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Journal Abstract Search
86 related items for PubMed ID: 638187
1. Fluorescence energy transfer between epsilon-ATP at the nucleotide binding site and N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide at Cys-373 of G-actin. Miki M, Mihashi K. Biochim Biophys Acta; 1978 Mar 28; 533(1):163-72. PubMed ID: 638187 [Abstract] [Full Text] [Related]
2. 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]
3. Fluorescence resonance energy transfer between the nucleotide binding site and Cys-10 in G-actin and F-actin. Miki M, Barden JA, dos Remedios CG. Biochim Biophys Acta; 1986 Jul 25; 872(1-2):76-82. PubMed ID: 3089284 [Abstract] [Full Text] [Related]
4. Distance between nucleotide site and cysteine-373 of G-actin by resonance energy transfer measurements. Cheung HC, Liu BM. J Muscle Res Cell Motil; 1984 Feb 25; 5(1):65-80. PubMed ID: 6715528 [Abstract] [Full Text] [Related]
5. Spatial relationship between the nucleotide-binding site, Lys-61 and Cys-374 in actin and a conformational change induced by myosin subfragment-1 binding. Miki M, dos Remedios CG, Barden JA. Eur J Biochem; 1987 Oct 15; 168(2):339-45. PubMed ID: 3117545 [Abstract] [Full Text] [Related]
6. Detection of conformational changes in actin by fluorescence resonance energy transfer between tyrosine-69 and cysteine-374. Miki M. Biochemistry; 1991 Nov 12; 30(45):10878-84. PubMed ID: 1932011 [Abstract] [Full Text] [Related]
8. Fluorescence resonance energy transfer between sites in G-actin. The spatial relationship between Cys-10, Tyr-69, Cys-374, the high-affinity metal and the nucleotide. Barden JA, dos Remedios CG. Eur J Biochem; 1987 Oct 01; 168(1):103-9. PubMed ID: 3665911 [Abstract] [Full Text] [Related]
10. Fluorescence studies of 1,N6-ethenoadenosine triphosphate bound to G-actin: the nucleotide base is inaccessible to water. Harvey SC, Cheung HC. Biochem Biophys Res Commun; 1976 Dec 20; 73(4):865-8. PubMed ID: 15625854 [Abstract] [Full Text] [Related]
11. 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]
14. Fluorescence energy transfer between nucleotide binding sites in an F-actin filament. Miki M, Hambly BD, dos Remedios CG. Biochim Biophys Acta; 1986 Jun 05; 871(2):137-41. PubMed ID: 3707968 [Abstract] [Full Text] [Related]
15. Fluorescence study of N-(3-pyrene)maleimide conjugated to rabbit skeletal F-actin and plasmodium actin polymers. Kawasaki Y, Mihashi K, Tanaka H, Ohnuma H. Biochim Biophys Acta; 1976 Sep 28; 446(1):166-78. PubMed ID: 974110 [Abstract] [Full Text] [Related]
16. Location of a contact site between actin and myosin in the three-dimensional structure of the acto-S1 complex. Kasprzak AA, Chaussepied P, Morales MF. Biochemistry; 1989 Nov 14; 28(23):9230-8. PubMed ID: 2532548 [Abstract] [Full Text] [Related]
17. Fluorescence energy transfer between Cys-10 residues in F-actin filaments. Miki M, Barden JA, Hambly BD, dos Remedios CG. Biochem Int; 1986 May 14; 12(5):725-31. PubMed ID: 3089224 [Abstract] [Full Text] [Related]
18. Fluorescence energy transfer studies of human deoxycytidine kinase: role of cysteine 185 in the conformational changes that occur upon substrate binding. Mani RS, Usova EV, Cass CE, Eriksson S. Biochemistry; 2006 Mar 21; 45(11):3534-41. PubMed ID: 16533034 [Abstract] [Full Text] [Related]
19. Structural mapping of cysteine-63 of the chloroplast ATP synthase beta subunit. Colvert KK, Mills DA, Richter ML. Biochemistry; 1992 Apr 28; 31(16):3930-5. PubMed ID: 1533153 [Abstract] [Full Text] [Related]
20. Characterization of sulfhydryl groups on chloroplast coupling factor 1 exposed by heat activation. Cantley LC, Hammes GG. Biochemistry; 1976 Jan 13; 15(1):9-14. PubMed ID: 129152 [Abstract] [Full Text] [Related] Page: [Next] [New Search]