144 related articles for article (PubMed ID: 136275)
1. Comparative studies on amino and thiol groups in myosins from different sources.
Muhlrad A; Oplatka A; Lamed R
Biochim Biophys Acta; 1976 Nov; 452(1):227-38. PubMed ID: 136275
[TBL] [Abstract][Full Text] [Related]
2. The ATPase reaction in the steady state and in the initial burst catalyzed by chicken gizzard myosin in 0.6 M KCl1.
Onishi H; Yamada Y; Ikebe M; Suzuki H; Watanabe S
J Biochem; 1978 Jan; 83(1):129-35. PubMed ID: 24043
[TBL] [Abstract][Full Text] [Related]
3. The effect of pyrophosphate on the reaction of myosin with 2,4,6-trinitrobenzene sulphonate.
Setton A; Muhlrad A
J Muscle Res Cell Motil; 1988 Apr; 9(2):132-46. PubMed ID: 2843563
[TBL] [Abstract][Full Text] [Related]
4. Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6-10 S conformational transition.
Chandra TS; Nath N; Suzuki H; Seidel JC
J Biol Chem; 1985 Jan; 260(1):202-7. PubMed ID: 3155516
[TBL] [Abstract][Full Text] [Related]
5. Characterization of the ATPase activities of myosins isolated from the membrane and the cytoplasmic fractions of human platelets.
Peleg I; Muhlrad A; Eldor A; Groschel-Stewart U; Kahane I
Arch Biochem Biophys; 1984 Nov; 234(2):442-53. PubMed ID: 6149726
[TBL] [Abstract][Full Text] [Related]
6. Trinitrophenylation of rabbit skeletal myosin by 2,4,6-trinitrobenzene sulfonate and treatment of trinitrophenyl myosin with dithiothreitol.
Kodama S; Konno K; Arai K; Watanabe S
J Biochem; 1985 Mar; 97(3):831-6. PubMed ID: 2991209
[TBL] [Abstract][Full Text] [Related]
7. Chicken-gizzard actin. Interaction with skeletal-muscle myosin.
Próchniewicz E; Strzelecka-Gołaszewska H
Eur J Biochem; 1980 May; 106(1):305-12. PubMed ID: 6122569
[TBL] [Abstract][Full Text] [Related]
8. Unusual features of the Ca2+-ATPase activity of myosin from fast skeletal muscle of the frog: effect of actin and SH1 thiol group modification.
Strzelecka-Gołaszewska H; Pliszka B; Mossakowska M; Piwowar U
J Muscle Res Cell Motil; 1983 Apr; 4(2):191-206. PubMed ID: 6134751
[TBL] [Abstract][Full Text] [Related]
9. Trinitrophenylation of smooth muscle myosin.
Srivastava S; Ikebe M; Hartshorne DJ
Biochem Biophys Res Commun; 1985 Jan; 126(2):748-55. PubMed ID: 3156591
[TBL] [Abstract][Full Text] [Related]
10. Calcium sensitivity of contractile proteins from chicken gizzard muscle.
Ikebe M; Aiba T; Onishi H; Watanabe S
J Biochem; 1978 Jun; 83(6):1643-55. PubMed ID: 209016
[TBL] [Abstract][Full Text] [Related]
11. Comparison of the effects of smooth and skeletal tropomyosin on skeletal actomyosin subfragment 1 ATPase.
Lehrer SS; Morris EP
J Biol Chem; 1984 Feb; 259(4):2070-2. PubMed ID: 6230348
[TBL] [Abstract][Full Text] [Related]
12. High affinity of various smooth muscle myosins for skeletal F-actin demonstrated by enzyme kinetics and electron microscopy.
Krisanda JM; Breese SS; Murphy RA
Biochim Biophys Acta; 1982 Mar; 702(1):125-32. PubMed ID: 6121583
[TBL] [Abstract][Full Text] [Related]
13. Phosphorylation of gizzard myosin light chain and the ATPase reaction and superprecipitation of skeletal acto-gizzard myosin as functions of ATP concentration.
Ohtsuka I; Kasai M; Kimura K; Onishi H; Watanabe S
J Biochem; 1980 May; 87(5):1379-85. PubMed ID: 6446551
[TBL] [Abstract][Full Text] [Related]
14. Conformational differences in myosin, IV.[1-3] Radioactive labeling of specific thiol groups as influenced by ligand binding.
Schaub MC; Watterson JG; Waser PG
Hoppe Seylers Z Physiol Chem; 1975 Mar; 356(3):325-39. PubMed ID: 126941
[TBL] [Abstract][Full Text] [Related]
15. Radioactive labeling and location of specific thiol groups in myosin from fast, slow and cardiac muscles.
Pfister M; Schaub MC; Watterson JG; Knecht M; Waser PG
Biochim Biophys Acta; 1975 Nov; 410(1):193-209. PubMed ID: 73
[TBL] [Abstract][Full Text] [Related]
16. A comparative study of reactive--SH groups of cardiac and skeletal muscle myosins.
Klotz C; Leger JJ; Marotte F
Eur J Biochem; 1976 Jun; 65(2):607-11. PubMed ID: 133024
[TBL] [Abstract][Full Text] [Related]
17. The sulfhydryl groups involved in the active site of myosin B adenosinetriphosphatase. I. Relantionship of the sulfhydryl group responsible for Mg2+-ATPase activation to the S1 and S2 groups.
Yamashita T; Kobayashi M; Horigome T
J Biochem; 1975 May; 77(5):1037-46. PubMed ID: 125748
[TBL] [Abstract][Full Text] [Related]
18. Studies on the amino groups of myosin ATPase. III. Effect of nucleotides on the fluorescence of beta-naphthoquinone-4-sulfonate bound to amino groups of myosin.
Muhlrad A
Biochim Biophys Acta; 1977 Jan; 490(1):79-86. PubMed ID: 138447
[TBL] [Abstract][Full Text] [Related]
19. Structural and functional organization of gizzard myosin molecules: proteolytic digestion and N-iodo-acetyl-N-(5-sulfo-1-naphthyl)ethylene diamine modification.
Onishi H; Watanabe S
Adv Biophys; 1985; 19():21-42. PubMed ID: 2940817
[TBL] [Abstract][Full Text] [Related]
20. Modification of cardiac and smooth muscle myosins with 2,4,6-trinitrobenzenesulfonate. Evidence for differences in structure around the active sites of cardiac, smooth, and skeletal muscle myosin ATPase.
Srivastava SK; Tonomura Y; Inoue A
J Biochem; 1979 Sep; 86(3):725-31. PubMed ID: 159905
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
