On the public citation graph

Structure-function relationships in the sodium-potassium ATPase .alpha. subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme

0 signed · 448 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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/jcp.1041270202openalex-snapshot

Cellular basis for the species differences in sensitivity to cardiac glycosides (digitalis)

inferredcites →https://doi.org/10.1006/abio.1987.9999openalex-snapshot

Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

inferredcites →https://doi.org/10.1007/bf00499048openalex-snapshot

Biochemical basis for the low sensitivity of the rat heart to digitalis

inferredcites →https://doi.org/10.1007/bf01570731openalex-snapshot

Ouabain-resistant mutants of Chinese hamster ovary cells are not directly affected in Na+, K+-ATPase

inferredcites →https://doi.org/10.1016/0003-2697(83)90418-9openalex-snapshot

A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity

inferredcites →https://doi.org/10.1016/0003-9861(80)90448-8openalex-snapshot

A kinetic comparison of cardiac glycoside interactions with Na+,K+-ATPases from skeletal and cardiac muscle and from kidney

inferredcites →https://doi.org/10.1016/0006-2952(65)90269-8openalex-snapshot

Über die ursache der speciesunterschiede in der digitalisempfindlichkeit

inferredcites →https://doi.org/10.1016/0006-2952(72)90305-xopenalex-snapshot

Rates of dissociation of enzyme-ouabain complexes and K0.5 values in (Na+ + K+) adenosine triphosphatase from different species

inferredcites →https://doi.org/10.1016/0006-2952(86)90416-8openalex-snapshot

Origin of differences of inhibitory potency of cardiac glycosides in Na+/K+-transporting ATPase from human cardiac muscle, human brain cortex and guinea-pig cardiac muscle

inferredcites →https://doi.org/10.1016/0014-5793(86)80616-0openalex-snapshot

Pig kidney Na+,K+‐ATPase

inferredcites →https://doi.org/10.1016/0022-2836(80)90196-5openalex-snapshot

Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing

inferredcites →https://doi.org/10.1016/0167-4838(86)90192-5openalex-snapshot

Immunochemical comparison of cardiac glycoside-sensitive (lamb) and -insensitive (rat) kidney (Na+ + K+)-ATPase

inferredcites →https://doi.org/10.1016/0304-4157(82)90013-2openalex-snapshot

Mechanism of the Na+, K+ pump protein structure and conformations of the pure

inferredcites →https://doi.org/10.1016/0305-0491(83)90274-2openalex-snapshot

Origins of the different sensitivities of adenosinetriphosphatase preparations to ouabain

inferredcites →https://doi.org/10.1016/s0006-291x(86)80110-3openalex-snapshot

Computer-based search for steroid and dna binding sites on estrogen and glucocorticoid receptors

inferredcites →https://doi.org/10.1016/s0021-9258(17)35893-3openalex-snapshot

Biochemical and cross-resistance studies with HeLa cell mutants resistant to cardiac glycoside SC4453. Regulation of the resistant form of Na+/K+-ATPase in the mutant cells.

inferredcites →https://doi.org/10.1016/s0021-9258(18)34396-5openalex-snapshot

Evidence for the organization of the transmembrane segments of (Na,K)-ATPase based on labeling lipid-embedded and surface domains of the alpha-subunit.

inferredcites →https://doi.org/10.1016/s0021-9258(18)50519-6openalex-snapshot

Two molecular forms of (Na+ + K+)-stimulated ATPase in brain. Separation, and difference in affinity for strophanthidin.

inferredcites →https://doi.org/10.1016/s0021-9258(18)61025-7openalex-snapshot

Expression of hybrid (Na+ + K+)-ATPase molecules after transfection of mouse Ltk-cells with DNA encoding the beta-subunit of an avian brain sodium pump.

inferredcites →https://doi.org/10.1016/s0021-9258(18)61282-7openalex-snapshot

Multiple mRNAs from rat kidney and brain encode a single Na+,K+-ATPase beta subunit protein.

inferredcites →https://doi.org/10.1016/s0021-9258(18)67582-9openalex-snapshot

Reduced ouabain inhibition of Na,K-activated adenosine triphosphatase in cultured cell recipients of the ouabain-resistance gene.

inferredcites →https://doi.org/10.1016/s0021-9258(18)68932-xopenalex-snapshot

Ouabain-sensitive (Na+ + K+)-ATPase activity expressed in mouse L cells by transfection with DNA encoding the alpha-subunit of an avian sodium pump.

inferredcites →https://doi.org/10.1016/s0021-9258(19)43378-4openalex-snapshot

Purification and Characterization of and [3H]Ouabain Binding to the Transport Adenosine Triphosphatase from Outer Medulla of Canine Kidney

inferredcites →https://doi.org/10.1016/s0021-9258(19)68263-3openalex-snapshot

Evidence that a Na+/Ca2+ antiport system regulates murine erythroleukemia cell differentiation.

inferredcites →https://doi.org/10.1016/s0021-9258(20)82032-8openalex-snapshot

Interaction of (Na+,K+)-ATPases and digitalis genins. A general model for inhibitory activity.

inferredcites →https://doi.org/10.1016/s0022-3565(25)28298-2openalex-snapshot

POSSIBLE INVOLVEMENT OF CARDIAC Na+ , K+-ADENOSINE TRIPHOSPHATASE IN THE MECHANISM OF ACTION OF CARDIAC GLYCOSIDES

inferredcites →https://doi.org/10.1016/s0022-3565(25)29983-9openalex-snapshot

CARDENOLIDE ANALOGS. V. CARDIOTONIC ACTIVITY OF SEMISYNTHETIC ANALOGS OF DIGITOXIGENIN

inferredcites →https://doi.org/10.1016/s0031-6997(25)06643-8openalex-snapshot

Interaction of cardiac glycosides with (Na+ + K+)-activated ATPase. A biochemical link to digitalis-induced inotropy.

