Vercellino I, Sazanov LA. SCA drives the compositional diversity of mammalian respirasomes. Nature Structural and Molecular Biology. 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 LA. From the ack box”10.1042/BCJ20210285__to mino effect”10.1042/BCJ20210285__mechanism: What have we learned from the structures of respiratory complex I. The Biochemical Journal. 2023;480(5):319-333. doi:10.1042/BCJ20210285
LibreCat: https://research-explorer.ista.ac.at/record/12757
DOI: 10.1042/BCJ20210285
WoS: 000957065700001
PMID: 36920092

Zhao Z, Vercellino I, Knoppová J, et al. The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis. Nature Communications. 2023;14. 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 I, Sazanov LA. The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. 2022;23:141–161. 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 D, Sazanov LA. Structure of respiratory complex I – An emerging blueprint for the mechanism. Current Opinion in Structural Biology. 2022;74. 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 D, González-Vioque E, Dibley MG, et al. Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUF subunit. Communications Biology. 2022;5(1). 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 V, Petrova O, Kampjut D, Wojciechowska-Bason A, Breese Z, Sazanov LA. A universal coupling mechanism of respiratory complex I. Nature. 2022;609(7928):808-814. 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 L, Kolb M, Stadlmann J, et al. Naphthylphthalamic acid associates with and inhibits PIN auxin transporters. PNAS. 2021;118(1). doi:10.1073/pnas.2020857118
LibreCat: https://research-explorer.ista.ac.at/record/8993
DOI: 10.1073/pnas.2020857118
WoS: 000607270100073
PMID: 33443187

Kampjut D, Steiner J, Sazanov LA. Cryo-EM grid optimization for membrane proteins. iScience. 2021;24(3). 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 I, Sazanov LA. Structure and assembly of the mammalian mitochondrial supercomplex CIII<sub>2</sub>CIV. Nature. 2021;598(7880):364-367. 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 MJW, De Haas R, Willems PHGM, et al. NDUF deletion triggers loss of NDUF in Nduf/ mice and Leigh syndrome patients: A stabilizing role for NDUFA. Biochimica et Biophysica Acta - Bioenergetics. 2020;1861(8). 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 C, Khaniya U, Chan CK, et al. Charge transfer and chemo-mechanical coupling in respiratory complex I. Journal of the American Chemical Society. 2020;142(20):9220-9230. doi:10.1021/jacs.9b13450
LibreCat: https://research-explorer.ista.ac.at/record/8040
DOI: 10.1021/jacs.9b13450
WoS: 000537415600020
PMID: 32347721

Gupta C, Khaniya U, Chan C, et al. Charge transfer and chemo-mechanical coupling in respiratory complex I. 2020. doi:10.1021/jacs.9b13450.s002
LibreCat: https://research-explorer.ista.ac.at/record/9326
DOI: 10.1021/jacs.9b13450.s002

Gupta C, Khaniya U, Chan CK, et al. Supporting information. 2020. doi:10.1021/jacs.9b13450.s001
LibreCat: https://research-explorer.ista.ac.at/record/9713
DOI: 10.1021/jacs.9b13450.s001

Gupta C, Khaniya U, Chan CK, et al. Movies. 2020. doi:10.1021/jacs.9b13450.s002
LibreCat: https://research-explorer.ista.ac.at/record/9878
DOI: 10.1021/jacs.9b13450.s002

Gutierrez-Fernandez J, Kaszuba K, Minhas GS, et al. Key role of quinone in the mechanism of respiratory complex I. Nature Communications. 2020;11(1). 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 G, Zhou L, Sazanov LA. Cryo-EM structure of the entire mammalian F-type ATP synthase. Nature Structural and Molecular Biology. 2020;27(11):1077-1085. 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 D, Sazanov LA. The coupling mechanism of mammalian respiratory complex I. Science. 2020;370(6516). doi:10.1126/science.abc4209
LibreCat: https://research-explorer.ista.ac.at/record/8737
DOI: 10.1126/science.abc4209
WoS: 000583031800004
PMID: 32972993

