Published in Biokhimiia on November 07, 1968
[Correlation adaptometry as a method of screening of the population]. Vestn Akad Med Nauk SSSR (1988) 0.79
[Increased substrate selectivity during transition from Ca2+-activated to K+,EDTA-activated nucleoside triphosphatase activity of heavy meromyosin]. Biokhimiia (1988) 0.77
[Kinetic analysis of hydrolysis of free ATP and MgATP by natural actomyosin]. Biokhimiia (1976) 0.76
[Effect of the ionic strength and modification of the sulfhydryl groups on the kinetics of the ATPase reaction of myosin]. Biokhimiia (1974) 0.75
[Role of cations in the occurrence of differences in the myosin hydrolysis of ATP and ITP]. Nauchnye Doki Vyss Shkoly Biol Nauki (1982) 0.75
[Study of the magnesium inhibition of the myosin ATPase reaction]. Biokhimiia (1975) 0.75
[Dialdehyde derivatives of purine mononucleotides: substrate properties and affinity modification of myosin ATPase]. Biokhimiia (1985) 0.75
[pH-dependence characteristics of Ca-ATPase activity of heavy meromyosin with modified SH-groups]. Biokhimiia (1977) 0.75
[Alkaline activation of myosin ATPase: some thermodynamic characteristics]. Biokhimiia (1976) 0.75
[Study of the stationary kinetics of the myosin ATPase reaction in the presence of calcium]. Biokhimiia (1975) 0.75
[Affinity modification of heavy meromyosin and subfragment 1 by mixed anhydrides of [14C] AMP, epsilon AMP and mesitylene carboxylic acid]. Biokhimiia (1982) 0.75
[The effect of natural imidazole compounds on the adenosine triphosphatase activity of myosin]. Biokhimiia (1968) 0.75
[Comparative study of the effect of imidazole compounds on ATPase activity of myosin isolated from muscles of various animals]. Biokhimiia (1969) 0.75
[Several peculiarities of the purine-base fixation of the substrate in the active sites of myosin Ca2+-ATPase]. Biokhimiia (1984) 0.75
[Characterization of two types of binding sites of substrate-like inhibitors in the heavy meromyosin molecule]. Biokhimiia (1982) 0.75
[Kinetics of the interaction of a phosphorylating substrate analog with the Ca-ATPase of myosin and heavy meromyosin]. Nauchnye Doki Vyss Shkoly Biol Nauki (1982) 0.75
[Kinetic study of the pH-dependence of maximal rate of Ca-ATP hydrolysis by myosin]. Biokhimiia (1977) 0.75
[Affinity modification of myosin with protected active centers: confirmation of the existence of an allosteric substrate-binding segment]. Biokhimiia (1989) 0.75
[Effect of storage conditions on the kinetic properties of myosin ATPase]. Biokhimiia (1976) 0.75
[Complex formation between carnosine and ATP]. Dokl Akad Nauk SSSR (1971) 0.75
[Early differential diagnosis of gallbladder diseases]. Sov Med (1988) 0.75
[Inhibition of the Ca-ATPase activity of heavy meromyosin by phosphorylating analogs of the substrate]. Biokhimiia (1980) 0.75
[Effect of Ca2+ ion concentration on the kinetics of ATP hydrolysis by myosin]. Biokhimiia (1975) 0.75
[The effect of sulfhydryl reagents and the role of SH-groups in the ATPase activity of myosin]. Biokhimiia (1974) 0.75
[Interaction of potassium and magnesium ions in the ATPase activity of heavy meromyosin]. Nauchnye Doki Vyss Shkoly Biol Nauki (1981) 0.75
[The effect of imidazole compounds on the ATPase activity of myosin during heat denaturation and in the presence of some reagents]. Biokhimiia (1968) 0.75
Investigation of myosin substrate-binding site using phosphorylating analogs of the substrate. Biochem Int (1985) 0.75
[Characteristics of affinity modification of myosin ATPase under the action of monoaldehyde derivatives of ADP]. Biokhimiia (1991) 0.75