S. Karlish

发表

Structure and mechanism of Na,K-ATPase: functional sites and their interactions.

K. Håkansson, P. L. Jørgensen, S. Karlish, 2003, Annual review of physiology.

Selective Fe2+-catalyzed Oxidative Cleavage of Gastric H+,K+-ATPase

G. Sachs, K. Munson, S. Karlish, 2001, The Journal of Biological Chemistry.

Investigation of electrogenic partial reactions in detergent-solubilized Na,K-ATPase.

M. Habeck, A. Katz, H. Apell, 2009, Biochemistry.

Purification of Na+,K+-ATPase Expressed in Pichia pastoris Reveals an Essential Role of Phospholipid-Protein Interactions*

C. Ebel, M. le Maire, A. Shainskaya, 2005, Journal of Biological Chemistry.

Fe2+-catalyzed Oxidative Cleavages of Ca2+-ATPase Reveal Novel Features of Its Pumping Mechanism*

C. Jaxel, V. Labas, J. Møller, 2004, Journal of Biological Chemistry.

Molecular Modeling of SCH28080 Binding to the Gastric H,K‐ATPase and MgATP Interactions with SERCA‐ and Na,K‐ATPases

G. Sachs, O. Vagin, K. Munson, 2003, Annals of the New York Academy of Sciences.

Preface

A. B. Maunsbach, P. L. Jørgensen, S. Karlish, 2003 .

Investigating the Energy Transduction Mechanism of P‐type ATPases with Fe2+‐Catalyzed Oxidative Cleavage

S. Karlish, S. Karlish, 2003, Annals of the New York Academy of Sciences.

Structural Organization and Energy Transduction Mechanism of Na+,K+-ATPase Studied with Transition Metal-Catalyzed Oxidative Cleavage

M. Shimon, S. Karlish, R. Goldshleger, 2001, Journal of bioenergetics and biomembranes.

The complex ATP–Fe2+ serves as a specific affinity cleavage reagent in ATP-Mg2+ sites of Na,K-ATPase: Altered ligation of Fe2+ (Mg2+) ions accompanies the E1P→E2P conformational change

S. Karlish, R. Goldshleger, G. Patchornik, 2000 .

The effect of membrane potential on the mammalian sodium‐potassium pump reconstituted into phospholipid vesicles.

A. Rephaeli, W. Stein, S. Karlish, 1987, The Journal of physiology.

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)-->E(2) conformational change.

S. Karlish, R. Goldshleger, G. Patchornik, 2000, Proceedings of the National Academy of Sciences of the United States of America.

A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase resembles cell adhesion molecules.

Y. Peleg, S. Albeck, K. Gottschalk, 2009, Biochemistry.

Familial hyperkalemia and hypertension and a hypothesis to explain proximal renal tubular acidosis

H. Mayan, Z. Farfel, S. Karlish, 2019, Proceedings of the National Academy of Sciences.

A modle for active transport of sodium and potassium ions as mediated by a tetrameric enzyme.

W. R. Lieb, W. Stein, Y. Eilam, 1973, Proceedings of the National Academy of Sciences of the United States of America.

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

A. Katz, S. Karlish, F. Noël, 2018, Journal of pharmacological and toxicological methods.

Stimulation, Inhibition, or Stabilization of Na,K-ATPase Caused by Specific Lipid Interactions at Distinct Sites

M. Habeck, A. Shevchenko, C. Toyoshima, 2014, The Journal of Biological Chemistry.

Digoxin Derivatives with Enhanced Selectivity for the α2 Isoform of Na,K-ATPase

A. Katz, D. Heller, Y. Barkana, 2014, The Journal of Biological Chemistry.

P-Type Pumps: Na+,K+-ATPase

S. Karlish, H. Haviv, 2013 .

Solubilization of a complex of tryptic fragments of Na,K-ATPase containing occluded Rb ions and bound ouabain.

S. Karlish, D. Tal, E. Or, 1996, Biochemistry.

Guanidinium derivatives act as high affinity antagonists of Na+ ions in occlusion sites of Na+,K(+)-ATPase.

H. Mayan, S. Karlish, D. Tal, 1992, The Journal of biological chemistry.

Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein.

