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3. Characterization of modified myosin at low ionic strength. Enzymatic and spin-label studies. Stone DB, Prevost SC. Biochemistry; 1973 Oct 09; 12(21):4206-11. PubMed ID: 4355555 [No Abstract] [Full Text] [Related]
4. Enzymatic studies on the interaction of myosin and heavy meromyosin with 1,N 6 -ethenoadenosine triphosphate ( ATP), a fluorescent analog of ATP. McCubbin WD, Willick GE, Kay CM. Biochem Biophys Res Commun; 1973 Feb 05; 50(3):926-33. PubMed ID: 4265978 [No Abstract] [Full Text] [Related]
5. Transient phase of adenosine triphosphate hydrolysis by myosin, heavy meromyosin, and subfragment 1. Taylor EW. Biochemistry; 1977 Feb 22; 16(4):732-9. PubMed ID: 138438 [Abstract] [Full Text] [Related]
11. Reaction intermediates of H-meromyosin-ATPase and ultraviolet difference spectrum of H-meromyosin induced by ATP. Shibata-Sekiya K. J Biochem; 1976 Mar 22; 79(3):621-3. PubMed ID: 133105 [Abstract] [Full Text] [Related]
13. Temperature dependence of the decay of the UV absorption difference spectrum of heavy meromyosin induced by adenosine triphosphate and inosine triphosphate. Morita F, Ishigami F. J Biochem; 1977 Feb 22; 81(2):305-12. PubMed ID: 14941 [Abstract] [Full Text] [Related]
16. Transient detection of spin-labeled myosin subfragment 1 conformational states during ATP hydrolysis. Ostap EM, White HD, Thomas DD. Biochemistry; 1993 Jul 06; 32(26):6712-20. PubMed ID: 8392368 [Abstract] [Full Text] [Related]
17. Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Miyata H, Asai H. J Biochem; 1981 Jul 06; 90(1):133-9. PubMed ID: 7026547 [Abstract] [Full Text] [Related]
19. Structure and function of the two heads of the myosin molecule. III. Cooperativity of the two heads of the myosin molecule, shown by the effect of modification of head A with rho-chloromercuribenzoate on the interaction of head B with F-actin. Shibata-Sekiya K, Tonomura Y. J Biochem; 1976 Dec 06; 80(6):1371-80. PubMed ID: 138679 [Abstract] [Full Text] [Related]