Vercellino, Irene, and Leonid A. Sazanov. “SCA Drives the Compositional Diversity of Mammalian Respirasomes.”10.1038/s41594-024-01255-0__Nature Structural and Molecular Biology, Springer Nature, 2024, doi:10.1038/s41594-024-01255-0.
LibreCat: https://research-explorer.ista.ac.at/record/15323
DOI: 10.1038/s41594-024-01255-0
PMID: 38575788

Sazanov, Leonid A. “From the ‘black Box’ to ‘Domino Effect’ Mechanism: What Have We Learned from the Structures of Respiratory Complex I.”10.1042/BCJ20210285__The Biochemical Journal, vol. 480, no. 5, Portland Press, 2023, pp. 319–33, doi:10.1042/BCJ20210285.
LibreCat: https://research-explorer.ista.ac.at/record/12757
DOI: 10.1042/BCJ20210285
WoS: 000957065700001
PMID: 36920092

Zhao, Ziyu, et al. “The Ycf48 Accessory Factor Occupies the Site of the Oxygen-Evolving Manganese Cluster during Photosystem II Biogenesis.”10.1038/s41467-023-40388-6__Nature Communications, vol. 14, 4681, Springer Nature, 2023, doi:10.1038/s41467-023-40388-6.
LibreCat: https://research-explorer.ista.ac.at/record/14040
DOI: 10.1038/s41467-023-40388-6
WoS: 001042606700004

Vercellino, Irene, and Leonid A. Sazanov. “The Assembly, Regulation and Function of the Mitochondrial Respiratory Chain.”10.1038/s41580-021-00415-0__Nature Reviews Molecular Cell Biology, vol. 23, Springer Nature, 2022, pp. 141–161, doi:10.1038/s41580-021-00415-0.
LibreCat: https://research-explorer.ista.ac.at/record/10182
DOI: 10.1038/s41580-021-00415-0
WoS: 000705697100001
PMID: 34621061

Kampjut, Domen, and Leonid A. Sazanov. “Structure of Respiratory Complex I – An Emerging Blueprint for the Mechanism.”10.1016/j.sbi.2022.102350__Current Opinion in Structural Biology, vol. 74, 102350, Elsevier, 2022, doi:10.1016/j.sbi.2022.102350.
LibreCat: https://research-explorer.ista.ac.at/record/11167
DOI: 10.1016/j.sbi.2022.102350
WoS: 000829029500020
PMID: 35316665

Molina-Granada, David, et al. “Most Mitochondrial DGTP Is Tightly Bound to Respiratory Complex I through the NDUF Subunit.”10.1038/s42003-022-03568-6__Communications Biology, vol. 5, no. 1, 620, Springer Nature, 2022, doi:10.1038/s42003-022-03568-6.
LibreCat: https://research-explorer.ista.ac.at/record/11551
DOI: 10.1038/s42003-022-03568-6
WoS: 000815098500002
PMID:  35739187

Kravchuk, Vladyslav, et al. “A Universal Coupling Mechanism of Respiratory Complex I.”10.1038/s41586-022-05199-7__Nature, vol. 609, no. 7928, Springer Nature, 2022, pp. 808–14, doi:10.1038/s41586-022-05199-7.
LibreCat: https://research-explorer.ista.ac.at/record/12138
DOI: 10.1038/s41586-022-05199-7
WoS: 000854788200001
PMID: 36104567

Abas, Lindy, et al. “Naphthylphthalamic Acid Associates with and Inhibits PIN Auxin Transporters.”10.1073/pnas.2020857118__PNAS, vol. 118, no. 1, e2020857118, National Academy of Sciences, 2021, doi:10.1073/pnas.2020857118.
LibreCat: https://research-explorer.ista.ac.at/record/8993
DOI: 10.1073/pnas.2020857118
WoS: 000607270100073
PMID: 33443187

Kampjut, Domen, et al. “Cryo-EM Grid Optimization for Membrane Proteins.”10.1016/j.isci.2021.102139__IScience, vol. 24, no. 3, 102139, Elsevier, 2021, doi:10.1016/j.isci.2021.102139.
LibreCat: https://research-explorer.ista.ac.at/record/9205
DOI: 10.1016/j.isci.2021.102139
WoS: 000631646000012
PMID: 33665558