U. Pick, S. Karlish, 1980, Biochimica et biophysica acta.

Do Src Kinase and Caveolin Interact Directly with Na,K-ATPase?*

Y. Peleg, A. Katz, T. Mehlman, 2016, The Journal of Biological Chemistry.

Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart

M. Habeck, G. Sachs, L. Dada, 2016, The Journal of Biological Chemistry.

Molecular Mechanisms and Kinetic Effects of FXYD1 and Phosphomimetic Mutants on Purified Human Na,K-ATPase*

M. Habeck, Y. Peleg, M. Eisenstein, 2015, The Journal of Biological Chemistry.

Stabilization of Na(+),K(+)-ATPase purified from Pichia pastoris membranes by specific interactions with lipids.

S. Karlish, R. Goldshleger, D. Tal, 2007, Biochemistry.

Role of FXYD proteins in ion transport.

H. Garty, S. Karlish, 2006, Annual review of physiology.

Tryptophan fluorescence of (Na+ + K+)-ATPase as a tool for study of the enzyme mechanism.

S. Karlish, D. W. Yates, 1978, Biochimica et biophysica acta.

Cardiac glycosides induced toxicity in human cells expressing α1-, α2-, or α3-isoforms of Na-K-ATPase.

H. Garty, S. Karlish, Marina Cherniavsky Lev, 2015, American journal of physiology. Cell physiology.

Renal Na,K-ATPase in genetic hypertension.

G. Bianchi, P. Parenti, A. Shainskaya, 1996, Hypertension.

Characterization of Disulfide Cross-links between Fragments of Proteolyzed Na,K-ATPase

S. Karlish, R. Goldshleger, E. Or, 1999, The Journal of Biological Chemistry.

Insulin Mimetic Effects of Vanadium

S. Amir, H. Degani, J. Sack, 1990 .

Evidence for the presence of ‘Ouabain like’ compound in human cerebrospinal fluid

R. Rimón, J. Palo, J. Deutsch, 1985, Brain Research.

A transient increase in amino acid transport modulated by insulin in differentiating muscle cells

Z. Farfel, S. Karlish, J. Prives, 1979, Journal of cellular physiology.

Endogenous "ouabain-like" activity in bovine plasma.

D. Lichtstein, S. Karlish, D. Tal, 1986, Biochemical and biophysical research communications.

Energy transfer inhibition and ion movements in isolated chloroplasts.

M. Avron, S. Karlish, 1971, European journal of biochemistry.

On the mechanism of uncoupling in chloroplasts by ion-permeability inducing agents.

M. Avron, S. Karlish, N. Shavit, 1969, European journal of biochemistry.

ATP hydrolysis associated with an uncoupled sodium flux through the sodium pump: evidence for allosteric effects of intracellular ATP and extracellular sodium

I. Glynn, S. Karlish, S. Karlish, 1976, The Journal of physiology.

Evidence against Na+-pump mediation of Ca2+-activated K+ transport and diuretic-sensitive (Na+/K+)-cotransport.

V. Lew, J. Ellory, S. Karlish, 1981, Biochimica et biophysica acta.

A Ca-dependent K channel in “luminal” membranes from the renal outer medulla

S. Karlish, C. Burnham, R. Braw, 2005, The Journal of Membrane Biology.

Na+/K+/Cl(-)-cotransporter mediated Rb+ fluxes in membrane vesicles from kidneys of normotensive and hypertensive rats.

P. Parenti, P. Ferrari, S. Karlish, 1990, Biochimica et biophysica acta.

Evidence that the cation occlusion domain of Na/K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments.

A. Shainskaya, S. Karlish, 1994, The Journal of biological chemistry.

Cation activation of the pig kidney sodium pump: transmembrane allosteric effects of sodium.

W. Stein, S. Karlish, 1985, The Journal of physiology.

Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension.

P. Manunta, G. Bianchi, P. Ferrari, 1999, The American journal of physiology.

Sidedness of the effects of sodium and potassium ions on the conformational state of the sodium—potassium pump

U. Pick, S. Karlish, S. Karlish, 1981, The Journal of physiology.

THE EFFECTS OF AN ANTISERUM TO Na+, K+‐ATPase ON THE ION‐TRANSPORTING AND HYDROLYTIC ACTIVITIES OF THE ENZYME *

V. Lew, I. Glynn, P. L. Jørgensen, 1974, Annals of the New York Academy of Sciences.

Hypermagnesuria in Humans Following Acute Intravenous Administration of Digoxin

H. Mayan, Z. Farfel, S. Karlish, 2017, Nephron.

The sodium pump.

