Leonid A Sazanov

Sazanov Group

73 Publications

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[73]
2024 | Journal Article | IST-REx-ID: 15323
I. Vercellino and L. A. Sazanov, “SCAF1 drives the compositional diversity of mammalian respirasomes,” Nature Structural and Molecular Biology. Springer Nature, 2024.
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[72]
2023 | Journal Article | IST-REx-ID: 12757 | OA
L. A. Sazanov, “From the ‘black box’ to ‘domino effect’ mechanism: What have we learned from the structures of respiratory complex I,” The Biochemical Journal, vol. 480, no. 5. Portland Press, pp. 319–333, 2023.
[Published Version] View | DOI | Download Published Version (ext.) | WoS | PubMed | Europe PMC
 
[71]
2023 | Journal Article | IST-REx-ID: 14040 | OA
Z. Zhao et al., “The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis,” Nature Communications, vol. 14. Springer Nature, 2023.
[Published Version] View | Files available | DOI | WoS
 
[70]
2022 | Journal Article | IST-REx-ID: 10182
I. Vercellino and L. A. Sazanov, “The assembly, regulation and function of the mitochondrial respiratory chain,” Nature Reviews Molecular Cell Biology, vol. 23. Springer Nature, pp. 141–161, 2022.
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[69]
2022 | Journal Article | IST-REx-ID: 11167 | OA
D. Kampjut and L. A. Sazanov, “Structure of respiratory complex I – An emerging blueprint for the mechanism,” Current Opinion in Structural Biology, vol. 74. Elsevier, 2022.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[68]
2022 | Journal Article | IST-REx-ID: 11551 | OA
D. Molina-Granada et al., “Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUFA10 subunit,” Communications Biology, vol. 5, no. 1. Springer Nature, 2022.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[67]
2022 | Journal Article | IST-REx-ID: 12138 | OA
V. Kravchuk, O. Petrova, D. Kampjut, A. Wojciechowska-Bason, Z. Breese, and L. A. Sazanov, “A universal coupling mechanism of respiratory complex I,” Nature, vol. 609, no. 7928. Springer Nature, pp. 808–814, 2022.
[Submitted Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[66]
2021 | Journal Article | IST-REx-ID: 8993 | OA
L. Abas et al., “Naphthylphthalamic acid associates with and inhibits PIN auxin transporters,” PNAS, vol. 118, no. 1. National Academy of Sciences, 2021.
[Published Version] View | Files available | DOI | Download Published Version (ext.) | WoS | PubMed | Europe PMC
 
[65]
2021 | Journal Article | IST-REx-ID: 9205 | OA
D. Kampjut, J. Steiner, and L. A. Sazanov, “Cryo-EM grid optimization for membrane proteins,” iScience, vol. 24, no. 3. Elsevier, 2021.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[64]
2021 | Journal Article | IST-REx-ID: 10146
I. Vercellino and L. A. Sazanov, “Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV,” Nature, vol. 598, no. 7880. Springer Nature, pp. 364–367, 2021.
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[63]
2020 | Journal Article | IST-REx-ID: 7788 | OA
M. J. W. Adjobo-Hermans et al., “NDUFS4 deletion triggers loss of NDUFA12 in Ndufs4−/− mice and Leigh syndrome patients: A stabilizing role for NDUFAF2,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1861, no. 8. Elsevier, 2020.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[62]
2020 | Journal Article | IST-REx-ID: 8040
C. Gupta et al., “Charge transfer and chemo-mechanical coupling in respiratory complex I,” Journal of the American Chemical Society, vol. 142, no. 20. American Chemical Society, pp. 9220–9230, 2020.
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[61]
2020 | Research Data Reference | IST-REx-ID: 9326 | OA
C. Gupta et al., “Charge transfer and chemo-mechanical coupling in respiratory complex I.” American Chemical Society, 2020.
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[60]
2020 | Research Data Reference | IST-REx-ID: 9713
C. Gupta et al., “Supporting information.” American Chemical Society , 2020.
[Published Version] View | Files available | DOI
 
[59]
2020 | Research Data Reference | IST-REx-ID: 9878
C. Gupta et al., “Movies.” American Chemical Society, 2020.
[Published Version] View | Files available | DOI
 
