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Biokhimiia (Moscow, Russia)|April 1, 1987
[Kinetics of adrenodoxin reductase oxidation by non-physiologic electron acceptors]N K Chenas, I A Martsinkiavichene, Iu Iu Kulis, et al.Bioorganicheskaia Khimiia|February 1, 1986
[Molecular organization of the reductase complex in adrenal cortex mitochondria. Study using bifunctional reagents]S A Usanov, I V Turko, V L Chashchin, et al.Biochimica Et Biophysica Acta|April 29, 1985
Cross-linking studies of adrenocortical cytochrome P-450scc. Evidence for a covalent complex with adrenodoxin and localization of the adrenodoxin-binding domainV L Chashchin, I V Turko, A A Akhrem, et al.Biochimica Et Biophysica Acta|November 9, 1984
Chemical modification of adrenocortical cytochrome P-450scc with tetranitromethaneS A Usanov, I A Pikuleva, V L Chashchin, et al.Biochemistry. Biokhimiia|April 13, 2005
Engineering of proteolytically stable NADPH-cytochrome P450 reductaseT A Bonina, A A Gilep, R W Estabrook, et al.Biochemistry. Biokhimiia|October 3, 2006
Role of C-terminal sequence of cytochrome P450scc in folding and functional activityN V Strushkevich, I N Harnastai, G I Lepesheva, et al.Archives of Biochemistry and Biophysics|June 9, 2001
Expression, purification, and physical properties of recombinant flavocytochrome fusion proteins containing rat cytochrome b(5) linked to NADPH-cytochrome P450 reductase by different membrane-binding segmentsA A Gilep, O L Guryev, S A Usanov, et al.Biokhimiia (Moscow, Russia)|November 1, 1993
[Interrelationship of microsomal and mitochondrial systems for hydroxylating steroids from cattle adrenal cortex: effect of highly-purified components of the mitochondrial monoxygenase system on hydroxylation of steroids by microsomes]V M Guzov, I N Zel'ko, A A Chernogolov, et al.Biochemistry. Biokhimiia|August 19, 2008
Engineering, expression, and purification of "soluble" human cytochrome P45017alpha and its functional characterizationT A Pechurskaya, O P Lukashevich, A A Gilep, et al.Biochemistry. Biokhimiia|August 15, 2006
Expression of outer mitochondrial membrane cytochrome b5 in Escherichia coli. purification of the recombinant protein and studies of its interaction with electron-transfer partnersG V Sergeev, A A Gilep, R W Estabrook, et al.Pageof 13