메뉴 건너뛰기




Volumn 338, Issue 2, 2005, Pages 224-236

Detection of small differences in actomyosin function using actin labeled with different phalloidin conjugates

Author keywords

Alexa 488 phalloidin; Biotin XX phalloidin; Bovine cardiac actin; In vitro motility assay; Rabbit skeletal muscle actin; Rhodamine phalloidin

Indexed keywords

COENZYMES; IONIC STRENGTH; MAMMALS;

EID: 14644441607     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.12.012     Document Type: Article
Times cited : (27)

References (38)
  • 1
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction: Interference microscopy of living muscle fibres
    • A.F. Huxley, and R. Niedergerke Structural changes in muscle during contraction: interference microscopy of living muscle fibres Nature 173 1954 971 973
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 2
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • H. Huxley, and J. Hanson Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation Nature 173 1954 973 976
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.1    Hanson, J.2
  • 3
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • A.F. Huxley Muscle structure and theories of contraction Prog. Biophys. Biophys. Chem. 7 1957 255 318
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 5
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • S.J. Kron, and J.A. Spudich Fluorescent actin filaments move on myosin fixed to a glass surface Proc. Natl. Acad. Sci. USA 83 1986 6272 6276
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 7
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Y. Harada, K. Sakurada, T. Aoki, D.D. Thomas, and T. Yanagida Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay J. Mol. Biol. 216 1990 49 68
    • (1990) J. Mol. Biol. , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 8
    • 0023145911 scopus 로고
    • Sliding movement of single actin filaments on one-headed myosin filaments
    • Y. Harada, A. Noguchi, A. Kishino, and T. Yanagida Sliding movement of single actin filaments on one-headed myosin filaments Nature 326 1987 805 808
    • (1987) Nature , vol.326 , pp. 805-808
    • Harada, Y.1    Noguchi, A.2    Kishino, A.3    Yanagida, T.4
  • 9
    • 0026522849 scopus 로고
    • Factors affecting movement of F-actin filaments propelled by skeletal-muscle heavy meromyosin
    • E. Homsher, F. Wang, and J.R. Sellers Factors affecting movement of F-actin filaments propelled by skeletal-muscle heavy meromyosin Am. J. Physiol. 262 1992 C714 C723
    • (1992) Am. J. Physiol. , vol.262
    • Homsher, E.1    Wang, F.2    Sellers, J.R.3
  • 10
    • 0029924132 scopus 로고    scopus 로고
    • Calcium regulation of thin filament movement in an in vitro motility assay
    • E. Homsher, B. Kim, A. Bobkova, and L.S. Tobacman Calcium regulation of thin filament movement in an in vitro motility assay Biophys. J. 70 1996 1881 1892
    • (1996) Biophys. J. , vol.70 , pp. 1881-1892
    • Homsher, E.1    Kim, B.2    Bobkova, A.3    Tobacman, L.S.4
  • 11
    • 0035092686 scopus 로고    scopus 로고
    • A myosin II mutation uncouples ATPase activity from motility and shortens step size
    • C.T. Murphy, R.S. Rock, and J.A. Spudich A myosin II mutation uncouples ATPase activity from motility and shortens step size Nat. Cell Biol. 3 2001 311 315
    • (2001) Nat. Cell Biol. , vol.3 , pp. 311-315
    • Murphy, C.T.1    Rock, R.S.2    Spudich, J.A.3
  • 14
    • 0026633888 scopus 로고
    • Velocity of movement of actin filaments in in vitro motility assay: Measured by fluorescence correlation spectroscopy
    • J. Borejdo, and S. Burlacu Velocity of movement of actin filaments in in vitro motility assay: measured by fluorescence correlation spectroscopy Biophys. J. 61 1992 1267 1280
    • (1992) Biophys. J. , vol.61 , pp. 1267-1280
    • Borejdo, J.1    Burlacu, S.2
  • 15
    • 0029953418 scopus 로고    scopus 로고
    • Modulation of actin conformation and inhibition of actin filament velocity by calponin
