On the public citation graph

Role of magnesium ions in the conformational change reported by fluorescein 5'-isothiocyanate modification of sodium-potassium-ATPase

https://doi.org/10.1021/bi00074a007
0 signed · 43 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.
Claim with ORCID
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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/jss.400030313openalex-snapshot
Magnetic resonance and kinetic studies of the mechanism of membrane‐bound sodium and potassium ION‐activated adenosine triphosphatase
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/10.1016/0005-2736(74)90292-2openalex-snapshot
Purification and characterization of (Na+ + K+)-ATPase III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate
inferredcites →https://doi.org/10.1016/0005-2736(83)90373-5openalex-snapshot
Effect of magnesium ions on the high-affinity binding of eosin to the (Na+ + K+)-ATPase
inferredcites →https://doi.org/10.1016/0005-2744(75)90114-xopenalex-snapshot
Functionally distinct classes of K+ sites on the (Na+ + K+)- dependent ATPase
inferredcites →https://doi.org/10.1016/0005-2744(78)90261-9openalex-snapshot
Tryptophan fluorescence of (Na+ + K+)-ATPase as a tool for study of the enzyme mechanism
inferredcites →https://doi.org/10.1016/0006-291x(78)91292-5openalex-snapshot
Lithium-7 NMR as a probe of monovalent cation sites at the active site of (Na+ + K+)-ATPase from kidney
inferredcites →https://doi.org/10.1016/0014-5793(74)81162-2openalex-snapshot
Direct measurement of proton release by yeast enolase upon binding magnesium ions
inferredcites →https://doi.org/10.1016/0014-5793(80)80244-4openalex-snapshot
Distance determinations at the active site of kidney (Na+ + K+)‐ATPase by Mn(II) ion electron paramagnetic resonance
inferredcites →https://doi.org/10.1016/0167-4838(89)90133-7openalex-snapshot
Modification of ligand binding to the Na+/K+-activated ATPase
inferredcites →https://doi.org/10.1016/0926-6569(64)90078-1openalex-snapshot
Sodium, potassium-requiring adenosinetriphosphatase activity I. Purification and properties
inferredcites →https://doi.org/10.1016/s0021-9258(19)42121-2openalex-snapshot
Thallium-205 Nuclear Relaxation and Kinetic Studies of Sodium and Potassium Ion-activated Adenosine Triphosphatase
inferredcites →https://doi.org/10.1016/s0021-9258(19)42657-4openalex-snapshot
Magnetic Resonance and Kinetic Studies of the Mechanism of Sodium and Potassium Ion-activated Adenosine Triphosphatase
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)69786-3openalex-snapshot
Characterization of 2',3'-O-(2,4,6-trinitrocyclohexadienylidine)adenosine 5'-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP.
inferredcites →https://doi.org/10.1016/s0021-9258(19)83820-6openalex-snapshot
The active site structure of Na+- and K+-stimulated ATPase. Location of a specific fluorescein isothiocyanate reactive site.
inferredcites →https://doi.org/10.1021/bi00228a022openalex-snapshot
Temperature dependence of the rates of conformational changes reported by fluorescein 5'-isothiocyanate modification of the hydrogen ion-potassium- and sodium-potassium-ATPases
inferredcites →https://doi.org/10.1021/bi00413a039openalex-snapshot
Proton nuclear magnetic resonance studies of the conformation of an ATP analog at the active site of sodium-potassium ATPase from kidney medulla
inferredcites →https://doi.org/10.1021/bi00668a002openalex-snapshot
Calorimetric studies of the interaction of magnesium and phosphate with (Na+ and K+ion)-dependent ATPase: evidence for a ligand-induced conformational change in the enzyme
inferredcites →https://doi.org/10.1038/269165a0openalex-snapshot
Reversal of the Na-K pump and apparent affinity for intracellular potassium
inferredcites →https://doi.org/10.1038/282333a0openalex-snapshot
Vanadate inhibits (Na+ + K+)ATPase by blocking a conformational change of the unphosphorylated form
inferredcites →https://doi.org/10.1073/pnas.71.4.1083openalex-snapshot
Calorimetric Studies of the Role of Magnesium Ions in Yeast Enolase Catalysis
inferredcites →https://doi.org/10.1080/10739148708543650openalex-snapshot
The Method of Successive Integration: a General Technique for Recasting Kinetic Equations in a Readily Soluble Form Which Is Linear in the Coefficients and Sufficiently Rapid for Real Time Instrumental Use.
inferredcites →https://doi.org/10.1111/j.1748-1716.1992.tb09410.xopenalex-snapshot
X‐ray micro‐analysis of cultured respiratory epithelial cells from patients with cystic fibrosis
inferredcites →https://doi.org/10.1113/jphysiol.1973.sp010234openalex-snapshot
The interaction of sodium and potassium with the sodium pump in red cells
inferredcites →https://doi.org/10.1146/annurev.ph.53.030191.001355openalex-snapshot
Mechanisms Of Magnesium Transport
inferredcites →https://doi.org/10.3891/acta.chem.scand.16-0479openalex-snapshot
Heats of Hydrolysis of N-Acetyl Imidazole and Butyl Acetamide in Aqueous Solution.

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/10.1002/1873-3468.14689openalex-snapshot
Crystal structures of Na + ,K + ‐ATPase reveal the mechanism that converts the K + ‐bound form to Na + ‐bound form and opens and closes the cytoplasmic gate
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/10.1007/978-3-642-72511-1_106openalex-snapshot
Mechanism of the Conformational Change in Fluorescein 5′-Isothiocyanate-Modified Na+/K+ ATPase
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/s002329900511openalex-snapshot
Ion Selectivity of the Cytoplasmic Binding Sites of the Na,K-ATPase: I. Sodium Binding is Associated with a Conformational Rearrangement
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.jmb.2007.03.029openalex-snapshot
Sulfate Acts as Phosphate Analog on the Monomeric Catalytic Fragment of the CPx-ATPase CopB from Sulfolobus solfataricus
inferred← citeshttps://doi.org/10.1016/s0006-3495(01)75856-0openalex-snapshot
Rate Limitation of the Na+,K+-ATPase Pump Cycle
inferred← citeshttps://doi.org/10.1016/s0014-5793(97)00624-8openalex-snapshot
Extracellular Mg2+ regulates the intracellular Na+ concentration in rat sublingual acini
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/bi00213a022openalex-snapshot
Time resolution of fluorescence changes observed in titrations of fluorescein 5'-isothiocyanate-modified sodium-potassium-ATPase with monovalent cations
inferred← citeshttps://doi.org/10.1074/jbc.m105886200openalex-snapshot
The Occlusion of Rb+ in the Na+/K+-ATPase
inferred← citeshttps://doi.org/10.1074/jbc.m105887200openalex-snapshot
The Occlusion of Rb+ in the Na+/K+-ATPase
inferred← citeshttps://doi.org/10.1074/jbc.m412319200openalex-snapshot
Evidence Calcium Pump Binds Magnesium before Inorganic Phosphate
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.