[58]
2020 | Journal Article | IST-REx-ID: 8318 | OA
J. Gutierrez-Fernandez et al., “Key role of quinone in the mechanism of respiratory complex I,” Nature Communications, vol. 11, no. 1. Springer Nature, 2020.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[57]
2020 | Journal Article | IST-REx-ID: 8581
G. Pinke, L. Zhou, and L. A. Sazanov, “Cryo-EM structure of the entire mammalian F-type ATP synthase,” Nature Structural and Molecular Biology, vol. 27, no. 11. Springer Nature, pp. 1077–1085, 2020.
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[56]
2020 | Journal Article | IST-REx-ID: 8737 | OA
D. Kampjut and L. A. Sazanov, “The coupling mechanism of mammalian respiratory complex I,” Science, vol. 370, no. 6516. American Association for the Advancement of Science, 2020.
[Submitted Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[55]
2020 | Journal Article | IST-REx-ID: 8284 | OA
J. Steiner and L. A. Sazanov, “Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter,” eLife, vol. 9. eLife Sciences Publications, 2020.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[54]
2019 | Journal Article | IST-REx-ID: 6859
L. Zhou and L. A. Sazanov, “Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase,” Science, vol. 365, no. 6455. AAAS, 2019.
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[53]
2019 | Journal Article | IST-REx-ID: 7395 | OA
J. A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, and L. A. Sazanov, “Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk,” Molecular Cell, vol. 75, no. 6. Cell Press, p. 1131–1146.e6, 2019.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[52]
2019 | Journal Article | IST-REx-ID: 6848 | OA
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.
[Submitted Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[51]
2018 | Journal Article | IST-REx-ID: 152 | OA
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.
[Submitted Version] View | Files available | DOI | WoS
 
[50]
2017 | Journal Article | IST-REx-ID: 443 | OA
R. Hardie et al., “Mitochondrial mutations and metabolic adaptation in pancreatic cancer,” Cancer & Metabolism, vol. 5, no. 2. BioMed Central, 2017.
[Published Version] View | Files available | DOI
 
[49]
2017 | Book Chapter | IST-REx-ID: 444
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.
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[48]
2017 | Journal Article | IST-REx-ID: 515 | OA
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.
[Submitted Version] View | Files available | DOI
 
[47]
2016 | Journal Article | IST-REx-ID: 1209 | OA
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.
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[46]
2016 | Journal Article | IST-REx-ID: 1226 | OA
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.
[Submitted Version] View | DOI | Download Submitted Version (ext.) | PubMed | Europe PMC
 
