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Volumn 53, Issue 32, 2014, Pages 5298-5306

Analytical comparison of natural and pharmaceutical ventricular myosin activators

Author keywords

[No Author keywords available]

Indexed keywords

MUSCLE;

EID: 84906263368     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500730t     Document Type: Article
Times cited : (30)

References (40)
  • 1
    • 79958708392 scopus 로고    scopus 로고
    • The significance of regulatory light chain phosphorylation in cardiac physiology
    • Scruggs, S. B. and Solaro, R. J. (2011) The significance of regulatory light chain phosphorylation in cardiac physiology Arch. Biochem. Biophys. 510, 129-134
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 129-134
    • Scruggs, S.B.1    Solaro, R.J.2
  • 4
    • 84874590973 scopus 로고    scopus 로고
    • Qdot Labeled Actin Super-Resolution Motility Assay Measures Low Duty Cycle Muscle Myosin Step-Size
    • Wang, Y., Ajtai, K., and Burghardt, T. P. (2013) Qdot Labeled Actin Super-Resolution Motility Assay Measures Low Duty Cycle Muscle Myosin Step-Size Biochemistry 52, 1611-1621
    • (2013) Biochemistry , vol.52 , pp. 1611-1621
    • Wang, Y.1    Ajtai, K.2    Burghardt, T.P.3
  • 5
    • 84901335911 scopus 로고    scopus 로고
    • Ventricular Myosin Modifies in Vitro Step-Size When Phosphorylated
    • Wang, Y., Ajtai, K., and Burghardt, T. P. (2014) Ventricular Myosin Modifies In Vitro Step-Size When Phosphorylated J. Mol. Cell. Cardiol. 72, 231-237
    • (2014) J. Mol. Cell. Cardiol. , vol.72 , pp. 231-237
    • Wang, Y.1    Ajtai, K.2    Burghardt, T.P.3
  • 6
    • 0017044811 scopus 로고
    • Energetics and mechanism of actomyosin adenosine triphosphatase
    • White, H. D. and Taylor, E. W. (1976) Energetics and mechanism of actomyosin adenosine triphosphatase Biochemistry 15, 5818-5826
    • (1976) Biochemistry , vol.15 , pp. 5818-5826
    • White, H.D.1    Taylor, E.W.2
  • 7
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • Marston, S. B. and Taylor, E. W. (1980) Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles J. Mol. Biol. 139, 573-600
    • (1980) J. Mol. Biol. , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 8
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron, S. J. and Spudich, J. A. (1986) Fluorescent actin filaments move on myosin fixed to a glass surface Proc. Natl. Acad. Sci. U.S.A. 83, 6272-6276
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 9
    • 0024991350 scopus 로고
    • Myosin step size: Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • Uyeda, T. Q. P., Kron, S. J., and Spudich, J. A. (1990) Myosin step size: Estimation from slow sliding movement of actin over low densities of heavy meromyosin J. Mol. Biol. 214, 699-710
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 10
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • Harris, D. E. and Warshaw, D. M. (1993) Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro J. Biol. Chem. 268, 14764-14768
    • (1993) J. Biol. Chem. , vol.268 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 13
    • 12144265571 scopus 로고    scopus 로고
    • Blebbistatin, a myosin II inhibitor, is photoinactivated by blue lights
    • Sakamoto, T., Limouze, J., Combs, C., Straight, A. F., and Sellers, J. R. (2005) Blebbistatin, a myosin II inhibitor, is photoinactivated by blue lights Biochemistry 44, 584-588
    • (2005) Biochemistry , vol.44 , pp. 584-588
    • Sakamoto, T.1    Limouze, J.2    Combs, C.3    Straight, A.F.4    Sellers, J.R.5
  • 14
    • 18744393735 scopus 로고    scopus 로고
    • The structural basis of blebbistatin inhibition and specificity for myosin II
    • Allingham, J. S., Smith, R., and Rayment, I. (2005) The structural basis of blebbistatin inhibition and specificity for myosin II Nat. Struct. Mol. Biol. 12, 378-379
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 378-379
