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Volumn 76, Issue 2, 1999, Pages 1001-1007

Effects of SH1 and SH2 modifications on myosin similarities and differences

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (MAGNESIUM); F ACTIN; MYOSIN;

EID: 0033039455     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77264-4     Document Type: Article
Times cited : (28)

References (35)
  • 1
    • 0024561651 scopus 로고
    • Fluorescent modification and orientation of myosin sulfhydryl 2 in skeletal muscle fibers
    • Ajtai, K., and T. P. Burghardt. 1989. Fluorescent modification and orientation of myosin sulfhydryl 2 in skeletal muscle fibers. Biochemistry. 28:2204-2210.
    • (1989) Biochemistry , vol.28 , pp. 2204-2210
    • Ajtai, K.1    Burghardt, T.P.2
  • 2
    • 0030877014 scopus 로고    scopus 로고
    • Activation of regulated actin by SH1-modified myosin subfragment 1
    • Bobkov, A. A., E. A. Bobkova, E. Homsher, and E. Reisler. 1997. Activation of regulated actin by SH1-modified myosin subfragment 1. Biochemistry. 36:7733-7738.
    • (1997) Biochemistry , vol.36 , pp. 7733-7738
    • Bobkov, A.A.1    Bobkova, E.A.2    Homsher, E.3    Reisler, E.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0017590855 scopus 로고
    • Effect of nucleotide binding on the proximity of the essential sulphydryl groups of myosin: Chemical probing of movement of residues during conformational transitions
    • Burke, M., and E. Reisler. 1977. Effect of nucleotide binding on the proximity of the essential sulphydryl groups of myosin: chemical probing of movement of residues during conformational transitions. Biochemistry. 16:5559-5563.
    • (1977) Biochemistry , vol.16 , pp. 5559-5563
    • Burke, M.1    Reisler, E.2
  • 5
    • 0030893622 scopus 로고    scopus 로고
    • In vitro actin filament sliding velocities produced by mixtures of different types of myosin
    • Cuda, G., E. Pate, R. Cooke, and J. R. Sellers. 1997. In vitro actin filament sliding velocities produced by mixtures of different types of myosin. Biophys. J. 72:1767-1779.
    • (1997) Biophys. J. , vol.72 , pp. 1767-1779
    • Cuda, G.1    Pate, E.2    Cooke, R.3    Sellers, J.R.4
  • 7
    • 0014952464 scopus 로고
    • Self-association in the myosin system at high ionic strength: Sensitivity of the interaction to pH and ionic environment
    • Godfrey, J., and W. F. Harrington. 1970. Self-association in the myosin system at high ionic strength: sensitivity of the interaction to pH and ionic environment. Biochemistry. 9:886-893.
    • (1970) Biochemistry , vol.9 , pp. 886-893
    • Godfrey, J.1    Harrington, W.F.2
  • 8
    • 0029797832 scopus 로고    scopus 로고
    • Differential scanning calorimetric study of the complexes of modified myosin subfragment 1 with ADP and vanadate or beryllium fluoride
    • Golitsina, N. L., A. A. Bobkov, I. V. Dedova, D. A. Pavlov, O. P. Nikolaeva, V. N. Orlov, and D. I. Levitsky. 1996. Differential scanning calorimetric study of the complexes of modified myosin subfragment 1 with ADP and vanadate or beryllium fluoride. J. Muscle Res. Cell Motil. 17:475-485.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 475-485
    • Golitsina, N.L.1    Bobkov, A.A.2    Dedova, I.V.3    Pavlov, D.A.4    Nikolaeva, O.P.5    Orlov, V.N.6    Levitsky, D.I.7
  • 9
    • 0026724931 scopus 로고
    • Movement of Cys-697 in myosin ATPase associated with ATP hydrolysis
    • Hiratsuka, T., 1992. Movement of Cys-697 in myosin ATPase associated with ATP hydrolysis. J. Biol. Chem. 267:14941-14948.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14941-14948
    • Hiratsuka, T.1
  • 11
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate
