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Volumn 86, Issue 5, 2004, Pages 3009-3019

Cross-Bridge Number, Position, and Angle in Target Zones of Cryofixed Isometrically Active Insect Flight Muscle

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MONOMER;

EID: 2142648732     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74350-7     Document Type: Article
Times cited : (37)

References (59)
  • 1
    • 0042092511 scopus 로고    scopus 로고
    • Myosin head configuration in relaxed insect flight muscle: X-ray modeled resting cross-bridges in a pre-powerstroke state are poised for actin binding
    • AL-Khayat, H. A., L. Hudson, M. K. Reedy, T. C. Irving, and J. M. Squire. 2003. Myosin head configuration in relaxed insect flight muscle: x-ray modeled resting cross-bridges in a pre-powerstroke state are poised for actin binding. Biophys. J. 85:1063-1079.
    • (2003) Biophys. J. , vol.85 , pp. 1063-1079
    • Al-Khayat, H.A.1    Hudson, L.2    Reedy, M.K.3    Irving, T.C.4    Squire, J.M.5
  • 3
    • 0036421146 scopus 로고    scopus 로고
    • Molecular modeling of averaged rigor cross-bridges from tomograms of insect flight muscle
    • Chen, L. F., H. Winkler, M. K. Reedy, M. C. Reedy, and K. A. Taylor. 2002. Molecular modeling of averaged rigor cross-bridges from tomograms of insect flight muscle. J. Struct. Biol. 138:92-104.
    • (2002) J. Struct. Biol. , vol.138 , pp. 92-104
    • Chen, L.F.1    Winkler, H.2    Reedy, M.K.3    Reedy, M.C.4    Taylor, K.A.5
  • 6
    • 0026580032 scopus 로고
    • Electron microscopy of the actin-myosin head complex in the presence of ATP
    • Frado, L.-L., and R. Craig. 1992. Electron microscopy of the actin-myosin head complex in the presence of ATP. J. Mol. Biol. 223:391-397.
    • (1992) J. Mol. Biol. , vol.223 , pp. 391-397
    • Frado, L.-L.1    Craig, R.2
  • 7
    • 0029968751 scopus 로고    scopus 로고
    • Force responses following stepwise length changes of rat skeletal muscle fibre types
    • Galler, S., K. Hilber, and D. Pette. 1996. Force responses following stepwise length changes of rat skeletal muscle fibre types. J. Physiol. 493:219-227.
    • (1996) J. Physiol. , vol.493 , pp. 219-227
    • Galler, S.1    Hilber, K.2    Pette, D.3
  • 8
    • 0021201855 scopus 로고
    • Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle
    • Geeves, M. A., R. S. Goody, and H. Gutfreund. 1984. Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle. J. Muscle Res. Cell Motil. 5:351-361.
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 351-361
    • Geeves, M.A.1    Goody, R.S.2    Gutfreund, H.3
  • 9
    • 0023161165 scopus 로고
    • Kinetics of the actomyosin ATPase in muscle fibers
    • Goldman, Y. E. 1987. Kinetics of the actomyosin ATPase in muscle fibers. Annu. Rev. Physiol. 49:637-654.
    • (1987) Annu. Rev. Physiol. , vol.49 , pp. 637-654
    • Goldman, Y.E.1
  • 10
    • 0032478543 scopus 로고    scopus 로고
    • Wag the tail: Structural dynamics of actomyosin
    • Goldman, Y. E. 1998. Wag the tail: structural dynamics of actomyosin. Cell. 93:1-4.
    • (1998) Cell , vol.93 , pp. 1-4
    • Goldman, Y.E.1
  • 11
    • 0036214903 scopus 로고    scopus 로고
    • A model of cross-bridge attachment to actin in the A-M-ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle
    • Gu, J., S. Xu, and L. C. Yu. 2002. A model of cross-bridge attachment to actin in the A-M-ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle. Biophys. J. 82:2123-2133.
    • (2002) Biophys. J. , vol.82 , pp. 2123-2133
    • Gu, J.1    Xu, S.2    Yu, L.C.3
  • 12
    • 0001547482 scopus 로고
    • The apparent rates of crossbridge attachment and detachment estimated from ATPase activity in insect flight muscle
    • Güth, K., K. J. V. Poole, D. Maughan, and H. J. Kuhn. 1987. The apparent rates of crossbridge attachment and detachment estimated from ATPase activity in insect flight muscle. Biophys. J. 52:1039-1045.