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

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

Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. Structures of respiratory supercomplex I+II reveal functional and conformational crosstalk. Molecular Cell. 2019;75(6):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 D, Sazanov LA. Structure and mechanism of mitochondrial proton-translocating transhydrogenase. Nature. 2019;573(7773):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 K, Sazanov LA. Mammalian mitochondrial complex I structure and disease causing mutations. Trends in Cell Biology. 2018;28(10):835-867. 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 R, Van Dam E, Cowley M, et al. Mitochondrial mutations and metabolic adaptation in pancreatic cancer. Cancer &; Metabolism. 2017;5(2). doi:10.1186/s40170-017-0164-1
LibreCat: https://research-explorer.ista.ac.at/record/443
DOI: 10.1186/s40170-017-0164-1

Sazanov LA. Structure of respiratory complex I: “Minimal”10.1039/9781788010405-00025__bacterial and luxe”10.1039/9781788010405-00025__mammalian versions. In: Wikström M, ed. Mechanisms of Primary Energy Transduction in Biology . Mechanisms of Primary Energy Transduction in Biology . Royal Society of Chemistry; 2017:25-59. doi:10.1039/9781788010405-00025
LibreCat: https://research-explorer.ista.ac.at/record/444
DOI: 10.1039/9781788010405-00025

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

Letts JA, Degliesposti G, Fiedorczuk K, Skehel M, Sazanov LA. Purification of ovine respiratory complex i results in a highly active and stable preparation. Journal of Biological Chemistry. 2016;291(47):24657-24675. doi:10.1074/jbc.M116.735142
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. Atomic structure of the entire mammalian mitochondrial complex i. Nature. 2016;538(7625):406-410. doi:10.1038/nature19794
LibreCat: https://research-explorer.ista.ac.at/record/1226
DOI: 10.1038/nature19794
PMID: 27595392

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

Holt P, Efremov R, Nakamaru Ogiso E, Sazanov LA. Reversible FMN dissociation from Escherichia coli respiratory complex I. Biochimica et Biophysica Acta - Bioenergetics. 2016;1857(11):1777-1785. 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 J, Baradaran R, Sazanov LA. Structure of bacterial respiratory complex I. Biochimica et Biophysica Acta - Bioenergetics. 2016;1857(7):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 LA. A giant molecular proton pump: structure and mechanism of respiratory complex I. Nature Reviews Molecular Cell Biology. 2015;16(6):375-388. doi:10.1038/nrm3997
LibreCat: https://research-explorer.ista.ac.at/record/1638
DOI: 10.1038/nrm3997

Letts JA, Sazanov LA. Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions. Current Opinion in Structural Biology. 2015;33(8):135-145. 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 M, Bielawski J, Sazanov LA, Gharrett A. Review and meta-analysis of natural selection in mitochondrial complex I in metazoans. Journal of Zoological Systematics and Evolutionary Research. 2014;53(1):1-17. doi:10.1111/jzs.12079
LibreCat: https://research-explorer.ista.ac.at/record/1981
DOI: 10.1111/jzs.12079

Heikal A, Nakatani Y, Dunn E, et al. Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation. Molecular Microbiology. 2014;91(5):950-964. doi:10.1111/mmi.12507
LibreCat: https://research-explorer.ista.ac.at/record/1980
DOI: 10.1111/mmi.12507

Sazanov LA. The mechanism of coupling between electron transfer and proton translocation in respiratory complex I. Journal of Bioenergetics and Biomembranes. 2014;46(4):247-253. doi:10.1007/s10863-014-9554-z
LibreCat: https://research-explorer.ista.ac.at/record/1979
DOI: 10.1007/s10863-014-9554-z

Sazanov LA, Baradaran R, Efremov R, Berrisford J, Minhas G. A long road towards the structure of respiratory complex I, a giant molecular proton pump. Biochemical Society Transactions. 2013;41(5):1265-1271. doi:10.1042/BST20130193
LibreCat: https://research-explorer.ista.ac.at/record/1977
DOI: 10.1042/BST20130193

Baradaran R, Berrisford J, Minhas G, Sazanov LA. Crystal structure of the entire respiratory complex i. Nature. 2013;494(7438):443-448. doi:10.1038/nature11871
LibreCat: https://research-explorer.ista.ac.at/record/1978
DOI: 10.1038/nature11871