    • Kodama, T., K. Fukui, and K. Kometani. 1986. The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. J. Biochem. 99:1465-1472.
    • (1986) J. Biochem. , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 12
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian, S. S., and S. Lowey. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85:55-72.
    • (1982) Methods Enzymol. , vol.85 , pp. 55-72
    • Margossian, S.S.1    Lowey, S.2
  • 15
    • 0029964532 scopus 로고    scopus 로고
    • Light-directed generation of the actin-activated ATPase. Activity of caged heavy meromyosin
    • Marriott, G., and M. Heidecker. 1996. Light-directed generation of the actin-activated ATPase. Activity of caged heavy meromyosin. Biochemistry 35:3170-3174.
    • (1996) Biochemistry , vol.35 , pp. 3170-3174
    • Marriott, G.1    Heidecker, M.2
  • 16
    • 0028906383 scopus 로고
    • Role of charged amino acid pairs in subdomain 1 of actin in interactions with myosin
    • Miller, C. J., and E. Reisler 1995. Role of charged amino acid pairs in subdomain 1 of actin in interactions with myosin. Biochemistry 34: 2694-2700.
    • (1995) Biochemistry , vol.34 , pp. 2694-2700
    • Miller, C.J.1    Reisler, E.2
  • 17
    • 0018182108 scopus 로고
    • Interaction of spin-labeled and N-(iodoacetylaminoethyl)-5-naphthylamine-1-sulfonic acid SH1-blocked heavy meromyosin and myosin with actin and adenosine triphosphate
    • Mulhern, S. A., and E. Eisenberg. 1978. Interaction of spin-labeled and N-(iodoacetylaminoethyl)-5-naphthylamine-1-sulfonic acid SH1-blocked heavy meromyosin and myosin with actin and adenosine triphosphate. Biochemistry. 17:4419-4425.
    • (1978) Biochemistry , vol.17 , pp. 4419-4425
    • Mulhern, S.A.1    Eisenberg, E.2
  • 18
    • 0027267468 scopus 로고
    • Transient detection of spin-labeled myosin subfragment 1 conformational states during ATP hydrolysis
    • Ostap, E. M., H. D. White, and D. D. Thomas. 1993. Transient detection of spin-labeled myosin subfragment 1 conformational states during ATP hydrolysis. Biochemistry. 32:6712-6720.
    • (1993) Biochemistry , vol.32 , pp. 6712-6720
    • Ostap, E.M.1    White, H.D.2    Thomas, D.D.3
  • 19
    • 0030836303 scopus 로고    scopus 로고
    • Cold-sensitive mutants G680V and G691C of Dictyostelium myosin II confer dramatically different biochemical defects
    • Patterson, B., K. M. Ruppel, Y. Wu, and J. A. Spudich. 1997. Cold-sensitive mutants G680V and G691C of Dictyostelium myosin II confer dramatically different biochemical defects. J. Biol. Chem. 212: 27612-27617.
    • (1997) J. Biol. Chem. , vol.212 , pp. 27612-27617
    • Patterson, B.1    Ruppel, K.M.2    Wu, Y.3    Spudich, J.A.4
  • 20
    • 0029978938 scopus 로고    scopus 로고
    • Complexes of myosin subfragment-1 with adenosine diphosphate and phosphate analogs: Probes of active site and protein conformation
    • Phan, B. C., P. Cheung, W. F. Stafford, and E. Reisler. 1996. Complexes of myosin subfragment-1 with adenosine diphosphate and phosphate analogs: probes of active site and protein conformation. Biophys. Chem. 59:341-349.
    • (1996) Biophys. Chem. , vol.59 , pp. 341-349
    • Phan, B.C.1    Cheung, P.2    Stafford, W.F.3    Reisler, E.4
  • 21
    • 0024403442 scopus 로고
    • Studies of ligand-induced conformational perturbations in myosin subfragment 1
    • Rajasekharan, K. N., M. Mayadevi, and M. Burke. 1989. Studies of ligand-induced conformational perturbations in myosin subfragment 1. J. Biol. Chem. 25:10810-10819.
    • (1989) J. Biol. Chem. , vol.25 , pp. 10810-10819
    • Rajasekharan, K.N.1    Mayadevi, M.2    Burke, M.3
  • 23