    • Y.S. Borovikov, K.Y. Horiuchi, S.V. Avrova, and S. Chacko Modulation of actin conformation and inhibition of actin filament velocity by calponin Biochemistry 35 1996 13849 13857
    • (1996) Biochemistry , vol.35 , pp. 13849-13857
    • Borovikov, Y.S.1    Horiuchi, K.Y.2    Avrova, S.V.3    Chacko, S.4
  • 16
    • 0031055303 scopus 로고    scopus 로고
    • Calcium regulation of skeletal muscle thin filament motility in vitro
    • A.M. Gordon, M.A. LaMadrid, Y. Chen, Z.X. Luo, and P.B. Chase Calcium regulation of skeletal muscle thin filament motility in vitro Biophys. J. 72 1997 1295 1307
    • (1997) Biophys. J. , vol.72 , pp. 1295-1307
    • Gordon, A.M.1    Lamadrid, M.A.2    Chen, Y.3    Luo, Z.X.4    Chase, P.B.5
  • 17
    • 0042929855 scopus 로고    scopus 로고
    • Cardiotonic bipyridine amrinone slows myosin-induced actin filament sliding at saturating [MgATP]
    • J. Klinth, A. Arner, and A. Månsson Cardiotonic bipyridine amrinone slows myosin-induced actin filament sliding at saturating [MgATP] J. Muscle Res. Cell Motil. 24 2003 15 32
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 15-32
    • Klinth, J.1    Arner, A.2    Månsson, A.3
  • 20
    • 0038652089 scopus 로고    scopus 로고
    • The working stroke upon myosin-nucleotide complexes binding to actin
    • W. Steffen, D. Smith, and J. Sleep The working stroke upon myosin-nucleotide complexes binding to actin Proc. Natl. Acad. Sci. USA 100 2003 6434 6439
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6434-6439
    • Steffen, W.1    Smith, D.2    Sleep, J.3
  • 21
    • 0142187316 scopus 로고    scopus 로고
    • Random walks with thin filaments: Application of in vitro motility assay to the study of actomyosin regulation
    • S. Marston Random walks with thin filaments: application of in vitro motility assay to the study of actomyosin regulation J. Muscle Res. Cell Motil. 24 2003 149 156
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 149-156
    • Marston, S.1
  • 23
    • 0033500246 scopus 로고    scopus 로고
    • A single-fiber in vitro motility assay: In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers
    • E. Thedinga, N. Karim, T. Kraft, and B. Brenner A single-fiber in vitro motility assay: in vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers J. Muscle Res. Cell Motil. 20 1999 785 796
    • (1999) J. Muscle Res. Cell Motil. , vol.20 , pp. 785-796
    • Thedinga, E.1    Karim, N.2    Kraft, T.3    Brenner, B.4
  • 24
    • 0032426470 scopus 로고    scopus 로고
    • Fluorescent phalloidin enables visualization of actin without effects on myosin's actin filament sliding velocity and hydrolytic properties in vitro
    • P. VanBuren, K. Begin, and D.M. Warshaw Fluorescent phalloidin enables visualization of actin without effects on myosin's actin filament sliding velocity and hydrolytic properties in vitro J. Mol. Cell. Cardiol. 30 1998 2777 2783
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 2777-2783
    • Vanburen, P.1    Begin, K.2    Warshaw, D.M.3
  • 25
    • 33748578087 scopus 로고    scopus 로고
    • Two fluorophores in the in vitro motility assay for the simultaneous studies of different actins
    • M. Balaz, M. Sundberg, and A. Månsson Two fluorophores in the in vitro motility assay for the simultaneous studies of different actins J. Muscle Res. Cell Motil. 25 2004 251
    • (2004) J. Muscle Res. Cell Motil. , vol.25 , pp. 251
    • Balaz, M.1    Sundberg, M.2    Månsson, A.3
  • 26
    • 85030813837 scopus 로고    scopus 로고
    • Simultaneous studies of different actins in the in vitro motility assay
    • Paper presented, Long Beach, CA
    • M. Balaz, A. Månsson, Simultaneous studies of different actins in the in vitro motility assay, Paper presented at the annual meeting of the Biophysical Society, Long Beach, CA, 2005
    • (2005) Annual Meeting of the Biophysical Society
    • Balaz, M.1    Månsson, A.2
  • 27
    • 0027236561 scopus 로고
    • Dynamic interaction between cardiac myosin isoforms modifies velocity of actomyosin sliding in vitro