[45]
2016 | Journal Article | IST-REx-ID: 1232
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.
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[44]
2016 | Journal Article | IST-REx-ID: 1288
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.
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[43]
2016 | Journal Article | IST-REx-ID: 1521
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.
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[42]
2015 | Journal Article | IST-REx-ID: 1638
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.
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[41]
2015 | Journal Article | IST-REx-ID: 1683
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.
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[40]
2014 | Book Review | IST-REx-ID: 1981
M. Garvin, J. Bielawski, L. A. Sazanov, and A. Gharrett, “Review and meta-analysis of natural selection in mitochondrial complex I in metazoans,” Journal of Zoological Systematics and Evolutionary Research, vol. 53, no. 1. Wiley-Blackwell, pp. 1–17, 2014.
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[39]
2014 | Journal Article | IST-REx-ID: 1980
A. Heikal et al., “Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation,” Molecular Microbiology, vol. 91, no. 5. Wiley-Blackwell, pp. 950–964, 2014.
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[38]
2014 | Journal Article | IST-REx-ID: 1979
L. A. Sazanov, “The mechanism of coupling between electron transfer and proton translocation in respiratory complex I,” Journal of Bioenergetics and Biomembranes, vol. 46, no. 4. Springer, pp. 247–253, 2014.
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[37]
2013 | Journal Article | IST-REx-ID: 1977
L. A. Sazanov, R. Baradaran, R. Efremov, J. Berrisford, and G. Minhas, “A long road towards the structure of respiratory complex I, a giant molecular proton pump,” Biochemical Society Transactions, vol. 41, no. 5. Portland Press, pp. 1265–1271, 2013.
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[36]
2013 | Journal Article | IST-REx-ID: 1978
R. Baradaran, J. Berrisford, G. Minhas, and L. A. Sazanov, “Crystal structure of the entire respiratory complex i,” Nature, vol. 494, no. 7438. Nature Publishing Group, pp. 443–448, 2013.
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[35]
2012 | Book Review | IST-REx-ID: 1976
R. Efremov and L. A. Sazanov, “The coupling mechanism of respiratory complex i - A structural and evolutionary perspective,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1817, no. 10. Elsevier, pp. 1785–1795, 2012.
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[34]
2012 | Journal Article | IST-REx-ID: 1972
R. Efremov and L. A. Sazanov, “Structure of Escherichia coli OmpF porin from lipidic mesophase,” Journal of Structural Biology, vol. 178, no. 3. Academic Press, pp. 311–318, 2012.
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[33]
2011 | Journal Article | IST-REx-ID: 1975
C. Yip, M. Harbour, K. Jayawardena, I. Fearnley, and L. A. Sazanov, “Evolution of respiratory complex I "Supernumerary" subunits are present in the α-proteobacterial enzyme,” Journal of Biological Chemistry, vol. 286, no. 7. American Society for Biochemistry and Molecular Biology, pp. 5023–5033, 2011.
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[32]
2011 | Journal Article | IST-REx-ID: 1973
R. Efremov and L. A. Sazanov, “Structure of the membrane domain of respiratory complex i,” Nature, vol. 476, no. 7361. Nature Publishing Group, pp. 414–421, 2011.
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[31]
2011 | Journal Article | IST-REx-ID: 1974
R. Efremov and L. A. Sazanov, “Respiratory complex I: ‘steam engine’ of the cell?,” Current Opinion in Structural Biology, vol. 21, no. 4. Elsevier, pp. 532–540, 2011.
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[30]
2010 | Journal Article | IST-REx-ID: 1970
R. Efremov, R. Baradaran, and L. A. Sazanov, “The architecture of respiratory complex I,” Nature, vol. 465, no. 7297. Nature Publishing Group, pp. 441–445, 2010.
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[29]
2009 | Journal Article | IST-REx-ID: 1971
J. Berrisford and L. A. Sazanov, “Structural basis for the mechanism of respiratory complex I,” Journal of Biological Chemistry, vol. 284, no. 43. American Society for Biochemistry and Molecular Biology, pp. 29773–29783, 2009.
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[28]
2008 | Journal Article | IST-REx-ID: 1967
J. Berrisford, C. Thompson, and L. A. Sazanov, “Chemical and NADH-induced, ROS-dependent, cross-linking between sublimits of complex I from Escherichia coli and Thermus thermophilus,” Biochemistry, vol. 47, no. 39. ACS, pp. 10262–10270, 2008.
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[27]
2008 | Journal Article | IST-REx-ID: 1968
D. Morgan and L. A. Sazanov, “Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1777, no. 7–8. Elsevier, pp. 711–718, 2008.
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[26]
2007 | Journal Article | IST-REx-ID: 1965
E. Baranova, P. Holt, and L. A. Sazanov, “Projection structure of the membrane domain of Escherichia coli respiratory Complex I at 8 Å resolution,” Journal of Molecular Biology, vol. 366, no. 1. Elsevier, pp. 140–154, 2007.
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[25]
2007 | Journal Article | IST-REx-ID: 1969
E. Baranova, D. Morgan, and L. A. Sazanov, “Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I,” Journal of Structural Biology, vol. 159, no. 2 SPEC. ISS. Academic Press, pp. 238–242, 2007.
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[24]
2007 | Journal Article | IST-REx-ID: 1964
L. A. Sazanov, “Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain,” Biochemistry, vol. 46, no. 9. ACS, pp. 2275–2288, 2007.
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[23]
2006 | Journal Article | IST-REx-ID: 1961
L. A. Sazanov and P. Hinchliffe, “Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus,” Science, vol. 311, no. 5766. American Association for the Advancement of Science, pp. 1430–1436, 2006.
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[22]
2006 | Journal Article | IST-REx-ID: 1966
