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11. Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies

15. The reason for the low Ca 2+ -sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is “freezing” of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle

16. The primary cause of muscle disfunction associated with substitutions E240K and R244G in tropomyosin is aberrant behavior of tropomyosin and response of actin and myosin during ATPase cycle

43. Caldesmon inhibits both force development and transition of actin monomers from “OFF” to “ON” conformational state by changing its position in thin filaments

45. The effect of myosin light chain phosphorylation and Mg2+ on the conformation of myosin in thick filaments of glycerinated fibers of rabbit skeletal muscle.

46. Effect of troponin-tropomyosin complex and Ca2+ on conformational changes in F-actin induced by myosin subfragment-1.

47. Effect of Ca2+ Binding to 5,5 -Dithiobis(2-nitrobenzoic acid) Light Chains on Conformational Changes of F-Actin Caused by Myosin Subfragment-1.

49. Secretion from permeabilised mast cells is enhanced by addition of gelsolin: contrasting effects of endogenous gelsolin

50. The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.

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