T. Hiratsuka

Publications57
h-index15
Citations1,138
Highly Influential Citations34
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New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes.
  • T. Hiratsuka
  • Chemistry, Biology
    Biochimica et biophysica acta
  • 15 February 1983
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Preparation and properties of 2'(or 3')-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate, an analog of adenosine triphosphate.
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Fluorescent and colored trinitrophenylated analogs of ATP and GTP.
  • T. Hiratsuka
  • Biology, Chemistry
    European journal of biochemistry
  • 1 September 2003
TLDR
This review is intended as a broad overview of currently extensively used applications of the nucleotide analogs in various biological systems.
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Conformational changes in the 23-kilodalton NH2-terminal peptide segment of myosin ATPase associated with ATP hydrolysis.
  • T. Hiratsuka
  • Biology, Chemistry
    The Journal of biological chemistry
  • 5 November 1990
TLDR
The results indicate that conformational changes associated with ATP hydrolysis occur in the vicinity of the fluorophore attached to the 23-kDa NH2-terminal peptide segment of S-1.
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New fluorescent analogs of cAMP and cGMP available as substrates for cyclic nucleotide phosphodiesterase.
  • T. Hiratsuka
  • Chemistry, Biology
    The Journal of biological chemistry
  • 25 November 1982
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Cardiac myosin from pig heart ventricle. Purification and enzymatic properties.
TLDR
The purified myosin was free from nucleic acid, actin, tropomyosin, Troponin, the 150,000 molecular weight protein and other contaminants, and the pH-activity profiles and the effects of SH modification were of the skeletalMyosin type except that the activities were lower.
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Deletion of the Myopathy Loop of Dictyostelium Myosin II and Its Impact on Motor Functions*
TLDR
It is likely that the observed defects resulted mainly from a loss of the cluster of hydrophobic residues, since replacement of Asp403 or Arg402 with alanine generated a mutant with less severe or no defects compared with those of the deletion mutant.
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Behavior of Cys-707 (SH1) in myosin associated with ATP hydrolysis revealed with a fluorescent probe linked directly to the sulfur atom.
  • T. Hiratsuka
  • Chemistry, Biology
    The Journal of biological chemistry
  • 25 November 1993
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Nucleotide-induced closure of the ATP-binding pocket in myosin subfragment-1.
  • T. Hiratsuka
  • Chemistry, Biology
    The Journal of biological chemistry
  • 4 November 1994
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Monitoring the myosin ATPase reaction using a sensitive fluorescent probe: pyrene-labeled ATP.
  • T. Hiratsuka
  • Chemistry, Biology
    Biophysical journal
  • 1 February 1997
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