Zobrazeno 1 - 10
of 36
pro vyhledávání: '"E V, Lukasheva"'
Autor:
H. M. Treshalina, N. V. Andronova, J. R. Tcherkassova, E. Yu. Klinski, G. Babayeva, E. V. Lukasheva, M. I. Treshchalin, S. A. Tsurkan
Publikováno v:
Сибирский онкологический журнал, Vol 18, Iss 6, Pp 75-81 (2020)
Introduction. the ability of the small intestine (internalization) to absorb water-soluble anticancer cytostatics determines the possibility of their oral administration. the ex-vivo express method that simulates the internalization of substances usi
Externí odkaz:
https://doaj.org/article/63a8968c442b412ca10b74da86b9b6ae
Autor:
S Sh Karshieva, E. V. Lukasheva, A. Yu. Arinbasarova, Vadim S. Pokrovsky, M V Komarova, A. G. Medentzev, Gulalek Babayeva, Alexander N. Lukashev
Publikováno v:
Amino Acids. 53:111-118
L-lysine α-oxidase (LO) is an L-amino acid oxidase with antitumor, antimicrobial and antiviral properties. Pharmacokinetic (PK) studies were carried out by measuring LO concentration in plasma and tissue samples by enzyme immunoassay. L-lysine conce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb5362bc606bd5838d6dc9043568f47c
https://doi.org/10.1007/s00726-020-02930-4
https://doi.org/10.1007/s00726-020-02930-4
Autor:
Andrey A. Zamyatnin, E. V. Lukasheva, Elena Strekalova, Olga E. Chepikova, Vincent L. Cryns, Dmitry Malin
Publikováno v:
Breast Cancer Res Treat
PURPOSE: Transformed cells are vulnerable to depletion of certain amino acids. Lysine oxidase (LO) catalyzes the oxidative deamination of lysine, resulting in lysine depletion and hydrogen peroxide production. Although LO has broad antitumor activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1729c558eafb00e271bd76e709082d9d
https://doi.org/10.1007/s10549-020-05801-4
https://doi.org/10.1007/s10549-020-05801-4
Autor:
Gulalek Babayeva, A. G. Medentsev, Marina G Makletsova, Alexander N. Lukashev, Anna Yu. Arinbasarova, E. V. Lukasheva
Publikováno v:
Pharmaceuticals, Vol 13, Iss 398, p 398 (2020)
Pharmaceuticals
Volume 13
Issue 11
Pharmaceuticals
Volume 13
Issue 11
The fungal glycoprotein l-lysine &alpha
oxidase (LO) catalyzes the oxidative deamination of l-lysine (l-lys). LO may be internalized in the intestine and shows antitumor, antibacterial, and antiviral effects in vivo. The main mechanisms of its e
oxidase (LO) catalyzes the oxidative deamination of l-lysine (l-lys). LO may be internalized in the intestine and shows antitumor, antibacterial, and antiviral effects in vivo. The main mechanisms of its e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f37753aea326902052dbadd7c9b8cfe
https://www.mdpi.com/1424-8247/13/11/398
https://www.mdpi.com/1424-8247/13/11/398
Autor:
V S, Pokrovsky, A N, Lukashev, G, Babayeva, S Sh, Karshieva, A Yu, Arinbasarova, A G, Medentzev, M V, Komarova, E V, Lukasheva
Publikováno v:
Amino acids. 53(1)
L-lysine α-oxidase (LO) is an L-amino acid oxidase with antitumor, antimicrobial and antiviral properties. Pharmacokinetic (PK) studies were carried out by measuring LO concentration in plasma and tissue samples by enzyme immunoassay. L-lysine conce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::88100d9759252f3189bf10939b08c842
https://pubmed.ncbi.nlm.nih.gov/33398529
https://pubmed.ncbi.nlm.nih.gov/33398529
Publikováno v:
Pharmaceuticals
Pharmaceuticals, Vol 14, Iss 1070, p 1070 (2021)
Pharmaceuticals, Vol 14, Iss 1070, p 1070 (2021)
L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H2O2, ammonia, and α-keto-ε-aminocaproate. Multiple in vitro and in vivo studies have reported cytotoxic, antitumor, antimetastatic, and antitumor activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09002359a30b083f91ff09aca76c1634
https://doi.org/10.3390/ph14111070
https://doi.org/10.3390/ph14111070
Publikováno v:
Biochemistry and Biophysics Reports, Vol 9, Iss C, Pp 9-12 (2017)
The present work aims to investigate the kinetic characteristics of homodimer enzyme L-lysine α-oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D, taking into account allosteric effects. The enzyme was first shown to reveal positive coopera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83a6b476f27f77839d1e73baf5fe1cbb
Autor:
E. V. Lukasheva, Tatiana N. Fedorova, Temirbolat T. Berezov, Yu. S. Ribakova, A. Yu. Arinbasarova, A. G. Medentzev, M. G. Makletsova
Publikováno v:
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry. 8:130-133
L-Amino acid oxidases (L-AAO; EC 1.4.3.2) comprise a group of flavoproteins that catalyze oxidative deamination of L-alpha amino acids to corresponding alpha-keto acids, NH3 and H2O2. Most of these enzymes are homodimers with molecular mass of 100–
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8fc208d464ecb6d90fa64c26a1c21768
https://doi.org/10.1134/s1990750814020061
https://doi.org/10.1134/s1990750814020061
Publikováno v:
Microbiology. 81:684-687
In this article, we report on Some physiological aspects of the synthesis of extracellular L-lysine-α-oxidase (LO) by the fungus Trichoderma cf. aureoviride Rifai VKM F-4268D under salt stress conditions and discuss the possible role of this enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad0e4330acd320e10f340a469c4cf95c
https://doi.org/10.1134/s0026261712050025
https://doi.org/10.1134/s0026261712050025
Autor:
A. Yu. Arinbasarova, K. V. Makrushin, E. V. Lukasheva, A. G. Medentsev, V. V. Ashin, T. T. Berezov
Publikováno v:
Microbiology. 81:549-554
L-lysine-α-oxidase (LO) synthesized by the fungus Trichoderma cf. aureoviride Rifai VKM F-4268D under salt stress conditions was isolated and characterized. The newly developed method for the isolation and purification of the enzyme was based on its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bc24c977dfa247de60893be01e6c32a
https://doi.org/10.1134/s0026261712050037
https://doi.org/10.1134/s0026261712050037