Cargando…

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

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 glutathionylation determines Na,K-ATPase redox sensitivit...

Descripción completa

Detalles Bibliográficos
Autores principales:	Dergousova, Elena A., Petrushanko, Irina Yu., Klimanova, Elizaveta A., Mitkevich, Vladimir A., Ziganshin, Rustam H., Lopina, Olga D., Makarov, Alexander A.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2017
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5372730/ https://www.ncbi.nlm.nih.gov/pubmed/28230807 http://dx.doi.org/10.3390/biom7010018

Ejemplares similares

Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding
por: Petrushanko, Irina Yu., et al.
Publicado: (2014)

Depth of the Steroid Core Location Determines the Mode of Na,K-ATPase Inhibition by Cardiotonic Steroids
por: Tverskoi, Artem M., et al.
Publicado: (2021)

Basal Glutathionylation of Na,K-ATPase α-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis
por: Mitkevich, Vladimir A., et al.
Publicado: (2016)

Direct interaction of beta-amyloid with Na,K-ATPase as a putative regulator of the enzyme function
por: Petrushanko, Irina Yu., et al.
Publicado: (2016)

Phosphorylation of the Amyloid-Beta Peptide Inhibits Zinc-Dependent Aggregation, Prevents Na,K-ATPase Inhibition, and Reduces Cerebral Plaque Deposition
por: Barykin, Evgeny P., et al.
Publicado: (2018)

Transcriptomic Changes in Endothelial Cells Triggered by Na,K-ATPase Inhibition: A Search for Upstream Na(+)(i)/K(+)(i) Sensitive Genes
por: Klimanova, Elizaveta A., et al.
Publicado: (2020)

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
por: Petrushanko, Irina Yu., et al.
Publicado: (2017)

Na,K-ATPase as a target for endogenous cardiotonic steroids: What's the evidence?
por: Orlov, Sergei N., et al.
Publicado: (2020)

Ouabain-Induced Cell Death and Survival. Role of α1-Na,K-ATPase-Mediated Signaling and [Na(+)](i)/[K(+)](i)-Dependent Gene Expression
por: Lopina, Olga Dmitrievna, et al.
Publicado: (2020)

Interaction Interface of Aβ(42) with Human Na,K-ATPase Studied by MD and ITC and Inhibitor Screening by MD
por: Adzhubei, Alexei A., et al.
Publicado: (2022)

Na(+)(i),K(+)(i)-Dependent and -Independent Signaling Triggered by Cardiotonic Steroids: Facts and Artifacts
por: Orlov, Sergei N., et al.
Publicado: (2017)

Na,K-ATPase Acts as a Beta-Amyloid Receptor Triggering Src Kinase Activation
por: Petrushanko, Irina Yu., et al.
Publicado: (2022)

Transcriptional regulators of Na,K-ATPase subunits
por: Li, Zhiqin, et al.
Publicado: (2015)

Tuning of the Na,K-ATPase by the beta subunit
por: Hilbers, Florian, et al.
Publicado: (2016)

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
por: Yan, Yanling, et al.
Publicado: (2016)

Time- and dose dependent actions of cardiotonic steroids on transcriptome and intracellular content of Na(+) and K(+): a comparative analysis
por: Klimanova, Elizaveta A., et al.
Publicado: (2017)

“Oxygen Sensing” by Na,K-ATPase: These Miraculous Thiols
por: Bogdanova, Anna, et al.
Publicado: (2016)

β subunit affects Na(+) and K(+) affinities of Na(+)/K(+)-ATPase: Na(+) and K(+) affinities of a hybrid Na(+)/K(+)-ATPase composed of insect α and mammalian β subunits
por: Homareda, Haruo, et al.
Publicado: (2022)

Effect of 2-Cys Peroxiredoxins Inhibition on Redox Modifications of Bull Sperm Proteins
por: Mostek-Majewska, Agnieszka, et al.
Publicado: (2021)