Efremov R, Sazanov LA. The coupling mechanism of respiratory complex i - A structural and evolutionary perspective. Biochimica et Biophysica Acta - Bioenergetics. 2012;1817(10):1785-1795. 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 R, Sazanov LA. Structure of Escherichia coli OmpF porin from lipidic mesophase. Journal of Structural Biology. 2012;178(3):311-318. 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 C, Harbour M, Jayawardena K, Fearnley I, Sazanov LA. Evolution of respiratory complex I &;quot;Supernumerary&;quot; subunits are present in the ;1-proteobacterial enzyme. Journal of Biological Chemistry. 2011;286(7):5023-5033. doi:10.1074/jbc.M110.194993
LibreCat: https://research-explorer.ista.ac.at/record/1975
DOI: 10.1074/jbc.M110.194993

Efremov R, Sazanov LA. Structure of the membrane domain of respiratory complex i. Nature. 2011;476(7361):414-421. doi:10.1038/nature10330
LibreCat: https://research-explorer.ista.ac.at/record/1973
DOI: 10.1038/nature10330

Efremov R, Sazanov LA. Respiratory complex I: “steam engine”10.1016/j.sbi.2011.07.002__of the cell? Current Opinion in Structural Biology. 2011;21(4):532-540. 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 R, Baradaran R, Sazanov LA. The architecture of respiratory complex I. Nature. 2010;465(7297):441-445. doi:10.1038/nature09066
LibreCat: https://research-explorer.ista.ac.at/record/1970
DOI: 10.1038/nature09066

Berrisford J, Sazanov LA. Structural basis for the mechanism of respiratory complex I. Journal of Biological Chemistry. 2009;284(43):29773-29783. doi:10.1074/jbc.M109.032144
LibreCat: https://research-explorer.ista.ac.at/record/1971
DOI: 10.1074/jbc.M109.032144

Berrisford J, Thompson C, Sazanov LA. Chemical and NADH-induced, ROS-dependent, cross-linking between sublimits of complex I from Escherichia coli and Thermus thermophilus. Biochemistry. 2008;47(39):10262-10270. doi:10.1021/bi801160u
LibreCat: https://research-explorer.ista.ac.at/record/1967
DOI: 10.1021/bi801160u

Morgan D, Sazanov LA. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochimica et Biophysica Acta - Bioenergetics. 2008;1777(7-8):711-718. 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 E, Holt P, Sazanov LA. Projection structure of the membrane domain of Escherichia coli respiratory Complex I at 8 Å resolution. Journal of Molecular Biology. 2007;366(1):140-154. 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 E, Morgan D, Sazanov LA. Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I. Journal of Structural Biology. 2007;159(2 SPEC. ISS.):238-242. 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 LA. Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry. 2007;46(9):2275-2288. doi:10.1021/bi602508x
LibreCat: https://research-explorer.ista.ac.at/record/1964
DOI: 10.1021/bi602508x

Sazanov LA, Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science. 2006;311(5766):1430-1436. doi:10.1126/science.1123809
LibreCat: https://research-explorer.ista.ac.at/record/1961
DOI: 10.1126/science.1123809

Hinchliffe P, Carroll J, Sazanov LA. Identification of a novel subunit of respiratory complex I from Thermus thermophilus. Biochemistry. 2006;45(14):4413-4420. doi:10.1021/bi0600998
LibreCat: https://research-explorer.ista.ac.at/record/1966
DOI: 10.1021/bi0600998

Hinchliffe P, Sazanov LA. Biochemistry: Organization of iron-sulfur clusters in respiratory complex I. Science. 2005;309(5735):771-774. doi:10.1126/science.1113988
LibreCat: https://research-explorer.ista.ac.at/record/1962
DOI: 10.1126/science.1113988

Mamedova A, Holt P, Carroll J, Sazanov LA. Substrate-induced conformational change in bacterial complex I. Journal of Biological Chemistry. 2004;279(22):23830-23836. doi:10.1074/jbc.M401539200
LibreCat: https://research-explorer.ista.ac.at/record/1963
DOI: 10.1074/jbc.M401539200

