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Showing results for maruta soka
Search for Marta Sokal instead (1 results)
Formation and characterization of kinesin.ADP.fluorometal complexes.
Shibuya H, Kondo K, Kimura N, Maruta S. Shibuya H, et al. J Biochem. 2002 Oct;132(4):573-9. doi: 10.1093/oxfordjournals.jbchem.a003259. J Biochem. 2002. PMID: 12359072 Free article.
We have previously demonstrated that, in the presence of ADP, myosin forms stable ternary complexes with new phosphate analogues of aluminum fluoride (AlF(4)(-)) and beryllium fluoride (BeF(n)), and these stable complexes mimic the transient state along the ATPase kinetic pathway …
We have previously demonstrated that, in the presence of ADP, myosin forms stable ternary complexes with new phosphate analogues of aluminum …
Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction.
Maruta S, Homma K. Maruta S, et al. J Biochem. 2000 Oct;128(4):695-704. doi: 10.1093/oxfordjournals.jbchem.a022803. J Biochem. 2000. PMID: 11011153 Free article.
Myosin has three highly-conserved, unique loops [B (320-327), M (677-689), and N (127-136)] at the entrance of the ATP binding cleft, and we previously showed that the effects of actin are mediated by a conformational change in loop M [Maruta and Homma (1998) J. Biochem. 1 …
Myosin has three highly-conserved, unique loops [B (320-327), M (677-689), and N (127-136)] at the entrance of the ATP binding cleft, and we …
37 results