I. Glynn, S. Karlish, S J Karlish, 1975, Annual review of physiology.

Occluded cations in active transport.

I. Glynn, S. Karlish, 1990, Annual review of biochemistry.

[17] Measurement of active and passive Na+ and K+ fluxes in reconstittued vesicles

S. Karlish, 1988 .

INTERCONVERSIONS BETWEEN SUB-CONFORMATIONAL STATES OF THE NA/K PUMP, SHOWING SIGMOID OR HYPERBOLIC ACTIVATION OF RB MOVEMENTS

W. Stein, S. Karlish, 1983 .

PROTEIN CONFORMATIONAL CHANGES IN (Na, K)‐ATPase AND THE ROLE OF CATION OCCLUSION IN ACTIVE TRANSPORT

W. Stein, S. Karlish, 1982, Annals of the New York Academy of Sciences.

Conformational transitions between Na+-bound and K+-bound forms of (Na+ + K+)-ATPase, studied with formycin nucleotides.

I. Glynn, S. Karlish, D. W. Yates, 1978, Biochimica et biophysica acta.

AN UNCOUPLED EFFLUX OF SODIUM IONS FROM HUMAN RED CELLS, PROBABLY ASSOCIATED WITH Na‐DEPENDENT ATPase ACTIVITY

I. Glynn, S. Karlish, I. M. Glynn, 1974, Annals of the New York Academy of Sciences.

Reconstitution in phospholipid vesicles of calcium-activated potassium channel from outer renal medulla

P. L. Jørgensen, D. Klaerke, S. Karlish, 2005, The Journal of Membrane Biology.

Organization of the Cation Binding Domain of the Na+/K+-pump

S. Hoving, A. Shainskaya, S. Karlish, 1994 .

2 – The Mechanism of Cation Transport by the Na+, K+-ATPase

S. Karlish, 1989 .

Rb+ occlusion in renal (Na+ + K+)-ATPase characterized with a simple manual assay.

S. Karlish, M. Shani, R. Goldschleger, 1987, Biochimica et biophysica acta.

Conformational transitions in fluorescein-labeled (Na,K)ATPase reconstituted into phospholipid vesicles.

D. Richards, A. Rephaeli, S. Karlish, 1986, The Journal of biological chemistry.

Organization of the Transmembrane Segments of Na,K-ATPase. Labeling of Lipid Embedded and Surface Domains of the a-Subunit and Its Tryptic Fragments with [125] lodonaphthylazide, [32P]ATP, and Photolabeled Ouabain

C. Gitler, S. Karlish, Peter Lethj⊘rgensen, 1983 .

Effects of ATP or phosphate on passive rubidium fluxes mediated by Na‐K‐ATPase reconstituted into phospholipid vesicles

W. Stein, S. Karlish, S. J. D. Karlish, 1982, The Journal of physiology.

Identification of a membrane-embedded segment of the large polypeptide chain of (Na+, K+)ATPase

P. L. Jørgensen, C. Gitler, S. Karlish, 1977, Nature.

Locations, abundances, and possible functions of FXYD ion transport regulators in rat renal medulla.

B. Honoré, J. Frøkiaer, H. Vorum, 2006, American journal of physiology. Renal physiology.

FXYD Proteins: New Tissue‐ and Isoform‐Specific Regulators of Na,K‐ATPase

K. Geering, H. Garty, P. Béguin, 2003, Annals of the New York Academy of Sciences.

Passive rubidium fluxes mediated by Na‐K‐ATPase reconstituted into phospholipid vesicles when ATP‐ and phosphate‐free

W. Stein, S. Karlish, S. Karlish, 1982, The Journal of physiology.

Electrogenic and electroneutral transport modes of renal Na/K ATPase reconstituted into proteoliposomes

Y. Shahak, S. Karlish, R. Goldshleger, 1990, The Journal of Membrane Biology.

Structure-activity relations of amiloride derivatives, acting as antagonists of cation binding on Na+/K(+)-ATPase.

H. Mayan, E. Cragoe, S. Karlish, 1993, Biochimica et biophysica acta.

Identification of Na+/K+-ATPase inhibitors in bovine plasma as fatty acids and hydrocarbons.

G. van Hall, S. Karlish, D. Tal, 1989, Biochimica et biophysica acta.

Electrical potential accelerates the E1P(Na)----E2P conformational transition of (Na,K)-ATPase in reconstituted vesicles.

