Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Natalya V. Strushkevich"'
Autor:
Andrey Gilep, Irina Grabovec, Vladimir I. Dolgopalets, Tatsiana Varaksa, T. V. Shkel, Yu. G. Charnou, Natalya V. Strushkevich
Publikováno v:
Proceedings of the National Academy of Sciences of Belarus, Chemical Series. 54:450-454
The interaction of human monooxygenases and pathogenic fungi with previously obtained esters of isomeric 7-methyl-19-nor-testosterones and a number of heteroaromatic acids – derivatives of pyridine and pyrazine, was studied. Interaction with the ac
Autor:
T. V. Shkel, Sergei A. Usanov, N. V. Ivanchina, A S Ivanov, Andrey Gilep, Irina Grabovec, Natalya V. Strushkevich, Alla A. Kicha, V. A. Stonik, L. A. Kaluzhskiy, Oksana Gnedenko, P V Ershov
Publikováno v:
Biomedical Chemistry: Research and Methods; Vol. 1 No. 4 (2018); e00055
Biomedical Chemistry: Research and Methods; Том 1 № 4 (2018); e00055
Biomedical Chemistry: Research and Methods
Biomedical Chemistry: Research and Methods; Том 1 № 4 (2018); e00055
Biomedical Chemistry: Research and Methods
The development of the integral platform “From Gene to Lead”, consolidated computer methods, bioinformatics researches, and experimental approaches, significantly accelerated and optimized base structure search in the field of drug design. The ne
Autor:
Ronald W. Estabrook, Natalya V. Strushkevich, Sandra E. Graham, Julian A. Peterson, Tamara N. Azeva, Andrei A. Gilep, Galina I. Lepesheva, Sergey A. Usanov
Publikováno v:
Biochemistry. 41:8310-8320
The present study was undertaken to evaluate the role of positively charged amino acid residues proposed to reside on the proximal surface of bovine cytochrome P450 cholesterol side chain cleavage (P450scc, CYP11A1) and to determine which residues ma
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1434:31-43
Bovine adrenocortical cytochrome P450scc (P450scc) was expressed in Escherichia coli and purified as the substrate bound, high-spin complex (16.7 nmol of heme per mg of protein, expression level in E. coli about 400-700 nmol/l). The recombinant prote