    • M. Sata, S. Sugiura, H. Yamashita, S. Momomura, and T. Serizawa Dynamic interaction between cardiac myosin isoforms modifies velocity of actomyosin sliding in vitro Circ. Res. 73 1993 696 704
    • (1993) Circ. Res. , vol.73 , pp. 696-704
    • Sata, M.1    Sugiura, S.2    Yamashita, H.3    Momomura, S.4    Serizawa, T.5
  • 29
    • 0037444025 scopus 로고    scopus 로고
    • Multivariate statistics in analysis of data from the in vitro motility assay
    • A. Månsson, and S. Tågerud Multivariate statistics in analysis of data from the in vitro motility assay Anal. Biochem. 314 2003 281 293
    • (2003) Anal. Biochem. , vol.314 , pp. 281-293
    • Månsson, A.1    Tågerud, S.2
  • 30
    • 0026593496 scopus 로고
    • Phallotoxin and actin binding assay by fluorescence enhancement
    • Z.J. Huang, R.P. Haugland, W.M. You, and R.P. Haugland Phallotoxin and actin binding assay by fluorescence enhancement Anal. Biochem. 200 1992 199 204
    • (1992) Anal. Biochem. , vol.200 , pp. 199-204
    • Huang, Z.J.1    Haugland, R.P.2    You, W.M.3    Haugland, R.P.4
  • 31
    • 0033808411 scopus 로고    scopus 로고
    • Actomyosin interactions in a novel single muscle fiber in vitro motility assay
    • P. Hook, and L. Larsson Actomyosin interactions in a novel single muscle fiber in vitro motility assay J. Muscle Res. Cell Motil. 21 2000 357 365
    • (2000) J. Muscle Res. Cell Motil. , vol.21 , pp. 357-365
    • Hook, P.1    Larsson, L.2
  • 32
    • 0141856436 scopus 로고    scopus 로고
    • Two-dimensional manipulation and orientation of actin-myosin systems with dielectrophoresis
    • S.B. Asokan, L. Jawerth, R.L. Carroll, R.E. Cheney, S. Washburn, and R. Superfine Two-dimensional manipulation and orientation of actin-myosin systems with dielectrophoresis Nano Lett. 3 2003 431 437
    • (2003) Nano Lett. , vol.3 , pp. 431-437
    • Asokan, S.B.1    Jawerth, L.2    Carroll, R.L.3    Cheney, R.E.4    Washburn, S.5    Superfine, R.6
  • 33
    • 0035677405 scopus 로고    scopus 로고
    • Phalloidin affects the myosin-dependent sliding velocities of actin filaments in a bound-divalent cation dependent manner
    • K. Tokuraku, and T.Q.P. Uyeda Phalloidin affects the myosin-dependent sliding velocities of actin filaments in a bound-divalent cation dependent manner J. Muscle Res. Cell Motil. 22 2001 371 378
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 371-378
    • Tokuraku, K.1    Uyeda, T.Q.P.2
  • 34
    • 10944231111 scopus 로고    scopus 로고
    • The tail of myosin reduces actin filament velocity in the in vitro motility assay
    • B. Guo, and W.H. Guilford The tail of myosin reduces actin filament velocity in the in vitro motility assay Cell Motil. Cytoskel. 59 2004 264 272
    • (2004) Cell Motil. Cytoskel. , vol.59 , pp. 264-272
    • Guo, B.1    Guilford, W.H.2
  • 35
    • 0018553475 scopus 로고
    • The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle
    • J. Vandekerckhove, and K. Weber The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle Differentiation 14 1979 123 133
    • (1979) Differentiation , vol.14 , pp. 123-133
    • Vandekerckhove, J.1    Weber, K.2
  • 36
    • 0027223768 scopus 로고
    • Smooth and skeletal-muscle actin are mechanically indistinguishable in the in vitro motility assay
    • D.E. Harris, and D.M. Warshaw Smooth and skeletal-muscle actin are mechanically indistinguishable in the in vitro motility assay Circ. Res. 72 1993 219 224
    • (1993) Circ. Res. , vol.72 , pp. 219-224
    • Harris, D.E.1    Warshaw, D.M.2
  • 37
    • 0030450050 scopus 로고    scopus 로고
    • Polymerization and in vitro motility properties of yeast actin: A comparison with rabbit skeletal alpha-actin
    • E. Kim, C.J. Miller, and E. Reisler Polymerization and in vitro motility properties of yeast actin: a comparison with rabbit skeletal alpha-actin Biochemistry 35 1996 16566 16572
    • (1996) Biochemistry , vol.35 , pp. 16566-16572
    • Kim, E.1    Miller, C.J.2    Reisler, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.