• Publications
  • Influence
Synergistic inhibition of oxidation in dispersed phosphatidylcholine liposomes by a combination of vitamin E and cysteine.
Oxidations of soybean phosphatidylcholine liposomes in an aqueous dispersion initiated by free radicals generated initially either in the aqueous phase or in the lipid phase were efficientlyExpand
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Removing the two C-terminal residues of actin affects the filament structure.
We define conditions under which the two C-terminal residues of actin, Cys-374 and Phe-375, can be selectively removed by proteolysis with trypsin. This modification had little effect on theExpand
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Membrane potential-linked reversed electron transfer in the beef heart cytochrome bc1 complex reconstituted into potassium-loaded phospholipid vesicles.
The cytochrome bc1 complex purified from beef heart mitochondria was incorporated into potassium (K+)-loaded phospholipid vesicles by a cholate dialysis method to study the reverse reaction ofExpand
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The mechanism of inhibition of the actin-activated myosin MgATPase by calponin.
Calponin inhibits the actin-activated ATPase of smooth muscle myosin and thus has been proposed as a thin filament-based regulatory component in smooth muscle. To obtain information on the mechanismExpand
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Localization of the phalloidin and nucleotide-binding sites on actin.
Phalloidin was found to block nucleotide exchange in F-actin, without interfering with nucleotide hydrolysis. This inhibition of nucleotide exchange occurs under conditions in which monomers are ableExpand
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The recovery of the polymerizability of Lys-61-labelled actin by the addition of phalloidin. Fluorescence polarization and resonance-energy-transfer measurements.
  • M. Miki
  • Chemistry, Medicine
  • European journal of biochemistry
  • 1 April 1987
Modification of Lys-61 in actin with fluorescein-5-isothiocyanate (FITC) blocks actin polymerization [Burtnick, L. D. (1984) Biochim. Biophys. Acta 791, 57-62]. FITC-labelled actin recovered itsExpand
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Interaction of phalloidin with chemically modified actin.
Modification of Tyr-69 with tetranitromethane impairs the polymerizability of actin in accordance with the previous report [Lehrer, S. S. and Elzinga, M. (1972) Fed. Proc. 31, 502]. PhalloidinExpand
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Domain motion in actin observed by fluorescence resonance energy transfer.
Actin is composed of two well-separated globular domains which are further subdivided into two subdomains [Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., & Holmes, K. C. (1990) Nature 347,Expand
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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.
The method of fluorescence energy transfer is used to measure the distance from the nucleotide binding site to Cys-373 of G-actin. The fluorescent ATP analogue 1-N6-ethenoadenosine 5'-triphosphateExpand
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Fluorescence anisotropy of labeled F-actin: influence of divalent cations on the interaction between F-actin and myosin heads.
The interaction between F-actin and soluble proteolytic fragments of myosin, heavy meromyosin and myosin subfragment 1 without ATP, has been studied by measuring the static anisotropy and theExpand
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