    • 0020023995 scopus 로고
    • Sulfhydryl modification and labeling of myosin
    • Reisler, E. 1982. Sulfhydryl modification and labeling of myosin. Methods Enymol. 85:84-93.
    • (1982) Methods Enymol. , vol.85 , pp. 84-93
    • Reisler, E.1
  • 24
    • 0016253136 scopus 로고
    • Cooperative role of two sulfhydryl groups in myosin
    • Reisler, E., M. Burke, and W. F. Harrington. 1974a. Cooperative role of two sulfhydryl groups in myosin. Biochemistry. 13:2014-2022.
    • (1974) Biochemistry , vol.13 , pp. 2014-2022
    • Reisler, E.1    Burke, M.2    Harrington, W.F.3
  • 25
    • 0016268979 scopus 로고
    • Spatial proximity of the two essential sulfhydryl groups of myosin
    • Reisler, E., M. Burke, S. Himmelfarb, and W. F. Harrington. 1974b. Spatial proximity of the two essential sulfhydryl groups of myosin. Biochemistry. 13:3837-3840.
    • (1974) Biochemistry , vol.13 , pp. 3837-3840
    • Reisler, E.1    Burke, M.2    Himmelfarb, S.3    Harrington, W.F.4
  • 26
    • 0026712239 scopus 로고
    • Cooperativity of thiol-modified myosin filaments: ATPase and motility assays of myosin function
    • Root, D. D., and E. Reisler. 1992. Cooperativity of thiol-modified myosin filaments: ATPase and motility assays of myosin function. Biophys. J. 63:730-740.
    • (1992) Biophys. J. , vol.63 , pp. 730-740
    • Root, D.D.1    Reisler, E.2
  • 27
  • 28
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II)-ADP-vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith, C. A., and I. Rayment. 1996. X-ray structure of the magnesium(II)-ADP-vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry. 35:5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 29
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction: Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction: biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin. J. Biol Chem. 246:4866-4876.
    • (1971) J. Biol Chem. , vol.246 , pp. 4866-4876
    • Spudich, J.A.1    Watt, S.2
  • 31
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda, T. Q. P., P. D. Abramson, and J. Spudich. 1996. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl Acad. Sci. U.S.A. 93:4459-4464.
    • (1996) Proc. Natl Acad. Sci. U.S.A. , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.P.1    Abramson, P.D.2    Spudich, J.3
  • 32
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin: Effects of divalent cations on proteolytic susceptibility
    • Weeds, A. G., and B. Pope. 1977. Studies on the chymotryptic digestion of myosin: effects of divalent cations on proteolytic susceptibility. J. Mol. biol. 111: 129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 33
    • 0019321959 scopus 로고
    • Cross-linking of myosin subfragment 1: Nucleotide-enhanced modification by a variety of bifunctional reagents
    • Wells, J. A., C. Knoeber, M. C. Sheldon, M. M. Werber, and R. G. Yount. 1980. Cross-linking of myosin subfragment 1: nucleotide-enhanced modification by a variety of bifunctional reagents. J. Biol. Chem. 255: 11135-11140.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11135-11140
    • Wells, J.A.1    Knoeber, C.2    Sheldon, M.C.3    Werber, M.M.4    Yount, R.G.5
  • 34
    • 0018868611 scopus 로고
    • Reaction of 5,5′-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: Evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active site
    • Wells, J. A., and R. G. Yount. 1980. Reaction of 5,5′-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active site. Biochemistry. 19:1711-1717.
    • (1980) Biochemistry , vol.19 , pp. 1711-1717
    • Wells, J.A.1    Yount, R.G.2


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