Zobrazeno 1 - 10
of 14
pro vyhledávání: '"E A, Dergousova"'
Autor:
Yuri M. Poluektov, Irina Yu. Petrushanko, Olga D. Lopina, E. A. Dergousova, Alexander A. Makarov, Vladimir A. Mitkevich
Publikováno v:
Biochemical and Biophysical Research Communications. 510:86-90
The functioning of the N, K-ATPase depends on the redox status of cells and its activity is inhibited by oxidative stress and hypoxia. We previously found that redox sensitivity of the Na,K-ATPase is mediated by glutathionylation of the α-subunit. A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d27b7564120ae1d00730a426f03462ec
https://doi.org/10.1016/j.bbrc.2019.01.052
https://doi.org/10.1016/j.bbrc.2019.01.052
Autor:
Vladimir A. Mitkevich, Alexander A. Makarov, Rustam H. Ziganshin, E. A. Dergousova, I. Yu. Petrushanko, E. A. Klimanova, Olga D. Lopina
Publikováno v:
Molecular Biology. 52:247-250
Na,K-ATPase is a transmembrane enzyme that creates a gradient of sodium and potassium, which is necessary for the viability of animal cells. The activity of Na,K-ATPase depends on the redox status of the cell, decreasing with oxidative stress and hyp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85135d708e6f945fa015f5dbdd673274
https://doi.org/10.1134/s0026893318020024
https://doi.org/10.1134/s0026893318020024
Publikováno v:
Biochemistry (Moscow). 81:249-254
It was shown earlier that a 67-kDa protein purified from mouse kidney using polyclonal antibodies against melittin (a peptide from bee venom) interacted with Na,K-ATPase from rabbit kidney. In this study, a 43-kDa proteolytic fragment of Na,K-ATPase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3f5aa611af948d60fc7f08bf0dd9b26
https://doi.org/10.1134/s000629791603007x
https://doi.org/10.1134/s000629791603007x
Autor:
Yuri M. Poluektov, Olga D. Lopina, Irina Yu. Petrushanko, A. A. Makarov, Vladimir A. Mitkevich, E. A. Klimanova, E. A. Dergousova
Publikováno v:
Biochemistry. Biokhimiia. 83(8)
We found earlier that Na,K-ATPase is purified from duck salt glands in partially glutathionylated state (up to 13 of the 23 cysteine residues of the Na,K-ATPase catalytic α-subunit can be S-glutathionylated). To determine the effect of glutathionyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7d3b0cd764cb23a03e2febb13060024
https://pubmed.ncbi.nlm.nih.gov/30208833
https://pubmed.ncbi.nlm.nih.gov/30208833
Autor:
Rustam H. Ziganshin, E. A. Klimanova, E. A. Dergousova, Irina Yu. Petrushanko, Alexander A. Makarov, Olga D. Lopina, Vladimir A. Mitkevich
Publikováno v:
Biomolecules; Volume 7; Issue 1; Pages: 18
Biomolecules, Vol 7, Iss 1, p 18 (2017)
Biomolecules
Biomolecules, Vol 7, Iss 1, p 18 (2017)
Biomolecules
Sodium-potassium adenosine triphosphatase (Na,K-ATPase) creates a gradient of sodium and potassium ions necessary for the viability of animal cells, and it is extremely sensitive to intracellular redox status. Earlier we found that regulatory glutath
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b6da577d789f8c57d7de78d069e31c
Autor:
E A, Dergousova, I Yu, Petrushanko, E A, Klimanova, V A, Mitkevich, R H, Ziganshin, O D, Lopina, A A, Makarov
Publikováno v:
Molekuliarnaia biologiia. 52(2)
Na,K-ATPase is a transmembrane enzyme that creates a gradient of sodium and potassium, which is necessary for the viability of animal cells. The activity of Na,K-ATPase depends on the redox status of the cell, decreasing with oxidative stress and hyp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6cbfe11d9f048ffac205a353d9bfb07d
https://pubmed.ncbi.nlm.nih.gov/29695697
https://pubmed.ncbi.nlm.nih.gov/29695697
Autor:
Omolara O. Ogunshola, Irina Yu. Petrushanko, Yulia V. Kamanina, Valentina A. Lakunina, E. A. Dergousova, K. M. Burnysheva, Olga D. Lopina, Alexander A. Makarov, Anastasia A. Anashkina, Vladimir A. Mitkevich, Alexei A. Adzhubei, Anna Bogdanova
Publikováno v:
Scientific Reports
By maintaining the Na+ and K+ transmembrane gradient mammalian Na,K-ATPase acts as a key regulator of neuronal electrotonic properties. Na,K-ATPase has an important role in synaptic transmission and memory formation. Accumulation of beta-amyloid (Aβ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e3452b8aa4082d064f94c1ac5f255e0
Autor:
I Iu, Petrushanko, O V, Simonenko, K M, Burnysheva, E A, Klimanova, E A, Dergousova, V A, Mit'kevich, O D, Lopina, A A, Makarov
Publikováno v:
Molekuliarnaia biologiia. 49(1)
Decreasing the amount of oxygen in the tissues under hypoxic and ischemic conditions, observed at a number of pathologic processes, inevitably leads to their damage. One of the main causes of cell damage and death is a violation of the systems mainta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0973429b281eb92908dfceb1cbf7e6c3
https://pubmed.ncbi.nlm.nih.gov/25916122
https://pubmed.ncbi.nlm.nih.gov/25916122
Autor:
Irina Yu. Petrushanko, Anastasia A. Anashkina, E. A. Dergousova, E. A. Klimanova, Vladimir A. Mitkevich, Alexander A. Makarov, Olga D. Lopina
Publikováno v:
Scientific Reports
Active transport of sodium and potassium ions by Na,K-ATPase is accompanied by the enzyme conformational transition between E1 and E2 states. ATP and ADP bind to Na,K-ATPase in the E1 conformation with similar affinity but the properties of enzyme in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6a0e5a613aaafcc697e7288198d0eb0
https://doi.org/10.1038/srep05165
https://doi.org/10.1038/srep05165
Publikováno v:
Biochemistry. Biokhimiia. 79(2)
A partially purified Na,K-ATPase preparation from rat heart containing α1- and α2-isoforms of the enzyme was shown to include both subunits in S-glutathionylated state. Glutathionylation of the α1-subunit (but not of the α2-subunit) was partially
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adff09e633af01862f98134034f6f88d
https://pubmed.ncbi.nlm.nih.gov/24794731
https://pubmed.ncbi.nlm.nih.gov/24794731