    • (1987) Biophys. J. , vol.52 , pp. 1039-1045
    • Güth, K.1    Poole, K.J.V.2    Maughan, D.3    Kuhn, H.J.4
  • 13
    • 0021329308 scopus 로고
    • Geometrical constraints affecting crossbridge formation in insect flight muscle
    • Haselgrove, J. C., and M. K. Reedy, 1984. Geometrical constraints affecting crossbridge formation in insect flight muscle. J. Muscle Res. Cell Motil. 5:3-24.
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 3-24
    • Haselgrove, J.C.1    Reedy, M.K.2
  • 14
    • 0027220075 scopus 로고
    • Structural change of crossbridges of rabbit skeletal muscle during isometric contraction
    • Hirose, K., and T. Wakabayashi. 1993. Structural change of crossbridges of rabbit skeletal muscle during isometric contraction. J. Muscle Res. Cell Motil. 14:432-445.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 432-445
    • Hirose, K.1    Wakabayashi, T.2
  • 15
    • 0027291949 scopus 로고
    • Flash and smash: Rapid freezing of muscle fibers activated by photolysis of caged ATP
    • Hirose, K., T. D. Lenart, J. M. Murray, C. Franzini-Armstrong, and Y. E. Goldman. 1993. Flash and smash: rapid freezing of muscle fibers activated by photolysis of caged ATP. Biophys. J. 65:397-408.
    • (1993) Biophys. J. , vol.65 , pp. 397-408
    • Hirose, K.1    Lenart, T.D.2    Murray, J.M.3    Franzini-Armstrong, C.4    Goldman, Y.E.5
  • 16
    • 0027959756 scopus 로고
    • Structural changes in muscle crossbridges accompanying force generation
    • Hirose, K., C. Franzini-Armstrong, Y. E. Goldman, and J. M. Murray. 1994. Structural changes in muscle crossbridges accompanying force generation. J. Cell Biol. 127:763-778.
    • (1994) J. Cell Biol. , vol.127 , pp. 763-778
    • Hirose, K.1    Franzini-Armstrong, C.2    Goldman, Y.E.3    Murray, J.M.4
  • 17
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever-arm hypothesis of muscle contraction
    • Holmes, K. C. 1997. The swinging lever-arm hypothesis of muscle contraction. Curr. Biol. 7:R112-R118.
    • (1997) Curr. Biol. , vol.7
    • Holmes, K.C.1
  • 19
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and R. M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 20
    • 0020485885 scopus 로고
    • Flexibility of myosin rod determined for dilute solution viscoelastic measurements
    • Hvidt, S., F. H. Nestler, M. L. Greaser, and J. D. Ferry. 1982. Flexibility of myosin rod determined for dilute solution viscoelastic measurements. Biochemistry. 21:4064-4073.
    • (1982) Biochemistry , vol.21 , pp. 4064-4073
    • Hvidt, S.1    Nestler, F.H.2    Greaser, M.L.3    Ferry, J.D.4
  • 24
    • 0032426674 scopus 로고    scopus 로고
    • Three-dimensional image analysis of myosin head in function as captured by quick-freeze deep-etch replica electron microscopy
    • Katayama, E., G. Ohmori, and N. Baba. 1998. Three-dimensional image analysis of myosin head in function as captured by quick-freeze deep-etch replica electron microscopy. Adv. Exp. Med. Biol. 453:37-45.
    • (1998) Adv. Exp. Med. Biol. , vol.453 , pp. 37-45
    • Katayama, E.1    Ohmori, G.2    Baba, N.3
  • 25
    • 0035997061 scopus 로고    scopus 로고
    • Direct modeling of x- ray diffraction pattern from skeletal muscle in rigor
    • Koubassova, N. A., and A. K. Tsaturyan. 2002. Direct modeling of x- ray diffraction pattern from skeletal muscle in rigor. Biophys. J. 83:1082-1097.
    • (2002) Biophys. J. , vol.83 , pp. 1082-1097
    • Koubassova, N.A.1    Tsaturyan, A.K.2
  • 26
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J. R., D. N. Mastronarde, and J. R. McIntosh. 1996. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 28
    • 0031958205 scopus 로고    scopus 로고
    • The stiffness of skeletal muscle in isometric contraction and rigor: The fraction of myosin heads bound to actin
    • Linari, M., I. Dobbie, M. Reconditi, N. Koubassova, M. Irving, G. Piazzesi, and V. Lombardi. 1998. The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin. Biophys. J. 74:2459-2473.
