Zobrazeno 1 - 10
of 86
pro vyhledávání: '"Bazhulina NP"'
Autor:
Elena A. Morozova, Yury Belyi, Natalya V. Anufrieva, S.V. Revtovich, Mikhail I. Kotlov, Vasiliy S. Koval, Bazhulina Np, Tatyana V. Demidkina, Hideyuki Hayashi, Vitalia V. Kulikova
Publikováno v:
IUBMB Life. 71:1815-1823
O-acetylhomoserine sulfhydrylase (OAHS) is a pyridoxal 5'-phosphate-dependent enzyme involved in microbial methionine biosynthesis. In this study, we report gene cloning, protein purification, and some biochemical characteristics of OAHS from Clostri
Autor:
Galegov Ga, E. D. Moiseeva, S. L. Grokhovsky, A. N. Surovaya, Bazhulina Np, G. V. Gursky, V. L. Andronova, S. Yu. Lepehina
Publikováno v:
Biophysics. 61:227-232
The binding of a dimeric distamycin analog (Pt–bis–Dst) to poly[d(A–T)]poly[d(A–T)], poly(dA)poly(dT), and duplex O23 with the sequence 5’-GCCAATATATATATATTATTAGG-3’, which occurs at the origin of replication (OriS) of the herpes simplex
Autor:
Vitalia V. Kulikova, Bazhulina Np, Gennadii B. Zavilgelsky, D I Degtev, Tatyana V. Demidkina, Natalya V. Anufrieva, E Yu Gnuchikh, Ilya V. Manukhov, Elena A. Morozova, A N Rodionov
Publikováno v:
Acta Naturae. 7:128-135
The problem of resistance to antibiotics requires the development of new classes of broad-spectrum antimicrobial drugs. The concept of pro-drugs allows researchers to look for new approaches to obtain effective drugs with improved pharmacokinetic and
Autor:
Alexei Nikulin, Elena A. Morozova, Yaroslav V. Tkachev, Nicolai G. Faleev, Vladimir P. Timofeev, Natalya V. Anufrieva, Tatyana V. Demidkina, Bazhulina Np, S.V. Revtovich
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854:1220-1228
In the spatial structure of methionine γ-lyase (MGL, EC 4.4.1.11) from Citrobacter freundii, Tyr58 is located at H-bonding distance to the oxygen atom of the phosphate “handle” of pyridoxal 5′-phosphate (PLP). It was replaced for phenylalanine
Autor:
E. D. Moiseeva, Bazhulina Np, A. N. Surovaya, Sergueï L. Grokhovsky, Y.G. Gursky, G. V. Gursky
Publikováno v:
Journal of biomolecular structuredynamics. 35(4)
In the present paper, the interactions of the origin binding protein (OBP) of herpes simplex virus type 1 (HSV1) with synthetic four-way Holliday junctions (HJs) were studied using electrophoresis mobility shift assay and the FRET method and compared
Autor:
S. L. Grokhovsky, A. M. Nikitin, Bazhulina Np, Galegov Ga, M. V. Golovkin, V. L. Andronova, A. N. Surovaya, Y.G. Gursky, V. S. Arkhipova, G. V. Gursky
Publikováno v:
Biophysics. 57:153-162
Data obtained show that antiviral activities of bis-linked netropsin derivatives are targeted by specific complexes formed by helicase UL9 of herpes simplex virus type 1 with viral DNA replication origins, represented by two OriS sites and one OriL s
Autor:
V.L. Andronova, V. S. Arkhipova, Galegov Ga, Y.G. Gursky, S. L. Grokhovsky, A. N. Surovaya, G. V. Gursky, Bazhulina Np
Publikováno v:
Biophysics. 55:204-214
The protein binding to the origin of replication of the herpes simplex virus type 1 is DNA helicase encoded by the UL9 gene of the herpes virus. The protein specifically binds to two binding sites in the viral DNA replication origins OriS or OriL. In
Publikováno v:
Biophysics. 53:344-351
The binding of Pt-bis-Nt and its modified analog Pt*-bis-Nt, which has two additional glycine residues in the linker between two netropsin fragments, to DNA has been studied. The elongation of the linker in the bis-netropsin molecule increases the cy
Publikováno v:
Doklady Biochemistry and Biophysics. 391:225-228
Autor:
Elena N. Khurs, R. M. Khomutov, Tatyana V. Demidkina, Yurii N. Zhukov, Olga Gogoleva, Bazhulina Np, Maria V. Barbolina, N. G. Faleev, Vassili M. Belikov
Publikováno v:
European Journal of Biochemistry. 267:6897-6902
The phosphinic analogues of tyrosine and pyruvate were first demonstrated to be substrates in the reactions of elimination and synthesis catalyzed by tyrosine phenol-lyase. Kinetic parameters of the enzymatic process were determined, and the first en