Vercellino, Irene, and Leonid A. Sazanov. “Structure and Assembly of the Mammalian Mitochondrial Supercomplex CIII<sub>2</sub>CIV.”10.1038/s41586-021-03927-z__Nature, vol. 598, no. 7880, Springer Nature, 2021, pp. 364–67, doi:10.1038/s41586-021-03927-z.
LibreCat: https://research-explorer.ista.ac.at/record/10146
DOI: 10.1038/s41586-021-03927-z
WoS: 000704581600001
PMID: 34616041

Adjobo-Hermans, Merel J. W., et al. “NDUF Deletion Triggers Loss of NDUF in Nduf/ Mice and Leigh Syndrome Patients: A Stabilizing Role for NDUFA.”10.1016/j.bbabio.2020.148213__Biochimica et Biophysica Acta - Bioenergetics, vol. 1861, no. 8, 148213, Elsevier, 2020, doi:10.1016/j.bbabio.2020.148213.
LibreCat: https://research-explorer.ista.ac.at/record/7788
DOI: 10.1016/j.bbabio.2020.148213
WoS: 000540842000012
PMID: 32335026

Gupta, Chitrak, et al. “Charge Transfer and Chemo-Mechanical Coupling in Respiratory Complex I.”10.1021/jacs.9b13450__Journal of the American Chemical Society, vol. 142, no. 20, American Chemical Society, 2020, pp. 9220–30, doi:10.1021/jacs.9b13450.
LibreCat: https://research-explorer.ista.ac.at/record/8040
DOI: 10.1021/jacs.9b13450
WoS: 000537415600020
PMID: 32347721

Gupta, Chitrak, et al. Charge Transfer and Chemo-Mechanical Coupling in Respiratory Complex I. American Chemical Society, 2020, doi:10.1021/jacs.9b13450.s002.
LibreCat: https://research-explorer.ista.ac.at/record/9326
DOI: 10.1021/jacs.9b13450.s002

Gupta, Chitrak, et al. Supporting Information. American Chemical Society , 2020, doi:10.1021/jacs.9b13450.s001.
LibreCat: https://research-explorer.ista.ac.at/record/9713
DOI: 10.1021/jacs.9b13450.s001

Gupta, Chitrak, et al. Movies. American Chemical Society, 2020, doi:10.1021/jacs.9b13450.s002.
LibreCat: https://research-explorer.ista.ac.at/record/9878
DOI: 10.1021/jacs.9b13450.s002

Gutierrez-Fernandez, Javier, et al. “Key Role of Quinone in the Mechanism of Respiratory Complex I.”10.1038/s41467-020-17957-0__Nature Communications, vol. 11, no. 1, 4135, Springer Nature, 2020, doi:10.1038/s41467-020-17957-0.
LibreCat: https://research-explorer.ista.ac.at/record/8318
DOI: 10.1038/s41467-020-17957-0
WoS: 000607072900001
PMID: 32811817

Pinke, Gergely, et al. “Cryo-EM Structure of the Entire Mammalian F-Type ATP Synthase.”10.1038/s41594-020-0503-8__Nature Structural and Molecular Biology, vol. 27, no. 11, Springer Nature, 2020, pp. 1077–85, doi:10.1038/s41594-020-0503-8.
LibreCat: https://research-explorer.ista.ac.at/record/8581
DOI: 10.1038/s41594-020-0503-8
WoS: 000569299400004
PMID: 32929284

Kampjut, Domen, and Leonid A. Sazanov. “The Coupling Mechanism of Mammalian Respiratory Complex I.”10.1126/science.abc4209__Science, vol. 370, no. 6516, eab09, American Association for the Advancement of Science, 2020, doi:10.1126/science.abc4209.
LibreCat: https://research-explorer.ista.ac.at/record/8737
DOI: 10.1126/science.abc4209
WoS: 000583031800004
PMID: 32972993