inferredcites →https://doi.org/10.1016/s0031-6997(25)06680-3openalex-snapshot

The Sodium-Potassium Adenosine Triphosphatase: Pharmacological, Physiological and Biochemical Aspects

inferredcites →https://doi.org/10.1016/s0070-2161(08)60591-2openalex-snapshot

Principal Conformations of the α-Subunit and Ion Translocation

inferredcites →https://doi.org/10.1021/bi00289a012openalex-snapshot

Specific photoaffinity labeling of the digitalis binding site of the sodium and potassium ion-activated adenosine triphosphatase induced by energy transfer

inferredcites →https://doi.org/10.1021/bi00373a001openalex-snapshot

Molecular cloning of three distinct forms of the Na+,K+-ATPase .alpha.-subunit from rat brain

inferredcites →https://doi.org/10.1021/bi00610a037openalex-snapshot

Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the (sodium-potassium ion)-dependent ATPase

inferredcites →https://doi.org/10.1021/bi00622a030openalex-snapshot

Anthroylouabain: a specific fluorescent probe for the cardiac glycoside receptor of the sodium-potassium ATPase

inferredcites →https://doi.org/10.1038/254304a0openalex-snapshot

Structural invariants in protein folding

inferredcites →https://doi.org/10.1038/316691a0openalex-snapshot

Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA

inferredcites →https://doi.org/10.1038/316733a0openalex-snapshot

Primary structure of the α-subunit of Torpedo californica (Na+ + K+)ATPase deduced from cDNA sequence

inferredcites →https://doi.org/10.1038/321429a0openalex-snapshot

Amino-acid sequence of the β-subunit of the (Na+ + K+)ATPase deduced from a cDNA

inferredcites →https://doi.org/10.1073/pnas.71.6.2352openalex-snapshot

Photoaffinity Labeling of the Ouabain-Binding Site on (Na + + K + ) Adenosinetriphosphatase

inferredcites →https://doi.org/10.1073/pnas.77.8.4529openalex-snapshot

Ouabain-binding-site photoaffinity probes that label both subunits of Na+,K+-ATPase.

inferredcites →https://doi.org/10.1073/pnas.81.5.1489openalex-snapshot

Molecular cloning of the mouse ouabain-resistance gene.

inferredcites →https://doi.org/10.1073/pnas.82.2.488openalex-snapshot

Rapid and efficient site-specific mutagenesis without phenotypic selection.

inferredcites →https://doi.org/10.1093/nar/14.7.2833openalex-snapshot

Molecular cloning and sequence analysis of human Na, K-ATPase β–subunit

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a121726openalex-snapshot

Primary Structure of the α-Subunit of Human Na, K-ATPase Deduced from cDNA Sequence1

inferredcites →https://doi.org/10.1126/science.3039660openalex-snapshot

Ouabain Resistance Conferred by Expression of the cDNA for a Murine Na + , K + -ATPase α Subunit

inferredcites →https://doi.org/10.1126/science.3296192openalex-snapshot

Tinkering with Enzymes: What Are We Learning?

inferredcites →https://doi.org/10.1128/jvi.50.2.606-614.1984openalex-snapshot

Infection of eucaryotic cells by helper-independent recombinant adenoviruses: early region 1 is not obligatory for integration of viral DNA

inferredcites →https://doi.org/10.1146/annurev.ph.41.030179.001145openalex-snapshot

Sugar, Amino Acid, and NA+ Cotransport in the Proximal Tubule

inferredcites →https://doi.org/10.1152/physrev.1972.52.3.563openalex-snapshot

Electrogenic sodium pump in nerve and muscle cells.

inferredcites →https://doi.org/10.1152/physrev.1977.57.3.510openalex-snapshot

Regulation of cellular volume.

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.phytochem.2020.112577zenodo-depositor-declared

A previously undescribed phenylethanoid glycoside from Callicarpa kwangtungensis Chun acts as an agonist of the Na/K-ATPase signal transduction pathway

inferred← citeshttps://doi.org/10.1002/9781119085126.ch14openalex-snapshot

Cation Uptake Studies with Atomic Absorption Spectrophotometry (AAS)

inferred← citeshttps://doi.org/10.1002/9781119085126.ch4openalex-snapshot

Probing Conformational Transitions of Membrane Proteins with Voltage Clamp Fluorometry (VCF)

inferred← citeshttps://doi.org/10.1002/9781119650263.ch16openalex-snapshot

Predicting Human Pharmacodynamics

inferred← citeshttps://doi.org/10.1002/adsc.201100163openalex-snapshot

Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes

inferred← citeshttps://doi.org/10.1002/ange.19891011029openalex-snapshot

Synthese und pharmakologische Eigenschaften eines neuartigen herzwirksamen Steroids

inferred← citeshttps://doi.org/10.1002/anie.198913591openalex-snapshot

Synthesis and Pharmacological Properties of a Novel Cardioactive Steroid

inferred← citeshttps://doi.org/10.1002/cphy.c200018openalex-snapshot

Structure and Function of Na,K‐ATPase—The Sodium‐Potassium Pump

inferred← citeshttps://doi.org/10.1002/eji.201242740openalex-snapshot

Small molecule inhibitors of ROR γt: Targeting T h17 cells and other applications

inferred← citeshttps://doi.org/10.1002/humu.20229openalex-snapshot

Rare missense variants inATP1A2 in families with clustering of common forms of migraine

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1992.tb05218.xopenalex-snapshot

Mutation of a cysteine in the first transmembrane segment of Na,K‐ATPase alpha subunit confers ouabain resistance.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb06975.xopenalex-snapshot

The C‐terminal 165 amino acids of the plasma membrane Ca(2+)‐ATPase confer Ca2+/calmodulin sensitivity on the Na+,K(+)‐ATPase alpha‐subunit.

inferred← citeshttps://doi.org/10.1002/j.2040-4603.2022.tb00195.xopenalex-snapshot