    • Allingham, J.S.1    Smith, R.2    Rayment, I.3
  • 16
    • 84906218760 scopus 로고    scopus 로고
    • The affect of omecamtive mecarbil on the phosphate dissociation and motile properties of the recombinant human β-cardica heavymeromyosin
    • Liu, Y., White, H. D., Winkelmann, D. A., and Forgacs, E. (2013) The affect of omecamtive mecarbil on the phosphate dissociation and motile properties of the recombinant human β-cardica heavymeromyosin Biophys. J. 104, 153a
    • (2013) Biophys. J. , vol.104
    • Liu, Y.1    White, H.D.2    Winkelmann, D.A.3    Forgacs, E.4
  • 18
    • 0013877728 scopus 로고
    • On the molecular weight of myosin II
    • Tonomura, Y., Appel, P., and Morales, M. (1966) On the molecular weight of myosin II Biochemistry 5, 515-521
    • (1966) Biochemistry , vol.5 , pp. 515-521
    • Tonomura, Y.1    Appel, P.2    Morales, M.3
  • 19
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A. G. and Taylor, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin Nature 257, 54-56
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 20
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D. and Spudich, J. A. (1982) Purification of muscle actin Methods Enzymol. 85, 164-179
    • (1982) Methods Enzymol. , vol.85 , pp. 164-179
    • Pardee, J.D.1    Spudich, J.A.2
  • 21
    • 70349655895 scopus 로고    scopus 로고
    • Removal of the cardiac myosin regulatory light chain increases isometric force production
    • Pant, K., Watt, J., Greenberg, M., Jones, M., Szczesna-Cordary, D., and Moore, J. R. (2009) Removal of the cardiac myosin regulatory light chain increases isometric force production FASEB J. 23, 3571-3580
    • (2009) FASEB J. , vol.23 , pp. 3571-3580
    • Pant, K.1    Watt, J.2    Greenberg, M.3    Jones, M.4    Szczesna-Cordary, D.5    Moore, J.R.6
  • 22
    • 0000154206 scopus 로고
    • The Colorimetric Determination of Phosphorus
    • Fiske, C. H. and Subbarow, Y. (1925) The Colorimetric Determination of Phosphorus J. Biol. Chem. 66, 375-400
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 23
    • 0000710582 scopus 로고
    • Evanescent field excitation of fluorescence by epi-illumination microscopy
    • Stout, A. L. and Axelrod, D. (1989) Evanescent field excitation of fluorescence by epi-illumination microscopy Appl. Opt. 28, 5237-5242
    • (1989) Appl. Opt. , vol.28 , pp. 5237-5242
    • Stout, A.L.1    Axelrod, D.2
  • 24
    • 84855958004 scopus 로고    scopus 로고
    • Chapter nine: Methods for Cell and Particle Tracking
    • (Conn, P. M. Ed.) pp, Academic Press, New York
    • Meijering, E., Dzyubachyk, O., and Smal, I. (2012) Chapter nine: Methods for Cell and Particle Tracking. In Methods in Enzymology (Conn, P. M., Ed.) pp 183-200, Academic Press, New York.
    • (2012) Methods in Enzymology , pp. 183-200
    • Meijering, E.1    Dzyubachyk, O.2    Smal, I.3
  • 25
    • 0000534160 scopus 로고
    • Position measurement with a resolution and noise-limited instrument
    • Bobroff, N. (1986) Position measurement with a resolution and noise-limited instrument Rev. Sci. Instrum. 57, 1152-1157
    • (1986) Rev. Sci. Instrum. , vol.57 , pp. 1152-1157
    • Bobroff, N.1
  • 26
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • Thompson, R. E., Larson, D. R., and Webb, W. W. (2002) Precise nanometer localization analysis for individual fluorescent probes Biophys. J. 82, 2775-2783
    • (2002) Biophys. J. , vol.82 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 28
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in vertebrate muscle fibres
    • Gordon, A. M., Huxley, A. F., and Julian, F. J. (1966) The variation in isometric tension with sarcomere length in vertebrate muscle fibres J. Physiol. (Oxford, U.K.) 184, 170-192
    • (1966) J. Physiol. (Oxford, U.K.) , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 29
    • 0032104084 scopus 로고    scopus 로고