Steiner, Julia, and Leonid A. Sazanov. “Structure and Mechanism of the Mrp Complex, an Ancient Cation/Proton Antiporter.”10.7554/eLife.59407__ELife, vol. 9, e59407, eLife Sciences Publications, 2020, doi:10.7554/eLife.59407.
LibreCat: https://research-explorer.ista.ac.at/record/8284
DOI: 10.7554/eLife.59407
WoS: 000562123600001
PMID: 32735215

Zhou, Long, and Leonid A. Sazanov. “Structure and Conformational Plasticity of the Intact Thermus Thermophilus V/A-Type ATPase.”10.1126/science.aaw9144__Science, vol. 365, no. 6455, ea, AAAS, 2019, doi:10.1126/science.aaw9144.
LibreCat: https://research-explorer.ista.ac.at/record/6859
DOI: 10.1126/science.aaw9144
WoS: 000482464000043
PMID: 31439765

Letts, James A., et al. “Structures of Respiratory Supercomplex I+II Reveal Functional and Conformational Crosstalk.”10.1016/j.molcel.2019.07.022__Molecular Cell, vol. 75, no. 6, Cell Press, 2019, p. 1131–1146.e6, doi:10.1016/j.molcel.2019.07.022.
LibreCat: https://research-explorer.ista.ac.at/record/7395
DOI: 10.1016/j.molcel.2019.07.022
WoS: 000486614200006
PMID: 31492636

Kampjut, Domen, and Leonid A. Sazanov. “Structure and Mechanism of Mitochondrial Proton-Translocating Transhydrogenase.”10.1038/s41586-019-1519-2__Nature, vol. 573, no. 7773, Springer Nature, 2019, pp. 291–295, doi:10.1038/s41586-019-1519-2.
LibreCat: https://research-explorer.ista.ac.at/record/6848
DOI: 10.1038/s41586-019-1519-2
WoS: 000485415400061
PMID: 31462775

Fiedorczuk, Karol, and Leonid A. Sazanov. “Mammalian Mitochondrial Complex I Structure and Disease Causing Mutations.”10.1016/j.tcb.2018.06.006__Trends in Cell Biology, vol. 28, no. 10, Elsevier, 2018, pp. 835–67, doi:10.1016/j.tcb.2018.06.006.
LibreCat: https://research-explorer.ista.ac.at/record/152
DOI: 10.1016/j.tcb.2018.06.006
WoS: 000445118200007

Hardie, Rae, et al. “Mitochondrial Mutations and Metabolic Adaptation in Pancreatic Cancer.”10.1186/s40170-017-0164-1__Cancer &; Metabolism, vol. 5, no. 2, BioMed Central, 2017, doi:10.1186/s40170-017-0164-1.
LibreCat: https://research-explorer.ista.ac.at/record/443
DOI: 10.1186/s40170-017-0164-1

Sazanov, Leonid A. “Structure of Respiratory Complex I: ‘Minimal’ Bacterial and ‘de Luxe’ Mammalian Versions.”10.1039/9781788010405-00025__Mechanisms of Primary Energy Transduction in Biology , edited by Mårten Wikström, Royal Society of Chemistry, 2017, pp. 25–59, doi:10.1039/9781788010405-00025.
LibreCat: https://research-explorer.ista.ac.at/record/444
DOI: 10.1039/9781788010405-00025

Letts, James A., and Leonid A. Sazanov. “Clarifying the Supercomplex: The Higher-Order Organization of the Mitochondrial Electron Transport Chain.”10.1038/nsmb.3460__Nature Structural and Molecular Biology, vol. 24, no. 10, Nature Publishing Group, 2017, pp. 800–08, doi:10.1038/nsmb.3460.
LibreCat: https://research-explorer.ista.ac.at/record/515
DOI: 10.1038/nsmb.3460

Letts, James A., et al. “Purification of Ovine Respiratory Complex i Results in a Highly Active and Stable Preparation.”10.1074/jbc.M116.735142__Journal of Biological Chemistry, vol. 291, no. 47, American Society for Biochemistry and Molecular Biology, 2016, pp. 24657–75, doi:10.1074/jbc.M116.735142.
LibreCat: https://research-explorer.ista.ac.at/record/1209
DOI: 10.1074/jbc.M116.735142