Structure and Function of Na,K‐ATPase—The Sodium‐Potassium Pump

inferred← citeshttps://doi.org/10.1002/jcp.1041480220openalex-snapshot

Involvement of second messenger systems in stimulation of angiotensin converting enzyme of bovine endothelial cells

inferred← citeshttps://doi.org/10.1002/jnr.490270108openalex-snapshot

Differentiation of rat hippocampal neurons induced by estrogen in vitro: Effects on neuritogenesis and Na,K‐ATPase activity

inferred← citeshttps://doi.org/10.1002/mrd.20383openalex-snapshot

The human Na,K-ATPase alpha4 isoform is a ouabain-sensitive alpha isoform that is expressed in sperm

inferred← citeshttps://doi.org/10.1006/abbi.1999.1124openalex-snapshot

Functional Role of Oxygen-Containing Residues in the Fifth Transmembrane Segment of the Na,K-ATPase α Subunit

inferred← citeshttps://doi.org/10.1006/abbi.1999.1198openalex-snapshot

Stimulation of Ouabain Binding to Na,K-ATPase in 40% Dimethyl Sulfoxide by a Factor from Na,K-ATPase Preparations

inferred← citeshttps://doi.org/10.1006/abbi.1999.1278openalex-snapshot

Alanine Scanning Mutagenesis of Oxygen-Containing Amino Acids in the Transmembrane Region of the Na,K-ATPase

inferred← citeshttps://doi.org/10.1006/bbrc.1997.6981openalex-snapshot

The α2L111R,N122D Isoform of the Na,K-ATPase Expressed in HeLa Cells Does Not Undergo an Adipocyte-like Increase in Activity in Response to Insulin

inferred← citeshttps://doi.org/10.1007/978-1-4899-1146-9_6openalex-snapshot

Transport across Membranes

inferred← citeshttps://doi.org/10.1007/978-1-4939-3179-8_25openalex-snapshot

Voltage Clamp Fluorometry of P-Type ATPases

inferred← citeshttps://doi.org/10.1007/978-1-4939-3179-8_27openalex-snapshot

Electrophysiological Characterization of Na,K-ATPases Expressed in Xenopus laevis Oocytes Using Two-Electrode Voltage Clamping

inferred← citeshttps://doi.org/10.1007/978-3-0348-8998-8_1openalex-snapshot

In search of ideal inotropic steroids: Recent progress

inferred← citeshttps://doi.org/10.1007/978-3-319-24750-2_18openalex-snapshot

Regulation of Membrane Na+-K+ ATPase in Health and Disease

inferred← citeshttps://doi.org/10.1007/978-3-642-72511-1_133openalex-snapshot

Structure and Biological Activity of the Na+/K+-ATPase Inhibitor Isolated from Bovine Hypothalamus: Difference from Ouabain

inferred← citeshttps://doi.org/10.1007/978-3-642-72511-1_134openalex-snapshot

Identification and physiological significance of Na+/K+-pump inhibitors in rats

inferred← citeshttps://doi.org/10.1007/978-3-642-72511-1_157openalex-snapshot

Na+/K+-pump α3 Isoform in Rat Vascular Smooth Muscle and its Physiological Role

inferred← citeshttps://doi.org/10.1007/978-3-642-72511-1_17openalex-snapshot

Ca2+/Calmodulin-Sensitive Na+/K+-ATPase Activity Expressed in Chimeric Molecules between the Plasma Membrane Ca2+-ATPase and the Na+/K+-ATPase α-Subunit

inferred← citeshttps://doi.org/10.1007/978-3-642-72511-1_47openalex-snapshot

Structure and Function of Ion Pumps Studied by Atomic Force Microscopy and Gene-transfer Experiments Using Chimeric Na+/K+- and Ca2+ ATPases

inferred← citeshttps://doi.org/10.1007/978-3-642-72511-1_48openalex-snapshot

Na,K-ATPase: Cardiac Glycoside Binding and Functional Importance of Negatively Charged Amino Acids of Transmembrane Regions

inferred← citeshttps://doi.org/10.1007/978-3-642-76983-2_1openalex-snapshot

Na,K-ATPase, Structure and Transport Mechanism

inferred← citeshttps://doi.org/10.1007/978-3-642-79301-1_20openalex-snapshot

Amino Acid Residues Involved in Ouabain Sensitivity and Cation Binding

inferred← citeshttps://doi.org/10.1007/978-94-011-3990-8_36openalex-snapshot

Sarcoplasmic reticulum Ca2+ ATPases

inferred← citeshttps://doi.org/10.1007/bf00169051openalex-snapshot

The action of 22,23-dihydrobufalin and other cardioactive steroids on contraction and active sodium/potassium transport of sheep cardiac Purkinje fibres

inferred← citeshttps://doi.org/10.1007/bf00214122openalex-snapshot

Digitalis receptor sugar binding site characteristics: A model based upon studies of Na+, K+-ATPase preparations with differing digitalis sensitivities

inferred← citeshttps://doi.org/10.1007/bf00233248openalex-snapshot

Differentiation between isoforms of Na+/K+-transporting ATPase from human and guinea-pig cardiac muscle through use of digitalis derivatives as analytical probes

inferred← citeshttps://doi.org/10.1007/bf00768846openalex-snapshot

The Na,K-ATPase

inferred← citeshttps://doi.org/10.1007/bf00768847openalex-snapshot

Na,K-ATPase: Isoform structure, function, and expression

inferred← citeshttps://doi.org/10.1007/bf00769038openalex-snapshot

Differential distribution of (Na, K)-ATPase? isoforms in the central nervous system

inferred← citeshttps://doi.org/10.1007/bf01869450openalex-snapshot

Subunit assembly and functional maturation of Na,K-ATPase

inferred← citeshttps://doi.org/10.1007/bf02445255openalex-snapshot

Effect of antidigoxin monoclonal antibodies on cardiac disturbances caused by high concentrations of digoxin

inferred← citeshttps://doi.org/10.1007/bfb0030902openalex-snapshot

Isoforms of the Na,K-ATPase: Family members in search of function

inferred← citeshttps://doi.org/10.1007/pl00005138openalex-snapshot

Na+/K+ pump inhibition and positive inotropic effect of digitoxigenin and some C-22-substituted derivatives in sheep cardiac preparations