    • Comparison of Unitary Displacements and Forces between 2 Cardiac Myosin Isoforms by the Optical Trap Technique: Molecular Basis for Cardiac Adaptation
    • Sugiura, S., Kobayakawa, N., Fujita, H., Yamashita, H., Momomura, S.-i., Chaen, S., Omata, M., and Sugi, H. (1998) Comparison of Unitary Displacements and Forces Between 2 Cardiac Myosin Isoforms by the Optical Trap Technique: Molecular Basis for Cardiac Adaptation Circ. Res. 82, 1029-1034
    • (1998) Circ. Res. , vol.82 , pp. 1029-1034
    • Sugiura, S.1    Kobayakawa, N.2    Fujita, H.3    Yamashita, H.4    Momomura, S.-I.5    Chaen, S.6    Omata, M.7    Sugi, H.8
  • 30
    • 0033198519 scopus 로고    scopus 로고
    • Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms
    • Palmiter, K. A., Tyska, M. J., Dupuis, D. E., Alpert, N. R., and Warshaw, D. M. (1999) Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms J. Physiol. (Oxford, U.K.) 519, 669-678
    • (1999) J. Physiol. (Oxford, U.K.) , vol.519 , pp. 669-678
    • Palmiter, K.A.1    Tyska, M.J.2    Dupuis, D.E.3    Alpert, N.R.4    Warshaw, D.M.5
  • 31
    • 74149089074 scopus 로고    scopus 로고
    • Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitro
    • Debold, E. P., Saber, W., Cheema, Y., Bookwalter, C. S., Trybus, K. M., Warshaw, D. M., and VanBuren, P. (2010) Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitro J. Mol. Cell. Cardiol. 48, 286-292
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 286-292
    • Debold, E.P.1    Saber, W.2    Cheema, Y.3    Bookwalter, C.S.4    Trybus, K.M.5    Warshaw, D.M.6    Vanburen, P.7
  • 32
    • 84855908966 scopus 로고    scopus 로고
    • Smooth muscle myosin light chain kinase efficiently phosphorylates serine 15 of cardiac myosin regulatory light chain
    • Josephson, M. P., Sikkink, L. A., Penheiter, A. R., Burghardt, T. P., and Ajtai, K. (2011) Smooth muscle myosin light chain kinase efficiently phosphorylates serine 15 of cardiac myosin regulatory light chain Biochem. Biophys. Res. Commun. 416, 367-371
    • (2011) Biochem. Biophys. Res. Commun. , vol.416 , pp. 367-371
    • Josephson, M.P.1    Sikkink, L.A.2    Penheiter, A.R.3    Burghardt, T.P.4    Ajtai, K.5
  • 33
    • 34247606028 scopus 로고    scopus 로고
    • Myosin at work: Motor adaptations for a variety of cellular functions
    • OConnell, C. B., Tyska, M. J., and Mooseker, M. S. (2007) Myosin at work: Motor adaptations for a variety of cellular functions Biochim. Biophys. Acta 1773, 615-630
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 615-630
    • Oconnell, C.B.1    Tyska, M.J.2    Mooseker, M.S.3
  • 34
    • 0026522849 scopus 로고
    • Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin
    • Homsher, E., Wang, F., and Sellers, J. R. (1992) Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin Am. J. Physiol. 31, C714-C723
    • (1992) Am. J. Physiol. , vol.31
    • Homsher, E.1    Wang, F.2    Sellers, J.R.3
  • 36
    • 77955506679 scopus 로고    scopus 로고
    • Improvement of cardiac function by a cardiac myosin activator in conscious dogs with systolic heart failure
    • Shen, Y. T., Malik, F., Zhao, X., Depre, C., Dhar, S. K., Abarzua, P., Morgans, D. J., and Vatner, S. F. (2010) Improvement of cardiac function by a cardiac myosin activator in conscious dogs with systolic heart failure Circ.: Heart Failure 3, 522-527
    • (2010) Circ.: Heart Failure , vol.3 , pp. 522-527
    • Shen, Y.T.1    Malik, F.2    Zhao, X.3    Depre, C.4    Dhar, S.K.5    Abarzua, P.6    Morgans, D.J.7    Vatner, S.F.8
  • 38
    • 84863058123 scopus 로고    scopus 로고
    • The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts
    • Muthu, P., Kazmierczak, K., Jones, M., and Szczesna-Cordary, D. (2012) The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts J. Cell. Mol. Med. 16, 911-919
    • (2012) J. Cell. Mol. Med. , vol.16 , pp. 911-919
    • Muthu, P.1    Kazmierczak, K.2    Jones, M.3    Szczesna-Cordary, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.