P. Hinchliffe, J. Carroll, and L. A. Sazanov, “Identification of a novel subunit of respiratory complex I from Thermus thermophilus,” Biochemistry, vol. 45, no. 14. ACS, pp. 4413–4420, 2006.
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[21]
2005 | Journal Article | IST-REx-ID: 1962
P. Hinchliffe and L. A. Sazanov, “Biochemistry: Organization of iron-sulfur clusters in respiratory complex I,” Science, vol. 309, no. 5735. American Association for the Advancement of Science, pp. 771–774, 2005.
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[20]
2004 | Journal Article | IST-REx-ID: 1963
A. Mamedova, P. Holt, J. Carroll, and L. A. Sazanov, “Substrate-induced conformational change in bacterial complex I,” Journal of Biological Chemistry, vol. 279, no. 22. American Society for Biochemistry and Molecular Biology, pp. 23830–23836, 2004.
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[19]
2003 | Journal Article | IST-REx-ID: 1959
P. Holt, D. Morgan, and L. A. Sazanov, “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, vol. 278, no. 44. American Society for Biochemistry and Molecular Biology, pp. 43114–43120, 2003.
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[18]
2003 | Journal Article | IST-REx-ID: 1960
L. A. Sazanov, J. Carroll, P. Holt, L. Toime, and I. Fearnley, “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, vol. 278, no. 21. American Society for Biochemistry and Molecular Biology, pp. 19483–19491, 2003.
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[17]
2000 | Journal Article | IST-REx-ID: 1957
L. A. Sazanov and J. Walker, “Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms,” Journal of Molecular Biology, vol. 302, no. 2. Elsevier, pp. 455–464, 2000.
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[16]
2000 | Journal Article | IST-REx-ID: 1958
L. A. Sazanov, S. Peak Chew, I. Fearnley, and J. Walker, “Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme,” Biochemistry, vol. 39, no. 24. ACS, pp. 7229–7235, 2000.
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[15]
1998 | Journal Article | IST-REx-ID: 1956 | OA
L. A. Sazanov, P. Burrows, and P. Nixon, “The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes,” PNAS, vol. 95, no. 3. National Academy of Sciences, pp. 1319–1324, 1998.
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[14]
1998 | Journal Article | IST-REx-ID: 1955 | OA
P. Burrows, L. A. Sazanov, Z. Sváb, P. Maliga, and P. Nixon, “Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes,” EMBO Journal, vol. 17, no. 4. Wiley-Blackwell, pp. 868–876, 1998.
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[13]
1998 | Journal Article | IST-REx-ID: 1954
L. A. Sazanov, P. Burrows, and P. Nixon, “The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves,” FEBS Letters, vol. 429, no. 1. Elsevier, pp. 115–118, 1998.
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[12]
1996 | Conference Paper | IST-REx-ID: 1942
L. A. Sazanov, P. Burrows, and P. J. Nixon, “Presence of a large protein complex containing the ndhK gene product and possessing NADH-specific dehydrogenase activity in thylakoid membranes of higher plant chloroplasts,” presented at the IPC: International Photosynthesis Congress, 1996, vol. 2, pp. 705–708.
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[11]
1996 | Journal Article | IST-REx-ID: 1952
T. Bizouarn, L. A. Sazanov, S. Aubourg, and J. Jackson, “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, vol. 1273, no. 1. Elsevier, pp. 4–12, 1996.
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[10]
1996 | Journal Article | IST-REx-ID: 1951
L. A. Sazanov, P. Burrows, and P. Nixon, “Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids,” Biochemical Society Transactions, vol. 24, no. 3. Portland Press, pp. 739–743, 1996.
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[9]
1995 | Journal Article | IST-REx-ID: 1943 | OA
L. A. Sazanov and B. Jackson, “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, vol. 1231, no. 3. Elsevier, pp. 304–312, 1995.
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[8]
1994 | Journal Article | IST-REx-ID: 1949 | OA
L. A. Sazanov and J. 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,” FEBS Letters, vol. 344, no. 2–3. Elsevier, pp. 109–116, 1994.
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[7]
1994 | Journal Article | IST-REx-ID: 1953 | OA
A. Efanov, A. Koshkin, L. A. Sazanov, O. I. Borodulina, S. Varfolomeev, and S. Zaǐtsev, “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, vol. 355, no. 2. Elsevier, pp. 114–116, 1994.
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[6]
1993 | Journal Article | IST-REx-ID: 1947
L. A. Sazanov and J. Jackson, “Activation and inhibition of mitochondrial transhydrogenase by metal ions,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1144, no. 2. Elsevier, pp. 225–228, 1993.
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[5]
1993 | Journal Article | IST-REx-ID: 1948
L. A. Sazanov and J. Jackson, “Possible functions of the NADP-linked isocitrate dehydrogenase and H+ -transhydrogenase in heart mitochondria ,” Biochemical Society Transactions, vol. 21, no. 3. Portland Press, p. 260, 1993.
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[4]
1993 | Journal Article | IST-REx-ID: 1950
J. Jackson et al., “Proton-translocating transhydrogenase in bacteria,” Biochemical Society Transactions, vol. 21, no. 4. Portland Press, pp. 1010–1013, 1993.
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[3]
1992 | Journal Article | IST-REx-ID: 1945
L. A. Sazanov and S. Zaǐtsev, “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, pp. 1443–1460, 1992.
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[2]
1991 | Journal Article | IST-REx-ID: 1946
S. Zaǐtsev, L. A. Sazanov, A. Koshkin, G. Sud’Ina, and S. Varfolomeev, “Respiratory burst inhibition in human neutrophils by ultra-low doses of [D-Ala2] methionine enkephalinamide,” FEBS Letters, vol. 291, no. 1. Elsevier, pp. 84–86, 1991.
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[1]
1988 | Journal Article | IST-REx-ID: 1941
L. A. Sazanov, V. A. Karavaev, and A. K. Kukushkin, “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, pp. 3351–3354, 1988.
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Marked Publication(s)