    • (1998) Biophys. J. , vol.74 , pp. 2459-2473
    • Linari, M.1    Dobbie, I.2    Reconditi, M.3    Koubassova, N.4    Irving, M.5    Piazzesi, G.6    Lombardi, V.7
  • 30
    • 0015506180 scopus 로고
    • Structure of insect fibrillar flight muscle in the presence and absence of ATP
    • Miller, A., and R. T. Tregear. 1972. Structure of insect fibrillar flight muscle in the presence and absence of ATP. J. Mol. Biol. 70:85-104.
    • (1972) J. Mol. Biol. , vol.70 , pp. 85-104
    • Miller, A.1    Tregear, R.T.2
  • 31
    • 0028964579 scopus 로고
    • Single molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers
    • Molloy, J. E., J. E. Bums, J. C. Sparrow, R. T. Tregear, J. Kendrick-Jones, and D. C. S. White, 1995. Single molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers. Biophys. J. 68:298s-350s.
    • (1995) Biophys. J. , vol.68
    • Molloy, J.E.1    Bums, J.E.2    Sparrow, J.C.3    Tregear, R.T.4    Kendrick-Jones, J.5    White, D.C.S.6
  • 32
    • 0026351550 scopus 로고
    • The 4-stranded helical arrangement of myosin heads on insect (Lethocerus) flight muscle thick filaments
    • Morris, E. P., J. M. Squire, and G. W. Fuller. 1991. The 4-stranded helical arrangement of myosin heads on insect (Lethocerus) flight muscle thick filaments. J. Struct. Biol. 107:237-249.
    • (1991) J. Struct. Biol. , vol.107 , pp. 237-249
    • Morris, E.P.1    Squire, J.M.2    Fuller, G.W.3
  • 35
    • 0024913973 scopus 로고
    • Use of image analysis to quantitate changes in form of mitochondrial DNA after x-irradiation
    • O'Neill, R. R, L. G. Mitchell, C. R. Merril, and W. S. Rasband. 1989. Use of image analysis to quantitate changes in form of mitochondrial DNA after x-irradiation. Appl. Theor. Electrophor. 1:163-167.
    • (1989) Appl. Theor. Electrophor. , vol.1 , pp. 163-167
    • O'Neill, R.R.1    Mitchell, L.G.2    Merril, C.R.3    Rasband, W.S.4
  • 38
    • 0014432527 scopus 로고
    • Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice
    • Reedy, M. K. 1968. Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice. J. Mol. Biol. 31:155-176.
    • (1968) J. Mol. Biol. , vol.31 , pp. 155-176
    • Reedy, M.K.1
  • 39
    • 0027491122 scopus 로고
    • Experiments on rigor crossbridge action and filament sliding in insect flight muscle
    • Reedy, M. K., C. Lucaveche, M. C. Reedy, and B. Somasundaram. 1993. Experiments on rigor crossbridge action and filament sliding in insect flight muscle. Adv. In Exp. Med. and Biology. 332:33-44.
    • (1993) Adv. In Exp. Med. and Biology , vol.332 , pp. 33-44
    • Reedy, M.K.1    Lucaveche, C.2    Reedy, M.C.3    Somasundaram, B.4
  • 40
    • 0028235402 scopus 로고
    • Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerus flight muscle
    • Reedy, M. C., M. K. Reedy, K. R. Leonard, and B. Bullard. 1994. Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerus flight muscle. J. Mol. Biol. 239:52-67.
    • (1994) J. Mol. Biol. , vol.239 , pp. 52-67
    • Reedy, M.C.1    Reedy, M.K.2    Leonard, K.R.3    Bullard, B.4
  • 41
    • 26744478083 scopus 로고    scopus 로고
    • Tension transients in single fibres from insect flight muscle
    • Reedy, M. K., M. Linari, C. Piperio, and G. Piazzesi. 1998. Tension transients in single fibres from insect flight muscle. Pflugers Arch. 436:R20.
    • (1998) Pflugers Arch. , vol.436
    • Reedy, M.K.1    Linari, M.2    Piperio, C.3    Piazzesi, G.4
  • 44
    • 0027999088 scopus 로고
    • Oblique section 3-D reconstruction of relaxed insect flight muscle reveals the cross-bridge lattice in helical registration
    • Schmitz, H., C. Lucaveche, M. K. Reedy, and K. A. Taylor. 1994. Oblique section 3-D reconstruction of relaxed insect flight muscle reveals the cross-bridge lattice in helical registration. Biophys. J. 67:1620-1633.
