On the public citation graph
Ion Selectivity of the Cytoplasmic Binding Sites of the Na,K-ATPase: I. Sodium Binding is Associated with a Conformational Rearrangement
0 signed · 92 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/bbpc.198800249openalex-snapshot
Cation Selectivity of Membrane Proteins
inferredcites →https://doi.org/10.1006/abbi.1997.9879openalex-snapshot
Chemical Modification with Dihydro-4,4′-diisothiocyanostilbene-2,2′-disulfonate Reveals the Distance between K480and K501in the ATP-Binding Domain of the Na,K-ATPase
inferredcites →https://doi.org/10.1007/978-1-4615-7425-5_12openalex-snapshot
The Sodium- and Potassium-Activated Adenosinetriphosphatase System
inferredcites →https://doi.org/10.1007/978-1-4684-4601-2_2openalex-snapshot
The Na+, K+-Transporting Adenosine Triphosphatase
inferredcites →https://doi.org/10.1007/bf00196828openalex-snapshot
Investigation of ion binding to the cytoplasmic binding sites of the Na,K-pump
inferredcites →https://doi.org/10.1007/bf00744678openalex-snapshot
Characterization of conformational changes in (Na,K) ATPase labeled with fluorescein at the active site
inferredcites →https://doi.org/10.1007/bf01870529openalex-snapshot
Charge translocation by the Na,K-pump: I. Kinetics of local field changes studied by time-resolved fluorescence measurements
inferredcites →https://doi.org/10.1007/bf01870530openalex-snapshot
Charge translocation by the Na,K-pump: II. Ion binding and release at the extracellular face
inferredcites →https://doi.org/10.1007/bf01870531openalex-snapshot
A negative slope in the current-voltage relationship of the Na+/K+ pump inXenopus oocytes produced by reduction of external [K+]
inferredcites →https://doi.org/10.1007/bf01870942openalex-snapshot
Structural basis for E1–E2 conformational transitions in Na, K-pump and Ca-pump proteins
inferredcites →https://doi.org/10.1016/0005-2736(91)90137-wopenalex-snapshot
The reaction sequence of the Na+/K+-ATPase: rapid kinetic measurements distinguish between alternative schemes
inferredcites →https://doi.org/10.1016/0014-5793(92)80151-6openalex-snapshot
Fluorescence study on cardiac glycoside binding to the Na,K‐pump Ouabain binding is associated with movement of electrical charge
inferredcites →https://doi.org/10.1016/0076-6879(74)32029-0openalex-snapshot
[26] Isolation of (Na+ + K+)-ATPase
inferredcites →https://doi.org/10.1016/0304-4157(95)00017-8openalex-snapshot
Structural organization, ion transport, and energy transduction of P-type ATPases
inferredcites →https://doi.org/10.1016/s0006-3495(92)81859-3openalex-snapshot
Structural dynamics and oligomeric interactions of Na+,K(+)-ATPase as monitored using fluorescence energy transfer
inferredcites →https://doi.org/10.1016/s0006-3495(95)79965-9openalex-snapshot
Electrogenicity of the sodium transport pathway in the Na,K-ATPase probed by charge-pulse experiments
inferredcites →https://doi.org/10.1016/s0021-9258(17)31850-1openalex-snapshot
Binding of sodium ions and cardiotonic steroids to native and selectively trypsinized Na,K pump, detected by charge movements.
inferredcites →https://doi.org/10.1016/s0021-9258(17)42732-3openalex-snapshot
The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)37653-1openalex-snapshot
Microenvironment of two different extrinsic fluorescence probes in Na+,K+-ATPase changes out of phase during sequential appearance of reaction intermediates.
inferredcites →https://doi.org/10.1016/s0021-9258(18)48408-6openalex-snapshot
Extensive digestion of Na+,K(+)-ATPase by specific and nonspecific proteases with preservation of cation occlusion sites.
inferredcites →https://doi.org/10.1016/s0021-9258(19)44725-xopenalex-snapshot
Activation by Adenosine Triphosphate in the Phosphorylation Kinetics of Sodium and Potassium Ion Transport Adenosine Triphosphatase
inferredcites →https://doi.org/10.1016/s0021-9258(19)69162-3openalex-snapshot
Conformational changes of renal sodium plus potassium ion-transport adenosine triphosphatase labeled with fluorescein.
inferredcites →https://doi.org/10.1016/s0021-9258(19)84555-6openalex-snapshot
Conformational transitions in fluorescein-labeled (Na,K)ATPase reconstituted into phospholipid vesicles.