Fiedorczuk, Karol, et al. “Atomic Structure of the Entire Mammalian Mitochondrial Complex I.”10.1038/nature19794__Nature, vol. 538, no. 7625, Nature Publishing Group, 2016, pp. 406–10, doi:10.1038/nature19794.
LibreCat: https://research-explorer.ista.ac.at/record/1226
DOI: 10.1038/nature19794
PMID: 27595392

Letts, James A., et al. “The Architecture of Respiratory Supercomplexes.”10.1038/nature19774__Nature, vol. 537, no. 7622, Nature Publishing Group, 2016, pp. 644–48, doi:10.1038/nature19774.
LibreCat: https://research-explorer.ista.ac.at/record/1232
DOI: 10.1038/nature19774

Holt, Peter, et al. “Reversible FMN Dissociation from Escherichia Coli Respiratory Complex I.”10.1016/j.bbabio.2016.08.008__Biochimica et Biophysica Acta - Bioenergetics, vol. 1857, no. 11, Elsevier, 2016, pp. 1777–85, doi:10.1016/j.bbabio.2016.08.008.
LibreCat: https://research-explorer.ista.ac.at/record/1288
DOI: 10.1016/j.bbabio.2016.08.008

Berrisford, John, et al. “Structure of Bacterial Respiratory Complex I.”10.1016/j.bbabio.2016.01.012__Biochimica et Biophysica Acta - Bioenergetics, vol. 1857, no. 7, Elsevier, 2016, pp. 892–901, doi:10.1016/j.bbabio.2016.01.012.
LibreCat: https://research-explorer.ista.ac.at/record/1521
DOI: 10.1016/j.bbabio.2016.01.012

Sazanov, Leonid A. “A Giant Molecular Proton Pump: Structure and Mechanism of Respiratory Complex I.”10.1038/nrm3997__Nature Reviews Molecular Cell Biology, vol. 16, no. 6, Nature Publishing Group, 2015, pp. 375–88, doi:10.1038/nrm3997.
LibreCat: https://research-explorer.ista.ac.at/record/1638
DOI: 10.1038/nrm3997

Letts, James A., and Leonid A. Sazanov. “Gaining Mass: The Structure of Respiratory Complex I-from Bacterial towards Mitochondrial Versions.”10.1016/j.sbi.2015.08.008__Current Opinion in Structural Biology, vol. 33, no. 8, Elsevier, 2015, pp. 135–45, doi:10.1016/j.sbi.2015.08.008.
LibreCat: https://research-explorer.ista.ac.at/record/1683
DOI: 10.1016/j.sbi.2015.08.008

Garvin, Michael, et al. “Review and Meta-Analysis of Natural Selection in Mitochondrial Complex I in Metazoans.”10.1111/jzs.12079__Journal of Zoological Systematics and Evolutionary Research, vol. 53, no. 1, Wiley-Blackwell, 2014, pp. 1–17, doi:10.1111/jzs.12079.
LibreCat: https://research-explorer.ista.ac.at/record/1981
DOI: 10.1111/jzs.12079

Heikal, Adam, et al. “Structure of the Bacterial Type II NADH Dehydrogenase: A Monotopic Membrane Protein with an Essential Role in Energy Generation.”10.1111/mmi.12507__Molecular Microbiology, vol. 91, no. 5, Wiley-Blackwell, 2014, pp. 950–64, doi:10.1111/mmi.12507.
LibreCat: https://research-explorer.ista.ac.at/record/1980
DOI: 10.1111/mmi.12507

Sazanov, Leonid A. “The Mechanism of Coupling between Electron Transfer and Proton Translocation in Respiratory Complex I.”10.1007/s10863-014-9554-z__Journal of Bioenergetics and Biomembranes, vol. 46, no. 4, Springer, 2014, pp. 247–53, doi:10.1007/s10863-014-9554-z.
LibreCat: https://research-explorer.ista.ac.at/record/1979
DOI: 10.1007/s10863-014-9554-z

Sazanov, Leonid A., et al. “A Long Road towards the Structure of Respiratory Complex I, a Giant Molecular Proton Pump.”10.1042/BST20130193__Biochemical Society Transactions, vol. 41, no. 5, Portland Press, 2013, pp. 1265–71, doi:10.1042/BST20130193.
LibreCat: https://research-explorer.ista.ac.at/record/1977
DOI: 10.1042/BST20130193