inferred← citeshttps://doi.org/10.1007/pl00005899openalex-snapshot

Characterization of the Fourth α Isoform of the Na,K-ATPase

inferred← citeshttps://doi.org/10.1007/s00018-012-1134-yopenalex-snapshot

Regulation of the cardiac sodium pump

inferred← citeshttps://doi.org/10.1007/s00049-002-8324-2openalex-snapshot

Alkaloid tolerance in Manduca sexta and phylogenetically related sphingids (Lepidoptera: Sphingidae)

inferred← citeshttps://doi.org/10.1007/s00232-002-1041-5openalex-snapshot

P-type ATPases in Caenorhabditis and Drosophila: Implications for Evolution of the P-type ATPase Subunit Families with Special Reference to the Na,K-ATPase and H,K-ATPase Subgroup

inferred← citeshttps://doi.org/10.1007/s002320010002openalex-snapshot

Reactivity of Cysteines in the Transmembrane Region of the Na,K-ATPase α Subunit Probed with Hg 2+

inferred← citeshttps://doi.org/10.1007/s002329900174openalex-snapshot

Regulation of Na,K-ATPase Transport Activity by Protein Kinase C

inferred← citeshttps://doi.org/10.1007/s003950200024openalex-snapshot

The cardiac sodium pump: structure and function

inferred← citeshttps://doi.org/10.1007/s00401-025-02906-2openalex-snapshot

Transient receptor potential vanilloid channel 2 contributes to multi-modal endoplasmic reticulum and perinuclear space dilations that can also be observed in prion-infected mice

inferred← citeshttps://doi.org/10.1007/s00415-023-11581-wopenalex-snapshot

The phenotypic spectrum of pathogenic ATP1A1 variants expands: the novel p.P600R substitution causes demyelinating Charcot–Marie–Tooth disease

inferred← citeshttps://doi.org/10.1007/s00424-008-0467-8openalex-snapshot

The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase

inferred← citeshttps://doi.org/10.1007/s00439-017-1862-zopenalex-snapshot

The CAPOS mutation in ATP1A3 alters Na/K-ATPase function and results in auditory neuropathy which has implications for management

inferred← citeshttps://doi.org/10.1007/s10340-014-0586-2openalex-snapshot

Predation on invasive cane toads (Rhinella marina) by native Australian rodents

inferred← citeshttps://doi.org/10.1007/s10682-025-10375-yopenalex-snapshot

Genetic signatures of bufadienolide resistance are poor predictors of cane toad toxin resistance in crocodilians

inferred← citeshttps://doi.org/10.1007/s10863-007-9106-xopenalex-snapshot

Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2+-ATPase, the gatekeeper and the pivot

inferred← citeshttps://doi.org/10.1007/s10863-017-9729-5openalex-snapshot

A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K+

inferred← citeshttps://doi.org/10.1007/s10886-023-01404-7openalex-snapshot

Identification of the NA+/K+-ATPase α-Isoforms in Six Species of Poison Dart Frogs and their Sensitivity to Cardiotonic Steroids

inferred← citeshttps://doi.org/10.1007/s13369-013-0828-2openalex-snapshot

The High and Low Affinity Binding Sites of Digitalis Glycosides to Na,K-ATPase

inferred← citeshttps://doi.org/10.1007/s13402-021-00588-yopenalex-snapshot

Digoxin treatment reactivates in vivo radioactive iodide uptake and correlates with favorable clinical outcome in non‐medullary thyroid cancer

inferred← citeshttps://doi.org/10.1016/0005-2736(89)90281-2openalex-snapshot

Characterization of fatty acid interaction with ouabain and vanadate binding to (Na+ + K+)-activated ATPase

inferred← citeshttps://doi.org/10.1016/0005-2736(90)90239-kopenalex-snapshot

Autoregulation of the phosphointermediate of Na+/K+-ATPase by the amino-terminal domain of the α-subunit

inferred← citeshttps://doi.org/10.1016/0006-291x(89)91078-4openalex-snapshot

Sodium transport defect of ouabain-resistant renal Na,K-ATPase

inferred← citeshttps://doi.org/10.1016/0006-291x(91)91733-sopenalex-snapshot

Expression of Na,K-ATPase isoforms in human heart

inferred← citeshttps://doi.org/10.1016/0006-2952(92)90568-4openalex-snapshot

Reversal of the effects of a low extracellular potassium concentration on the number and activity of Na+/K+ pumps in an epstein-barr virus-transformed human lymphocyte cell line

inferred← citeshttps://doi.org/10.1016/0014-2999(93)90999-xopenalex-snapshot

Arenobufagin, a compound in toad venom, blocks Na+K+ pump current in cardiac myocytes

inferred← citeshttps://doi.org/10.1016/0014-5793(89)80691-xopenalex-snapshot

Structure of the α1 subunit of horse Na,K‐ATPase gene

inferred← citeshttps://doi.org/10.1016/0014-5793(89)80793-8openalex-snapshot

Immunodetection of Na,K‐ATPase α3‐isoform in renal and nerve tissues

inferred← citeshttps://doi.org/10.1016/0014-5793(91)80379-hopenalex-snapshot

An organophosphorus compound, Vx, selectively inhibits the rat cardiac Na+,K+‐ATPase α1 isoform Biochemical basis of the cardiotoxicity of Vx

inferred← citeshttps://doi.org/10.1016/0014-5793(91)80400-wopenalex-snapshot

Ouabain‐ and Ca2+‐sensitive ATPase activity of chimeric Na‐ and Ca‐pump molecules

inferred← citeshttps://doi.org/10.1016/0014-5793(92)80507-dopenalex-snapshot

The A2 isoform of rat Na+,K+‐adenosine triphosphatase is active and exhibits high ouabain affinity when expressed in transfected fibroblasts