D. Richards, A. Rephaeli, S. Karlish, 1986, The Journal of biological chemistry.

Identification and reconstitution of a Na+/K+/Cl- cotransporter and K+ channel from luminal membranes of renal red outer medulla.

P. L. Jørgensen, S. Karlish, C. Burnham, 1985, Biochimica et biophysica acta.

Kinetic parameters of glucose efflux from human red blood cells under zero-trans conditions.

W. R. Lieb, W. Stein, S. Karlish, 1972, Biochimica et biophysica acta.

Interactions between Fragments of Trypsinized Na,K-ATPase Detected by Thermal Inactivation of Rb+ Occlusion and Dissociation of the M5/M6 Fragment*

A. Shainskaya, S. Karlish, Victor Nesaty, 1998, The Journal of Biological Chemistry.

Chymotryptic Digestion of the Cytoplasmic Domain of the Subunit of Na/K-ATPase Alters Kinetics of Occlusion of Rb Ions (*)

A. Shainskaya, S. Karlish, 1996, The Journal of Biological Chemistry.

ATP hydrolysis associated with an uncoupled efflux of Na through the Na pump.

I. Glynn, S. Karlish, 1975, The Journal of physiology.

Electron paramagnetic resonance studies and insulin-like effects of vanadium in rat adipocytes.

H. Degani, M. Gochin, Y. Shechter, 1981, Biochemistry.

Insulin-like stimulation of glucose oxidation in rat adipocytes by vanadyl (IV) ions

Y. Shechter, S. Karlish, 1980, Nature.

Conformational transitions of the H,K-ATPase studied with sodium ions as surrogates for protons.

G. Sachs, S. Bassilian, S. Karlish, 1990, The Journal of biological chemistry.

Dinitrophenol and valinomycin as uncouplers in isolated chloroplasts

M. Avron, S. Karlish, 1968, FEBS letters.

An Efficient One‐Pot Enzymatic Synthesis of Cardiac Glycosides with Varied Sugar Chain Lengths

A. Plotnikov, Zhen Zhou, R. Jiang, 2019, Advanced Synthesis & Catalysis.

Analysis of light-induced proton uptake in isolated chloroplasts.

M. Avron, S. Karlish, S. Karlish, 1968, Biochimica et biophysica acta.

Entrance port for Na(+) and K(+) ions on Na(+),K(+)-ATPase in the cytoplasmic loop between trans-membrane segments M6 and M7 of the alpha subunit. Proximity Of the cytoplasmic segment of the beta subunit.

H. Apell, A. Shainskaya, S. Karlish, 2000, The Journal of biological chemistry.

Structure of the Cation Occlusion Domain of Na+/K+ ATPase Studied by Proteolysis, Interaction with Ca2+ ions and Thermal Denaturation

A. Shainskaya, S. Karlish, 1994 .

POTASSIUM IONS ON THE CONFORMATIONAL STATE OF THE SODIUM-POTASSIUM PUMP BY S. J. D. KARLISH

U. Pick, S. Karlish, 2005 .

Different approaches to the mechanism of the sodium pump.

I. Glynn, S. Karlish, 1975, Ciba Foundation symposium.

A simple, rapid and efficient procedure for purification of calmodulin from human red cells

S. Muallem, S. Karlish, 1979, FEBS letters.

Hellebrin and its aglycone form hellebrigenin display similar in vitro growth inhibitory effects in cancer cells and binding profiles to the alpha subunits of the Na+/K+-ATPase

W. Berger, R. Kiss, M. Zehl, 2013, Molecular Cancer.

Selectivity of Digitalis Glycosides for Isoforms of Human Na,K-ATPase*

Elizabeta Bab-Dinitz, A. Katz, S. Karlish, 2010, The Journal of Biological Chemistry.

The Energy Transduction Mechanism of Na,K-ATPase Studied with Iron-catalyzed Oxidative Cleavage*

S. Karlish, R. Goldshleger, S. Karlish, 1999, The Journal of Biological Chemistry.

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

P. L. Jørgensen, C. Gitler, S. Karlish, 1982, The Journal of biological chemistry.

Defective conformational response in a selectively trypsinized (Na+ + K+)-ATPase studied with tryptophan fluorescence.

P. L. Jørgensen, S. Karlish, 1980, Biochimica et biophysica acta.

Fe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domains.