Baradaran, Rozbeh, et al. “Crystal Structure of the Entire Respiratory Complex I.”10.1038/nature11871__Nature, vol. 494, no. 7438, Nature Publishing Group, 2013, pp. 443–48, doi:10.1038/nature11871.
LibreCat: https://research-explorer.ista.ac.at/record/1978
DOI: 10.1038/nature11871

Efremov, Rouslan, and Leonid A. Sazanov. “The Coupling Mechanism of Respiratory Complex i - A Structural and Evolutionary Perspective.”10.1016/j.bbabio.2012.02.015__Biochimica et Biophysica Acta - Bioenergetics, vol. 1817, no. 10, Elsevier, 2012, pp. 1785–95, doi:10.1016/j.bbabio.2012.02.015.
LibreCat: https://research-explorer.ista.ac.at/record/1976
DOI: 10.1016/j.bbabio.2012.02.015

Efremov, Rouslan, and Leonid A. Sazanov. “Structure of Escherichia Coli OmpF Porin from Lipidic Mesophase.”10.1016/j.jsb.2012.03.005__Journal of Structural Biology, vol. 178, no. 3, Academic Press, 2012, pp. 311–18, doi:10.1016/j.jsb.2012.03.005.
LibreCat: https://research-explorer.ista.ac.at/record/1972
DOI: 10.1016/j.jsb.2012.03.005

Yip, Chui, et al. “Evolution of Respiratory Complex I &;quot;Supernumerary&;quot; Subunits Are Present in the ;1-Proteobacterial Enzyme.”10.1074/jbc.M110.194993__Journal of Biological Chemistry, vol. 286, no. 7, American Society for Biochemistry and Molecular Biology, 2011, pp. 5023–33, doi:10.1074/jbc.M110.194993.
LibreCat: https://research-explorer.ista.ac.at/record/1975
DOI: 10.1074/jbc.M110.194993

Efremov, Rouslan, and Leonid A. Sazanov. “Structure of the Membrane Domain of Respiratory Complex I.”10.1038/nature10330__Nature, vol. 476, no. 7361, Nature Publishing Group, 2011, pp. 414–21, doi:10.1038/nature10330.
LibreCat: https://research-explorer.ista.ac.at/record/1973
DOI: 10.1038/nature10330

Efremov, Rouslan, and Leonid A. Sazanov. “Respiratory Complex I: ‘steam Engine’ of the Cell?”10.1016/j.sbi.2011.07.002__Current Opinion in Structural Biology, vol. 21, no. 4, Elsevier, 2011, pp. 532–40, doi:10.1016/j.sbi.2011.07.002.
LibreCat: https://research-explorer.ista.ac.at/record/1974
DOI: 10.1016/j.sbi.2011.07.002

Efremov, Rouslan, et al. “The Architecture of Respiratory Complex I.”10.1038/nature09066__Nature, vol. 465, no. 7297, Nature Publishing Group, 2010, pp. 441–45, doi:10.1038/nature09066.
LibreCat: https://research-explorer.ista.ac.at/record/1970
DOI: 10.1038/nature09066

Berrisford, John, and Leonid A. Sazanov. “Structural Basis for the Mechanism of Respiratory Complex I.”10.1074/jbc.M109.032144__Journal of Biological Chemistry, vol. 284, no. 43, American Society for Biochemistry and Molecular Biology, 2009, pp. 29773–83, doi:10.1074/jbc.M109.032144.
LibreCat: https://research-explorer.ista.ac.at/record/1971
DOI: 10.1074/jbc.M109.032144

Berrisford, John, et al. “Chemical and NADH-Induced, ROS-Dependent, Cross-Linking between Sublimits of Complex I from Escherichia Coli and Thermus Thermophilus.”10.1021/bi801160u__Biochemistry, vol. 47, no. 39, ACS, 2008, pp. 10262–70, doi:10.1021/bi801160u.
LibreCat: https://research-explorer.ista.ac.at/record/1967
DOI: 10.1021/bi801160u