inferred← citeshttps://doi.org/10.1016/0014-5793(92)81530-yopenalex-snapshot

Molecular basis for the insensitivity of the Monarch (Danaus plexippus) to cardiac glycosides

inferred← citeshttps://doi.org/10.1016/0014-5793(94)00297-5openalex-snapshot

Structure, transmembrane topology and helix packing of P‐type ion pumps

inferred← citeshttps://doi.org/10.1016/0014-5793(94)00655-5openalex-snapshot

Cloning and characterization of the entire cDNA encoded by ATP1AL1 — a member of the human Na,K/H,K‐ATPase gene family

inferred← citeshttps://doi.org/10.1016/0016-5085(90)91159-4openalex-snapshot

The presence of H+,K+-ATPase in the crypt of rabbit distal colon demonstrated with monoclonal antibodies against gastric H+,K+-ATPase

inferred← citeshttps://doi.org/10.1016/0020-711x(90)90224-qopenalex-snapshot

Regulation of the abundance of sodium pumps in isolated animal cells

inferred← citeshttps://doi.org/10.1016/0022-2828(92)93165-gopenalex-snapshot

Myocardial Na+,K+-ATPase in tachycardia induced cardiomyopathy

inferred← citeshttps://doi.org/10.1016/0022-2828(95)90069-1openalex-snapshot

Significance of sodium pump isoforms in digitalis therapy

inferred← citeshttps://doi.org/10.1016/0024-3205(91)90402-wopenalex-snapshot

Digitalis sensitivity of Na+,K+-ATPase, myocytes and the heart

inferred← citeshttps://doi.org/10.1016/0047-6374(94)01551-vopenalex-snapshot

Age-related changes in vascular responses: a review

inferred← citeshttps://doi.org/10.1016/0304-4157(89)90019-1openalex-snapshot

Isozymes of the Na+/K+-ATPase

inferred← citeshttps://doi.org/10.1016/0304-4157(93)90012-dopenalex-snapshot

Structure-function relationships of cation binding in the Na+/K+-ATPase

inferred← citeshttps://doi.org/10.1016/0304-4157(93)90014-fopenalex-snapshot

Chemistry and energetics of transphosphorylations in the mechanism of Na+/K+-transporting ATPase: an attempt at a unifying model

inferred← citeshttps://doi.org/10.1016/0304-4157(95)00017-8openalex-snapshot

Structural organization, ion transport, and energy transduction of P-type ATPases

inferred← citeshttps://doi.org/10.1016/0304-4165(93)90073-hopenalex-snapshot

Isolation of an endogenous Na-pump specific inhibitor from normal pig urine: characterization and comparison with the inhibitor purified from bovine adrenal glands

inferred← citeshttps://doi.org/10.1016/0305-0491(94)00172-qopenalex-snapshot

An ouabain-sensitive Na+,K+-ATPase in tentacles of the sea anemone Stichodactyla helianthus

inferred← citeshttps://doi.org/10.1016/0378-1119(91)90151-zopenalex-snapshot

Cloning of a cDNA encoding an Artemia franciscana Na/K ATPase α-subunit

inferred← citeshttps://doi.org/10.1016/0888-7543(90)90569-gopenalex-snapshot

Use of denaturing gradient gel electrophoresis to detect point mutations in the factor VIII gene

inferred← citeshttps://doi.org/10.1016/0955-0674(89)90044-6openalex-snapshot

Ion pumps

inferred← citeshttps://doi.org/10.1016/0965-1748(94)90081-7openalex-snapshot

Ouabain-sensitive Na+/K+-ATPase activity in the reservoir zone of the midgut of Stomoxys calcitrans (diptera: muscidae)

inferred← citeshttps://doi.org/10.1016/1050-1738(93)90020-7openalex-snapshot

Multiple digitalis receptors

inferred← citeshttps://doi.org/10.1016/b978-0-08-057455-4.50030-xopenalex-snapshot

Sodium Pump Function

inferred← citeshttps://doi.org/10.1016/b978-0-12-013319-2.50009-7openalex-snapshot

Digitalis: Its Mode of Action, Receptor, and Structure–Activity Relationships

inferred← citeshttps://doi.org/10.1016/b978-0-12-374373-2.00022-4openalex-snapshot

Chloride Transporters in Presynaptic Inhibition, Pain and Neurogenic Inflammation

inferred← citeshttps://doi.org/10.1016/b978-0-12-381462-3.00023-9openalex-snapshot

Function of the Juxtaglomerular Apparatus

inferred← citeshttps://doi.org/10.1016/b978-0-12-509854-0.50006-1openalex-snapshot

Molecular Biological Approaches in Na+,K+-ATPase and H+,K+-ATPase Pump Studies

inferred← citeshttps://doi.org/10.1016/b978-0-12-656970-4.50018-xopenalex-snapshot

The Sodium Pump

inferred← citeshttps://doi.org/10.1016/b978-0-12-656971-1.50018-0openalex-snapshot

The Sodium Pump

inferred← citeshttps://doi.org/10.1016/b978-0-444-64057-4.00003-xopenalex-snapshot

Synthesis of Cardiac Steroids and Their Role on Heart Failure and Cancer

inferred← citeshttps://doi.org/10.1016/b978-012088488-9.50025-5openalex-snapshot

Function of the Juxtaglomerular Apparatus

inferred← citeshttps://doi.org/10.1016/j.abb.2008.05.017openalex-snapshot

Mechanistic studies of sodium pump

inferred← citeshttps://doi.org/10.1016/j.bbabio.2008.12.019openalex-snapshot

P-type ATPases as drug targets: Tools for medicine and science

inferred← citeshttps://doi.org/10.1016/j.bbabio.2009.03.021openalex-snapshot

Voltage clamp fluorometry: Combining fluorescence and electrophysiological methods to examine the structure–function of the Na+/K+-ATPase

inferred← citeshttps://doi.org/10.1016/j.bbabio.2016.08.009openalex-snapshot

Neurological disease mutations of α3 Na+,K+-ATPase: Structural and functional perspectives and rescue of compromised function