S. Karlish, R. Goldshleger, R Goldshleger, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Identification of the Site of Inhibition by Omeprazole of a α-β Fusion Protein of the H,K-ATPase Using Site-directed Mutagenesis*

G. Sachs, S. Karlish, N. Lambrecht, 1998, The Journal of Biological Chemistry.

General and specific lipid-protein interactions in Na,K-ATPase.

M. Habeck, C. Toyoshima, R. Kanai, 2015, Biochimica et biophysica acta.

Transport studies by optical methods.

G. Sachs, S. Karlish, E. Rabon, 1990, Methods in enzymology.

A simple and sensitive procedure for measuring isotope fluxes through ion-specific channels in heterogenous populations of membrane vesicles.

H. Garty, B. Rudy, S. Karlish, 1983, The Journal of biological chemistry.

Chemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion.

W. Stein, S. Karlish, R. Goldshleger, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Immunocytochemical Localization of Na,K‐ATPase Gamma Subunit and CHIF in Inner Medulla of Rat Kidney

H. Vorum, H. Garty, K. Pihakaski-Maunsbach, 2003, Annals of the New York Academy of Sciences.

Characterization of conformational changes in (Na,K) ATPase labeled with fluorescein at the active site

S. Karlish, S. Karlish, 1980, Journal of bioenergetics and biomembranes.

Evidence for tryptophan residues in the cation transport path of the Na(+),K(+)-ATPase.

G. Yudowski, P. J. Garrahan, S. Karlish, 2003, Biochemistry.

Functional Properties of Na,K-ATPase, and Their Structural Implications, as Detected with Biophysical Techniques

H. Apell, S. Karlish, 2001, The Journal of Membrane Biology.

Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties

K. Geering, H. Garty, S. Karlish, 2002, Proceedings of the National Academy of Sciences of the United States of America.

A new variant of the gamma subunit of renal Na,K-ATPase. Identification by mass spectrometry, antibody binding, and expression in cultured cells.

M. Mann, B. Kuster, M. Mann, 2000, The Journal of biological chemistry.

Functional Interactions of Phospholemman (PLM) (FXYD1) with Na+,K+-ATPase

H. Garty, S. Karlish, M. Lindzen, 2006, Journal of Biological Chemistry.

Structural Interactions between FXYD Proteins and Na+,K+-ATPase

K. Gottschalk, H. Garty, S. Karlish, 2006, Journal of Biological Chemistry.

Functional Role and Immunocytochemical Localization of the γa and γb Forms of the Na,K-ATPase γ Subunit*

N. Farman, F. Cluzeaud, S. Karlish, 2001, The Journal of Biological Chemistry.

Regulatory interaction between calmodulin and ATP on the red cell Ca2+ pump.

S. Muallem, S. Karlish, 1980, Biochimica et biophysica acta.

Studies on the mechanism of regulation of the red-cell Ca2+ pump by calmodulin and ATP.

S. Muallem, S. Karlish, 1981, Biochimica et biophysica acta.

Minimal functional unit for transport and enzyme activities of (Na+ + K+)-ATPase as determined by radiation inactivation.

E. Kempner, S. Karlish, 1984, Biochimica et biophysica acta.

Regulation of the Ca2+-pump by calmodulin in intact cells.

S. Muallem, S. Karlish, 1982, Biochimica et biophysica acta.

Regulation of the conformation transition in the Ca-ATPase from sarcoplasmic reticulum by pH, temperature, and calcium ions.

U. Pick, S. Karlish, 1982, The Journal of biological chemistry.

A missense mutation converts the Na+,K+-ATPase into an ion channel and causes therapy-resistant epilepsy

M. Lindskog, H. Brismar, A. Lindstrand, 2021, The Journal of biological chemistry.

Covalent Cross-links between the γ Subunit (FXYD2) and α and β Subunits of Na,K-ATPase

B. Küster, K. Gottschalk, H. Garty, 2005, Journal of Biological Chemistry.

Interaction between cytoplasmic sodium binding sites and cardiotonic steroids

B. Schwappach, H. Apell, S. Karlish, 1994 .

Inactivation of Rb+ and Na+ occlusion on (Na+,K+)-ATPase by modification of carboxyl groups.

S. Karlish, R. Goldshleger, D. Tal, 1988, The Journal of biological chemistry.

Structural and functional interactions between FXYD5 and the Na+-K+-ATPase.