Morgan, David, and Leonid A. Sazanov. “Three-Dimensional Structure of Respiratory Complex I from Escherichia Coli in Ice in the Presence of Nucleotides.”10.1016/j.bbabio.2008.03.023__Biochimica et Biophysica Acta - Bioenergetics, vol. 1777, no. 7–8, Elsevier, 2008, pp. 711–18, doi:10.1016/j.bbabio.2008.03.023.
LibreCat: https://research-explorer.ista.ac.at/record/1968
DOI: 10.1016/j.bbabio.2008.03.023

Baranova, Ekaterina, et al. “Projection Structure of the Membrane Domain of Escherichia Coli Respiratory Complex I at 8 Å Resolution.”10.1016/j.jmb.2006.11.026__Journal of Molecular Biology, vol. 366, no. 1, Elsevier, 2007, pp. 140–54, doi:10.1016/j.jmb.2006.11.026.
LibreCat: https://research-explorer.ista.ac.at/record/1965
DOI: 10.1016/j.jmb.2006.11.026

Baranova, Ekaterina, et al. “Single Particle Analysis Confirms Distal Location of Subunits NuoL and NuoM in Escherichia Coli Complex I.”10.1016/j.jsb.2007.01.009__Journal of Structural Biology, vol. 159, no. 2 SPEC. ISS., Academic Press, 2007, pp. 238–42, doi:10.1016/j.jsb.2007.01.009.
LibreCat: https://research-explorer.ista.ac.at/record/1969
DOI: 10.1016/j.jsb.2007.01.009

Sazanov, Leonid A. “Respiratory Complex I: Mechanistic and Structural Insights Provided by the Crystal Structure of the Hydrophilic Domain.”10.1021/bi602508x__Biochemistry, vol. 46, no. 9, ACS, 2007, pp. 2275–88, doi:10.1021/bi602508x.
LibreCat: https://research-explorer.ista.ac.at/record/1964
DOI: 10.1021/bi602508x

Sazanov, Leonid A., and Philip Hinchliffe. “Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus Thermophilus.”10.1126/science.1123809__Science, vol. 311, no. 5766, American Association for the Advancement of Science, 2006, pp. 1430–36, doi:10.1126/science.1123809.
LibreCat: https://research-explorer.ista.ac.at/record/1961
DOI: 10.1126/science.1123809

Hinchliffe, Philip, et al. “Identification of a Novel Subunit of Respiratory Complex I from Thermus Thermophilus.”10.1021/bi0600998__Biochemistry, vol. 45, no. 14, ACS, 2006, pp. 4413–20, doi:10.1021/bi0600998.
LibreCat: https://research-explorer.ista.ac.at/record/1966
DOI: 10.1021/bi0600998

Hinchliffe, Philip, and Leonid A. Sazanov. “Biochemistry: Organization of Iron-Sulfur Clusters in Respiratory Complex I.”10.1126/science.1113988__Science, vol. 309, no. 5735, American Association for the Advancement of Science, 2005, pp. 771–74, doi:10.1126/science.1113988.
LibreCat: https://research-explorer.ista.ac.at/record/1962
DOI: 10.1126/science.1113988

Mamedova, Aygun, et al. “Substrate-Induced Conformational Change in Bacterial Complex I.”10.1074/jbc.M401539200__Journal of Biological Chemistry, vol. 279, no. 22, American Society for Biochemistry and Molecular Biology, 2004, pp. 23830–36, doi:10.1074/jbc.M401539200.
LibreCat: https://research-explorer.ista.ac.at/record/1963
DOI: 10.1074/jbc.M401539200

Holt, Peter, et al. “The Location of NuoL and NuoM Subunits in the Membrane Domain of the Escherichia Coli Complex I: Implications for the Mechanism of Proton Pumping.”10.1074/jbc.M308247200__Journal of Biological Chemistry, vol. 278, no. 44, American Society for Biochemistry and Molecular Biology, 2003, pp. 43114–20, doi:10.1074/jbc.M308247200.
LibreCat: https://research-explorer.ista.ac.at/record/1959
DOI: 10.1074/jbc.M308247200