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73 Publications

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[73]
2024 | Journal Article | IST-REx-ID: 15323
I. Vercellino and L. A. Sazanov, “SCAF1 drives the compositional diversity of mammalian respirasomes,” Nature Structural and Molecular Biology. Springer Nature, 2024.
View | DOI | PubMed | Europe PMC
 
[72]
2023 | Journal Article | IST-REx-ID: 12757 | OA
L. A. Sazanov, “From the ‘black box’ to ‘domino effect’ mechanism: What have we learned from the structures of respiratory complex I,” The Biochemical Journal, vol. 480, no. 5. Portland Press, pp. 319–333, 2023.
[Published Version] View | DOI | Download Published Version (ext.) | WoS | PubMed | Europe PMC
 
[71]
2023 | Journal Article | IST-REx-ID: 14040 | OA
Z. Zhao et al., “The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis,” Nature Communications, vol. 14. Springer Nature, 2023.
[Published Version] View | Files available | DOI | WoS
 
[70]
2022 | Journal Article | IST-REx-ID: 10182
I. Vercellino and L. A. Sazanov, “The assembly, regulation and function of the mitochondrial respiratory chain,” Nature Reviews Molecular Cell Biology, vol. 23. Springer Nature, pp. 141–161, 2022.
View | DOI | WoS | PubMed | Europe PMC
 
[69]
2022 | Journal Article | IST-REx-ID: 11167 | OA
D. Kampjut and L. A. Sazanov, “Structure of respiratory complex I – An emerging blueprint for the mechanism,” Current Opinion in Structural Biology, vol. 74. Elsevier, 2022.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[68]
2022 | Journal Article | IST-REx-ID: 11551 | OA
D. Molina-Granada et al., “Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUFA10 subunit,” Communications Biology, vol. 5, no. 1. Springer Nature, 2022.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[67]
2022 | Journal Article | IST-REx-ID: 12138 | OA
V. Kravchuk, O. Petrova, D. Kampjut, A. Wojciechowska-Bason, Z. Breese, and L. A. Sazanov, “A universal coupling mechanism of respiratory complex I,” Nature, vol. 609, no. 7928. Springer Nature, pp. 808–814, 2022.
[Submitted Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[66]
2021 | Journal Article | IST-REx-ID: 8993 | OA
L. Abas et al., “Naphthylphthalamic acid associates with and inhibits PIN auxin transporters,” PNAS, vol. 118, no. 1. National Academy of Sciences, 2021.
[Published Version] View | Files available | DOI | Download Published Version (ext.) | WoS | PubMed | Europe PMC
 
[65]
2021 | Journal Article | IST-REx-ID: 9205 | OA
D. Kampjut, J. Steiner, and L. A. Sazanov, “Cryo-EM grid optimization for membrane proteins,” iScience, vol. 24, no. 3. Elsevier, 2021.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[64]
2021 | Journal Article | IST-REx-ID: 10146
I. Vercellino and L. A. Sazanov, “Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV,” Nature, vol. 598, no. 7880. Springer Nature, pp. 364–367, 2021.
View | Files available | DOI | WoS | PubMed | Europe PMC
 
[63]
2020 | Journal Article | IST-REx-ID: 7788 | OA
M. J. W. Adjobo-Hermans et al., “NDUFS4 deletion triggers loss of NDUFA12 in Ndufs4−/− mice and Leigh syndrome patients: A stabilizing role for NDUFAF2,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1861, no. 8. Elsevier, 2020.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[62]
2020 | Journal Article | IST-REx-ID: 8040
C. Gupta et al., “Charge transfer and chemo-mechanical coupling in respiratory complex I,” Journal of the American Chemical Society, vol. 142, no. 20. American Chemical Society, pp. 9220–9230, 2020.
View | Files available | DOI | WoS | PubMed | Europe PMC
 
[61]
2020 | Research Data Reference | IST-REx-ID: 9326 | OA
C. Gupta et al., “Charge transfer and chemo-mechanical coupling in respiratory complex I.” American Chemical Society, 2020.
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[60]
2020 | Research Data Reference | IST-REx-ID: 9713
C. Gupta et al., “Supporting information.” American Chemical Society , 2020.
[Published Version] View | Files available | DOI
 
[59]
2020 | Research Data Reference | IST-REx-ID: 9878
C. Gupta et al., “Movies.” American Chemical Society, 2020.
[Published Version] View | Files available | DOI
 
[58]
2020 | Journal Article | IST-REx-ID: 8318 | OA
J. Gutierrez-Fernandez et al., “Key role of quinone in the mechanism of respiratory complex I,” Nature Communications, vol. 11, no. 1. Springer Nature, 2020.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[57]
2020 | Journal Article | IST-REx-ID: 8581
G. Pinke, L. Zhou, and L. A. Sazanov, “Cryo-EM structure of the entire mammalian F-type ATP synthase,” Nature Structural and Molecular Biology, vol. 27, no. 11. Springer Nature, pp. 1077–1085, 2020.
View | Files available | DOI | WoS | PubMed | Europe PMC
 