inferredcites →https://doi.org/10.1021/bi00048a001openalex-snapshot
Organization of P-type ATPases: significance of structural diversity
inferredcites →https://doi.org/10.1021/bi00051a031openalex-snapshot
Fluorescent styryl dyes as probes for Na,K-ATPase reaction mechanism: significance of the charge of the hydrophilic moiety of RH dyes
inferredcites →https://doi.org/10.1021/bi00074a007openalex-snapshot
Role of magnesium ions in the conformational change reported by fluorescein 5'-isothiocyanate modification of sodium-potassium-ATPase
inferredcites →https://doi.org/10.1021/bi960407+openalex-snapshot
Estimation of the Distance Change between Cysteine-457 and the Nucleotide Binding Site When Sodium Pump Changes Conformation from E 1 to E 2 by Fluorescence Energy Transfer Measurements
inferredcites →https://doi.org/10.1021/bi971030qopenalex-snapshot
Leucine 332 at the Boundary Between the Fourth Transmembrane Segment and the Cytoplasmic Domain of Na+,K+-ATPase Plays a Pivotal Role in the Ion Translocating Conformational Changes
inferredcites →https://doi.org/10.1021/bi972813eopenalex-snapshot
Dephosphorylation Kinetics of Pig Kidney Na+,K+-ATPase
inferredcites →https://doi.org/10.1073/pnas.94.18.9596openalex-snapshot
Fe-catalyzed cleavage of the α subunit of Na/K-ATPase: Evidence for conformation-sensitive interactions between cytoplasmic domains
inferredcites →https://doi.org/10.1085/jgp.104.2.197openalex-snapshot
Partial reactions of the Na,K-ATPase: determination of rate constants.
inferredcites →https://doi.org/10.1111/j.1749-6632.1997.tb52260.xopenalex-snapshot
Functional Consequences of Mutations in the Transmembrane Core Region for Cation Translocation and Energy Transduction in the Na+, K+‐ATPase and the SR Ca2+‐ATPasea
inferredcites →https://doi.org/10.1111/j.1749-6632.1997.tb52294.xopenalex-snapshot
Eosin, Energy Transfer, and RH421 Report the Same Conformational Change in sodium pump as Fluoresceina
inferredcites →https://doi.org/10.1126/science.7682009openalex-snapshot
Extracellular Access to the Na,K Pump: Pathway Similar to Ion Channel
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4774308openalex-extracted
Does (Na+, K+)-Atpase Vary within the Macrobrachium Amazonicum Complex?
inferred← citeshttps://doi.org/10.1002/9781119085126.ch2openalex-snapshot
Study of Ion Pump Activity Using Black Lipid Membranes
inferred← citeshttps://doi.org/10.1006/abio.2000.4828openalex-snapshot
Preparation of Na,K-ATPase Specifically Modified on the Anti-fluorescein Antibody-Inaccessible Site by Fluorescein 5′-Isothiocyanate
inferred← citeshttps://doi.org/10.1007/s00232-001-0125-yopenalex-snapshot
Detection of Charge Movements in Ion Pumps by a Family of Styryl Dyes
inferred← citeshttps://doi.org/10.1007/s00232-005-0767-2openalex-snapshot
Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives
inferred← citeshttps://doi.org/10.1007/s00232-013-9600-5openalex-snapshot
Surface Charges of the Membrane Crucially Affect Regulation of Na,K-ATPase by Phospholemman (FXYD1)
inferred← citeshttps://doi.org/10.1007/s00232-017-9978-6openalex-snapshot
A Kinetic Characterization of the Gill (Na+, K+)-ATPase from the Semi-terrestrial Mangrove Crab Cardisoma guanhumi Latreille, 1825 (Decapoda, Brachyura)
inferred← citeshttps://doi.org/10.1007/s00232-020-00153-yopenalex-snapshot
Partial Reactions of the Na,K-ATPase: Determination of Activation Energies and an Approach to Mechanism
inferred← citeshttps://doi.org/10.1007/s002320010051openalex-snapshot
Ion Selectivity of the Cytoplasmic Binding Sites of the Na,K-ATPase: II. Competition of Various Cations
inferred← citeshttps://doi.org/10.1007/s10254-003-0018-9openalex-snapshot
Structure-function relationship in P-type ATPases—a biophysical approach
inferred← citeshttps://doi.org/10.1007/s10863-010-9306-7openalex-snapshot
Electrogenic plasma membrane H+-ATPase activity using voltage sensitive dyes
inferred← citeshttps://doi.org/10.1007/s12551-023-01082-5openalex-snapshot
The Na+,K+-ATPase and its stoichiometric ratio: some thermodynamic speculations
inferred← citeshttps://doi.org/10.1016/j.bioelechem.2003.09.021openalex-snapshot
How do P-Type ATPases transport ions?