Sazanov, Leonid A., et al. “A Role for Native Lipids in the Stabilization and Two Dimensional Crystallization of the Escherichia Coli NADH Ubiquinone Oxidoreductase (Complex I).”10.1074/jbc.M208959200__Journal of Biological Chemistry, vol. 278, no. 21, American Society for Biochemistry and Molecular Biology, 2003, pp. 19483–91, doi:10.1074/jbc.M208959200.
LibreCat: https://research-explorer.ista.ac.at/record/1960
DOI: 10.1074/jbc.M208959200

Sazanov, Leonid A., and John Walker. “Cryo-Electron Crystallography of Two Sub-Complexes of Bovine Complex I Reveals the Relationship between the Membrane and Peripheral Arms.”10.1006/jmbi.2000.4079__Journal of Molecular Biology, vol. 302, no. 2, Elsevier, 2000, pp. 455–64, doi:10.1006/jmbi.2000.4079.
LibreCat: https://research-explorer.ista.ac.at/record/1957
DOI: 10.1006/jmbi.2000.4079
PMID: 10970745

Sazanov, Leonid A., et al. “Resolution of the Membrane Domain of Bovine Complex I into Subcomplexes: Implications for the Structural Organization of the Enzyme.”10.1021/bi000335t__Biochemistry, vol. 39, no. 24, ACS, 2000, pp. 7229–35, doi:10.1021/bi000335t.
LibreCat: https://research-explorer.ista.ac.at/record/1958
DOI: 10.1021/bi000335t
PMID: 10852722

Sazanov, Leonid A., et al. “The Plastid Ndh Genes Code for an NADH-Specific Dehydrogenase: Isolation of a Complex I Analogue from Pea Thylakoid Membranes.”10.1073/pnas.95.3.1319__PNAS, vol. 95, no. 3, National Academy of Sciences, 1998, pp. 1319–24, doi:10.1073/pnas.95.3.1319.
LibreCat: https://research-explorer.ista.ac.at/record/1956
DOI: 10.1073/pnas.95.3.1319
PMID: 9448329 

Burrows, Paul, et al. “Identification of a Functional Respiratory Complex in Chloroplasts through Analysis of Tobacco Mutants Containing Disrupted Plastid Ndh Genes.”10.1093/emboj/17.4.868__EMBO Journal, vol. 17, no. 4, Wiley-Blackwell, 1998, pp. 868–76, doi:10.1093/emboj/17.4.868.
LibreCat: https://research-explorer.ista.ac.at/record/1955
DOI: 10.1093/emboj/17.4.868
PMID: 9463365

Sazanov, Leonid A., et al. “The Chloroplast Ndh Complex Mediates the Dark Reduction of the Plastoquinone Pool in Response to Heat Stress in Tobacco Leaves.”10.1016/S0014-5793(98)00573-0__FEBS Letters, vol. 429, no. 1, Elsevier, 1998, pp. 115–18, doi:10.1016/S0014-5793(98)00573-0.
LibreCat: https://research-explorer.ista.ac.at/record/1954
DOI: 10.1016/S0014-5793(98)00573-0
PMID: 9657394 

Sazanov, Leonid A., et al. 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, Kluwer, 1996, pp. 705–08.
LibreCat: https://research-explorer.ista.ac.at/record/1942

Bizouarn, Tania, et al. “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.”10.1016/0005-2728(95)00125-5__Biochimica et Biophysica Acta - Bioenergetics, vol. 1273, no. 1, Elsevier, 1996, pp. 4–12, doi:10.1016/0005-2728(95)00125-5.
LibreCat: https://research-explorer.ista.ac.at/record/1952
DOI: 10.1016/0005-2728(95)00125-5
PMID: 8573594 

Sazanov, Leonid A., et al. “Detection and Characterization of a Complex I-like NADH-Specific Dehydrogenase from Pea Thylakoids.”10.1042/bst0240739__Biochemical Society Transactions, vol. 24, no. 3, Portland Press, 1996, pp. 739–43, doi:10.1042/bst0240739.
LibreCat: https://research-explorer.ista.ac.at/record/1951
DOI: 10.1042/bst0240739
PMID: 8878837