inferred← citeshttps://doi.org/10.1016/j.bbcan.2007.06.002openalex-snapshot

Cardiotonic steroids on the road to anti-cancer therapy

inferred← citeshttps://doi.org/10.1016/j.bbrc.2008.09.137openalex-snapshot

Dual activity of the H1-H2 domain of the (Na + +K + )-ATPase

inferred← citeshttps://doi.org/10.1016/j.bpj.2015.09.015openalex-snapshot

Importance of the Voltage Dependence of Cardiac Na/K ATPase Isozymes

inferred← citeshttps://doi.org/10.1016/j.bpj.2016.09.042openalex-snapshot

Intracellular Requirements for Passive Proton Transport through the Na+,K+-ATPase

inferred← citeshttps://doi.org/10.1016/j.cbpa.2021.110906openalex-snapshot

Identification of Na+/K+-ATPase α/β isoforms in Rhinella marina tissues by RNAseq and a molecular docking approach at the protein level to evaluate α isoform affinities for bufadienolides

inferred← citeshttps://doi.org/10.1016/j.cbpa.2024.111696openalex-snapshot

Primary amino acid sequences of decapod (Na+, K+)-ATPase provide evolutionary insights into osmoregulatory mechanisms

inferred← citeshttps://doi.org/10.1016/j.cub.2021.03.089openalex-snapshot

Concerted evolution reveals co-adapted amino acid substitutions in Na+K+-ATPase of frogs that prey on toxic toads

inferred← citeshttps://doi.org/10.1016/j.cub.2026.07.054openalex-snapshot

Concerted evolution reveals co-adapted amino acid substitutions in Na+K+-ATPase of frogs that prey on toxic toads.

inferred← citeshttps://doi.org/10.1016/j.ebiom.2017.06.011openalex-snapshot

Inhibition of Non Canonical HIV-1 Tat Secretion Through the Cellular Na + ,K + -ATPase Blocks HIV-1 Infection

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2010.10.003openalex-snapshot

Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance

inferred← citeshttps://doi.org/10.1016/j.ibmb.2013.09.006openalex-snapshot

Amino acid substitutions of Na,K-ATPase conferring decreased sensitivity to cardenolides in insects compared to mammals

inferred← citeshttps://doi.org/10.1016/j.ibmb.2017.08.005openalex-snapshot

Substitutions in the cardenolide binding site and interaction of subunits affect kinetics besides cardenolide sensitivity of insect Na,K-ATPase

inferred← citeshttps://doi.org/10.1016/j.jmgm.2005.02.001openalex-snapshot

Elucidation of the Na+, K+-ATPase digitalis binding site

inferred← citeshttps://doi.org/10.1016/j.jsb.2010.12.004openalex-snapshot

Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase

inferred← citeshttps://doi.org/10.1016/j.nbd.2019.104577openalex-snapshot

Factors in the disease severity of ATP1A3 mutations: Impairment, misfolding, and allele competition

inferred← citeshttps://doi.org/10.1016/j.nbd.2025.106954openalex-snapshot

Alternating hemiplegia of childhood associated mutations in Atp1a3 reveal diverse neurological alterations in mice

inferred← citeshttps://doi.org/10.1016/j.neubiorev.2013.09.013openalex-snapshot

Zebrafish as a novel model to assess Na+/K+-ATPase-related neurological disorders

inferred← citeshttps://doi.org/10.1016/j.phymed.2025.156804openalex-snapshot

The cardiac glycoside periplocymarin sensitizes gastric cancer to ferroptosis via the ATP1A1-Src-YAP/TAZ-TFRC axis

inferred← citeshttps://doi.org/10.1016/j.phytochem.2011.04.015openalex-snapshot

Coping with toxic plant compounds – The insect’s perspective on iridoid glycosides and cardenolides

inferred← citeshttps://doi.org/10.1016/j.taap.2012.04.016openalex-snapshot

The H1–H2 domain of the α1 isoform of Na+–K+–ATPase is involved in ouabain toxicity in rat ventricular myocytes

inferred← citeshttps://doi.org/10.1016/j.vascn.2018.09.001openalex-snapshot

Revisiting the binding kinetics and inhibitory potency of cardiac glycosides on Na+,K+-ATPase (α1β1): Methodological considerations

inferred← citeshttps://doi.org/10.1016/j.ydbio.2005.11.004openalex-snapshot

Na+/K+-ATPase regulates tight junction formation and function during mouse preimplantation development

inferred← citeshttps://doi.org/10.1016/j.yjmcc.2013.06.003openalex-snapshot

Cardiac sodium transport and excitation–contraction coupling

inferred← citeshttps://doi.org/10.1016/s0005-2728(98)00043-7openalex-snapshot

Structure-function relationships of E1-E2 transitions and cation binding in Na,K-pump protein

inferred← citeshttps://doi.org/10.1016/s0005-2736(01)00266-8openalex-snapshot

Molecular cloning of Na + -ATPase cDNA from a marine alga, Heterosigma akashiwo

inferred← citeshttps://doi.org/10.1016/s0005-2736(97)00167-3openalex-snapshot

Asssembly of the chimeric - and - β-subunit with the - α-subunit

inferred← citeshttps://doi.org/10.1016/s0005-2736(99)00245-xopenalex-snapshot

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

inferred← citeshttps://doi.org/10.1016/s0006-3495(92)81807-6openalex-snapshot

Molecular dissection of functional domains of the E1E2-ATPase using sodium and calcium pump chimeric molecules

inferred← citeshttps://doi.org/10.1016/s0006-3495(96)79562-0openalex-snapshot

The carbohydrate moieties of the beta-subunit of Na+, K(+)-ATPase: their lateral motions and proximity to the cardiac glycoside site

inferred← citeshttps://doi.org/10.1016/s0006-8993(02)02725-7openalex-snapshot

Changes in brain Na, K-ATPase isoform expression and enzymatic activity after aortic constriction