[56]
2020 | Journal Article | IST-REx-ID: 8737 | OA
D. Kampjut and L. A. Sazanov, “The coupling mechanism of mammalian respiratory complex I,” Science, vol. 370, no. 6516. American Association for the Advancement of Science, 2020.
[Submitted Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[55]
2020 | Journal Article | IST-REx-ID: 8284 | OA
J. Steiner and L. A. Sazanov, “Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter,” eLife, vol. 9. eLife Sciences Publications, 2020.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[54]
2019 | Journal Article | IST-REx-ID: 6859
L. Zhou and L. A. Sazanov, “Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase,” Science, vol. 365, no. 6455. AAAS, 2019.
View | Files available | DOI | WoS | PubMed | Europe PMC
 
[53]
2019 | Journal Article | IST-REx-ID: 7395 | OA
J. A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, and L. A. Sazanov, “Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk,” Molecular Cell, vol. 75, no. 6. Cell Press, p. 1131–1146.e6, 2019.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[52]
2019 | Journal Article | IST-REx-ID: 6848 | OA
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.
[Submitted Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[51]
2018 | Journal Article | IST-REx-ID: 152 | OA
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.
[Submitted Version] View | Files available | DOI | WoS
 
[50]
2017 | Journal Article | IST-REx-ID: 443 | OA
R. Hardie et al., “Mitochondrial mutations and metabolic adaptation in pancreatic cancer,” Cancer & Metabolism, vol. 5, no. 2. BioMed Central, 2017.
[Published Version] View | Files available | DOI
 
[49]
2017 | Book Chapter | IST-REx-ID: 444
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.
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 515 | OA
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.
[Submitted Version] View | Files available | DOI
 
[47]
2016 | Journal Article | IST-REx-ID: 1209 | OA
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.
[Submitted Version] View | DOI | Download Submitted Version (ext.)
 
[46]
2016 | Journal Article | IST-REx-ID: 1226 | OA
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.
[Submitted Version] View | DOI | Download Submitted Version (ext.) | PubMed | Europe PMC
 
[45]
2016 | Journal Article | IST-REx-ID: 1232
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.
View | DOI
 
[44]
2016 | Journal Article | IST-REx-ID: 1288
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.
View | DOI
 
[43]
2016 | Journal Article | IST-REx-ID: 1521
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.
View | DOI
 
[42]
2015 | Journal Article | IST-REx-ID: 1638
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.
View | DOI
 
[41]
2015 | Journal Article | IST-REx-ID: 1683
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.
View | DOI
 
[40]
2014 | Book Review | IST-REx-ID: 1981
M. Garvin, J. Bielawski, L. A. Sazanov, and A. Gharrett, “Review and meta-analysis of natural selection in mitochondrial complex I in metazoans,” Journal of Zoological Systematics and Evolutionary Research, vol. 53, no. 1. Wiley-Blackwell, pp. 1–17, 2014.
View | DOI
 
[39]
2014 | Journal Article | IST-REx-ID: 1980
A. Heikal et al., “Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation,” Molecular Microbiology, vol. 91, no. 5. Wiley-Blackwell, pp. 950–964, 2014.
View | DOI
 
[38]
2014 | Journal Article | IST-REx-ID: 1979
L. A. Sazanov, “The mechanism of coupling between electron transfer and proton translocation in respiratory complex I,” Journal of Bioenergetics and Biomembranes, vol. 46, no. 4. Springer, pp. 247–253, 2014.
View | DOI
 
[37]
2013 | Journal Article | IST-REx-ID: 1977
L. A. Sazanov, R. Baradaran, R. Efremov, J. Berrisford, and G. Minhas, “A long road towards the structure of respiratory complex I, a giant molecular proton pump,” Biochemical Society Transactions, vol. 41, no. 5. Portland Press, pp. 1265–1271, 2013.
View | DOI
 
[36]
2013 | Journal Article | IST-REx-ID: 1978
R. Baradaran, J. Berrisford, G. Minhas, and L. A. Sazanov, “Crystal structure of the entire respiratory complex i,” Nature, vol. 494, no. 7438. Nature Publishing Group, pp. 443–448, 2013.
View | DOI
 
[35]
2012 | Book Review | IST-REx-ID: 1976
R. Efremov and L. A. Sazanov, “The coupling mechanism of respiratory complex i - A structural and evolutionary perspective,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1817, no. 10. Elsevier, pp. 1785–1795, 2012.
View | DOI
 
[34]
2012 | Journal Article | IST-REx-ID: 1972
R. Efremov and L. A. Sazanov, “Structure of Escherichia coli OmpF porin from lipidic mesophase,” Journal of Structural Biology, vol. 178, no. 3. Academic Press, pp. 311–318, 2012.
View | DOI
 
[33]
2011 | Journal Article | IST-REx-ID: 1975
C. Yip, M. Harbour, K. Jayawardena, I. Fearnley, and L. A. Sazanov, “Evolution of respiratory complex I "Supernumerary" subunits are present in the α-proteobacterial enzyme,” Journal of Biological Chemistry, vol. 286, no. 7. American Society for Biochemistry and Molecular Biology, pp. 5023–5033, 2011.
View | DOI
 
