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Items: 1 to 20 of 101

1.

Cysteine residues 244 and 458-459 within the catalytic subunit of Na,K-ATPase control the enzyme's hydrolytic and signaling function under hypoxic conditions.

Petrushanko IY, Mitkevich VA, Lakunina VA, Anashkina AA, Spirin PV, Rubtsov PM, Prassolov VS, Bogdanov NB, Hänggi P, Fuller W, Makarov AA, Bogdanova A.

Redox Biol. 2017 Oct;13:310-319. doi: 10.1016/j.redox.2017.05.021. Epub 2017 May 31.

2.

S-glutathionylation of the Na,K-ATPase catalytic α subunit is a determinant of the enzyme redox sensitivity.

Petrushanko IY, Yakushev S, Mitkevich VA, Kamanina YV, Ziganshin RH, Meng X, Anashkina AA, Makhro A, Lopina OD, Gassmann M, Makarov AA, Bogdanova A.

J Biol Chem. 2012 Sep 14;287(38):32195-205. doi: 10.1074/jbc.M112.391094. Epub 2012 Jul 13.

3.

Cross talk between S-nitrosylation and S-glutathionylation in control of the Na,K-ATPase regulation in hypoxic heart.

Yakushev S, Band M, Tissot van Patot MC, Gassmann M, Avivi A, Bogdanova A.

Am J Physiol Heart Circ Physiol. 2012 Dec 1;303(11):H1332-43. doi: 10.1152/ajpheart.00145.2012. Epub 2012 Sep 14.

4.

Identification of a mutant α1 Na/K-ATPase that pumps but is defective in signal transduction.

Lai F, Madan N, Ye Q, Duan Q, Li Z, Wang S, Si S, Xie Z.

J Biol Chem. 2013 May 10;288(19):13295-304. doi: 10.1074/jbc.M113.467381. Epub 2013 Mar 26.

5.

Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.

Dergousova EA, Petrushanko IY, Klimanova EA, Mitkevich VA, Ziganshin RH, Lopina OD, Makarov AA.

Biomolecules. 2017 Feb 21;7(1). pii: E18. doi: 10.3390/biom7010018.

6.

Heterogeneity of signal transduction by Na-K-ATPase α-isoforms: role of Src interaction.

Yu H, Cui X, Zhang J, Xie JX, Banerjee M, Pierre SV, Xie Z.

Am J Physiol Cell Physiol. 2018 Feb 1;314(2):C202-C210. doi: 10.1152/ajpcell.00124.2017. Epub 2017 Nov 8.

7.
8.

Expression of rat Na-K-ATPase α2 enables ion pumping but not ouabain-induced signaling in α1-deficient porcine renal epithelial cells.

Xie J, Ye Q, Cui X, Madan N, Yi Q, Pierre SV, Xie Z.

Am J Physiol Cell Physiol. 2015 Sep 15;309(6):C373-82. doi: 10.1152/ajpcell.00103.2015. Epub 2015 Jun 24.

9.

[The ability of cells to adjust to the low oxigen content associated with Na,K-ATPase glutationilation].

Petrushanko IIu, Simonenko OV, Burnysheva KM, Klimanova EA, Dergousova EA, Mit'kevich VA, Lopina OD, Makarov AA.

Mol Biol (Mosk). 2015 Jan-Feb;49(1):175-83. Russian.

10.

Protein Carbonylation of an Amino Acid Residue of the Na/K-ATPase α1 Subunit Determines Na/K-ATPase Signaling and Sodium Transport in Renal Proximal Tubular Cells.

Yan Y, Shapiro AP, Mopidevi BR, Chaudhry MA, Maxwell K, Haller ST, Drummond CA, Kennedy DJ, Tian J, Malhotra D, Xie ZJ, Shapiro JI, Liu J.

J Am Heart Assoc. 2016 Sep 9;5(9). pii: e003675. doi: 10.1161/JAHA.116.003675.