inferred← citeshttps://doi.org/10.1016/s0008-6363(98)00007-8openalex-snapshot

Modifications of myocardial Na+,K+-ATPase isoforms and Na+/Ca2+ exchanger in aldosterone/salt-induced hypertension in guinea pigs

inferred← citeshttps://doi.org/10.1016/s0014-5793(03)00418-6openalex-snapshot

Channel induction by palytoxin in yeast cells expressing Na+,K+‐ATPase or its chimera with sarco/endoplasmic reticulum Ca2+‐ATPase

inferred← citeshttps://doi.org/10.1016/s0014-5793(97)00182-8openalex-snapshot

Ubiquitination of Na,K‐ATPase α1 and α2 subunits

inferred← citeshttps://doi.org/10.1016/s0014-5793(98)00202-6openalex-snapshot

The Na+,K+‐ATPase carrying the carboxy‐terminal Ca2+/calmodulin binding domain of the Ca2+ pump has 2Na+,2K+ stoichiometry and lost charge movement in Na+/Na+ exchange

inferred← citeshttps://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.

inferred← citeshttps://doi.org/10.1016/s0021-9258(17)32067-7openalex-snapshot

Na+,K(+)-ATPase.

inferred← citeshttps://doi.org/10.1016/s0021-9258(17)32498-5openalex-snapshot

High yield expression of the Neurospora crassa plasma membrane H(+)-ATPase in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1016/s0021-9258(17)46764-0openalex-snapshot

Mutation of a tyrosine in the H3-H4 ectodomain of Na,K-ATPase alpha subunit confers ouabain resistance.

inferred← citeshttps://doi.org/10.1016/s0021-9258(17)46794-9openalex-snapshot

Expression of rat alpha 1 Na,K-ATPase containing substitutions of “essential” amino acids in the catalytic center.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)35791-0openalex-snapshot

Expression, purification, and properties of the plasma membrane Ca2+ pump and of its N-terminally truncated 105-kDa fragment.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)41582-7openalex-snapshot

Kinetic analysis of ouabain binding to native and mutated forms of Na,K-ATPase and identification of a new region involved in cardiac glycoside interactions.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)41740-1openalex-snapshot

Location of the cytoplasmic epitope for a K(+)-competitive antibody of the (H+,K+)-ATPase.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)41869-8openalex-snapshot

Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)41922-9openalex-snapshot

Ouabain-resistant transfectants of the murine ouabain resistance gene contain mutations in the alpha-subunit of the Na,K-ATPase.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)42269-7openalex-snapshot

Na,K-ATPase extracellular surface probed with a monoclonal antibody that enhances ouabain binding.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)46921-9openalex-snapshot

Studies on the membrane topology of the (Na,K)-ATPase.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)53014-3openalex-snapshot

Amino acid residues of the Na,K-ATPase involved in ouabain sensitivity do not bind the sugar moiety of cardiac glycosides.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)54875-4openalex-snapshot

Identification of cysteine residues in lamb kidney (Na,K)-ATPase essential for ouabain binding.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)55159-0openalex-snapshot

Identification of an extracytoplasmic region of H+,K(+)-ATPase labeled by a K(+)-competitive photoaffinity inhibitor.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)55270-4openalex-snapshot

Vascular smooth muscle expresses a truncated Na+, K(+)-ATPase alpha-1 subunit isoform.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)55391-6openalex-snapshot

Comparison of the substrate dependence properties of the rat Na,K-ATPase alpha 1, alpha 2, and alpha 3 isoforms expressed in HeLa cells.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)55392-8openalex-snapshot

Identification of sequences mediating interleukin-6 induction of a rat T kininogen gene.

inferred← citeshttps://doi.org/10.1016/s0021-9258(18)71525-1openalex-snapshot

Characterization of the Human Na,K-ATPase α2 Gene and Identification of Intragenic Restriction Fragment Length Polymorphisms

inferred← citeshttps://doi.org/10.1016/s0021-9258(19)39197-5openalex-snapshot

Structure-function studies of Na,K-ATPase. Site-directed mutagenesis of the border residues from the H1-H2 extracellular domain of the alpha subunit.

inferred← citeshttps://doi.org/10.1016/s0021-9258(19)39543-2openalex-snapshot

Synthesis and assembly of functional mammalian Na,K-ATPase in yeast.

inferred← citeshttps://doi.org/10.1016/s0021-9258(19)47148-2openalex-snapshot

A model for the stepwise radiation inactivation of the α2-dimer of Na,K-ATPase

inferred← citeshttps://doi.org/10.1016/s0021-9258(19)49484-2openalex-snapshot

Intramolecular fusion of Na pump subunits assures exclusive assembly of the fused alpha and beta subunit domains into a functional enzyme in cells also expressing endogenous Na pump subunits.

inferred← citeshttps://doi.org/10.1016/s0021-9258(19)51056-0openalex-snapshot

Identification of an amino acid substitution in human alpha 1 Na,K-ATPase which confers differentially reduced affinity for two related cardiac glycosides.

inferred← citeshttps://doi.org/10.1016/s0021-9258(19)74436-6openalex-snapshot

Random mutagenesis of the sheep Na,K-ATPase alpha-1 subunit generates a novel T797N mutation that results in a ouabain-resistant enzyme.

