The thermodynamic essence of the reversible inactivation of Na+/K+-transporting ATPase by various digitalis derivatives is relaxation of enzyme conformational energy
References (49)
- et al.
Trends Pharmacol. Sci.
(1984) - et al.
Trends Pharmacol. Sci.
(1980) - et al.
Biochim. Biophys. Acta
(1966) - et al.
J. Biol. Chem.
(1951) Adv. Protein Chem.
(1964)- et al.
Biochem. Pharmac.
(1984) - et al.
J. Biol. Chem.
(1974) - et al.
J. Biol. Chem.
(1977) - et al.
J. Biol. Chem.
(1982)
J. Biol. Chem.
(1969)
Biochim. Biophys. Acta
(1973)
J. Biol. Chem.
(1975)
Klin. Wochenschr.
(1964)
Experientia
(1963)
Arzneim. Forsch.
(1964)
Naunyn-Schmiedeberg's Arch. Pharmacol.
(1985)
Annu. Rev. Biophys. Bioeng.
(1983)
Revised Tentative Rules for Nomenclature of Steroids
Biochemistry
(1969)
Khim. Prirodn. Soed.
(1976)
Khim. Prirodn. Soed.
(1977)
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