DOI: 10.1007/bf00713152. Distance between nucleotide site and cysteine-373 of G-actin by resonance energy transfer measurements

Distance between nucleotide site and cysteine-373 of G-actin by resonance energy transfer measurements

10.1007/bf00713152

Crossref journal-article

Springer Science and Business Media LLC

Journal of Muscle Research and Cell Motility (297)

Bibliography

Cheung, H. C., & Liu, B.-M. (1984). Distance between nucleotide site and cysteine-373 of G-actin by resonance energy transfer measurements. Journal of Muscle Research and Cell Motility, 5(1), 65â80.

Authors 2

Herbert C. Cheung (first)
Bang-Maw Liu (additional)

References 29 Referenced 7

ABODERIN, A. A., BOEDEFELD, E. & LUISI, P. L. (1973) Reaction of chicken egg white lysozyme with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole.Biochim. Biophys. Acta 328, 20–30. (10.1016/0005-2795(73)90325-5) / Biochim. Biophys. Acta by A. A. Aboderin (1973)
AEBI, U., SMITH, P. R., ISENBERG, G. & POLLARD, T. D. (1980) Structure of crystalline actin sheets.Nature Lond. 288, 296–8. (10.1038/288296a0) / Nature Lond. by U. Aebi (1980)
CANTLEY, L. C. & HAMMES, G. G. (1975) Fluorescence energy transfer between ligand binding sites on chloroplast coupling factor.Biochemistry 14, 2966–81. / Biochemistry by L. C. Cantley (1975)
CHEUNG, H. C., COOKE, R. & SMITH, L. (1971) The G-actin → F-actin transformation as studied by the fluorescence of bound dansyl cystine.Archs Biochem. Biophys. 142, 333–9. (10.1016/0003-9861(71)90291-8) / Archs Biochem. Biophys. by H. C. Cheung (1971)
CHEUNG, H. C., WANG, C. K. & GARLAND, G. (1982) Fluorescence energy transfer studies of skeletal troponin C: proximity between methionine-25 and cysteine 98.Biochemistry 21, 5135–42. (10.1021/bi00264a005) / Biochemistry by H. C. Cheung (1982)
CHEUNG, H. C., GONSOULIN, F. & GARLAND, F. (1983) Fluorescence energy transfer studies on the proximity of the two essential thiols of myosin subfragment-1.J. biol. Chem. 258, 5775–86. (10.1016/S0021-9258(20)81961-9) / J. biol. Chem. by H. C. Cheung (1983)
DALE, R. E., EISINGER, J. & BLUMBERG, W. E. (1979) The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer.Biophys. J. 26, 161–93. (10.1016/S0006-3495(79)85243-1) / Biophys. J. by R. E. Dale (1979)
DETMERS, P., WEBER, A., ELZINGA, M. & STEPHENS, R. E. (1981) 7-Chloro-4-nitrobenzeno-2-oxa-1,3-diazole actin as a probe for actin polymerization.J. biol. Chem. 256, 99–105. (10.1016/S0021-9258(19)70103-3) / J. biol. Chem. by P. Detmers (1981)
ELLMAN, G. L. (1959) Tissue sulfhydryl groups.Archs Biochem. Biophys. 82, 70–7. (10.1016/0003-9861(59)90090-6) / Archs Biochem. Biophys. by G. L. Ellman (1959)
ELZINGA, M., COLLINS, J. H., KUEHL, W. M. & ADELSTEIN, R. S. (1973) Complete amino-acid sequence of actin of rabbit skeletal muscle.Proc. natn. Acad. Sci. U.S.A. 70, 2687–91. (10.1073/pnas.70.9.2687) / Proc. natn. Acad. Sci. U.S.A. by M. Elzinga (1973)
HARVEY, S. C., CHEUNG, H. C. & THAMES, K. E. (1977) Cooperativity in F-actin filaments on binding of myosin subfragments, demonstrated by fluorescence of 1,N6-ethenoadenosine diphosphate.Archs Biochem. Biophys. 179, 391–6. (10.1016/0003-9861(77)90126-6) / Archs Biochem. Biophys. by S. C. Harvey (1977)
HOUK, T. W. & UE, K. (1974) The measurement of actin concentration in solution: a comparison of methods,Analyt. Biochem. 62, 66–74. (10.1016/0003-2697(74)90367-4) / Analyt. Biochem. by T. W. Houk (1974)
KAWATO, S., KINOSITA, K. & IKEGAMI, A. (1977) Dynamic structure of lipid bilayers studied by nanosecond fluorescence techniques.Biochemistry 16, 2349–24. (10.1021/bi00630a002) / Biochemistry by S. Kawato (1977)
LIN, T. I. & DOWBEN, R. M. (1983) Studies on the spatial arrangement of muscle thin filament proteins using fluorescence energy transfer.J. biol. Chem. 258, 5142–50. (10.1016/S0021-9258(18)32550-X) / J. biol. Chem. by T. I. Lin (1983)
LIU, B. M., CHEUNG, H. C. & MESTECKY, J. (1981) Nanosecond fluorescence spectroscopy of human immunoglobulin A.Biochemistry 20, 1997–2003. (10.1021/bi00510a040) / Biochemistry by B. M. Liu (1981)