inferred← citeshttps://doi.org/10.1016/s0021-9258(19)89476-0openalex-snapshot

Topological analysis of H+,K(+)-ATPase using in vitro translation

inferred← citeshttps://doi.org/10.1016/s0021-9258(20)88270-2openalex-snapshot

Site-directed Mutagenesis of a Conserved, Extracellular Aspartic Acid Residue Affects the Ouabain Sensitivity of Sheep Na,K-ATPase

inferred← citeshttps://doi.org/10.1016/s0022-1910(97)00168-6openalex-snapshot

Insect Na+/K+-ATPase

inferred← citeshttps://doi.org/10.1016/s0040-4020(01)89231-0openalex-snapshot

An approach to bufadienolides from deoxycholic acid. Reactions of a steroidal αβ-unsaturated aldehyde with some O-silylated ketene acetals

inferred← citeshttps://doi.org/10.1016/s0070-2161(08)60453-0openalex-snapshot

Chapter 3 Structural Requirements for Subunit Assembly of the Na, K-ATPase

inferred← citeshttps://doi.org/10.1016/s0070-2161(08)60454-2openalex-snapshot

Chapter 4 Structure–Function Relationship of Na,K-ATPase: The Digitalis Receptor

inferred← citeshttps://doi.org/10.1016/s0079-6468(08)70377-1openalex-snapshot

4 Approach to the Chemotopography of the Digitalis Recognition Matrix in Na+/K+-transporting ATPase as a Step in the Rational Design of New Inotropic Steroids

inferred← citeshttps://doi.org/10.1016/s0163-7258(99)00037-6openalex-snapshot

Vascular sodium pump endothelial modulation and alterations in some pathological processes and aging

inferred← citeshttps://doi.org/10.1016/s1054-3589(08)60434-2openalex-snapshot

Endogenous Cardiac Glycosides

inferred← citeshttps://doi.org/10.1016/s1359-6446(97)01001-5openalex-snapshot

Toward the discovery of digitalis derivatives with inotropic selectivity

inferred← citeshttps://doi.org/10.1016/s1569-2558(08)60153-8openalex-snapshot

The Gastric H+-K+-ATPase

inferred← citeshttps://doi.org/10.1016/s1569-2582(97)80050-5openalex-snapshot

Chapter 25 Cardiac glycosides

inferred← citeshttps://doi.org/10.1016/s1874-5342(06)80007-3openalex-snapshot

The sodium PUMP

inferred← citeshttps://doi.org/10.1016/s1874-5342(06)80008-5openalex-snapshot

The gastric H+/K+-ATPase

inferred← citeshttps://doi.org/10.1017/s0031182001008484openalex-snapshot

Cloning and characterization of a muscle isoform of a Na,K-ATPase alpha subunit (SNaK1) fromSchistosoma mansoni

inferred← citeshttps://doi.org/10.1021/bi00053a020openalex-snapshot

Substitution of transmembrane residues with hydrogen-bonding potential in the .alpha. subunit of sodium-potassium ATPase reveals alterations in ouabain sensitivity

inferred← citeshttps://doi.org/10.1021/bi00062a012openalex-snapshot

The carboxy terminus of sodium and potassium ion transporting ATPase is located on the cytoplasmic surface of the membrane

inferred← citeshttps://doi.org/10.1021/bi00064a040openalex-snapshot

The epitope for the inhibitory antibody M7-PB-E9 contains Ser-646 and Asp-652 of the sheep sodium-potassium-ATPase .alpha.-subunit

inferred← citeshttps://doi.org/10.1021/bi00122a019openalex-snapshot

Effects of ouabain on the rotational dynamics of renal sodium-potassium ATPase studied by saturation-transfer EPR

inferred← citeshttps://doi.org/10.1021/bi00180a015openalex-snapshot

Analysis of Amino Acid Residues in the H5-H6 Transmembrane and Extracellular Domains of Na,K-ATPase .alpha. Subunit Identifies Threonine 797 as a Determinant of Ouabain Sensitivity

inferred← citeshttps://doi.org/10.1021/bi00212a018openalex-snapshot

Site-directed mutagenesis of the sodium-potassium-ATPase: Consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains

inferred← citeshttps://doi.org/10.1021/bi00220a035openalex-snapshot

Immunochemical and spectroscopic characterization of two fluorescein 5'-isothiocyanate labeling sites on sodium-potassium ATPase

inferred← citeshttps://doi.org/10.1021/bi800092kopenalex-snapshot

Characterization of Na,K-ATPase and H,K-ATPase Enzymes with Glycosylation-Deficient β-Subunit Variants by Voltage-Clamp Fluorometry in Xenopus Oocytes

inferred← citeshttps://doi.org/10.1021/tx500290kopenalex-snapshot

Na + ,K + -ATPase Isoform Selectivity for Digitalis-Like Compounds Is Determined by Two Amino Acids in the First Extracellular Loop

inferred← citeshttps://doi.org/10.1038/cddis.2017.94openalex-snapshot

Digoxin-induced retinal degeneration depends on rhodopsin

inferred← citeshttps://doi.org/10.1038/nature09309openalex-snapshot

Neurological disease mutations compromise a C-terminal ion pathway in the Na+/K+-ATPase

inferred← citeshttps://doi.org/10.1038/nature09978openalex-snapshot

Digoxin and its derivatives suppress TH17 cell differentiation by antagonizing RORγt activity

inferred← citeshttps://doi.org/10.1038/nmeth.1781openalex-snapshot

Decoding cell lineage from acquired mutations using arbitrary deep sequencing

inferred← citeshttps://doi.org/10.1038/s41586-019-1344-7openalex-snapshot

Structure and autoregulation of a P4-ATPase lipid flippase

inferred← citeshttps://doi.org/10.1038/s41598-019-50009-2openalex-snapshot

Distinct effects of Q925 mutation on intracellular and extracellular Na+ and K+ binding to the Na+, K+-ATPase

inferred← citeshttps://doi.org/10.1038/s42255-019-0122-zopenalex-snapshot

Cardiac glycosides are broad-spectrum senolytics

inferred← citeshttps://doi.org/10.1038/s42255-021-00371-1openalex-snapshot

Inhibition of the IL-17A axis in adipocytes suppresses diet-induced obesity and metabolic disorders in mice

inferred← citeshttps://doi.org/10.1038/srep20442openalex-snapshot

Tuning of the Na,K-ATPase by the beta subunit

inferred← citeshttps://doi.org/10.1039/c4mt00238eopenalex-snapshot

Mechanisms of cell uptake and toxicity of the anticancer drug cisplatin

inferred← citeshttps://doi.org/10.1039/d0np00047gopenalex-snapshot

Natural products as modulators of retinoic acid receptor-related orphan receptors (RORs)

showing the first 200 of 398

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.