H. Garty, S. Karlish, I. Lubarski, 2007, American journal of physiology. Renal physiology.

Structural and functional interactions between FXYD5 and the Na+-K+-ATPase.

H. Garty, S. Karlish, I. Lubarski, 2007, American journal of physiology. Renal physiology.

Interaction with the Na,K-ATPase and Tissue Distribution of FXYD5 (Related to Ion Channel)*

H. Garty, K. Pihakaski-Maunsbach, A. B. Maunsbach, 2005, Journal of Biological Chemistry.

Surface Charges of the Membrane Crucially Affect Regulation of Na,K-ATPase by Phospholemman (FXYD1)

A. Katz, H. Apell, Erica Cirri, 2013, The Journal of Membrane Biology.

Phospholemman (FXYD1) raises the affinity of the human α1β1 isoform of Na,K-ATPase for Na ions.

N. Mishra, A. Katz, H. Apell, 2011, Biochemistry.

Specific phospholipid binding to Na,K-ATPase at two distinct sites

M. Habeck, M. Sharon, S. Karlish, 2017, Proceedings of the National Academy of Sciences.

FXYD proteins: tissue-specific regulators of the Na,K-ATPase.

H. Garty, S. Karlish, 2005, Seminars in nephrology.

Evidence for an interaction between adducin and Na+-K+-ATPase: relation to genetic hypertension.

P. Manunta, G. Bianchi, P. Ferrari, 1999, American journal of physiology. Heart and circulatory physiology.

Ouabain-induced Internalization and Lysosomal Degradation of the Na+/K+-ATPase

H. Garty, O. Golani, S. Karlish, 2013, The Journal of Biological Chemistry.

Mutational analysis of the K+-competitive inhibitor site of gastric H,K-ATPase.

G. Sachs, O. Vagin, K. Munson, 2001, Biochemistry.

Ion channel-mediated fluxes in membrane vesicles: selective amplification of isotope uptake by electrical diffusion potentials.

H. Garty, S. Karlish, 1989, Methods in enzymology.

Digoxin derivatives with selectivity for the α2β3 isoform of Na,K-ATPase potently reduce intraocular pressure

M. Habeck, A. Katz, D. Heller, 2015, Proceedings of the National Academy of Sciences.

Vanadate inhibits (Na+ + K+)ATPase by blocking a conformational change of the unphosphorylated form

I. Glynn, S. Karlish, L. Beaugé, 1979, Nature.

Elementary steps of the (Na+ + K+)-ATPase mechanism, studied with formycin nucleotides.

I. Glynn, S. Karlish, D. W. Yates, 1978, Biochimica et biophysica acta.

The ATP-Mg2+ binding site and cytoplasmic domain interactions of Na+,K+-ATPase investigated with Fe2+-catalyzed oxidative cleavage and molecular modeling.

G. Sachs, A. Shainskaya, K. Munson, 2002, Biochemistry.

Metal-catalysed cleavage of Na,K-ATPase as a tool for study of structure-function relations.

S. Karlish, R. Goldshleger, E. Or, 1998, Acta physiologica Scandinavica. Supplementum.

The ATP-Mg 2 + Binding Site and Cytoplasmic Domain Interactions of Na + , K +-ATPase Investigated with Fe 2 +-Catalyzed Oxidative Cleavage and Molecular Modeling †

G. Sachs, A. Shainskaya, K. Munson, 2022 .

Probing the cation binding site of Na + /K + -ATPase with competitive Na + antagonists

A. Shainskaya, S. Karlish, R. Goldshleger, 1994 .

Effects of competitive sodium-like antagonists on Na,K-ATPase suggest that cation occlusion from the cytoplasmic surface occurs in two steps.

A. Shainskaya, S. Karlish, D. Tal, 1993, The Journal of biological chemistry.

Extensive digestion of Na+,K(+)-ATPase by specific and nonspecific proteases with preservation of cation occlusion sites.

S. Hoving, J. Capasso, S. Karlish, 1992, The Journal of biological chemistry.

A 19-kDa C-terminal tryptic fragment of the alpha chain of Na/K-ATPase is essential for occlusion and transport of cations.