    • (1994) Biophys. J. , vol.67 , pp. 1620-1633
    • Schmitz, H.1    Lucaveche, C.2    Reedy, M.K.3    Taylor, K.A.4
  • 46
    • 0030724661 scopus 로고    scopus 로고
    • Tomographic 3D reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol
    • Schmitz, H., M. C. Reedy, M. K. Reedy, R. T. Tregear, H. Winkler, and K. A. Taylor. 1997. Tomographic 3D reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol. J. Cell Biol. 139:695-707.
    • (1997) J. Cell Biol. , vol.139 , pp. 695-707
    • Schmitz, H.1    Reedy, M.C.2    Reedy, M.K.3    Tregear, R.T.4    Winkler, H.5    Taylor, K.A.6
  • 47
    • 0023749743 scopus 로고
    • Actin filament organization and myosin head labelling patterns in vertebrate skeletal muscles in the rigor and weak binding states
    • Squire, J. M., and J. J. Harford. 1988. Actin filament organization and myosin head labelling patterns in vertebrate skeletal muscles in the rigor and weak binding states. J. Muscle Res. Cell Motil. 9:344-358.
    • (1988) J. Muscle Res. Cell Motil. , vol.9 , pp. 344-358
    • Squire, J.M.1    Harford, J.J.2
  • 49
    • 0018688930 scopus 로고
    • Mechanism of the actomyosin adenosine triphosphatase. Evidence that adenosine 5′-triphosphate hydrolysis can occur without dissociation of the actomyosin complex
    • Stein, L. A., R. P. Schwartz, Jr., P. B. Chock, and E. Eisenberg. 1979. Mechanism of the actomyosin adenosine triphosphatase. Evidence that adenosine 5′-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. Biochemistry. 18:3895-3909.
    • (1979) Biochemistry , vol.18 , pp. 3895-3909
    • Stein, L.A.1    Schwartz Jr., R.P.2    Chock, P.B.3    Eisenberg, E.4
  • 50
    • 0019544621 scopus 로고
    • Mechanism of the actomyosin ATPase: Effect of actin on the ATP hydrolysis step
    • Stein, L. A., P. B. Chock, and E. Eisenberg. 1981. Mechanism of the actomyosin ATPase: effect of actin on the ATP hydrolysis step. Proc. Natl. Acad. Sci. USA. 78:1346-1350.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1346-1350
    • Stein, L.A.1    Chock, P.B.2    Eisenberg, E.3
  • 55
    • 0033582235 scopus 로고    scopus 로고
    • Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: Evidence that the start of the crossbridge power stroke in muscle has variable geometry
    • Walker, M., X.-Z. Zhang, W. Jiang, J. Trinick, and H. D. White. 1999. Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: evidence that the start of the crossbridge power stroke in muscle has variable geometry. Proc. Natl. Acad. Sci. USA. 96:465-470.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 465-470
    • Walker, M.1    Zhang, X.-Z.2    Jiang, W.3    Trinick, J.4    White, H.D.5
  • 57
    • 0030823636 scopus 로고    scopus 로고
    • Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate
    • White, H. D., B. Belknap, and M. R. Webb. 1997. Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate. Biochemistry. 36:11828-11836.
    • (1997) Biochemistry , vol.36 , pp. 11828-11836
    • White, H.D.1    Belknap, B.2    Webb, M.R.3
  • 58
    • 0030175214 scopus 로고    scopus 로고
    • Three-dimensional distortion correction applied to tomographic reconstructions of sectioned crystals
    • Winkler, H., and K. A. Taylor. 1996. Three-dimensional distortion correction applied to tomographic reconstructions of sectioned crystals. Ultramicroscopy. 63:125-132.
    • (1996) Ultramicroscopy , vol.63 , pp. 125-132
    • Winkler, H.1    Taylor, K.A.2
  • 59
    • 0018580286 scopus 로고
    • Filament geometry and the activation of insect flight muscles
    • Wray, J. S. 1979. Filament geometry and the activation of insect flight muscles. Nature. 280:325-326.
    • (1979) Nature , vol.280 , pp. 325-326
    • Wray, J.S.1


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