Oleynikov I, Firsov A, Azarkina N, Vygodina T
Int J Mol Sci. 2025; 26(2).
PMID: 39859248
PMC: 11765261.
DOI: 10.3390/ijms26020533.
Oleynikov I, Sudakov R, Radyukhin V, Arutyunyan A, Azarkina N, Vygodina T
Int J Mol Sci. 2023; 24(4).
PMID: 36835528
PMC: 9961948.
DOI: 10.3390/ijms24044119.
Oleynikov I, Sudakov R, Azarkina N, Vygodina T
Cells. 2022; 11(5).
PMID: 35269529
PMC: 8909594.
DOI: 10.3390/cells11050908.
Oleynikov I, Azarkina N, Vygodina T, Konstantinov A
Cells. 2020; 9(10).
PMID: 33003582
PMC: 7601700.
DOI: 10.3390/cells9102211.
Glancy B, Kane D, Kavazis A, Goodwin M, Willis W, Gladden L
J Physiol. 2020; 599(3):863-888.
PMID: 32358865
PMC: 8439166.
DOI: 10.1113/JP278930.
Functional and structural evaluation of bovine heart cytochrome c oxidase incorporated into bicelles.
Musatov A, Siposova K, Kubovcikova M, Lysakova V, Varhac R
Biochimie. 2015; 121:21-8.
PMID: 26616009
PMC: 4724332.
DOI: 10.1016/j.biochi.2015.11.018.
Bound cardiolipin is essential for cytochrome c oxidase proton translocation.
Musatov A, Robinson N
Biochimie. 2014; 105:159-64.
PMID: 25038566
PMC: 4163530.
DOI: 10.1016/j.biochi.2014.07.005.
Direct regulation of cytochrome c oxidase by calcium ions.
Vygodina T, Kirichenko A, Konstantinov A
PLoS One. 2013; 8(9):e74436.
PMID: 24058566
PMC: 3769247.
DOI: 10.1371/journal.pone.0074436.
Dual effect of heparin on Fe²⁺-induced cardiolipin peroxidation: implications for peroxidation of cytochrome c oxidase bound cardiolipin.
Musatov A
J Biol Inorg Chem. 2013; 18(7):729-37.
PMID: 23842788
PMC: 3783530.
DOI: 10.1007/s00775-013-1019-z.
Biogenesis and assembly of eukaryotic cytochrome c oxidase catalytic core.
Soto I, Fontanesi F, Liu J, Barrientos A
Biochim Biophys Acta. 2011; 1817(6):883-97.
PMID: 21958598
PMC: 3262112.
DOI: 10.1016/j.bbabio.2011.09.005.
Sequential dissociation of subunits from bovine heart cytochrome C oxidase by urea.
Sedlak E, Robinson N
Biochemistry. 2009; 48(34):8143-50.
PMID: 19663452
PMC: 2745730.
DOI: 10.1021/bi900773r.
Succinylated bovine heart mitochondrial cytochrome c oxidase.
Hillman K, WAINIO W
J Bioenerg Biomembr. 1977; 9(3):181-93.
PMID: 18265515
DOI: 10.1007/BF00743192.
A study of the intracellular organization of comuton regulation of mitochondrial processes in rat liver.
Elbakidze G, Medentsev A, Elbakidze A, Sharishev A
Dokl Biochem Biophys. 2006; 408:180-3.
PMID: 16913424
DOI: 10.1134/s1607672906030197.
Photolabeling of cardiolipin binding subunits within bovine heart cytochrome c oxidase.
Sedlak E, Panda M, Dale M, Weintraub S, Robinson N
Biochemistry. 2006; 45(3):746-54.
PMID: 16411750
PMC: 2561917.
DOI: 10.1021/bi050870z.
Conformational coupling in H+-pumps and ATP synthesis--its analysis with anisotropic inhibitors of energy transduction in oxidative phosphorylation.
Higuti T
Mol Cell Biochem. 1984; 61(1):37-61.
PMID: 6323966
DOI: 10.1007/BF00239605.
Crystallization of mitochondrial cytochrome oxidase.
Ozawa T, Tanaka M, Wakabayashi T
Proc Natl Acad Sci U S A. 1982; 79(23):7175-9.
PMID: 6296822
PMC: 347301.
DOI: 10.1073/pnas.79.23.7175.
On the enzymic mechanism of oxidative phosphorylation.
Green D, Vande Zande H
Proc Natl Acad Sci U S A. 1982; 79(4):1064-8.
PMID: 6280165
PMC: 345900.
DOI: 10.1073/pnas.79.4.1064.
Studies on the resolution of cytochrome oxidase.
Fry M, Green D
J Bioenerg Biomembr. 1981; 13(1-2):61-87.
PMID: 6262295
DOI: 10.1007/BF00744747.
Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase--cytochrome c complex.
Ozawa T, Suzuki H, Tanaka M
Proc Natl Acad Sci U S A. 1980; 77(2):928-30.
PMID: 6244593
PMC: 348395.
DOI: 10.1073/pnas.77.2.928.
The murine toxin of Pasteurella pestis: a study in its development.
Kadis S, MONTIE T, AJL S
Bacteriol Rev. 1966; 30(1):177-91.
PMID: 5324646
PMC: 378222.
DOI: 10.1128/br.30.1.177-191.1966.