inferred← citeshttps://doi.org/10.1016/j.bpj.2008.12.646openalex-snapshot
Investigation Of Electrogenic Partial Reactions In Detergent-solubilized Na,K-ATPase
inferred← citeshttps://doi.org/10.1016/j.bpj.2009.01.042openalex-snapshot
Mechanism of Mg2+ Binding in the Na+,K+-ATPase
inferred← citeshttps://doi.org/10.1016/j.bpj.2014.05.003openalex-snapshot
Does the Sodium Pump have Secret Levels?
inferred← citeshttps://doi.org/10.1016/j.cbpb.2024.110987openalex-snapshot
(Na+, K+)- ATPase kinetics in Macrobrachium pantanalense: highlighting intra- and interspecific variation within the Macrobrachium amazonicum complex
inferred← citeshttps://doi.org/10.1016/j.jtbi.2016.10.006openalex-snapshot
An approach to expand description of the pump and co-transporter steady-state current
inferred← citeshttps://doi.org/10.1016/j.semnephrol.2005.03.003openalex-snapshot
Structure-Function Relationships in the Na+,K+-Pump
inferred← citeshttps://doi.org/10.1016/s0005-2728(00)00055-4openalex-snapshot
Effects of fluorescent pseudo-ATP and ATP-metal analogs on secondary structure of Na+/K+-ATPase
inferred← citeshttps://doi.org/10.1016/s0006-3495(02)75384-8openalex-snapshot
Kinetics of the Ca2+, H+, and Mg2+ Interaction with the Ion-Binding Sites of the SR Ca-ATPase
inferred← citeshttps://doi.org/10.1016/s0014-5793(02)03510-xopenalex-snapshot
Regulation of the frontocortical sodium pump by Na+ in Alzheimer's disease: difference from the age‐matched control but similarity to the rat model
inferred← citeshttps://doi.org/10.1016/s0014-5793(99)01162-xopenalex-snapshot
Binding of the third Na+ ion to the cytoplasmic side of the Na,K‐ATPase is electrogenic
inferred← citeshttps://doi.org/10.1021/acs.biochem.5b00182openalex-snapshot
Probing the Extracellular Access Channel of the Na,K-ATPase
inferred← citeshttps://doi.org/10.1021/acs.biochem.6b01243openalex-snapshot
Modulation of the Na,K-ATPase by Magnesium Ions
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b00629openalex-snapshot
Unexpected Effects of K+ and Adenosine Triphosphate on the Thermal Stability of Na+,K+-ATPase
inferred← citeshttps://doi.org/10.1021/bi2001714openalex-snapshot
Phospholemman (FXYD1) Raises the Affinity of the Human α1β1 Isoform of Na,K-ATPase for Na Ions
inferred← citeshttps://doi.org/10.1021/bi400729eopenalex-snapshot
Mechanistic Analysis of the Pump Cycle of the KdpFABC P-Type ATPase
inferred← citeshttps://doi.org/10.1021/bi901148kopenalex-snapshot
Investigation of Electrogenic Partial Reactions in Detergent-Solubilized Na,K-ATPase
inferred← citeshttps://doi.org/10.1021/jp2124108openalex-snapshot
Opposing Effects of Na+ and K+ on the Thermal Stability of Na+,K+-ATPase
inferred← citeshttps://doi.org/10.1023/a:1010615422932openalex-snapshot
Structural Organization and Energy Transduction Mechanism of Na+,K+-ATPase Studied with Transition Metal-Catalyzed Oxidative Cleavage
inferred← citeshttps://doi.org/10.1038/s41467-026-75997-4openalex-snapshot
Active conformations of neuronal Na+, K+-ATPase isoforms and a disease-causing mutant
inferred← citeshttps://doi.org/10.1073/pnas.0711838105openalex-snapshot
Capsazepine, a synthetic vanilloid that converts the Na,K-ATPase to Na-ATPase
inferred← citeshttps://doi.org/10.1073/pnas.220332897openalex-snapshot
The complex ATP–Fe 2+ serves as a specific affinity cleavage reagent in ATP-Mg 2+ sites of Na,K-ATPase: Altered ligation of Fe 2+ (Mg 2+ ) ions accompanies the E 1 P→E 2 P conformational change
inferred← citeshttps://doi.org/10.1074/jbc.275.3.1749openalex-snapshot
Residues of the Fourth Transmembrane Segments of the Na,K-ATPase and the Gastric H,K-ATPase Contribute to Cation Selectivity
