These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
170 related articles for article (PubMed ID: 3514189)
1. [Cross-linking of SH-groups in myosin heads changes the type of conformation changes in F-actin induced by myosin subfragment 1 or heavy meromyosin]. Borovikov IuS; Konkol' I; Levitskiĭ DI Dokl Akad Nauk SSSR; 1986; 287(1):216-9. PubMed ID: 3514189 [No Abstract] [Full Text] [Related]
2. [High sensitivity to Ca2 ions of the conformational changes of F-actin, induced by the myosin 1 subfragment]. Borovikov IuS; Levitskiĭ DI Biokhimiia; 1984 May; 49(5):767-71. PubMed ID: 6743705 [TBL] [Abstract][Full Text] [Related]
3. Fluorescence polarization study on Ca2+-sensitivity of conformational changes in F-actin induced by the formation of F-actin-subfragment-1 complex. Borovikov YuS ; Levitsky DI Gen Physiol Biophys; 1985 Oct; 4(5):457-63. PubMed ID: 3934031 [TBL] [Abstract][Full Text] [Related]
4. [Effect of caldesmon on the type of conformation changes in F-actin induced by the binding of myosin 1 subfragment]. Borovikov IuS; Galazkiewicz B; Dabrowska R Biokhimiia; 1988 Feb; 53(2):179-81. PubMed ID: 3370245 [TBL] [Abstract][Full Text] [Related]
5. [The effect of proteolysis of myosin heads on conformational changes induced by them in F-actin]. Borovikov IuS; Kuleva NV; Khoroshev MI; Vdovina IB Biokhimiia; 1988 Oct; 53(10):1754-7. PubMed ID: 2976603 [TBL] [Abstract][Full Text] [Related]
6. [Effect of Ca2+ on the motility of myosin head in the F-actin-HMM complex]. Borovikov IuS; Wrotek M; Aksenova NB; Lebedeva NN; Kankol I Biokhimiia; 1988 Jan; 53(1):97-100. PubMed ID: 3282547 [TBL] [Abstract][Full Text] [Related]
7. [Phosphorylation of light chains of myosin from rabbit skeletal muscles affects the type of conformation changes of F-actin induced by heavy meromyosin]. Borovikov IuS; Konkol I; Szczesna D; Kirillina VP; Levitskiĭ DI Biokhimiia; 1986 Apr; 51(4):691-4. PubMed ID: 3518814 [TBL] [Abstract][Full Text] [Related]
8. [The disappearance of the dependence of actin-myosin interaction on the phosphorylation of myosin light chains in the "freezing" of the structure of heavy meromyosin by a bifunctional reagent]. Borovikov IuS; Szczesna D; Khoroshev MI; Kakol I Tsitologiia; 1990; 32(5):481-8. PubMed ID: 2275017 [TBL] [Abstract][Full Text] [Related]
9. Cooperative rigor binding of myosin to actin is a function of F-actin structure. Orlova A; Egelman EH J Mol Biol; 1997 Feb; 265(5):469-74. PubMed ID: 9048941 [TBL] [Abstract][Full Text] [Related]
10. Difference between subfragment-1 and heavy meromyosin in their interaction with F-actin. Yamamoto K; Sekine T J Biochem; 1986 Jan; 99(1):199-206. PubMed ID: 3514591 [TBL] [Abstract][Full Text] [Related]
11. Lactate dehydrogenase-induced conformational changes of F-actin in myosin-free ghost single fibres. Kirillina VP; Stabrovskaya VI; Borovikov YuS Gen Physiol Biophys; 1989 Oct; 8(5):435-46. PubMed ID: 2531693 [TBL] [Abstract][Full Text] [Related]
12. The effects of divalent cations on the rotational mobility of myosin, heavy meromyosin and myosin subfragment-1 and on the binding of heavy meromyosin to actin. Highsmith S Biochim Biophys Acta; 1978 Sep; 536(1):156-64. PubMed ID: 361092 [TBL] [Abstract][Full Text] [Related]
13. Modulation of actin conformation and inhibition of actin filament velocity by calponin. Borovikov YuS ; Horiuchi KY; Avrova SV; Chacko S Biochemistry; 1996 Oct; 35(43):13849-57. PubMed ID: 8901528 [TBL] [Abstract][Full Text] [Related]
14. [Caldesmon inhibits formation of strongly bound myosin cross-bridges and activates an ability of weakly bound cross-bridges to transform actin monomers to the off-conformation]. Vikhorev PG; Vikhoreva NN; Rosliakova MA; Chacko S; Borovikov IuS Tsitologiia; 2000; 42(5):444-53. PubMed ID: 10890050 [TBL] [Abstract][Full Text] [Related]
15. Fluorescence anisotropy of labeled F-actin: influence of divalent cations on the interaction between F-actin and myosin heads. Miki M; Wahl P; Auchet JC Biochemistry; 1982 Jul; 21(15):3661-5. PubMed ID: 6214272 [TBL] [Abstract][Full Text] [Related]
16. [Structural changes in muscle fiber contractile proteins studied by polarization ultraviolet fluorescence microscopy. VI. Conformational restructurings of F-actin induced by the binding of heavy meromyosin]. Borovikov IuS; Kirillina VP; Filatova LG Tsitologiia; 1982 May; 24(5):555-60. PubMed ID: 7048675 [TBL] [Abstract][Full Text] [Related]
17. [Structural changes in the contractile proteins of muscle fiber studied by polarization ultraviolet fluorescence microscopy. VII. The effect of Ca2+ on the nature of the conformational changes in F-actin induced by the binding of heavy meromyosin]. Borovikov IuS; Karandashov EA Tsitologiia; 1984 Apr; 26(4):432-7. PubMed ID: 6401151 [TBL] [Abstract][Full Text] [Related]
18. [DTNB-light chain controls the conformational rearrangements of F-actin induced by myosin subfragment I]. Borovikov IuS; Levitskiĭ DI; Kirillina VP; Poglazov BF Dokl Akad Nauk SSSR; 1981; 259(3):732-5. PubMed ID: 7306349 [No Abstract] [Full Text] [Related]
19. Effect of Ca2+ on conformation of actin in the F-actin--heavy meromyosin complex. Borovikov YS; Karandashov EA Biochem Int; 1983 Sep; 7(3):319-28. PubMed ID: 6383393 [TBL] [Abstract][Full Text] [Related]
20. [Conformational changes of actin induced by strong or weak myosin subfragment-1 binding]. Dedova IV; Avrova SV; Vikhoreva NN; Vikhorev RG; Hazlett TL; Van der Meer W; Dos Remedios CG; Borovikov IuS Tsitologiia; 2004; 46(8):719-34. PubMed ID: 15598019 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]