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Chemical identification of serine 181 at the ATP-binding site of myosin as a residue esterified selectively by the fluorescent reagent 9-anthroylnitrile.
Hiratsuka T, Katoh T. Hiratsuka T, et al. J Biol Chem. 2003 Aug 22;278(34):31891-4. doi: 10.1074/jbc.M303212200. Epub 2003 Jun 12. J Biol Chem. 2003. PMID: 12805386
The esterification reagent 9-anthroylnitrile (ANN) reacts with a serine residue in the NH2-terminal 23-kDa peptide segment of myosin subfragment-1 heavy chain to yield a fluorescent S1 derivative labeled by the anthroyl group (Hiratsuka, T. (1989) J. Biol. Chem. 264 …
The esterification reagent 9-anthroylnitrile (ANN) reacts with a serine residue in the NH2-terminal 23-kDa peptide segment of myosin subfrag …
Transmission of ADP.vanadate-induced conformational changes to three peptide segments of myosin subfragment-1.
Hiratsuka T. Hiratsuka T. J Biol Chem. 1990 Nov 5;265(31):18791-6. J Biol Chem. 1990. PMID: 2229042
In order to study the conformational changes associated with formation of the stable ternary complex of myosin subfragment-1 (S-1) with ADP and orthovanadate (Vi), S-1 was fluorescently labeled with 9-anthroylnitrile, 4-fluoro-7-nitrobenz-2-oxa-1,3-diazole, and 5-(iodoacetamido) …
In order to study the conformational changes associated with formation of the stable ternary complex of myosin subfragment-1 (S-1) with ADP …
Prodan fluorescence reflects differences in nucleotide-induced conformational states in the myosin head and allows continuous visualization of the ATPase reactions.
Hiratsuka T. Hiratsuka T. Biochemistry. 1998 May 19;37(20):7167-76. doi: 10.1021/bi973083d. Biochemistry. 1998. PMID: 9585528
This order agrees with those of the extent of hydrophobicity near the ribose of the corresponding nucleoside diphosphates (NDP) trapped to S-1 with orthovanadate (Vi) [Hiratsuka, T. (1984) J. Biochem. (Tokyo) 96, 155-162] and the ability of different NTPs to support …
This order agrees with those of the extent of hydrophobicity near the ribose of the corresponding nucleoside diphosphates (NDP) trapped to S …
Distinct structures of ATP and GTP complexes in the myosin ATPase.
Hiratsuka T. Hiratsuka T. J Biochem. 1984 Jul;96(1):155-62. doi: 10.1093/oxfordjournals.jbchem.a134807. J Biochem. 1984. PMID: 6238021
The active site of the myosin subfragment-1 ATPase was affinity-labeled with ribose-modified fluorescent analogs of ADP, dADP, CDP, UDP, IDP, and GDP in combination with vanadate, forming a stable myosin-nucleoside diphosphate-vanadate complex that is analogous to the normal myos …
The active site of the myosin subfragment-1 ATPase was affinity-labeled with ribose-modified fluorescent analogs of ADP, dADP, CDP, UDP, IDP …
Cross-linking of three heavy-chain domains of myosin adenosinetriphosphatase with a trifunctional alkylating reagent.
Hiratsuka T. Hiratsuka T. Biochemistry. 1988 May 31;27(11):4110-4. doi: 10.1021/bi00411a030. Biochemistry. 1988. PMID: 2970866
The present observation is consistent with the proposal that SH1 is close to both the 26- and 50-kDa domains of S-1 and that movement within S-1 associated with the nucleotide binding occurs around SH1 as well as around another reactive thiol, SH2 & Wong, A. G. (1986) Proc. N …
The present observation is consistent with the proposal that SH1 is close to both the 26- and 50-kDa domains of S-1 and that movement within …
Affinity labeling of the myosin ATPase with ribose-modified fluorescent nucleotides and vanadate.
Hiratsuka T. Hiratsuka T. J Biochem. 1984 Jul;96(1):147-54. doi: 10.1093/oxfordjournals.jbchem.a134806. J Biochem. 1984. PMID: 6238020
Ribose-modified fluorescent nucleotide analogs, 3'-O-anthraniloyl and 3'-O-(N-methylanthraniloyl) derivatives of AT(D)P, dAT(D)P, CT(D)P, UT(D)P, IT(D)P, and GT(D)P, were synthesized for use as substrates and affinity labels for the myosin ATPase [Hiratsuka, T. (198 …
Ribose-modified fluorescent nucleotide analogs, 3'-O-anthraniloyl and 3'-O-(N-methylanthraniloyl) derivatives of AT(D)P, dAT(D)P, CT(D)P, UT …
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