11.

Involvement of reactive oxygen species in a feed-forward mechanism of Na/K-ATPase-mediated signaling transduction.

Yan Y, Shapiro AP, Haller S, Katragadda V, Liu L, Tian J, Basrur V, Malhotra D, Xie ZJ, Abraham NG, Shapiro JI, Liu J.

J Biol Chem. 2013 Nov 22;288(47):34249-58. doi: 10.1074/jbc.M113.461020. Epub 2013 Oct 11.

12.

Functional role of cysteine residues in the (Na,K)-ATPase alpha subunit.

Shi HG, Mikhaylova L, Zichittella AE, Argüello JM.

Biochim Biophys Acta. 2000 Apr 5;1464(2):177-87.

13.

[Enhancement of Na,K-ATPase Activity as a Result of Removal of Redox Modifications from Cysteine Residues of the al Subunit: the Effect of Reducing Agents].

Dergousova EA, Petrushanko IY, Klimanova EA, Mitkevich VA, Ziganshin RH, Lopina OD, Makarov AA.

Mol Biol (Mosk). 2018 Mar-Apr;52(2):289-293. doi: 10.7868/S002689841802012X. Russian.

14.

Basal Glutathionylation of Na,K-ATPase α-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis.

Mitkevich VA, Petrushanko IY, Poluektov YM, Burnysheva KM, Lakunina VA, Anashkina AA, Makarov AA.

Oxid Med Cell Longev. 2016;2016:9092328. doi: 10.1155/2016/9092328. Epub 2016 Apr 27.

15.

Src-independent ERK signaling through the rat α3 isoform of Na/K-ATPase.

Madan N, Xu Y, Duan Q, Banerjee M, Larre I, Pierre SV, Xie Z.

Am J Physiol Cell Physiol. 2017 Mar 1;312(3):C222-C232. doi: 10.1152/ajpcell.00199.2016. Epub 2016 Nov 30.

16.

[Changes in the receptor function of Na,K-ATPase during hypoxia and ischemia].

Lakunina VA, Burnysheva KM, Mitkevich VA, Makarov AA, Petrushanko IY.

Mol Biol (Mosk). 2017 Jan-Feb;51(1):172-179. doi: 10.7868/S0026898417010104. Russian.

17.

NaKtide, a Na/K-ATPase-derived peptide Src inhibitor, antagonizes ouabain-activated signal transduction in cultured cells.

Li Z, Cai T, Tian J, Xie JX, Zhao X, Liu L, Shapiro JI, Xie Z.

J Biol Chem. 2009 Jul 31;284(31):21066-76. doi: 10.1074/jbc.M109.013821. Epub 2009 Jun 8.

18.

Glutathionylation of Na,K-ATPase Alpha-Subunit Alters Enzyme Conformation and Sensitivity to Trypsinolysis.

Dergousova EA, Poluektov YM, Klimanova EA, Petrushanko IY, Mitkevich VA, Makarov AA, Lopina OD.

Biochemistry (Mosc). 2018 Aug;83(8):969-981. doi: 10.1134/S0006297918080084.

19.

SH2 Ligand-Like Effects of Second Cytosolic Domain of Na/K-ATPase α1 Subunit on Src Kinase.

Banerjee M, Duan Q, Xie Z.

PLoS One. 2015 Nov 9;10(11):e0142119. doi: 10.1371/journal.pone.0142119. eCollection 2015.

20.

Involvement of Na/K-ATPase in hydrogen peroxide-induced activation of the Src/ERK pathway in LLC-PK1 cells.

Wang Y, Ye Q, Liu C, Xie JX, Yan Y, Lai F, Duan Q, Li X, Tian J, Xie Z.

Free Radic Biol Med. 2014 Jun;71:415-26. doi: 10.1016/j.freeradbiomed.2014.03.036. Epub 2014 Apr 1.

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