Publications in VIVO

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Gatto, Craig ISU Faculty Member

Positions

Faculty, Biological Sciences

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selected publications

article
- Bretylium, an organic quaternary amine, inhibits the Na, K-ATPase by binding to the extracellular K-site.. Blood cells, Mol., and Dis.. 32:394-400. 2004
- Bretylium, an Organic Quaternary Amine, Inhibits the Na,KATPase by Binding to the Extracellular K-site. Blood Cells Mol. Dis.. 3:394-400.
- Chemical Modification with Dihydro-4,4'-diisothiocyanostilbene-2,2'-disulfonate Reveals the Distance Between K480 and K501 in the ATP-binding Domain of the Na,K-ATPase. Arch. Biochem. Biophys.. 340:90-100.
- Conformational Coupling: The Moving Parts of an Ion Pump. J. Bioeng. Biomemb.. 33:383-388.
- Cys^577 is a Conformationally Mobile Residue in the ATP-binding Domain of the Na, K-ATPase alpha-subunit. J. Biol. Chem.. 274:24995-25003.
- Eosin, a Potent Inhibitor of the Plasma Membrane Ca Pump, Does not Inhibit the Cardiac Na-Ca Exchanger. Biochemistry. 34:965-972.
- F-actin and Myosin II Binding Domains in Supervillin. J. Biol. Chem.. 278:46094-46106.
- Heterologous Expression of Na, K-ATPase in Insect Cells: Intracellular Distribution of Pump Subunits. Am. J. Phys.-Cell Phys.. 28:C982-C992.
- Idenification of Critical Positive Charges in XIP, the Na/Ca Exchange Inhibitory Peptide. Arch. Biochem. Biophys.. 341:273-279.
- Inhibition of NA Pump by the Antiarrthmic Drug, Bretylium. Ann. NY Acad. Sci.. 986:620-622.
- Inhibition of the Red Blood Cell Calcium Pump by Eosin and Other Fluorescein Analogues. Am. J. Physiol.. 264:C1577-1586.
- Interaction Between Na, K-ATPase alpha-subunit ATP-binding Domains. J. Biol. Chem.. 278:9176-9184.
- Interaction Between Na, K-ATPase alpha-subunit ATP-binding Domains. J. Biol. Chem.. 278:9176-9184.
- Kinetic Characterization of Tetrapropylammonium Inhibition Reveals how ATP and Pi Alter Access to the Na, K-ATPase Transport Site. Am J. Physiol. Cell.
- Lingand-induced Conformational Changes in the Na,K-ATPase Alpha Subunit. Ann. N.Y. Acad. Sci.. 834:45-55.
- Stabilization of the H, K-ATPase M5M6 Membrane Hairpin by K+ ions: Mechanistic Significance for P2-type ATPases. J. Biol. Chem.. 274:13737-13740.
- Structural Changes Associated with the Coupling of ATP Hydrolysis and Cation Transport by the Na Pump. Acta Physiol. Scand. Suppl.. 643:99-105.
- The M4M5 Cytoplasmic Loop of the Na,K-ATPase, Overexpressed in Escherichia Coli, Binds Nucleoside Triphosphates with the same Selectivity as the Intact Native Protein. J. Biol. Chem.. 273:10578-10585.
- Use of Cysteine Replacements and Chemical Modification to Alter XIP, the Autoinhibitory Region of the Na-Ca Exchanger. Inhibition of the Activated Plasma Membrane Ca Pump. Ann N.Y. Acad. Sci.. 779:286-287.
thesis or dissertation
- Fluorescein Analog Inhibition of the Erythrocyte Calcium Pump