Borovikov YS - Search Results

1

Caldesmon inhibits the actin-myosin interaction by changing its spatial orientation and mobility during the ATPase activity cycle.

Kulikova N, Pronina OE, Dabrowska R, Borovikov YS. Kulikova N, et al. Among authors: borovikov ys. Biochem Biophys Res Commun. 2007 Jun 1;357(2):461-6. doi: 10.1016/j.bbrc.2007.03.154. Epub 2007 Apr 2. Biochem Biophys Res Commun. 2007. PMID: 17428444

2

Caldesmon restricts the movement of both C- and N-termini of tropomyosin on F-actin in ghost fibers during the actomyosin ATPase cycle.

Kulikova N, Pronina OE, Dabrowska R, Borovikov YS. Kulikova N, et al. Among authors: borovikov ys. Biochem Biophys Res Commun. 2006 Jun 23;345(1):280-6. doi: 10.1016/j.bbrc.2006.04.074. Epub 2006 Apr 27. Biochem Biophys Res Commun. 2006. PMID: 16678131

3

Caldesmon inhibits the rotation of smooth actin subdomain-1 and alters its mobility during the ATP hydrolysis cycle.

Kulikova N, Avrova SV, Borovikov YS. Kulikova N, et al. Among authors: borovikov ys. Biochem Biophys Res Commun. 2009 Dec 4;390(1):125-9. doi: 10.1016/j.bbrc.2009.09.079. Epub 2009 Sep 24. Biochem Biophys Res Commun. 2009. PMID: 19782047

4

Caldesmon weakens the bonding between myosin heads and actin in ghost fibers.

Nowak E, Borovikov YS, Dabrowska R. Nowak E, et al. Among authors: borovikov ys. Biochim Biophys Acta. 1989 Dec 21;999(3):289-92. doi: 10.1016/0167-4838(89)90011-3. Biochim Biophys Acta. 1989. PMID: 2605265

5

Comparison of Ca2+-dependent effects of caldesmon-tropomyosin-calmodulin and troponin-tropomyosin complexes on the structure of F-actin in ghost fibers and its interaction with myosin heads.

Dobrowolski Z, Borovikov YS, Nowak E, Gałazkiewicz B, Dabrowska R. Dobrowolski Z, et al. Among authors: borovikov ys. Biochim Biophys Acta. 1988 Sep 21;956(2):140-50. doi: 10.1016/0167-4838(88)90260-9. Biochim Biophys Acta. 1988. PMID: 3167066

6

Behavior of caldesmon upon interaction of thin filaments with myosin subfragment 1 in ghost fibers.

Borovikov YS, Wrzosek A, Kulikova N, Vikhorev P, Vikhoreva N, Dabrowska R. Borovikov YS, et al. Biochim Biophys Acta. 2004 Jun 1;1699(1-2):183-9. doi: 10.1016/j.bbapap.2004.02.013. Biochim Biophys Acta. 2004. PMID: 15158726

7

Caldesmon freezes the structure of actin filaments during the actomyosin ATPase cycle.

Borovikov YS, Kulikova N, Pronina OE, Khaimina SS, Wrzosek A, Dabrowska R. Borovikov YS, et al. Biochim Biophys Acta. 2006 Jun;1764(6):1054-62. doi: 10.1016/j.bbapap.2006.04.001. Epub 2006 Apr 7. Biochim Biophys Acta. 2006. PMID: 16713410

8

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

Pronina OE, Makuch R, Wrzosek A, Dabrowska R, Borovikov YS. Pronina OE, et al. Among authors: borovikov ys. Cell Biol Int. 2007 Apr;31(4):394-404. doi: 10.1016/j.cellbi.2007.01.026. Epub 2007 Jan 21. Cell Biol Int. 2007. PMID: 17321764

9

Troponin I and caldesmon restrict alterations in actin structure occurring on binding of myosin subfragment 1.

Nowak E, Borovikov YS, Khoroshev MI, Dabrowska R. Nowak E, et al. Among authors: borovikov ys. FEBS Lett. 1991 Apr 9;281(1-2):51-4. doi: 10.1016/0014-5793(91)80356-8. FEBS Lett. 1991. PMID: 2015908 Free article.

10

The effect of caldesmon on actin-myosin interaction in skeletal muscle fibers.

Gałazkiewicz B, Borovikov YS, Dabrowska R. Gałazkiewicz B, et al. Among authors: borovikov ys. Biochim Biophys Acta. 1987 Dec 18;916(3):368-75. doi: 10.1016/0167-4838(87)90182-8. Biochim Biophys Acta. 1987. PMID: 3689797

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