MIKI, M., OHNUMA, H. & MIHASHI, K. (1974) Interaction of actin water ε-ATP.FEBS Lett. 49, 17–9. (10.1016/0014-5793(74)80324-8) / FEBS Lett. by M. Miki (1974)
MIKI, M., KOUYAMA, T. & MIHASHI, K. (1976) Fluorescence study of ε-ADP bound to rabbit F-actin: structural changes in the adenine subsite of F-actin under the influence of heavy meromyosin.FEBS Lett. 66, 98–101. (10.1016/0014-5793(76)80594-7) / FEBS Lett. by M. Miki (1976)
MIKI, M. & MIHASHI, K. (1977) Fluorescence and flow dichroism of F-actin-ε-ATP: the orientation of the adenine plane relative to the long axis of F-actin.Biophys. Chem. 6, 101–6. (10.1016/0301-4622(76)80066-X) / Biophys. Chem. by M. Miki (1977)
MIKI, M. & MIHASHI, K. (1978) Fluorescence energy transfer between ε-ATP at the nucleotide binding site and N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide at Cys-373 of G-actin.Biochim. Biophys. Acta 533, 163–72. (10.1016/0005-2795(78)90560-3) / Biochim. Biophys. Acta by M. Miki (1978)
MIHASHI, K. & WAHL, P. (1975) Nanosecond pulse fluorometry in polarized light of G-actin-ε-ATP and F-actin-ε-ADP.FEBS Lett. 52, 8–12. (10.1016/0014-5793(75)80625-9) / FEBS Lett. by K. Mihashi (1975)
PARKER, C. A. & REESE, W. I. (1960) Correction of fluorescence spectra and measurement of fluorescence quantum efficiency.Analyst 85, 587–600. (10.1039/an9608500587) / Analyst by C. A. Parker (1960)
SCOTT, T. G., SPENCER, R. D., LEONARD, N. J. & WEBER, G. (1970) Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models.J. Am. Chem. Soc. 92, 687–95. (10.1021/ja00706a043) / J. Am. Chem. Soc. by T. G. Scott (1970)
SECRIST, J. A., BARRIO, J. R., LEONARD, N. J. & WEBER, G. (1972) Fluorescent modification of adenosine-containing coenzymes. Biological activities and spectroscopic properties.Biochemistry 11, 3499–506. (10.1021/bi00769a001) / Biochemistry by J. A. Secrist (1972)
SPUDICH, J. A. & WATT, W. (1971) The regulation of rabbit skeletal muscle contraction.J. biol. Chem. 246, 4866–71. (10.1016/S0021-9258(18)62016-2) / J. biol. Chem. by J. A. Spudich (1971)
TAKASHI, R. (1979) Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1.Biochemistry 18, 5164–9. (10.1021/bi00590a021) / Biochemistry by R. Takashi (1979)
THAMES, K. E., CHEUNG, H. C. & HARVEY, S. C. (1974) Binding of 1, N6-ethenoadenosine triphosphate to actin.Biochem. biophys. Res. Commun. 60, 1252–61. (10.1016/0006-291X(74)90333-7) / Biochem. biophys. Res. Commun. by K. E. Thames (1974)
YANAGIDA, T. & OOSAWA, F. (1978) Polarized fluorescence from ε-ADP incorporated into F-actin in a myosin-free single fiber: conformation of F-actin and changes induced in it by heavy meromyosin.J. molec. Biol. 126, 507–24. (10.1016/0022-2836(78)90056-6) / J. molec. Biol. by T. Yanagida (1978)
YANAGIDA, T. & OOSAWA, F. (1980) Conformational changes of F-actin-ε-ADP in thin filaments in myosin-free muscle fibers induced by Ca2+.J. molec. Biol. 140, 313–20. (10.1016/0022-2836(80)90108-4) / J. molec. Biol. by T. Yanagida (1980)
YANAGIDA, T. (1981) Angles of nucleotides bound to cross-bridges in glycerinated muscle fiber at various concentrations of ε-ATP, ε-ADP and ε-AMPPNP detected by polarized fluorescence.J. molec. Biol. 146, 539–60. (10.1016/0022-2836(81)90046-2) / J. molec. Biol. by T. Yanagida (1981)

Dates

Type	When
Created	19 years ago (Aug. 17, 2006, 12:08 p.m.)
Deposited	4 years ago (July 31, 2021, 9:40 a.m.)
Indexed	1 year, 9 months ago (Oct. 31, 2023, 1:20 a.m.)
Issued	41 years, 6 months ago (Feb. 1, 1984)
Published	41 years, 6 months ago (Feb. 1, 1984)
Published Print	41 years, 6 months ago (Feb. 1, 1984)

Funders 0

None

BibTeX

@article{Cheung_1984, title={Distance between nucleotide site and cysteine-373 of G-actin by resonance energy transfer measurements}, volume={5}, ISSN={1573-2657}, url={http://dx.doi.org/10.1007/bf00713152}, DOI={10.1007/bf00713152}, number={1}, journal={Journal of Muscle Research and Cell Motility}, publisher={Springer Science and Business Media LLC}, author={Cheung, Herbert C. and Liu, Bang-Maw}, year={1984}, month=feb, pages={65–80} }

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