[32]
2011 | Journal Article | IST-REx-ID: 1973
R. Efremov and L. A. Sazanov, “Structure of the membrane domain of respiratory complex i,” Nature, vol. 476, no. 7361. Nature Publishing Group, pp. 414–421, 2011.
View | DOI
 
[31]
2011 | Journal Article | IST-REx-ID: 1974
R. Efremov and L. A. Sazanov, “Respiratory complex I: ‘steam engine’ of the cell?,” Current Opinion in Structural Biology, vol. 21, no. 4. Elsevier, pp. 532–540, 2011.
View | DOI
 
[30]
2010 | Journal Article | IST-REx-ID: 1970
R. Efremov, R. Baradaran, and L. A. Sazanov, “The architecture of respiratory complex I,” Nature, vol. 465, no. 7297. Nature Publishing Group, pp. 441–445, 2010.
View | DOI
 
[29]
2009 | Journal Article | IST-REx-ID: 1971
J. Berrisford and L. A. Sazanov, “Structural basis for the mechanism of respiratory complex I,” Journal of Biological Chemistry, vol. 284, no. 43. American Society for Biochemistry and Molecular Biology, pp. 29773–29783, 2009.
View | DOI
 
[28]
2008 | Journal Article | IST-REx-ID: 1967
J. Berrisford, C. Thompson, and L. A. Sazanov, “Chemical and NADH-induced, ROS-dependent, cross-linking between sublimits of complex I from Escherichia coli and Thermus thermophilus,” Biochemistry, vol. 47, no. 39. ACS, pp. 10262–10270, 2008.
View | DOI
 
[27]
2008 | Journal Article | IST-REx-ID: 1968
D. Morgan and L. A. Sazanov, “Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1777, no. 7–8. Elsevier, pp. 711–718, 2008.
View | DOI
 
[26]
2007 | Journal Article | IST-REx-ID: 1965
E. Baranova, P. Holt, and L. A. Sazanov, “Projection structure of the membrane domain of Escherichia coli respiratory Complex I at 8 Å resolution,” Journal of Molecular Biology, vol. 366, no. 1. Elsevier, pp. 140–154, 2007.
View | DOI
 
[25]
2007 | Journal Article | IST-REx-ID: 1969
E. Baranova, D. Morgan, and L. A. Sazanov, “Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I,” Journal of Structural Biology, vol. 159, no. 2 SPEC. ISS. Academic Press, pp. 238–242, 2007.
View | DOI
 
[24]
2007 | Journal Article | IST-REx-ID: 1964
L. A. Sazanov, “Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain,” Biochemistry, vol. 46, no. 9. ACS, pp. 2275–2288, 2007.
View | DOI
 
[23]
2006 | Journal Article | IST-REx-ID: 1961
L. A. Sazanov and P. Hinchliffe, “Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus,” Science, vol. 311, no. 5766. American Association for the Advancement of Science, pp. 1430–1436, 2006.
View | DOI
 
[22]
2006 | Journal Article | IST-REx-ID: 1966
P. Hinchliffe, J. Carroll, and L. A. Sazanov, “Identification of a novel subunit of respiratory complex I from Thermus thermophilus,” Biochemistry, vol. 45, no. 14. ACS, pp. 4413–4420, 2006.
View | DOI
 
[21]
2005 | Journal Article | IST-REx-ID: 1962
P. Hinchliffe and L. A. Sazanov, “Biochemistry: Organization of iron-sulfur clusters in respiratory complex I,” Science, vol. 309, no. 5735. American Association for the Advancement of Science, pp. 771–774, 2005.
View | DOI
 
[20]
2004 | Journal Article | IST-REx-ID: 1963
A. Mamedova, P. Holt, J. Carroll, and L. A. Sazanov, “Substrate-induced conformational change in bacterial complex I,” Journal of Biological Chemistry, vol. 279, no. 22. American Society for Biochemistry and Molecular Biology, pp. 23830–23836, 2004.
View | DOI
 
[19]
2003 | Journal Article | IST-REx-ID: 1959
P. Holt, D. Morgan, and L. A. Sazanov, “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, vol. 278, no. 44. American Society for Biochemistry and Molecular Biology, pp. 43114–43120, 2003.
View | DOI
 
[18]
2003 | Journal Article | IST-REx-ID: 1960
L. A. Sazanov, J. Carroll, P. Holt, L. Toime, and I. Fearnley, “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, vol. 278, no. 21. American Society for Biochemistry and Molecular Biology, pp. 19483–19491, 2003.
View | DOI
 
