Dabrowska R - 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: dabrowska r. 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

Visualization of caldesmon binding to synthetic filaments of smooth muscle myosin.

Kulikova N, Podlubnaya Z, Makuch R, Dabrowska R. Kulikova N, et al. Among authors: dabrowska r. J Muscle Res Cell Motil. 2003;24(1):7-13. doi: 10.1023/a:1024843409429. J Muscle Res Cell Motil. 2003. PMID: 12953833

3

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: dabrowska r. 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

4

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: dabrowska r. 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.

5

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

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

6

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: dabrowska r. Biochim Biophys Acta. 1988 Sep 21;956(2):140-50. doi: 10.1016/0167-4838(88)90260-9. Biochim Biophys Acta. 1988. PMID: 3167066

7

The influence of caldesmon on papain proteolysis of monomeric smooth muscle myosin.

Kulikova N, Dabrowska R. Kulikova N, et al. Among authors: dabrowska r. Biochem Biophys Res Commun. 1996 Aug 5;225(1):195-202. doi: 10.1006/bbrc.1996.1153. Biochem Biophys Res Commun. 1996. PMID: 8769117

8

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. Among authors: dabrowska r. 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

9

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. Among authors: dabrowska r. 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

10

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: dabrowska r. 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

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