Holt P, Morgan D, Sazanov LA. 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. 2003;278(44):43114-43120. doi:10.1074/jbc.M308247200
LibreCat: https://research-explorer.ista.ac.at/record/1959
DOI: 10.1074/jbc.M308247200

Sazanov LA, Carroll J, Holt P, Toime L, Fearnley I. 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. 2003;278(21):19483-19491. doi:10.1074/jbc.M208959200
LibreCat: https://research-explorer.ista.ac.at/record/1960
DOI: 10.1074/jbc.M208959200

Sazanov LA, Walker J. Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms. Journal of Molecular Biology. 2000;302(2):455-464. doi:10.1006/jmbi.2000.4079
LibreCat: https://research-explorer.ista.ac.at/record/1957
DOI: 10.1006/jmbi.2000.4079
PMID: 10970745

Sazanov LA, Peak Chew S, Fearnley I, Walker J. Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme. Biochemistry. 2000;39(24):7229-7235. doi:10.1021/bi000335t
LibreCat: https://research-explorer.ista.ac.at/record/1958
DOI: 10.1021/bi000335t
PMID: 10852722

Sazanov LA, Burrows P, Nixon P. The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes. PNAS. 1998;95(3):1319-1324. 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 P, Sazanov LA, Sváb Z, Maliga P, Nixon P. Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO Journal. 1998;17(4):868-876. 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 LA, Burrows P, Nixon P. The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves. FEBS Letters. 1998;429(1):115-118. 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 LA, Burrows P, Nixon PJ. Presence of a large protein complex containing the ndhK gene product and possessing NADH-specific dehydrogenase activity in thylakoid membranes of higher plant chloroplasts. In: Vol 2. Kluwer; 1996:705-708.
LibreCat: https://research-explorer.ista.ac.at/record/1942

Bizouarn T, Sazanov LA, Aubourg S, Jackson J. 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. 1996;1273(1):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 LA, Burrows P, Nixon P. Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids. Biochemical Society Transactions. 1996;24(3):739-743. doi:10.1042/bst0240739
LibreCat: https://research-explorer.ista.ac.at/record/1951
DOI: 10.1042/bst0240739
PMID: 8878837

Sazanov LA, Jackson B. 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. 1995;1231(3):304-312. 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 LA, Jackson J. 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. 1994;344(2-3):109-116. 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 A, Koshkin A, Sazanov LA, Borodulina OI, Varfolomeev S, Za0tsev S. 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. 1994;355(2):114-116. 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 LA, Jackson J. Activation and inhibition of mitochondrial transhydrogenase by metal ions. Biochimica et Biophysica Acta - Bioenergetics. 1993;1144(2):225-228. 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 LA, Jackson J. Possible functions of the NADP-linked isocitrate dehydrogenase and H+ -transhydrogenase in heart mitochondria . Biochemical Society Transactions. 1993;21(3):260. doi:10.1042/bst021260s
LibreCat: https://research-explorer.ista.ac.at/record/1948
DOI: 10.1042/bst021260s
PMID: 8224412 

Jackson J, Cotton NPJ, Williams R, et al. Proton-translocating transhydrogenase in bacteria. Biochemical Society Transactions. 1993;21(4):1010-1013. doi:10.1042/bst0211010
LibreCat: https://research-explorer.ista.ac.at/record/1950
DOI: 10.1042/bst0211010
PMID: 8131888

Sazanov LA, Za0tsev S. Effect of superlow doses (10(-18)-10-(-14) M) of biologically active substances: general rules, features, and possible mechanisms. Biochemistry (Moscow). 1992;57(10):1443-1460.
LibreCat: https://research-explorer.ista.ac.at/record/1945
PMID: 1457592 

Za0tsev S, Sazanov LA, Koshkin A, Sud’Ina G, Varfolomeev S. Respiratory burst inhibition in human neutrophils by ultra-low doses of [D-Al] methionine enkephalinamide. FEBS Letters. 1991;291(1):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 LA, Karavaev VA, Kukushkin AK. Mathematical model of photosynthesis regulation accounts for the effects of changes in external conditions and observed oscillations. Russian Journal of Physical Chemistry B. 1988;52:3351-3354.
LibreCat: https://research-explorer.ista.ac.at/record/1941