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Journal Abstract Search
74 related items for PubMed ID: 3964288
1. The distances separating Tyr-69 from the high-affinity nucleotide and metal binding sites in actin. Barden JA, Miki M. Biochem Int; 1986 Feb; 12(2):321-9. PubMed ID: 3964288 [Abstract] [Full Text] [Related]
2. Fluorescence energy transfer between Tyr 69 and Cys 374 in actin. Barden JA. Biochem Int; 1985 Oct; 11(4):583-9. PubMed ID: 4084319 [Abstract] [Full Text] [Related]
3. The distance separating Cys-10 from the high-affinity metal binding site in actin. Miki M, Barden JA, dos Remedios CG. Biochem Int; 1986 Jun; 12(6):807-13. PubMed ID: 3741444 [Abstract] [Full Text] [Related]
5. A determination of the radial coordinate of Tyr-69 in F-actin using fluorescence energy transfer. Miki M, dos Remedios CG. Biochem Int; 1990 Oct; 22(1):125-32. PubMed ID: 2126434 [Abstract] [Full Text] [Related]
10. The catalytic site of AMP nucleosidase. Substrate specificity and pH effects with AMP and formycin 5'-PO4. DeWolf WE, Fullin FA, Schramm VL. J Biol Chem; 1979 Nov 10; 254(21):10868-75. PubMed ID: 40976 [No Abstract] [Full Text] [Related]
11. Calponin binds G-actin and F-actin with similar affinity. Ferjani I, Fattoum A, Maciver SK, Manai M, Benyamin Y, Roustan C. FEBS Lett; 2006 Sep 04; 580(20):4801-6. PubMed ID: 16901482 [Abstract] [Full Text] [Related]
12. Domain motion between the regulatory light chain and the nucleotide site in skeletal myosin. Xu J, Root DD. J Struct Biol; 1998 Oct 04; 123(2):150-61. PubMed ID: 9843669 [Abstract] [Full Text] [Related]
13. Effect of nucleotides and actin on the orientation of the light chain-binding domain in myosin subfragment 1. Smyczynski C, Kasprzak AA. Biochemistry; 1997 Oct 28; 36(43):13201-7. PubMed ID: 9341208 [Abstract] [Full Text] [Related]
14. Prodan fluorescence reflects differences in nucleotide-induced conformational states in the myosin head and allows continuous visualization of the ATPase reactions. Hiratsuka T. Biochemistry; 1998 May 19; 37(20):7167-76. PubMed ID: 9585528 [Abstract] [Full Text] [Related]
15. A conformational change in F-actin when myosin binds: fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374. Moens PD, dos Remedios CG. Biochemistry; 1997 Jun 17; 36(24):7353-60. PubMed ID: 9200683 [Abstract] [Full Text] [Related]
16. Estimation of the distance change between cysteine-457 and the nucleotide binding site when sodium pump changes conformation from E1 to E2 by fluorescence energy transfer measurements. Lin SH, Faller LD. Biochemistry; 1996 Jun 25; 35(25):8419-28. PubMed ID: 8679600 [Abstract] [Full Text] [Related]
17. Fluorescence energy transfer between points in G-actin: the nucleotide-binding site, the metal-binding site and Cys-373 residue. Miki M, Wahl P. Biochim Biophys Acta; 1985 Apr 05; 828(2):188-95. PubMed ID: 3978110 [Abstract] [Full Text] [Related]
18. Structural dynamics of actin during active interaction with myosin: different effects of weakly and strongly bound myosin heads. Prochniewicz E, Walseth TF, Thomas DD. Biochemistry; 2004 Aug 24; 43(33):10642-52. PubMed ID: 15311925 [Abstract] [Full Text] [Related]
19. Effect of replacement of the tightly bound Ca2+ by Ba2+ on actin polymerization. DalleDonne I, Milzani A, Colombo R. Arch Biochem Biophys; 1998 Mar 15; 351(2):141-8. PubMed ID: 9514647 [Abstract] [Full Text] [Related]
20. Fluorescence energy transfer measurements between the nucleotide binding site and Cys-373 in actin and their application to the kinetics of actin polymerization. Miki M, Iio T. Biochim Biophys Acta; 1984 Nov 09; 790(3):201-7. PubMed ID: 6487636 [Abstract] [Full Text] [Related] Page: [Next] [New Search]