inferred← citeshttps://doi.org/10.1074/jbc.275.3.2019openalex-snapshot
Entrance Port for Na+ and K+ Ions on Na+,K+-ATPase in the Cytoplasmic Loop between Trans-membrane Segments M6 and M7 of the α Subunit
inferred← citeshttps://doi.org/10.1074/jbc.m109.015099openalex-snapshot
The C Terminus of Na+,K+-ATPase Controls Na+ Affinity on Both Sides of the Membrane through Arg935
inferred← citeshttps://doi.org/10.1074/jbc.m110.123976openalex-snapshot
The Rapid-onset Dystonia Parkinsonism Mutation D923N of the Na+,K+-ATPase α3 Isoform Disrupts Na+ Interaction at the Third Na+ Site
inferred← citeshttps://doi.org/10.1074/jbc.m111552200openalex-snapshot
Differential Regulation of Renal Na,K-ATPase by Splice Variants of the γ Subunit
inferred← citeshttps://doi.org/10.1074/jbc.m702259200openalex-snapshot
Importance of Leu99 in Transmembrane Segment M1 of the Na+,K+-ATPase in the Binding and Occlusion of K+
inferred← citeshttps://doi.org/10.1085/jgp.200609505openalex-snapshot
Palytoxin-induced Effects on Partial Reactions of the Na,K-ATPase
inferred← citeshttps://doi.org/10.1111/j.1749-6632.2003.tb07150.xopenalex-snapshot
Toward an Understanding of Ion Transport through the Na,K‐ATPase
inferred← citeshttps://doi.org/10.1113/jphysiol.2014.279810openalex-snapshot
Species‐dependent adaptation of the cardiac Na+/K+ pump kinetics to the intracellular Na+ concentration
inferred← citeshttps://doi.org/10.1134/s1023193517030028openalex-snapshot
Mechanistic principles of ion transport in the Na,K-ATPase
inferred← citeshttps://doi.org/10.1134/s1990747808020116openalex-snapshot
Electrogenic transport of sodium ions in cytoplasmic and extracellular ion access channels of Na+,K+-ATPase probed by admittance measurement technique
inferred← citeshttps://doi.org/10.1134/s1990747813020074openalex-snapshot
The competition transport of sodium ions and protons in the cytoplasmic access channel of the Na+,K+-ATPase
inferred← citeshttps://doi.org/10.1134/s1990747815020105openalex-snapshot
Electrogenic binding of ions at the cytoplasmic side of the Na+,K+-ATPase
inferred← citeshttps://doi.org/10.1134/s1990747818050082openalex-snapshot
Binding of Potassium Ions Inside the Access Channel at the Cytoplasmic Side of Na+,K+-ATPase
inferred← citeshttps://doi.org/10.1134/s1990747822050117openalex-snapshot
Investigations of Electrogenic Ion Transport by Na+,K+-ATPase in Bilayer Lipid Membranes by Impedance Method
inferred← citeshttps://doi.org/10.11606/d.59.2002.tde-02022007-121223openalex-snapshot
Caracterização cinética da (Na+, K+)-ATPase da fração microsomal de tecido branquial de Callinectes danae (CRUSTACEA, PORTUNIDAE)
inferred← citeshttps://doi.org/10.11606/t.59.2006.tde-04122006-094016openalex-snapshot
Caracterização cinética da (Na+,K+)-ATPase da fração microsomal de tecido branquial do siri Callinectes danae aclimatado a salinidade de 15 o/oo.
inferred← citeshttps://doi.org/10.11606/t.59.2007.tde-12052007-095301openalex-snapshot
Caracterização cinética da (Na, K)-ATPase da fração microsomal do tecido branquial do ermitão intertidal Clibanarius vittatus
inferred← citeshttps://doi.org/10.1529/biophysj.104.055913openalex-snapshot
Electrogenic Partial Reactions of the Gastric H,K-ATPase
inferred← citeshttps://doi.org/10.3390/molecules26071905openalex-snapshot
Na+/K+-ATPase Revisited: On Its Mechanism of Action, Role in Cancer, and Activity Modulation
inferred← citeshttps://doi.org/10.7554/elife.16616openalex-snapshot
The selectivity of the Na+/K+-pump is controlled by binding site protonation and self-correcting occlusion
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.