W. Stein, S. Karlish, R. Goldshleger, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Neutralization of the Charge on Asp369 of Na+,K+-ATPase Triggers E1 ↔ E2 Conformational Changes*

S. Karlish, H. Haviv, Talya Belogus, 2009, The Journal of Biological Chemistry.

Novel Aromatic Isothiouronium Derivatives Which Act as High Affinity Competitive Antagonists of Alkali Metal Cations on Na/K-ATPase (*)

S. Hoving, S. Karlish, R. Goldshleger, 1995, The Journal of Biological Chemistry.

Stabilization of the α2 Isoform of Na,K-ATPase by Mutations in a Phospholipid Binding Pocket*

M. Ilan, S. Carmeli, O. Yarden, 2011, The Journal of Biological Chemistry.

Organization of the Membrane Domain of the Na/K‐Pump.

S. Karlish, 1997, Annals of the New York Academy of Sciences.

FXYD Proteins Stabilize Na,K-ATPase

Y. Peleg, N. Mishra, D. Voelker, 2011, The Journal of Biological Chemistry.

Purification of the human alpha2 Isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1.

H. Garty, S. Karlish, R. Goldshleger, 2007, Biochemistry.

Hellebrin and its aglycone form hellebrigenin display similar in vitro growth inhibitory effects in cancer cells and binding profiles to the alpha subunits of the Na+/K+-ATPase

W. Berger, R. Kiss, M. Zehl, 2013, Molecular Cancer.

Binding of sodium ions and cardiotonic steroids to native and selectively trypsinized Na,K pump, detected by charge movements.

B. Schwappach, H. Apell, S. Karlish, 1994, The Journal of biological chemistry.

Renal Mg handling, FXYD2 and the central role of the Na,K‐ATPase

H. Mayan, Z. Farfel, S. Karlish, 2018, Physiological reports.

Studies on conformational changes in Na,K-ATPase labeled with 5-iodoacetamidofluorescein.

S. Karlish, M. Steinberg, 1989, Journal of Biological Chemistry.

Structural integrity of the membrane domains in extensively trypsinized Na,K-ATPase from shark rectal glands.

D. Marsh, L. Sottrup-jensen, S. Karlish, 1994, Biochemistry.

Neutral Phospholipids Stimulate Na,K-ATPase Activity

M. Habeck, C. Toyoshima, R. Kanai, 2013, The Journal of Biological Chemistry.

A functional interaction between CHIF and Na-K-ATPase: implication for regulation by FXYD proteins.

N. Farman, H. Garty, S. Karlish, 2002, American journal of physiology. Renal physiology.

Generation and phenotypic analysis of CHIF knockout mice.

H. Garty, C. Asher, P. Lonai, 2002, American journal of physiology. Renal physiology.

Surface Charges of the Membrane Crucially Affect Regulation of Na,K-ATPase by Phospholemman (FXYD1)

A. Katz, H. Apell, Erica Cirri, 2013, The Journal of Membrane Biology.

Expression of Na+,K+-ATPase in Pichia pastoris

K. Gottschalk, D. Strugatsky, S. Karlish, 2003, Journal of Biological Chemistry.

Tissue-specific Distribution and Modulatory Role of the γ Subunit of the Na,K-ATPase

A. Therien, S. Karlish, R. Goldshleger, 1997, The Journal of Biological Chemistry.

Structure-Function Relations of Interactions between Na,K-ATPase, the γ Subunit, and Corticosteroid Hormone-induced Factor*

H. Garty, S. Karlish, Y. Lifshitz, 2003, Journal of Biological Chemistry.

Expression and Functional Role of the γ Subunit of the Na,K-ATPase in Mammalian Cells*

A. Therien, S. Karlish, R. Blostein, 1999, The Journal of Biological Chemistry.

Topology of the alpha-subunit of Na,K-ATPase based on proteolysis. Lability of the topological organization.

S. Karlish, R. Goldshleger, D. Tal, 1995, Biochemistry.

Location of Asn831 of the alpha chain of Na/K-ATPase at the cytoplasmic surface. Implication for topological models.

P. L. Jørgensen, S. Karlish, R. Goldshleger, 1993, The Journal of biological chemistry.

Digoxin Derivatives with Enhanced Selectivity for the α2 Isoform of Na,K-ATPase

A. Katz, D. Heller, Y. Barkana, 2014, The Journal of Biological Chemistry.

Stabilization of the α2 Isoform of Na,K-ATPase by Mutations in a Phospholipid Binding Pocket*

M. Ilan, S. Carmeli, O. Yarden, 2011, The Journal of Biological Chemistry.

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