[17]
2000 | Journal Article | IST-REx-ID: 1957
L. A. Sazanov and J. Walker, “Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms,” Journal of Molecular Biology, vol. 302, no. 2. Elsevier, pp. 455–464, 2000.
View | DOI | PubMed | Europe PMC
 
[16]
2000 | Journal Article | IST-REx-ID: 1958
L. A. Sazanov, S. Peak Chew, I. Fearnley, and J. Walker, “Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme,” Biochemistry, vol. 39, no. 24. ACS, pp. 7229–7235, 2000.
View | DOI | PubMed | Europe PMC
 
[15]
1998 | Journal Article | IST-REx-ID: 1956 | OA
L. A. Sazanov, P. Burrows, and P. Nixon, “The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes,” PNAS, vol. 95, no. 3. National Academy of Sciences, pp. 1319–1324, 1998.
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[14]
1998 | Journal Article | IST-REx-ID: 1955 | OA
P. Burrows, L. A. Sazanov, Z. Sváb, P. Maliga, and P. Nixon, “Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes,” EMBO Journal, vol. 17, no. 4. Wiley-Blackwell, pp. 868–876, 1998.
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[13]
1998 | Journal Article | IST-REx-ID: 1954
L. A. Sazanov, P. Burrows, and P. Nixon, “The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves,” FEBS Letters, vol. 429, no. 1. Elsevier, pp. 115–118, 1998.
View | DOI | PubMed | Europe PMC
 
[12]
1996 | Conference Paper | IST-REx-ID: 1942
L. A. Sazanov, P. Burrows, and P. J. Nixon, “Presence of a large protein complex containing the ndhK gene product and possessing NADH-specific dehydrogenase activity in thylakoid membranes of higher plant chloroplasts,” presented at the IPC: International Photosynthesis Congress, 1996, vol. 2, pp. 705–708.
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[11]
1996 | Journal Article | IST-REx-ID: 1952
T. Bizouarn, L. A. Sazanov, S. Aubourg, and J. Jackson, “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, vol. 1273, no. 1. Elsevier, pp. 4–12, 1996.
View | DOI | PubMed | Europe PMC
 
[10]
1996 | Journal Article | IST-REx-ID: 1951
L. A. Sazanov, P. Burrows, and P. Nixon, “Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids,” Biochemical Society Transactions, vol. 24, no. 3. Portland Press, pp. 739–743, 1996.
View | DOI | PubMed | Europe PMC
 
[9]
1995 | Journal Article | IST-REx-ID: 1943 | OA
L. A. Sazanov and B. Jackson, “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, vol. 1231, no. 3. Elsevier, pp. 304–312, 1995.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[8]
1994 | Journal Article | IST-REx-ID: 1949 | OA
L. A. Sazanov and J. 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,” FEBS Letters, vol. 344, no. 2–3. Elsevier, pp. 109–116, 1994.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[7]
1994 | Journal Article | IST-REx-ID: 1953 | OA
A. Efanov, A. Koshkin, L. A. Sazanov, O. I. Borodulina, S. Varfolomeev, and S. Zaǐtsev, “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, vol. 355, no. 2. Elsevier, pp. 114–116, 1994.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[6]
1993 | Journal Article | IST-REx-ID: 1947
L. A. Sazanov and J. Jackson, “Activation and inhibition of mitochondrial transhydrogenase by metal ions,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1144, no. 2. Elsevier, pp. 225–228, 1993.
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[5]
1993 | Journal Article | IST-REx-ID: 1948
L. A. Sazanov and J. Jackson, “Possible functions of the NADP-linked isocitrate dehydrogenase and H+ -transhydrogenase in heart mitochondria ,” Biochemical Society Transactions, vol. 21, no. 3. Portland Press, p. 260, 1993.
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[4]
1993 | Journal Article | IST-REx-ID: 1950
J. Jackson et al., “Proton-translocating transhydrogenase in bacteria,” Biochemical Society Transactions, vol. 21, no. 4. Portland Press, pp. 1010–1013, 1993.
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[3]
1992 | Journal Article | IST-REx-ID: 1945
L. A. Sazanov and S. Zaǐtsev, “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, pp. 1443–1460, 1992.
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[2]
1991 | Journal Article | IST-REx-ID: 1946
S. Zaǐtsev, L. A. Sazanov, A. Koshkin, G. Sud’Ina, and S. Varfolomeev, “Respiratory burst inhibition in human neutrophils by ultra-low doses of [D-Ala2] methionine enkephalinamide,” FEBS Letters, vol. 291, no. 1. Elsevier, pp. 84–86, 1991.
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[1]
1988 | Journal Article | IST-REx-ID: 1941
L. A. Sazanov, V. A. Karavaev, and A. K. Kukushkin, “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, pp. 3351–3354, 1988.
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