The Redox-Sensitive Na/K-ATPase Signaling in Uremic Cardiomyopathy
por: Liu, Jiang, et al.
Publicado: (2020)

Complex I within Oxidatively Stressed Bovine Heart Mitochondria Is Glutathionylated on Cys-531 and Cys-704 of the 75-kDa Subunit: POTENTIAL ROLE OF CYS RESIDUES IN DECREASING OXIDATIVE DAMAGE
por: Hurd, Thomas R., et al.
Publicado: (2008)

Redox index of Cys-thiol residues of serum apolipoprotein E and its diagnostic potential
por: Yamauchi, Kazuyoshi, et al.
Publicado: (2021)

Oxygen-induced Regulation of Na/K ATPase in Cerebellar Granule Cells
por: Petrushanko, Irina Yu., et al.
Publicado: (2007)

Na(+)(i)/K(+)(i) imbalance contributes to gene expression in endothelial cells exposed to elevated NaCl
por: Fedorov, D.A., et al.
Publicado: (2021)

Distinct Effects of Beta-Amyloid, Its Isomerized and Phosphorylated Forms on the Redox Status and Mitochondrial Functioning of the Blood–Brain Barrier Endothelium
por: Petrovskaya, Aleksandra V., et al.
Publicado: (2022)

RNases Disrupt the Adaptive Potential of Malignant Cells: Perspectives for Therapy
por: Mitkevich, Vladimir Alexandrovich, et al.
Publicado: (2019)

The β Subunit of the Na(+)/K(+)-ATPase Follows the Conformational State of the Holoenzyme
por: Dempski, Robert E., et al.
Publicado: (2005)

Regulation of Cardiac Contractility by the Alpha 2 Subunit of the Na(+)/K(+)-ATPase
por: Skogestad, Jonas, et al.
Publicado: (2022)

Role of the Rhamnosyl Residue of Ouabain in the Activation of the Na,K-ATPase Signaling Function
por: Rogachevskii, Ilya V., et al.
Publicado: (2023)

Maturation of the catalytic alpha-subunit of Na,K-ATPase during intracellular transport
Publicado: (1987)

The Polarized Distribution of Na(+),K(+)-ATPase: Role of the Interaction between β Subunits
por: Padilla-Benavides, Teresita, et al.
Publicado: (2010)

Bioinformatics approaches for classification and investigation of the evolution of the Na/K-ATPase alpha-subunit
por: Shahnazari, Marzieh, et al.
Publicado: (2022)

Amyloid β Modification: A Key to the Sporadic Alzheimer's Disease?
por: Barykin, Evgeny P., et al.
Publicado: (2017)

Docking and Molecular Dynamics-Based Identification of Interaction between Various Beta-Amyloid Isoforms and RAGE Receptor
por: Tolstova, Anna P., et al.
Publicado: (2022)

The adhesion molecule on glia (AMOG) is a homologue of the beta subunit of the Na,K-ATPase
Publicado: (1990)

Flexible selection of diversified Na(+)/K(+)-ATPase α-subunit isoforms for osmoregulation in teleosts
por: Wong, Marty Kwok-Shing, et al.
Publicado: (2016)

The Na, K-ATPase β-Subunit Isoforms Expression in Glioblastoma Multiforme: Moonlighting Roles
por: Rotoli, Deborah, et al.
Publicado: (2017)

Multiple Na,K-ATPase Subunits Colocalize in the Brush Border of Mouse Choroid Plexus Epithelial Cells
por: Baasch Christensen, Inga, et al.
Publicado: (2021)

The Na(+), K(+)-ATPase β1 subunit regulates epithelial tight junctions via MRCKα
por: Bai, Haiqing, et al.
Publicado: (2021)

Oligomerization and maturation of Na,K-ATPase: functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit
Publicado: (1996)

Cannot write session to /tmp/vufind_sessions/sess_vtunk25if7kgjcidavv117ls7n