
LibreCat: https://research-explorer.ista.ac.at/record/8581
DOI: 10.1038/s41594-020-0503-8
WoS: 000569299400004
PMID: 32929284

Kampjut D, Sazanov LA. 2020. The coupling mechanism of mammalian respiratory complex I. Science. 370(6516), eab09.
LibreCat: https://research-explorer.ista.ac.at/record/8737
DOI: 10.1126/science.abc4209
WoS: 000583031800004
PMID: 32972993

Steiner J. 2020. Biochemical and structural investigation of the Mrp antiporter, an ancestor of complex I. Institute of Science and Technology Austria.
LibreCat: https://research-explorer.ista.ac.at/record/8353
DOI: 10.15479/AT:ISTA:8353

Steiner J, Sazanov LA. 2020. Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter. eLife. 9, e59407.
LibreCat: https://research-explorer.ista.ac.at/record/8284
DOI: 10.7554/eLife.59407
WoS: 000562123600001
PMID: 32735215

Kampjut D. 2020. Molecular mechanisms of mitochondrial redox-coupled proton pumping enzymes. Institute of Science and Technology Austria.
LibreCat: https://research-explorer.ista.ac.at/record/8340
DOI: 10.15479/AT:ISTA:8340

Temnov AA, Rogov KA, Sklifas AN, Klychnikova EV, Hartl M, Djinovic-Carugo K, Charnagalov A. 2019. Protective properties of the cultured stem cell proteome studied in an animal model of acetaminophen-induced acute liver failure. Molecular Biology Reports.
LibreCat: https://research-explorer.ista.ac.at/record/6352
DOI: 10.1007/s11033-019-04765-z
WoS: 000470332600049

Zhou L, Sazanov LA. 2019. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science. 365(6455), ea.
LibreCat: https://research-explorer.ista.ac.at/record/6859
DOI: 10.1126/science.aaw9144
WoS: 000482464000043
PMID: 31439765

Qi C, Minin GD, Vercellino I, Wutz A, Korkhov VM. 2019. Structural basis of sterol recognition by human hedgehog receptor PTC. Science Advances. 5(9), ea.
LibreCat: https://research-explorer.ista.ac.at/record/6919
DOI: 10.1126/sciadv.aaw6490
WoS: 000491128800062

Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. 2019. Structures of respiratory supercomplex I+II reveal functional and conformational crosstalk. Molecular Cell. 75(6), 1131–1146.e6.
LibreCat: https://research-explorer.ista.ac.at/record/7395
DOI: 10.1016/j.molcel.2019.07.022
WoS: 000486614200006
PMID: 31492636

Kampjut D, Sazanov LA. 2019. Structure and mechanism of mitochondrial proton-translocating transhydrogenase. Nature. 573(7773), 291–295.
LibreCat: https://research-explorer.ista.ac.at/record/6848
DOI: 10.1038/s41586-019-1519-2
WoS: 000485415400061
PMID: 31462775

Fiedorczuk K, Sazanov LA. 2018. Mammalian mitochondrial complex I structure and disease causing mutations. Trends in Cell Biology. 28(10), 835–867.
LibreCat: https://research-explorer.ista.ac.at/record/152
DOI: 10.1016/j.tcb.2018.06.006
WoS: 000445118200007

Sazanov LA. 2017.Structure of respiratory complex I: “Minimal” bacterial and luxe” mammalian versions. In: Mechanisms of primary energy transduction in biology . , 25–59.
LibreCat: https://research-explorer.ista.ac.at/record/444
DOI: 10.1039/9781788010405-00025

Letts JA, Sazanov LA. 2017. Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain. Nature Structural and Molecular Biology. 24(10), 800–808.
LibreCat: https://research-explorer.ista.ac.at/record/515
DOI: 10.1038/nsmb.3460

Gutierrez-Fernandez J, Saleh M, Alcorlo M, Gómez Mejóa A, Pantoja Uceda D, Treviño M, Vob F, Abdullah M, Galán Bartual S, Seinen J, Sánchez Murcia P, Gago F, Bruix M, Hammerschmidt S, Hermoso J. 2016. Modular architecture and unique teichoic acid recognition features of choline-binding protein L CbpL contributing to pneumococcal pathogenesis. Scientific Reports. 6, 38094.
LibreCat: https://research-explorer.ista.ac.at/record/1186
DOI: 10.1038/srep38094

Letts JA, Degliesposti G, Fiedorczuk K, Skehel M, Sazanov LA. 2016. Purification of ovine respiratory complex i results in a highly active and stable preparation. Journal of Biological Chemistry. 291(47), 24657–24675.
LibreCat: https://research-explorer.ista.ac.at/record/1209
DOI: 10.1074/jbc.M116.735142

Fiedorczuk K, Letts JA, Degliesposti G, Kaszuba K, Skehel M, Sazanov LA. 2016. Atomic structure of the entire mammalian mitochondrial complex i. Nature. 538(7625), 406–410.
LibreCat: https://research-explorer.ista.ac.at/record/1226
DOI: 10.1038/nature19794
PMID: 27595392

Letts JA, Fiedorczuk K, Sazanov LA. 2016. The architecture of respiratory supercomplexes. Nature. 537(7622), 644–648.
LibreCat: https://research-explorer.ista.ac.at/record/1232
DOI: 10.1038/nature19774