Sazanov, Leonid A., and Baz Jackson. “Cyclic Reactions Catalysed by Detergent-Dispersed and Reconstituted Transhydrogenase from Beef Heart Mitochondria; Implications for the Mechanism of Proton Translocation.”10.1016/0005-2728(95)00096-2__Biochimica et Biophysica Acta - Bioenergetics, vol. 1231, no. 3, Elsevier, 1995, pp. 304–12, doi:10.1016/0005-2728(95)00096-2.
LibreCat: https://research-explorer.ista.ac.at/record/1943
DOI: 10.1016/0005-2728(95)00096-2
PMID: 7578218

Sazanov, Leonid A., and Julie Jackson. “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.”10.1016/0014-5793(94)00370-X__FEBS Letters, vol. 344, no. 2–3, Elsevier, 1994, pp. 109–16, doi:10.1016/0014-5793(94)00370-X.
LibreCat: https://research-explorer.ista.ac.at/record/1949
DOI: 10.1016/0014-5793(94)00370-X
PMID: 8187868

Efanov, Alexander, et al. “Inhibition of the Respiratory Burst in Mouse Macrophages by Ultra-Low Doses of an Opioid Peptide Is Consistent with a Possible Adaptation Mechanism.”10.1016/0014-5793(94)01109-5__FEBS Letters, vol. 355, no. 2, Elsevier, 1994, pp. 114–16, doi:10.1016/0014-5793(94)01109-5.
LibreCat: https://research-explorer.ista.ac.at/record/1953
DOI: 10.1016/0014-5793(94)01109-5
PMID: 7982481

Sazanov, Leonid A., and Julie Jackson. “Activation and Inhibition of Mitochondrial Transhydrogenase by Metal Ions.”10.1016/0005-2728(93)90177-H__Biochimica et Biophysica Acta - Bioenergetics, vol. 1144, no. 2, Elsevier, 1993, pp. 225–28, doi:10.1016/0005-2728(93)90177-H.
LibreCat: https://research-explorer.ista.ac.at/record/1947
DOI: 10.1016/0005-2728(93)90177-H
PMID: 8369341 

Sazanov, Leonid A., and Julie Jackson. “Possible Functions of the NADP-Linked Isocitrate Dehydrogenase and H+ -Transhydrogenase in Heart Mitochondria .”10.1042/bst021260s__Biochemical Society Transactions, vol. 21, no. 3, Portland Press, 1993, p. 260, doi:10.1042/bst021260s.
LibreCat: https://research-explorer.ista.ac.at/record/1948
DOI: 10.1042/bst021260s
PMID: 8224412 

Jackson, Julie, et al. “Proton-Translocating Transhydrogenase in Bacteria.”10.1042/bst0211010__Biochemical Society Transactions, vol. 21, no. 4, Portland Press, 1993, pp. 1010–13, doi:10.1042/bst0211010.
LibreCat: https://research-explorer.ista.ac.at/record/1950
DOI: 10.1042/bst0211010
PMID: 8131888

Sazanov, Leonid A., and Sergei Za0tsev. “Effect of Superlow Doses (10(-18)-10-(-14) M) of Biologically Active Substances: General Rules, Features, and Possible Mechanisms.” Biochemistry (Moscow), vol. 57, no. 10, Izdatel’stvo Nauka, 1992, pp. 1443–60.
LibreCat: https://research-explorer.ista.ac.at/record/1945
PMID: 1457592 

Za0tsev, Sergei, et al. “Respiratory Burst Inhibition in Human Neutrophils by Ultra-Low Doses of [D-Al] Methionine Enkephalinamide.”10.1016/0014-5793(91)81109-L__FEBS Letters, vol. 291, no. 1, Elsevier, 1991, pp. 84–86, doi:10.1016/0014-5793(91)81109-L.
LibreCat: https://research-explorer.ista.ac.at/record/1946
DOI: 10.1016/0014-5793(91)81109-L
PMID: 1936255 

Sazanov, Leonid A., et al. “Mathematical model of photosynthesis regulation accounts for the effects of changes in external conditions and observed oscillations.” Russian Journal of Physical Chemistry B, vol. 52, Elsevier, 1988, pp. 3351–54.
LibreCat: https://research-explorer.ista.ac.at/record/1941